|
Name |
Accession |
Description |
Interval |
E-value |
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
102-1145 |
0e+00 |
|
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: 615.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 102 PFSLAPMQHAMWVGRQENQQLGGVAGHLYVEFDGGGIDPERLRAAATALARRHPMLRVRFLPDGTQRIAPADEFGPFPVH 181
Cdd:COG1020 23 AQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRPVQVIQPVVAAPLPVVVLLVD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 182 VEDLRERSTGEADRRLAAIRAAKSHQQLDGAVFELAVTLLPAERSRLHVDLDMQAADAMSYRTLMADLAALYLGRDLPEL 261
Cdd:COG1020 103 LEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLLLAELLRLYLAAYAGAPLPLP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 262 GYTYRQYRHAIEAEDARPQPARDADRAWWARRLPELPDPPALPTTGGRAENQS---TRRWHWLDPHTRDALFARAQARGF 338
Cdd:COG1020 183 PLPIQYADYALWQREWLQGEELARQLAYWRQQLAGLPPLLELPTDRPRPAVQSyrgARVSFRLPAELTAALRALARRHGV 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 339 TPAMALAAGFANTLARWSTTSRFLLNVPLFGRQalHPDVDSLVGDFTSSLLLDVDLTRANTAAARAQVVQDAMRTAAAHS 418
Cdd:COG1020 263 TLFMVLLAAFALLLARYSGQDDVVVGTPVAGRP--RPELEGLVGFFVNTLPLRVDLSGDPSFAELLARVRETLLAAYAHQ 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 419 AYPGLAVLRDLSRHRGTQVLApvVFTSALGLGELFSSDV--TGQFGTPGWIISQGPQVLLDAQVTEFDGGVLVNWDVREG 496
Cdd:COG1020 341 DLPFERLVEELQPERDLSRNP--LFQVMFVLQNAPADELelPGLTLEPLELDSGTAKFDLTLTVVETGDGLRLTLEYNTD 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 497 VFPAGVIDAMFAHHIDELLRLASADEAWEAPGPPALPEAQRAVREAANG-RTAEPSGEALHDGFFRQAEQRPDAPAVFAS 575
Cdd:COG1020 419 LFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQLLAEWNAtAAPYPADATLHELFEAQAARTPDAVAVVFG 498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 576 SGDLSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIGVDQPRDRAERILESGGVSLAV 655
Cdd:COG1020 499 DQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYMLEDAGARLVL 578
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 656 VCGG--QRLSMPVPEVVLADILGGAPASTEITSARVDPAALAYVLFTSGSTGEPKGVEVTHDAAMNTVEFIGRHFDIGPA 733
Cdd:COG1020 579 TQSAlaARLPELGVPVLALDALALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPG 658
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 734 DRCLALSTLEGDISVMDVFVTLRTGGSIVVVDEVQRRDPDAWARLIDAHQVTVLHFMPGWLEMLVEVGRGRLSSVRVVPT 813
Cdd:COG1020 659 DRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLLRALLDAAPEALPSLRLVLV 738
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 814 GGDWVRPEVVRRLRVEAPGVRFAGLGGATETPVHNSIFEVTEPiPDDWTALPFGVPLPNNACRVVDDTGADCPDWVPGEY 893
Cdd:COG1020 739 GGEALPPELVRRWRARLPGARLVNLYGPTETTVDSTYYEVTPP-DADGGSVPIGRPIANTRVYVLDAHLQPVPVGVPGEL 817
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 894 WVSGRGIARGYRGRPDLTAERFVEH----DGRIWYRTGDLVRYWPDGTLEFVGRADHRVKISGYRVELGEVETALRRVPG 969
Cdd:COG1020 818 YIGGAGLARGYLNRPELTAERFVADpfgfPGARLYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQHPG 897
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 970 VRTAVAALIAVSGESDVLAAQVCADD-ASVTAEGIRQALADLVPAHMIPRHITVVERIGFTDAGKLDRRAVARELESAvs 1048
Cdd:COG1020 898 VREAVVVAREDAPGDKRLVAYVVPEAgAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAAAA-- 975
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 1049 qsqRPGHRAPSTPLQSALATIVGDLLGRQNIGIDDDFFALGGDSVLATQAVARIRAWLDAPDIMVADIFANRTVSALAAV 1128
Cdd:COG1020 976 ---AAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLLFLAAAAAAAAAAA 1052
|
1050
....*....|....*..
gi 497641516 1129 LGAGERDPGRLDQVAEL 1145
Cdd:COG1020 1053 AAAAAAAAAPLAAAAAP 1069
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
567-1039 |
4.21e-179 |
|
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: 533.77 E-value: 4.21e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 567 PDAPAVFASSGDLSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIGVDQPRDRAERIL 646
Cdd:cd12114 1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 647 ESGGVSLAVVCGGQRLSMPVPEVVLADILGGAPASTEITSARVDPAALAYVLFTSGSTGEPKGVEVTHDAAMNTVEFIGR 726
Cdd:cd12114 81 ADAGARLVLTDGPDAQLDVAVFDVLILDLDALAAPAPPPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTILDINR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 727 HFDIGPADRCLALSTLEGDISVMDVFVTLRTGGSIVVVDEVQRRDPDAWARLIDAHQVTVLHFMPGWLEMLVEVGR---G 803
Cdd:cd12114 161 RFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDPAHWAELIERHGVTLWNSVPALLEMLLDVLEaaqA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 804 RLSSVRVVPTGGDWVRPEVVRRLRVEAPGVRFAGLGGATETPVHNSIFEVTEPiPDDWTALPFGVPLPNNACRVVDDTGA 883
Cdd:cd12114 241 LLPSLRLVLLSGDWIPLDLPARLRALAPDARLISLGGATEASIWSIYHPIDEV-PPDWRSIPYGRPLANQRYRVLDPRGR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 884 DCPDWVPGEYWVSGRGIARGYRGRPDLTAERFVEH-DGRIWYRTGDLVRYWPDGTLEFVGRADHRVKISGYRVELGEVET 962
Cdd:cd12114 320 DCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHpDGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEA 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497641516 963 ALRRVPGVRTAVAALIAVSGESDVLAAQVC-ADDASVTAEGIRQALADLVPAHMIPRHITVVERIGFTDAGKLDRRAV 1039
Cdd:cd12114 400 ALQAHPGVARAVVVVLGDPGGKRLAAFVVPdNDGTPIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| Cyc_NRPS |
cd19535 |
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
102-521 |
1.74e-170 |
|
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Cyc (heterocyclization) domains catalyze two separate reactions in the creation of heterocyclized peptide products in nonribosomal peptide synthesis: amide bond formation followed by intramolecular cyclodehydration between a Cys, Ser, or Thr side chain and a carbonyl carbon on the peptide backbone to form a thiazoline, oxazoline, or methyloxazoline ring. Cyc-domains are homologous to standard NRPS Condensation (C) domains. C-domains typically have a conserved HHxxxD motif at the active site; Cyc-domains have an alternative, conserved DxxxxD active site motif, mutation of the aspartate residues in this motif can abolish or diminish condensation activity. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and Cyc-domains. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380458 [Multi-domain] Cd Length: 423 Bit Score: 509.34 E-value: 1.74e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 102 PFSLAPMQHAMWVGRQENQQLGGVAGHLYVEFDGGGIDPERLRAAATALARRHPMLRVRFLPDGTQRIAPADEFGPFPVH 181
Cdd:cd19535 1 PFPLTDVQYAYWIGRQDDQELGGVGCHAYLEFDGEDLDPDRLERAWNKLIARHPMLRAVFLDDGTQQILPEVPWYGITVH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 182 veDLRERSTGEADRRLAAIRAAKSHQQLD---GAVFELAVTLLPAERSRLHVDLDMQAADAMSYRTLMADLAALYLGRD- 257
Cdd:cd19535 81 --DLRGLSEEEAEAALEELRERLSHRVLDverGPLFDIRLSLLPEGRTRLHLSIDLLVADALSLQILLRELAALYEDPGe 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 258 -LPELGYTYRQYrhaIEAEDARPQPARDADRAWWARRLPELPDPPALPT---TGGRAENQSTRRWHWLDPHTRDALFARA 333
Cdd:cd19535 159 pLPPLELSFRDY---LLAEQALRETAYERARAYWQERLPTLPPAPQLPLakdPEEIKEPRFTRREHRLSAEQWQRLKERA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 334 QARGFTPAMALAAGFANTLARWSTTSRFLLNVPLFGRQALHPDVDSLVGDFTSSLLLDVDLTRANTAAARAQVVQDAMRT 413
Cdd:cd19535 236 RQHGVTPSMVLLTAYAEVLARWSGQPRFLLNLTLFNRLPLHPDVNDVVGDFTSLLLLEVDGSEGQSFLERARRLQQQLWE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 414 AAAHSAYPGLAVLRDLSRHRG-TQVLAPVVFTSALGLGELFsSDVTGQFGTPGWIISQGPQVLLDAQVTEFDGGVLVNWD 492
Cdd:cd19535 316 DLDHSSYSGVVVVRRLLRRRGgQPVLAPVVFTSNLGLPLLD-EEVREVLGELVYMISQTPQVWLDHQVYEEDGGLLLNWD 394
|
410 420
....*....|....*....|....*....
gi 497641516 493 VREGVFPAGVIDAMFAHHIDELLRLASAD 521
Cdd:cd19535 395 AVDELFPEGMLDDMFDAYVRLLERLADDD 423
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
154-1163 |
1.50e-139 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 468.87 E-value: 1.50e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 154 HPMLRVRFLPDGTQRIAPADEFGPFPVHVEDLRERSTGEADRRLAAIRAAKSHQQLD---GAVFELAVTLLPAERSRLHV 230
Cdd:PRK12467 100 HESLRTRFVQDEEGFRQVIDASLSLTIPLDDLANEQGRARESQIEAYINEEVARPFDlanGPLLRVRLLRLADDEHVLVV 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 231 DLDMQAADAMSYRTLMADLAALYLGR------DLPELGYTYRQY----RHAIEAEDarpqpaRDADRAWWARRLPELPDP 300
Cdd:PRK12467 180 TLHHIISDGWSMRVLVEELVQLYSAYsqgrepSLPALPIQYADYaiwqRSWLEAGE------RERQLAYWQEQLGGEHTV 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 301 PALPTTGGRAENQSTR----RWHwLDPHTRDALFARAQARGFTPAMALAAGFANTLARWSTTSRFLLNVPLFGRQALhpD 376
Cdd:PRK12467 254 LELPTDRPRPAVPSYRgarlRVD-LPQALSAGLKALAQREGVTLFMVLLASFQTLLHRYSGQSDIRIGVPNANRNRV--E 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 377 VDSLVGDFTSSLLLDVDLTRANTAAARAQVVQDAMRTAAAHSAYP--GLAVLRDLSRHRGTQVLAPVVF---TSALGLGE 451
Cdd:PRK12467 331 TERLIGFFVNTQVLKAEVDPQASFLELLQQVKRTALGAQAHQDLPfeQLVEALQPERSLSHSPLFQVMFnhqNTATGGRD 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 452 LFSSDVTGQFGTPGWIISQGPQVLLDAQVTEFDGGVLVNWDVREGVFPAGVIDAMFAHHIDELLRLASADEAWEAPGPPA 531
Cdd:PRK12467 411 REGAQLPGLTVEELSWARHTAQFDLALDTYESAQGLWAAFTYATDLFEATTIERLATHWRNLLEAIVAEPRRRLGELPLL 490
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 532 LPEAQRAVREAANGRTAEPSGEALHDGFFRQAEQRPDAPAVFASSGDLSYAQLRDQALAVAAALRAAGVTAGDTIAVMGP 611
Cdd:PRK12467 491 DAEERARELVRWNAPATEYAPDCVHQLIEAQARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVE 570
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 612 KTAEQIPALLGILSVGAVYLPIGVDQPRDRAERILESGGVSLAVVCGGQRLSMPVPEVV-------LADILGGAPAstEI 684
Cdd:PRK12467 571 RSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQSHLLAQLPVPAGLrslcldePADLLCGYSG--HN 648
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 685 TSARVDPAALAYVLFTSGSTGEPKGVEVTHDAAMNTVEFIGRHFDIGPADRCLALSTLEGDISVMDVFVTLRTGGSIVVV 764
Cdd:PRK12467 649 PEVALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLL 728
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 765 DEVQRRDPDAWARLIDAHQVTVLHFMPGWLEMLVEVGRGRL-SSVRVVPTGGDWVRPEVVRRLRVEAPGVRFAGLGGATE 843
Cdd:PRK12467 729 PPDCARDAEAFAALMADQGVTVLKIVPSHLQALLQASRVALpRPQRALVCGGEALQVDLLARVRALGPGARLINHYGPTE 808
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 844 TPVHNSIFEVTEpIPDDWTALPFGVPLPNNACRVVDDTGADCPDWVPGEYWVSGRGIARGYRGRPDLTAERFVEH----D 919
Cdd:PRK12467 809 TTVGVSTYELSD-EERDFGNVPIGQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDpfgaD 887
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 920 GRIWYRTGDLVRYWPDGTLEFVGRADHRVKISGYRVELGEVETALRRVPGVRTAVaaLIAVSGESDV-----LAAQVCAD 994
Cdd:PRK12467 888 GGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAV--VLAQPGDAGLqlvayLVPAAVAD 965
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 995 DA--SVTAEGIRQALADLVPAHMIPRHITVVERIGFTDAGKLDRRAVARELESAVSQSqrpgHRAPSTPLQSALATIVGD 1072
Cdd:PRK12467 966 GAehQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPKPDASAVQAT----FVAPQTELEKRLAAIWAD 1041
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 1073 LLGRQNIGIDDDFFALGGDSVLATQAVARIRAWLDApDIMVADIFANRTVSALAAVLGAGerdpgrlDQVAELYLEVIGM 1152
Cdd:PRK12467 1042 VLKVERVGLTDNFFELGGHSLLATQVISRVRQRLGI-QVPLRTLFEHQTLAGFAQAVAAQ-------QQGAQPALPDVDR 1113
|
1050
....*....|.
gi 497641516 1153 DAESVLAASQQ 1163
Cdd:PRK12467 1114 DQPLPLSYAQE 1124
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
567-1038 |
3.01e-138 |
|
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: 426.17 E-value: 3.01e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 567 PDAPAVFASSGDLSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIGVDQPRDRAERIL 646
Cdd:cd05930 1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 647 ESGGVSLAVVcggqrlsmpvpevvladilggapasteitsarvDPAALAYVLFTSGSTGEPKGVEVTHDAAMNTVEFIGR 726
Cdd:cd05930 81 EDSGAKLVLT---------------------------------DPDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQE 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 727 HFDIGPADRCLALSTLEGDISVMDVFVTLRTGGSIVVVDEVQRRDPDAWARLIDAHQVTVLHFMPGWLEMLVEVG-RGRL 805
Cdd:cd05930 128 AYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSLLRLLLQELeLAAL 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 806 SSVRVVPTGGDWVRPEVVRRLRVEAPGVRFAGLGGATETPVHNSIFEVTEPiPDDWTALPFGVPLPNNACRVVDDTGADC 885
Cdd:cd05930 208 PSLRLVLVGGEALPPDLVRRWRELLPGARLVNLYGPTEATVDATYYRVPPD-DEEDGRVPIGRPIPNTRVYVLDENLRPV 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 886 PDWVPGEYWVSGRGIARGYRGRPDLTAERFVEH---DGRIWYRTGDLVRYWPDGTLEFVGRADHRVKISGYRVELGEVET 962
Cdd:cd05930 287 PPGVPGELYIGGAGLARGYLNRPELTAERFVPNpfgPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEA 366
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497641516 963 ALRRVPGVRTAVAALIAVSGESDVLAAQ-VCADDASVTAEGIRQALADLVPAHMIPRHITVVERIGFTDAGKLDRRA 1038
Cdd:cd05930 367 ALLAHPGVREAAVVAREDGDGEKRLVAYvVPDEGGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKA 443
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
599-975 |
1.08e-131 |
|
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: 407.42 E-value: 1.08e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 599 GVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIGVDQPRDRAERILESGGVSLAVVCGGQRLSMP--VPEVVLADILG 676
Cdd:TIGR01733 21 GVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDSALASRLAglVLPVILLDPLE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 677 GAPASTEIT----SARVDPAALAYVLFTSGSTGEPKGVEVTHDAAMNTVEFIGRHFDIGPADRCLALSTLEGDISVMDVF 752
Cdd:TIGR01733 101 LAALDDAPAppppDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDPDDRVLQFASLSFDASVEEIF 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 753 VTLRTGGSIVVVDEVQRRDPDA-WARLIDAHQVTVLHFMPGWLEMLVEVGRGRLSSVRVVPTGGDWVRPEVVRRLRVEAP 831
Cdd:TIGR01733 181 GALLAGATLVVPPEDEERDDAAlLAALIAEHPVTVLNLTPSLLALLAAALPPALASLRLVILGGEALTPALVDRWRARGP 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 832 GVRFAGLGGATETPVHNSIFEVTEPIPDDWTALPFGVPLPNNACRVVDDTGADCPDWVPGEYWVSGRGIARGYRGRPDLT 911
Cdd:TIGR01733 261 GARLINLYGPTETTVWSTATLVDPDDAPRESPVPIGRPLANTRLYVLDDDLRPVPVGVVGELYIGGPGVARGYLNRPELT 340
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497641516 912 AERFVEH-----DGRIWYRTGDLVRYWPDGTLEFVGRADHRVKISGYRVELGEVETALRRVPGVRTAVA 975
Cdd:TIGR01733 341 AERFVPDpfaggDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
559-1038 |
4.18e-119 |
|
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: 376.93 E-value: 4.18e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 559 FFRQAEQRPDAPAVFASSGDLSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIGVDQP 638
Cdd:cd12117 3 FEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 639 RDRAERILESGGVSLAVVCGGQRLSMPVPEVVLADILGGAPASTEITSARVDPAALAYVLFTSGSTGEPKGVEVTHDAAM 718
Cdd:cd12117 83 AERLAFMLADAGAKVLLTDRSLAGRAGGLEVAVVIDEALDAGPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVAVTHRGVV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 719 NTVeFIGRHFDIGPADRCLALSTLEGDISVMDVFVTLRTGGSIVVVDEVQRRDPDAWARLIDAHQVTVLHFMPGWLEMLV 798
Cdd:cd12117 163 RLV-KNTNYVTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPDALGALIAEEGVTVLWLTAALFNQLA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 799 EVGRGRLSSVRVVPTGGDWVRPEVVRRLRVEAPGVRFAGLGGATETPVHNSIFEVTEPIPDDwTALPFGVPLPNNACRVV 878
Cdd:cd12117 242 DEDPECFAGLRELLTGGEVVSPPHVRRVLAACPGLRLVNGYGPTENTTFTTSHVVTELDEVA-GSIPIGRPIANTRVYVL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 879 DDTGADCPDWVPGEYWVSGRGIARGYRGRPDLTAERFVEH---DGRIWYRTGDLVRYWPDGTLEFVGRADHRVKISGYRV 955
Cdd:cd12117 321 DEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADpfgPGERLYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 956 ELGEVETALRRVPGVRTAVAALIAVSGESDVLAAQVCADDAsVTAEGIRQALADLVPAHMIPRHITVVERIGFTDAGKLD 1035
Cdd:cd12117 401 ELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVAEGA-LDAAELRAFLRERLPAYMVPAAFVVLDELPLTANGKVD 479
|
...
gi 497641516 1036 RRA 1038
Cdd:cd12117 480 RRA 482
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
9-1141 |
8.85e-116 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 398.38 E-value: 8.85e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 9 EDIRAEV-AELLGVDAdaVQPGSNLIGQGLDSIRIMTLAGRWRRQ-GIAVDFATLAETPTVEAWAELVNAGKPSAdrpae 86
Cdd:PRK12467 1032 EKRLAAIwADVLKVER--VGLTDNFFELGGHSLLATQVISRVRQRlGIQVPLRTLFEHQTLAGFAQAVAAQQQGA----- 1104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 87 padaPADAGRSGEDEPFSLAPMQHAMWVGRQENQQLGG----VAGHLYvefdgGGIDPERLRAAATALARRHPMLRVRFL 162
Cdd:PRK12467 1105 ----QPALPDVDRDQPLPLSYAQERQWFLWQLEPGSAAyhipQALRLK-----GPLDIEALERSFDALVARHESLRTTFV 1175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 163 PDGTQRIAPADEFGPFPVHVEDLRerSTGEADRRLAAIRAAKSHQQLD---GAVFELAVTLLPAERSRLHVDLDMQAADA 239
Cdd:PRK12467 1176 QEDGRTRQVIHPVGSLTLEEPLLL--AADKDEAQLKVYVEAEARQPFDleqGPLLRVGLLRLAADEHVLVLTLHHIVSDG 1253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 240 MSYRTLMADLAALYLGR------DLPELGYTYRQY----RHAIEAEDarpqpaRDADRAWWARRLPELPDPPALPTTGGR 309
Cdd:PRK12467 1254 WSMQVLVDELVALYAAYsqgqslQLPALPIQYADYavwqRQWMDAGE------RARQLAYWKAQLGGEQPVLELPTDRPR 1327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 310 AENQSTR----RWHwLDPHTRDALFARAQARGFTPAMALAAGFANTLARWSTTSRFLLNVPLFGRQALhpDVDSLVGDFT 385
Cdd:PRK12467 1328 PAVQSHRgarlAFE-LPPALAEGLRALARREGVTLFMLLLASFQTLLHRYSGQDDIRVGVPIANRNRA--ETEGLIGFFV 1404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 386 SSLLLDVDLTRANTAAARAQVVQDAMRTAAAHSAYP------GLAVLRDLSRHRGTQVLAPVVFTSALGLGELFSSDVTG 459
Cdd:PRK12467 1405 NTQVLRAEVDGQASFQQLLQQVKQAALEAQAHQDLPfeqlveALQPERSLSHSPLFQVMFNHQRDDHQAQAQLPGLSVES 1484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 460 QfgtpGWIiSQGPQVLLDAQVTEFDGGVLVNWDVREGVFPAGVIDAMFAHHIDELLRLASADEAWEAPGPPALPEAQRAV 539
Cdd:PRK12467 1485 L----SWE-SQTAQFDLTLDTYESSEGLQASLTYATDLFEASTIERLAGHWLNLLQGLVADPERRLGELDLLDEAERRQI 1559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 540 REAANGRTAE-PSGEALHDGFFRQAEQRPDAPAVFASSGDLSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIP 618
Cdd:PRK12467 1560 LEGWNATHTGyPLARLVHQLIEDQAAATPEAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVV 1639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 619 ALLGILSVGAVYLPIGVDQPRDRAERILESGGVSL----AVVCggQRLSMP--VPEVVL---ADILGGAPASTEITsaRV 689
Cdd:PRK12467 1640 GLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELlltqSHLQ--ARLPLPdgLRSLVLdqeDDWLEGYSDSNPAV--NL 1715
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 690 DPAALAYVLFTSGSTGEPKGVEVTHDAAMNTVEFIGRHFDIGPADRCLALSTLEGDISVMDVFVTLRTGGSIVVVDEVQR 769
Cdd:PRK12467 1716 APQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIAPPGAH 1795
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 770 RDPDAWARLIDAHQVTVLHFMPGWLEMLVEVGR--GRLSSVRVVPTGGDWVRPEVVRRLRVEAPGVRFAGLGGATETPVH 847
Cdd:PRK12467 1796 RDPEQLIQLIERQQVTTLHFVPSMLQQLLQMDEqvEHPLSLRRVVCGGEALEVEALRPWLERLPDTGLFNLYGPTETAVD 1875
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 848 NSIFEVTEPIPDDWTALPFGVPLPNNACRVVDDTGADCPDWVPGEYWVSGRGIARGYRGRPDLTAERFV-----EHDGRI 922
Cdd:PRK12467 1876 VTHWTCRRKDLEGRDSVPIGQPIANLSTYILDASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFVadpfgTVGSRL 1955
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 923 wYRTGDLVRYWPDGTLEFVGRADHRVKISGYRVELGEVETALRRVPGVRTAVaaLIAVSGE-SDVLAAQVCADDASVTAE 1001
Cdd:PRK12467 1956 -YRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAV--VIAQDGAnGKQLVAYVVPTDPGLVDD 2032
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 1002 GIRQ---------ALADLVPAHMIPRHITVVERIGFTDAGKLDRRAVAReleSAVSQSQRpGHRAPSTPLQSALATIVGD 1072
Cdd:PRK12467 2033 DEAQvalrailknHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKALPA---PDASELQQ-AYVAPQSELEQRLAAIWQD 2108
|
1130 1140 1150 1160 1170 1180
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497641516 1073 LLGRQNIGIDDDFFALGGDSVLATQAVARIRAwlDAPDIMVADIFANRTVSALAAVLGAGERDPgRLDQ 1141
Cdd:PRK12467 2109 VLGLEQVGLHDNFFELGGDSIISIQVVSRARQ--AGIRFTPKDLFQHQTVQSLAAVAQEGDGTV-SIDQ 2174
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
556-1038 |
1.55e-113 |
|
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: 362.36 E-value: 1.55e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 556 HDGFFRQAEQRPDAPAVFASSGDLSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIGV 635
Cdd:cd17646 1 HALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 636 DQPRDRAERILESGGVSLAVVCGGQRLSMPV-PEVVLADILGGAPASTEITSARVDPAALAYVLFTSGSTGEPKGVEVTH 714
Cdd:cd17646 81 GYPADRLAYMLADAGPAVVLTTADLAARLPAgGDVALLGDEALAAPPATPPLVPPRPDNLAYVIYTSGSTGRPKGVMVTH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 715 DAAMNTVEFIGRHFDIGPADRCLALSTLEGDISVMDVFVTLRTGGSIVVVDEVQRRDPDAWARLIDAHQVTVLHFMPGWL 794
Cdd:cd17646 161 AGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRDPAYLAALIREHGVTTCHFVPSML 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 795 EMLV-EVGRGRLSSVRVVPTGGDWVRPEVVRRLRvEAPGVRFAGLGGATETPVHNSIFEVTEPIPDdwTALPFGVPLPNN 873
Cdd:cd17646 241 RVFLaEPAAGSCASLRRVFCSGEALPPELAARFL-ALPGAELHNLYGPTEAAIDVTHWPVRGPAET--PSVPIGRPVPNT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 874 ACRVVDDTGADCPDWVPGEYWVSGRGIARGYRGRPDLTAERFVEH---DGRIWYRTGDLVRYWPDGTLEFVGRADHRVKI 950
Cdd:cd17646 318 RLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDpfgPGSRMYRTGDLARWRPDGALEFLGRSDDQVKI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 951 SGYRVELGEVETALRRVPGVRTAVAALIAVSGESDVLAAQVCADD--ASVTAEGIRQALADLVPAHMIPRHITVVERIGF 1028
Cdd:cd17646 398 RGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAgaAGPDTAALRAHLAERLPEYMVPAAFVVLDALPL 477
|
490
....*....|
gi 497641516 1029 TDAGKLDRRA 1038
Cdd:cd17646 478 TANGKLDRAA 487
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
11-1135 |
1.84e-113 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 391.45 E-value: 1.84e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 11 IRAEVAELLGVDAdaVQPGSNLIGQGLDSIRIMTLAGRWRRQ-GIAVDFATLAETPTVEAWAELVnagkpsADRPAEPAD 89
Cdd:PRK05691 591 IAAIWCEQLKVEQ--VAADDHFFLLGGNSIAATQVVARLRDElGIDLNLRQLFEAPTLAAFSAAV------ARQLAGGGA 662
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 90 APADAGRSGEDEPFSLAPMQHAMWVGRQENQQLGG--VAGHLYVEfdgGGIDPERLRAAATALARRHPMLRVRFLPDGTQ 167
Cdd:PRK05691 663 AQAAIARLPRGQALPQSLAQNRLWLLWQLDPQSAAynIPGGLHLR---GELDEAALRASFQRLVERHESLRTRFYERDGV 739
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 168 RIAPADEFGPFPVHVEDLRERSTGEADRRLAAIRAAKSHQQLD---GAVFELAVTLLPAERSRLHVDLDMQAADAMSYRT 244
Cdd:PRK05691 740 ALQRIDAQGEFALQRIDLSDLPEAEREARAAQIREEEARQPFDlekGPLLRVTLVRLDDEEHQLLVTLHHIVADGWSLNI 819
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 245 LMADLAALYLGR------DLPELGYTYRQY----RHAIEAEDARPQpardadRAWWARRLPELPDPPALPTT---GGRAE 311
Cdd:PRK05691 820 LLDEFSRLYAAAcqgqtaELAPLPLGYADYgawqRQWLAQGEAARQ------LAYWKAQLGDEQPVLELATDhprSARQA 893
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 312 NQSTRRWHWLDPHTRDALFARAQARGFTPAMALAAGFANTLARWSTTSRFLLNVPLFGRQalHPDVDSLVGDFTSSLLLD 391
Cdd:PRK05691 894 HSAARYSLRVDASLSEALRGLAQAHQATLFMVLLAAFQALLHRYSGQGDIRIGVPNANRP--RLETQGLVGFFINTQVLR 971
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 392 VDLTRANTAAARAQVVQDAMRTAAAHSAYPGLAVLRDLSRHRgTQVLAPVVFTSAlglgelfSSDVTGQFGTPGWIISQG 471
Cdd:PRK05691 972 AQLDGRLPFTALLAQVRQATLGAQAHQDLPFEQLVEALPQAR-EQGLFQVMFNHQ-------QRDLSALRRLPGLLAEEL 1043
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 472 P----QVLLDAQV-TEFD--GGVLVNWDVREGVFPAGVIDAMfAHHIDELLRlASADEAWEAPGPPALPEAQRAVREAAN 544
Cdd:PRK05691 1044 PwhsrEAKFDLQLhSEEDrnGRLTLSFDYAAELFDAATIERL-AEHFLALLE-QVCEDPQRALGDVQLLDAAERAQLAQW 1121
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 545 GRT-AEPSGEALHDGFFRQAEQRPDAPAVFASSGDLSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGI 623
Cdd:PRK05691 1122 GQApCAPAQAWLPELLNEQARQTPERIALVWDGGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAI 1201
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 624 LSVGAVYLPIGVDQPRDRAERILESGGVSLAVVCGGQRLSMPVPEVVLA---DILGGAPASTEITSARVDPAALAYVLFT 700
Cdd:PRK05691 1202 LKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQSHLLERLPQAEGVSAialDSLHLDSWPSQAPGLHLHGDNLAYVIYT 1281
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 701 SGSTGEPKGVEVTHDAAMNTVEFIGRHFDIGPADRCLALSTLEGDISVMDVFVTLRTGGSIVVVDEVQRRDPDAWARLID 780
Cdd:PRK05691 1282 SGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPISFDVSVWECFWPLITGCRLVLAGPGEHRDPQRIAELVQ 1361
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 781 AHQVTVLHFMPGWLEMLV-EVGRGRLSSVRVVPTGGDWVRPEVVRRLRVEAPGVRFAGLGGATETPVHNSIFEVTEpipD 859
Cdd:PRK05691 1362 QYGVTTLHFVPPLLQLFIdEPLAAACTSLRRLFSGGEALPAELRNRVLQRLPQVQLHNRYGPTETAINVTHWQCQA---E 1438
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 860 DWTALPFGVPLPNNACRVVDDTGADCPDWVPGEYWVSGRGIARGYRGRPDLTAERFVE----HDGRIWYRTGDLVRYWPD 935
Cdd:PRK05691 1439 DGERSPIGRPLGNVLCRVLDAELNLLPPGVAGELCIGGAGLARGYLGRPALTAERFVPdplgEDGARLYRTGDRARWNAD 1518
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 936 GTLEFVGRADHRVKISGYRVELGEVETALRRVPGVRTAVAALIAVSGESDVLAAQVCADDASVTAEGIRQALADLVPAHM 1015
Cdd:PRK05691 1519 GALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVREGAAGAQLVGYYTGEAGQEAEAERLKAALAAELPEYM 1598
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 1016 IPRHITVVERIGFTDAGKLDRRAVARelesavSQSQRPGHRAPSTPLQSALATIVGDLLGRQNIGIDDDFFALGGDSVLA 1095
Cdd:PRK05691 1599 VPAQLIRLDQMPLGPSGKLDRRALPE------PVWQQREHVEPRTELQQQIAAIWREVLGLPRVGLRDDFFALGGHSLLA 1672
|
1130 1140 1150 1160
....*....|....*....|....*....|....*....|....
gi 497641516 1096 TQAVARIRAWLDApDIMVADIFANRTVSALAAVLG----AGERD 1135
Cdd:PRK05691 1673 TQIVSRTRQACDV-ELPLRALFEASELGAFAEQVAriqaAGERN 1715
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
103-1132 |
1.25e-112 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 388.75 E-value: 1.25e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 103 FSLAPMQHAMWVGRQENQQLGGVAGHLYVEFDGggIDPERLRAAATALARRHPMLRVRFLPDG--TQRIAPADEFGPFPV 180
Cdd:PRK12467 2647 YPLSPMQQGMLFHTLYEGGAGDYINQMRVDVEG--LDVERFRTAWQAVIDRHEILRSGFLWDGelEEPLQVVYKQARLPF 2724
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 181 HVEDLRERSTGEAD-RRLAAIRAAKSHQQLDGAVFELAVTLLPAERSRL-----HVDLDmqaadAMSYRTLMADLAALYL 254
Cdd:PRK12467 2725 SRLDWRDRADLEQAlDALAAADRQQGFDLLSAPLLRLTLVRTGEDRHHLiytnhHILMD-----GWSGSQLLGEVLQRYF 2799
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 255 GRDLPELGYTYRQYRHAIEAEDArpqparDADRAWWARRLPELPDP----PALPTTGGRAENQSTRRWHWLDPHTRDALF 330
Cdd:PRK12467 2800 GQPPPAREGRYRDYIAWLQAQDA------EASEAFWKEQLAALEEPtrlaRALYPAPAEAVAGHGAHYLHLDATQTRQLI 2873
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 331 ARAQARGFTPAMALAAGFANTLARWSTTSRFLLNVPLFGRQALHPDVDSLVGDFTSSLLLDVDLTRANTAAARAQVVQDA 410
Cdd:PRK12467 2874 EFARRHRVTLNTLVQGAWLLLLQRFTGQDTVCFGATVAGRPAQLRGAEQQLGLFINTLPVIASPRAEQTVSDWLQQVQAQ 2953
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 411 MRTAAAHSAYPglavLRDLSR--HRGTQVL--APVVFT-------------SALGLGELFSSDVTGQFGTpgWIISQGPQ 473
Cdd:PRK12467 2954 NLALREFEHTP----LADIQRwaGQGGEALfdSILVFEnypisealkqgapSGLRFGAVSSREQTNYPLT--LAVGLGDT 3027
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 474 VLLdaqvtEFdggvlvNWDvREGVFPAGVidAMFAHHIDELLR-LASADEAWEAPGPPALPEAQRAVREAANGRTAE-PS 551
Cdd:PRK12467 3028 LEL-----EF------SYD-RQHFDAAAI--ERLAESFDRLLQaMLNNPAARLGELPTLAAHERRQVLHAWNATAAAyPS 3093
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 552 GEALHDGFFRQAEQRPDAPAVFASSGDLSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYL 631
Cdd:PRK12467 3094 ERLVHQLIEAQVARTPEAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYV 3173
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 632 PIGVDQPRDRAERILESGGVSLAVVCGGQRLSMPVPEVVLA---DILGGAPASTEITSARVDPAALAYVLFTSGSTGEPK 708
Cdd:PRK12467 3174 PLDPEYPRERLAYMIEDSGVKLLLTQAHLLEQLPAPAGDTAltlDRLDLNGYSENNPSTRVMGENLAYVIYTSGSTGKPK 3253
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 709 GVEVTHDAAMNTVEFIGRHFDIGPADRCLALSTLEGDISVMDVFVTLRTGGSIVVVDEvQRRDPDAWARLIDAHQVTVLH 788
Cdd:PRK12467 3254 GVGVRHGALANHLCWIAEAYELDANDRVLLFMSFSFDGAQERFLWTLICGGCLVVRDN-DLWDPEELWQAIHAHRISIAC 3332
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 789 FMPGWLEMLVEVGRGR-LSSVRVVPTGGDWVRPEVVRRLRVEAPGVRFAGLGGATETPVHNSIFEVTEPIPDDWTALPFG 867
Cdd:PRK12467 3333 FPPAYLQQFAEDAGGAdCASLDIYVFGGEAVPPAAFEQVKRKLKPRGLTNGYGPTEAVVTVTLWKCGGDAVCEAPYAPIG 3412
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 868 VPLPNNACRVVDDTGADCPDWVPGEYWVSGRGIARGYRGRPDLTAERFV----EHDGRIWYRTGDLVRYWPDGTLEFVGR 943
Cdd:PRK12467 3413 RPVAGRSIYVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVadpfSGSGGRLYRTGDLARYRADGVIEYLGR 3492
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 944 ADHRVKISGYRVELGEVETALRRVPGVRTAVAALIAVSGESDVLAAQVCADDASVTAEGIRQALADLVPAHMIPRHITVV 1023
Cdd:PRK12467 3493 IDHQVKIRGFRIELGEIEARLLQHPSVREAVVLARDGAGGKQLVAYVVPADPQGDWRETLRDHLAASLPDYMVPAQLLVL 3572
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 1024 ERIGFTDAGKLDRRAVAReLESAVSQSqrpgHRAPSTPLQSALATIVGDLLGRQNIGIDDDFFALGGDSVLATQAVARIR 1103
Cdd:PRK12467 3573 AAMPLGPNGKVDRKALPD-PDAKGSRE----YVAPRSEVEQQLAAIWADVLGVEQVGVTDNFFELGGDSLLALQVLSRIR 3647
|
1050 1060
....*....|....*....|....*....
gi 497641516 1104 AWLDApDIMVADIFANRTVSALAAVLGAG 1132
Cdd:PRK12467 3648 QSLGL-KLSLRDLMSAPTIAELAGYSPLG 3675
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
103-1149 |
9.78e-112 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 386.23 E-value: 9.78e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 103 FSLAPMQHAMWVGRQENQQLGGVAGHLYVEFDGggIDPERLRAAATALARRHPMLRVRFLPDGT--QRIAPADEFGPFPV 180
Cdd:PRK12316 4103 YPLSPMQQGMLFHSLYEQEAGDYINQMRVDVQG--LDVERFRAAWQAALDRHDVLRSGFVWQGElgRPLQVVHKQVSLPF 4180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 181 HVEDLRERSTGEAD-RRLAAIRAAKSHQQLDGAVFELAVTLLPAERSRLHVDLDMQAADAMSYRTLMADLAALYLGRDLP 259
Cdd:PRK12316 4181 AELDWRGRADLQAAlDALAAAERERGFDLQRAPLLRLVLVRTAEGRHHLIYTNHHILMDGWSNSQLLGEVLERYSGRPPA 4260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 260 ELGYTYRQYRHAIEAEDarpqpaRDADRAWWARRLPELPDPPALPTTGGRAENQSTRRW----HWLDPHTRDALFARAQA 335
Cdd:PRK12316 4261 QPGGRYRDYIAWLQRQD------AAASEAFWREQLAALDEPTRLAQAIARADLRSANGYgehvRELDATATARLREFART 4334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 336 RGFTPAMALAAGFANTLARWSTTSRFLLNVPLFGRQALHPDVDSLVGDFTSSLLLDVDLTRANTAAARAQVVQDAMRTAA 415
Cdd:PRK12316 4335 QRVTLNTLVQAAWLLLLQRYTGQDTVAFGATVAGRPAELPGIEGQIGLFINTLPVIATPRAQQSVVEWLQQVQRQNLALR 4414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 416 AHSAYPglavLRDLSRHRGtqvlapvvftsaLGLGELFSSDVTGQFGTPGWIISQG-PQVLLDAQVTEFDGGVL------ 488
Cdd:PRK12316 4415 EHEHTP----LYEIQRWAG------------QGGEALFDSLLVFENYPVSEALQQGaPGGLRFGEVTNHEQTNYpltlav 4478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 489 -------VNWDVREGVFPAGVIDAMFAHHIDELLRLASADEAWEAPGPPALPEAQRAVREAANGRTAE-PSGEALHDGFF 560
Cdd:PRK12316 4479 glgetlsLQFSYDRGHFDAATIERLARHLTNLLEAMAEDPQRRLGELQLLEKAEQQRIVALWNRTDAGyPATRCVHQLVA 4558
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 561 RQAEQRPDAPAVFASSGDLSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIGVDQPRD 640
Cdd:PRK12316 4559 ERARMTPDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRE 4638
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 641 RAERILESGGVSLAVVCGGQRLSMPVPEVVLADIL------GGAPASTeiTSARVDPAALAYVLFTSGSTGEPKGVEVTH 714
Cdd:PRK12316 4639 RLAYMMEDSGAALLLTQSHLLQRLPIPDGLASLALdrdedwEGFPAHD--PAVRLHPDNLAYVIYTSGSTGRPKGVAVSH 4716
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 715 DAAMNTVEFIGRHFDIGPADRCLALSTLEGDISVMDVFVTLRTGGSIVVVDEvQRRDPDAWARLIDAHQVTVLHFMPGWL 794
Cdd:PRK12316 4717 GSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVIRDD-SLWDPERLYAEIHEHRVTVLVFPPVYL 4795
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 795 EMLVE--VGRGRLSSVRVVPTGGDWVRPEVVRRLRVEAPGVRFAGLGGATETPVHNSIFEVTEPIPDDWTALPFGVPLPN 872
Cdd:PRK12316 4796 QQLAEhaERDGEPPSLRVYCFGGEAVAQASYDLAWRALKPVYLFNGYGPTETTVTVLLWKARDGDACGAAYMPIGTPLGN 4875
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 873 NACRVVDDTGADCPDWVPGEYWVSGRGIARGYRGRPDLTAERFV-----EHDGRIwYRTGDLVRYWPDGTLEFVGRADHR 947
Cdd:PRK12316 4876 RSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFVpdpfgAPGGRL-YRTGDLARYRADGVIDYLGRVDHQ 4954
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 948 VKISGYRVELGEVETALRRVPGVRTAVaaLIAVSGESDV-LAAQVCADDASVTAEGIRQA---------LADLVPAHMIP 1017
Cdd:PRK12316 4955 VKIRGFRIELGEIEARLREHPAVREAV--VIAQEGAVGKqLVGYVVPQDPALADADEAQAelrdelkaaLRERLPEYMVP 5032
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 1018 RHITVVERIGFTDAGKLDRRAVARELESAVSQSqrpgHRAPSTPLQSALATIVGDLLGRQNIGIDDDFFALGGDSVLATQ 1097
Cdd:PRK12316 5033 AHLVFLARMPLTPNGKLDRKALPQPDASLLQQA----YVAPRSELEQQVAAIWAEVLQLERVGLDDNFFELGGHSLLAIQ 5108
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|...
gi 497641516 1098 AVARIRAWLDApDIMVADIFANRTVSALAAVLG-AGERDPGRLDQVAELYLEV 1149
Cdd:PRK12316 5109 VTSRIQLELGL-ELPLRELFQTPTLAAFVELAAaAGSGDDEKFDDLEELLSEL 5160
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
16-1132 |
3.77e-110 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 381.61 E-value: 3.77e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 16 AELLGVDADAVQpgSNLIGQGLDSIRIMTLAGRWRRQ-GIAVDFATLAETPTVEAWAELVNAGKPSadrpaepadAPADA 94
Cdd:PRK12316 2526 QAVLKVEQVGLD--DHFFELGGHSLLATQVVSRVRQDlGLEVPLRILFERPTLAAFAASLESGQTS---------RAPVL 2594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 95 GRSGEDEPFSLAPMQHAMWVGRQENQqlGGVAGHLYVEFD-GGGIDPERLRAAATALARRHPMLRVRFLPDGTQRIAPAD 173
Cdd:PRK12316 2595 QKVTRVQPLPLSHAQQRQWFLWQLEP--ESAAYHLPSALHlRGVLDQAALEQAFDALVLRHETLRTRFVEVGEQTRQVIL 2672
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 174 EFGPfpvhVEDLRERSTGEADRRLAAIRAAKSHQQLD---GAVFELAVTLLPAERSRLHVDLDMQAADAMSYRTLMADLA 250
Cdd:PRK12316 2673 PNMS----LRIVLEDCAGVADAAIRQRVAEEIQRPFDlarGPLLRVRLLALDGQEHVLVITQHHIVSDGWSMQVMVDELV 2748
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 251 ALYLGRD------LPELGYTYRQYrhAIEAEDARPQPARDADRAWWARRLPELPDPPALPTTGGRAENQS---TRRWHWL 321
Cdd:PRK12316 2749 QAYAGARrgeqptLPPLPLQYADY--AAWQRAWMDSGEGARQLDYWRERLGGEQPVLELPLDRPRPALQShrgARLDVAL 2826
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 322 DPHTRDALFARAQARGFTPAMALAAGFANTLARWSTTSRFLLNVPLFGRQalHPDVDSLVGDFTSSLLLDVDLTRANTAA 401
Cdd:PRK12316 2827 DVALSRELLALARREGVTLFMLLLASFQVLLHRYSGQSDIRVGVPIANRN--RAETERLIGFFVNTQVLRAQVDAQLAFR 2904
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 402 ARAQVVQDAMRTAAAHSAYPGLAVLRDLSRHRGTQVLAPVVFTSALGLGELFSSDVTGQFGTPGWIISQGPQVLLDAQVT 481
Cdd:PRK12316 2905 DLLGQVKEQALGAQAHQDLPFEQLVEALQPERSLSHSPLFQVMYNHQSGERAAAQLPGLHIESFAWDGAATQFDLALDTW 2984
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 482 EFDGGVLVNWDVREGVFPAGVIDAMFAHHIDELLRLASADEAWEAPGPPALPEAQRAVREAANGRTAE-PSGEALHDGFF 560
Cdd:PRK12316 2985 ESAEGLGASLTYATDLFDARTVERLARHWQNLLRGMVENPQRSVDELAMLDAEERGQLLEAWNATAAEyPLERGVHRLFE 3064
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 561 RQAEQRPDAPAVFASSGDLSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIGVDQPRD 640
Cdd:PRK12316 3065 EQVERTPDAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEE 3144
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 641 RAERILESGGVSLAVVCGGQRLSMPVPEVVLADILGGAPASTEITSARVDPAALAYVLFTSGSTGEPKGVEVTHDAAMNT 720
Cdd:PRK12316 3145 RLAYMLEDSGAQLLLSQSHLRLPLAQGVQVLDLDRGDENYAEANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNH 3224
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 721 VEFIGRHFDIGPADRCLALSTLEGDISVMDVFVTLRTGGSIVVVDEVQRRDPDAWARLIDAHQVTVLHFMPGWLEM-LVE 799
Cdd:PRK12316 3225 LCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDPALLVELINSEGVDVLHAYPSMLQAfLEE 3304
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 800 VGRGRLSSVRVVPTGGDWVRPEVVRRLRVEAPgvrFAGLGGATETPVHNSIFEVTEPIPDdwtALPFGVPLPNNACRVVD 879
Cdd:PRK12316 3305 EDAHRCTSLKRIVCGGEALPADLQQQVFAGLP---LYNLYGPTEATITVTHWQCVEEGKD---AVPIGRPIANRACYILD 3378
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 880 DTGADCPDWVPGEYWVSGRGIARGYRGRPDLTAERFVEH---DGRIWYRTGDLVRYWPDGTLEFVGRADHRVKISGYRVE 956
Cdd:PRK12316 3379 GSLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDpfvPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIE 3458
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 957 LGEVETALRRVPGVRTAVaaLIAVSGESDVlAAQVCADDASVTAEGIRQALADLVPAHMIPRHITVVERIGFTDAGKLDR 1036
Cdd:PRK12316 3459 LGEIEARLLEHPWVREAV--VLAVDGRQLV-AYVVPEDEAGDLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDR 3535
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 1037 RAVAReleSAVSQSQRpGHRAPSTPLQSALATIVGDLLGRQNIGIDDDFFALGGDSVLATQAVARIRAwlDAPDIMVADI 1116
Cdd:PRK12316 3536 KALPR---PDAALLQQ-DYVAPVNELERRLAAIWADVLKLEQVGLTDNFFELGGDSIISLQVVSRARQ--AGIRFTPKDL 3609
|
1130
....*....|....*.
gi 497641516 1117 FANRTVSALAAVLGAG 1132
Cdd:PRK12316 3610 FQHQTIQGLARVARVG 3625
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
154-1133 |
7.90e-110 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 380.46 E-value: 7.90e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 154 HPMLRVRFLPDGTQRIAPADEFGPFPVHVEDLRERSTGEadrRLAAIRAAKSHQQL------DGAVFELAVTLLPAERSR 227
Cdd:PRK12316 100 HETLRTVFPRGADDSLAQVPLDRPLEVEFEDCSGLPEAE---QEARLRDEAQRESLqpfdlcEGPLLRVRLLRLGEEEHV 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 228 LHVDLDMQAADAMSYRTLMADLAALYLGR------DLPELGYTYRQY----RHAIEA-EDARpqpardaDRAWWARRLPE 296
Cdd:PRK12316 177 LLLTLHHIVSDGWSMNVLIEEFSRFYSAYatgaepGLPALPIQYADYalwqRSWLEAgEQER-------QLEYWRAQLGE 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 297 LPDPPALPTTGGRAENQSTR--RWHW-LDPHTRDALFARAQARGFTPAMALAAGFANTLARWSTTSRFLLNVPLFGRQal 373
Cdd:PRK12316 250 EHPVLELPTDHPRPAVPSYRgsRYEFsIDPALAEALRGTARRQGLTLFMLLLGAFNVLLHRYSGQTDIRVGVPIANRN-- 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 374 HPDVDSLVGDFTSSLLLDVDLTRANTAAARAQVVQDAMRTAAAHSAYP------GLAVLRDLSRHRGTQVL---APVVF- 443
Cdd:PRK12316 328 RAEVEGLIGFFVNTQVLRSVFDGRTRVATLLAGVKDTVLGAQAHQDLPferlveALKVERSLSHSPLFQVMynhQPLVAd 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 444 ------TSALGLGELFSSDVTGQFGtpgwiisqgpqvlLDAQVTEFDGGVLVNWDVREGVFPAGVIDAMfAHHIDELLRL 517
Cdd:PRK12316 408 iealdtVAGLEFGQLEWKSRTTQFD-------------LTLDTYEKGGRLHAALTYATDLFEARTVERM-ARHWQNLLRG 473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 518 ASADEAWEAPGPPALPEA--QRAVREAANGRTAEPSGEALHDGFFRQAEQRPDAPAVFASSGDLSYAQLRDQALAVAAAL 595
Cdd:PRK12316 474 MVENPQARVDELPMLDAEerGQLVEGWNATAAEYPLQRGVHRLFEEQVERTPEAPALAFGEETLDYAELNRRANRLAHAL 553
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 596 RAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIGVDQPRDRAERILESGGVSL-----------AVVCGGQRLSM 664
Cdd:PRK12316 554 IERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLllsqshlgrklPLAAGVQVLDL 633
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 665 PVPEVVLADILGGAPasteitSARVDPAALAYVLFTSGSTGEPKGVEVTHDAAMNTVEFIGRHFDIGPADRCLALSTLEG 744
Cdd:PRK12316 634 DRPAAWLEGYSEENP------GTELNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSF 707
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 745 DISVMDVFVTLRTGGSIVVVDEVQRRDPDAWARLIDAHQVTVLHFMPGWLEMLVEVGR-GRLSSVRVVPTGGDWVRPEVV 823
Cdd:PRK12316 708 DVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDvASCTSLRRIVCSGEALPADAQ 787
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 824 RRLRVEAPGVRFAGLGGATETPVHNSIFEVTEPIPDdwtALPFGVPLPNNACRVVDDTGADCPDWVPGEYWVSGRGIARG 903
Cdd:PRK12316 788 EQVFAKLPQAGLYNLYGPTEAAIDVTHWTCVEEGGD---SVPIGRPIANLACYILDANLEPVPVGVLGELYLAGRGLARG 864
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 904 YRGRPDLTAERFVEH---DGRIWYRTGDLVRYWPDGTLEFVGRADHRVKISGYRVELGEVETALRRVPGVRTAVaaLIAV 980
Cdd:PRK12316 865 YHGRPGLTAERFVPSpfvAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAA--VLAV 942
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 981 SGESdVLAAQVCADDASVTAEGIRQALADLVPAHMIPRHITVVERIGFTDAGKLDRRAVAReleSAVSQSQRpGHRAPST 1060
Cdd:PRK12316 943 DGKQ-LVGYVVLESEGGDWREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKALPA---PEASVAQQ-GYVAPRN 1017
|
970 980 990 1000 1010 1020 1030
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497641516 1061 PLQSALATIVGDLLGRQNIGIDDDFFALGGDSVLATQAVARIR--AWLDAPdimvADIFANRTVSALAAVLGAGE 1133
Cdd:PRK12316 1018 ALERTLAAIWQDVLGVERVGLDDNFFELGGDSIVSIQVVSRARqaGIQLSP----RDLFQHQTIRSLALVAKAGQ 1088
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
236-1139 |
3.04e-108 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 369.37 E-value: 3.04e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 236 AADAMSYRTLMADLAALY----LGRDLPELGYTYRQyrhAIEAEDARPQ--PARDADRAWWARRLPELPDPPALPTTGGR 309
Cdd:PRK10252 143 LVDGFSFPAITRRIAAIYcawlRGEPTPASPFTPFA---DVVEEYQRYRasEAWQRDAAFWAEQRRQLPPPASLSPAPLP 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 310 AENQSTRRWHWLDPHTRDAlFAR--AQARGFTPAMALAAGFANTLARWSTTSRFLLNVPLFGR------QALHPDVDSLV 381
Cdd:PRK10252 220 GRSASADILRLKLEFTDGA-FRQlaAQASGVQRPDLALALVALWLGRLCGRMDYAAGFIFMRRlgsaalTATGPVLNVLP 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 382 gdftssllLDVDLTRANTAAARAQVVQDAMRTAAAHSAYPGLAVLRDLSRHRGTQVL-APVV----FTSALGLGELFSsd 456
Cdd:PRK10252 299 --------LRVHIAAQETLPELATRLAAQLKKMRRHQRYDAEQIVRDSGRAAGDEPLfGPVLnikvFDYQLDFPGVQA-- 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 457 VTGQFGTpgwiisqGPqvLLDAQVTEF---DGGVLVNWDVREGVFPAGVIDAmfahHIDELLRL---ASADEAWEAPGPP 530
Cdd:PRK10252 369 QTHTLAT-------GP--VNDLELALFpdeHGGLSIEILANPQRYDEATLIA----HAERLKALiaqFAADPALLCGDVD 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 531 ALPEAQRAVREAANGRTAEPSGEALHDGFFRQAEQRPDAPAVFASSGDLSYAQLRDQALAVAAALRAAGVTAGDTIAVMG 610
Cdd:PRK10252 436 ILLPGEYAQLAQVNATAVEIPETTLSALVAQQAAKTPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVAL 515
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 611 PKTAEQIPALLGILSVGAVYLPIGVDQPRDRAERILESGGVSLAVVCGGQRLSMP-VPEVVLADILGGAPASTEITSARV 689
Cdd:PRK10252 516 PRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTADQLPRFAdVPDLTSLCYNAPLAPQGAAPLQLS 595
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 690 DPAALAYVLFTSGSTGEPKGVEVTHDAAMNTVEFIGRHFDIGPADRCLALSTLEGDISVMDVFVTLRTGGSIVVVDEVQR 769
Cdd:PRK10252 596 QPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAH 675
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 770 RDPDAWARLIDAHQVTVLHFMPGWLEMLV-----EVGRGRLSSVRVVPTGGDWVRPEVVRRLRvEAPGVRFAGLGGATET 844
Cdd:PRK10252 676 RDPLAMQQFFAEYGVTTTHFVPSMLAAFVasltpEGARQSCASLRQVFCSGEALPADLCREWQ-QLTGAPLHNLYGPTEA 754
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 845 PVHNSIFevtePIPDDWTA------LPFGVPLPNNACRVVDDTGADCPDWVPGEYWVSGRGIARGYRGRPDLTAERFVEH 918
Cdd:PRK10252 755 AVDVSWY----PAFGEELAavrgssVPIGYPVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIAD 830
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 919 ---DGRIWYRTGDLVRYWPDGTLEFVGRADHRVKISGYRVELGEVETALRRVPGVRTAVA------ALIAVSGESDVLAA 989
Cdd:PRK10252 831 pfaPGERMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVThacvinQAAATGGDARQLVG 910
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 990 QVCA-DDASVTAEGIRQALADLVPAHMIPRHITVVERIGFTDAGKLDRRAvareLESAVSQSQRPGhRAPSTPLQSALAT 1068
Cdd:PRK10252 911 YLVSqSGLPLDTSALQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKA----LPLPELKAQVPG-RAPKTGTETIIAA 985
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497641516 1069 IVGDLLGRQNIGIDDDFFALGGDSVLATQAVARIRAWLdAPDIMVADIFANRTVSALAAVLGAGERDPGRL 1139
Cdd:PRK10252 986 AFSSLLGCDVVDADADFFALGGHSLLAMKLAAQLSRQF-ARQVTPGQVMVASTVAKLATLLDAEEDESRRL 1055
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
559-1039 |
1.23e-107 |
|
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: 346.64 E-value: 1.23e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 559 FFRQAEQRPDAPAVFASSGDLSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIGVDQP 638
Cdd:cd17651 1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 639 RDRAERILESGGVSLAVVCGGQRLSMPVPE--VVLADILGGAPASTEITSARVDPAALAYVLFTSGSTGEPKGVEVTHDA 716
Cdd:cd17651 81 AERLAFMLADAGPVLVLTHPALAGELAVELvaVTLLDQPGAAAGADAEPDPALDADDLAYVIYTSGSTGRPKGVVMPHRS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 717 AMNTVEFIGRHFDIGPADRCLALSTLEGDISVMDVFVTLRTGGSIVVVDEVQRRDPDAWARLIDAHQVTVLHFMPGWLEM 796
Cdd:cd17651 161 LANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPPALAAWLDEQRISRVFLPTVALRA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 797 LVEVGR---GRLSSVRVVPTGGD-WVRPEVVRRLRVEAPGVRFAGLGGATETPVHNSifEVTEPIPDDWTA-LPFGVPLP 871
Cdd:cd17651 241 LAEHGRplgVRLAALRYLLTGGEqLVLTEDLREFCAGLPGLRLHNHYGPTETHVVTA--LSLPGDPAAWPApPPIGRPID 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 872 NNACRVVDDTGADCPDWVPGEYWVSGRGIARGYRGRPDLTAERFVEHD---GRIWYRTGDLVRYWPDGTLEFVGRADHRV 948
Cdd:cd17651 319 NTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPfvpGARMYRTGDLARWLPDGELEFLGRADDQV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 949 KISGYRVELGEVETALRRVPGVR-TAVAALIAVSGESDVLAAQVCADDASVTAEGIRQALADLVPAHMIPRHITVVERIG 1027
Cdd:cd17651 399 KIRGFRIELGEIEAALARHPGVReAVVLAREDRPGEKRLVAYVVGDPEAPVDAAELRAALATHLPEYMVPSAFVLLDALP 478
|
490
....*....|..
gi 497641516 1028 FTDAGKLDRRAV 1039
Cdd:cd17651 479 LTPNGKLDRRAL 490
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
567-1038 |
4.67e-107 |
|
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: 344.27 E-value: 4.67e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 567 PDAPAVFASSGDLSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIGVDQPRDRAERIL 646
Cdd:cd12116 1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 647 ESGGVSLAVVCGGQRLSMPVPEVVLADILGGAPASTEITSARVDPAALAYVLFTSGSTGEPKGVEVTHDAAMNTVEFIGR 726
Cdd:cd12116 81 EDAEPALVLTDDALPDRLPAGLPVLLLALAAAAAAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSMRE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 727 HFDIGPADRCLALSTLEGDISVMDVFVTLRTGGSIVVVDEVQRRDPDAWARLIDAHQVTVLHFMPGWLEMLVEVGRGRLS 806
Cdd:cd12116 161 RLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHSITVMQATPATWRMLLDAGWQGRA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 807 SVRVVpTGGDWVRPEVVRRLrvEAPGVRFAGLGGATETPVHNSIFEVTEPIPddwtALPFGVPLPNNACRVVDDTGADCP 886
Cdd:cd12116 241 GLTAL-CGGEALPPDLAARL--LSRVGSLWNLYGPTETTIWSTAARVTAAAG----PIPIGRPLANTQVYVLDAALRPVP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 887 DWVPGEYWVSGRGIARGYRGRPDLTAERFVEH----DGRIWYRTGDLVRYWPDGTLEFVGRADHRVKISGYRVELGEVET 962
Cdd:cd12116 314 PGVPGELYIGGDGVAQGYLGRPALTAERFVPDpfagPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEA 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497641516 963 ALRRVPGVRTAVAALIAVSGESDVLAAQVCADDASVTAEGIRQALADLVPAHMIPRHITVVERIGFTDAGKLDRRA 1038
Cdd:cd12116 394 ALAAHPGVAQAAVVVREDGGDRRLVAYVVLKAGAAPDAAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKA 469
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
103-1163 |
1.70e-104 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 364.66 E-value: 1.70e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 103 FSLAPMQHAMWVGRQENQQLGGVAGHLYVefDGGGIDPERLRAAATALARRHPMLRVRFLPDGTQRIAPADEFGPFPVHV 182
Cdd:PRK12316 1557 YPLSPMQQGMLFHSLYEQEAGDYINQLRV--DVQGLDPDRFRAAWQATVDRHEILRSGFLWQDGLEQPLQVIHKQVELPF 1634
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 183 EDLRERSTGEADRRLAAIRAAKSHQQLD---GAVFELAVTLLPAERSRLHVDLDMQAADAMSYRTLMADLAALYLGRDLP 259
Cdd:PRK12316 1635 AELDWRGREDLGQALDALAQAERQKGFDltrAPLLRLVLVRTGEGRHHLIYTNHHILMDGWSNAQLLGEVLQRYAGQPVA 1714
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 260 ELGYTYRQYRHAIEAEDarpqpaRDADRAWWARRLPELPDPPALPTTGGRAENQSTRRWHW--LDPHTRDALFARAQARG 337
Cdd:PRK12316 1715 APGGRYRDYIAWLQRQD------AAASEAFWKEQLAALEEPTRLAQAARTEDGQVGYGDHQqlLDPAQTRALAEFARAQK 1788
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 338 FTPAMALAAGFANTLARWSTTSRFLLNVPLFGRQALHPDVDSLVGDFTSSLLLDVDLTRANTAAARAQVVQDAMRTAAAH 417
Cdd:PRK12316 1789 VTLNTLVQAAWLLLLQRYTGQETVAFGATVAGRPAELPGIEQQIGLFINTLPVIAAPRPDQSVADWLQEVQALNLALREH 1868
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 418 SAYPglavLRDLSRHRGTQVLApvVFTSALgLGELFSSDVTGQFGTPGWI----ISQGPQVLLDAQVTEFDGGVL-VNWD 492
Cdd:PRK12316 1869 EHTP----LYDIQRWAGQGGEA--LFDSLL-VFENYPVAEALKQGAPAGLvfgrVSNHEQTNYPLTLAVTLGETLsLQYS 1941
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 493 VREGVFPAGVIDAMFAHHIDELLRLASADEAweAPGPPALPEA---QRAVREAANGRTAEPSGEALHDGFFRQAEQRPDA 569
Cdd:PRK12316 1942 YDRGHFDAAAIERLDRHLLHLLEQMAEDAQA--ALGELALLDAgerQRILADWDRTPEAYPRGPGVHQRIAEQAARAPEA 2019
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 570 PAVFASSGDLSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIGVDQPRDRAERILESG 649
Cdd:PRK12316 2020 IAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDS 2099
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 650 GVSLAVVCGGQRLSMPVPEVV----------LADILGGAPASteitsaRVDPAALAYVLFTSGSTGEPKGVEVTHDAAMN 719
Cdd:PRK12316 2100 GAALLLTQRHLLERLPLPAGVarlpldrdaeWADYPDTAPAV------QLAGENLAYVIYTSGSTGLPKGVAVSHGALVA 2173
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 720 TVEFIGRHFDIGPADRCLALSTLEGDISVMDVFVTLRTGGSIVVVDEVQRrDPDAWARLIDAHQVTVLHFMPGWLEMLVE 799
Cdd:PRK12316 2174 HCQAAGERYELSPADCELQFMSFSFDGAHEQWFHPLLNGARVLIRDDELW-DPEQLYDEMERHGVTILDFPPVYLQQLAE 2252
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 800 VGR--GRLSSVRVVPTGGDWVRPEVVRRLRVEAPGVRFAGLGGATETPVHNSIFEVTEPIPDDWTALPFGVPLPNNACRV 877
Cdd:PRK12316 2253 HAErdGRPPAVRVYCFGGEAVPAASLRLAWEALRPVYLFNGYGPTEAVVTPLLWKCRPQDPCGAAYVPIGRALGNRRAYI 2332
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 878 VDDTGADCPDWVPGEYWVSGRGIARGYRGRPDLTAERFV----EHDGRIWYRTGDLVRYWPDGTLEFVGRADHRVKISGY 953
Cdd:PRK12316 2333 LDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVpdpfSASGERLYRTGDLARYRADGVVEYLGRIDHQVKIRGF 2412
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 954 RVELGEVETALRRVPGVRTAVaaLIAVSGES-DVLAAQVCADD-ASVTAEGIRQALADLVPAHMIPRHITVVERIGFTDA 1031
Cdd:PRK12316 2413 RIELGEIEARLQAHPAVREAV--VVAQDGASgKQLVAYVVPDDaAEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPN 2490
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 1032 GKLDRRAVARELESAVSQSqrpgHRAPSTPLQSALATIVGDLLGRQNIGIDDDFFALGGDSVLATQAVARIRAWLDApDI 1111
Cdd:PRK12316 2491 GKLDRKALPKPDVSQLRQA----YVAPQEGLEQRLAAIWQAVLKVEQVGLDDHFFELGGHSLLATQVVSRVRQDLGL-EV 2565
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|..
gi 497641516 1112 MVADIFANRTVSALAAVLGAGErdpgrldQVAELYLEVIGMDAESVLAASQQ 1163
Cdd:PRK12316 2566 PLRILFERPTLAAFAASLESGQ-------TSRAPVLQKVTRVQPLPLSHAQQ 2610
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
567-1038 |
5.48e-100 |
|
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: 324.71 E-value: 5.48e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 567 PDAPAVFASSGDLSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIGVDQPRDRAERIL 646
Cdd:cd17649 1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 647 ESGGVSLavvcggqrlsmpvpevVLADilggapasteitsarvDPAALAYVLFTSGSTGEPKGVEVTHDAAMNTVEFIGR 726
Cdd:cd17649 81 EDSGAGL----------------LLTH----------------HPRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAE 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 727 HFDIGPADRCLALSTLEGDISVMDVFVTLRTGGSIVVVDEVQRRDPDAWARLIDAHQVTVLHFMPG----WLEMLVEVGR 802
Cdd:cd17649 129 RYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGVTVLDLPPAylqqLAEEADRTGD 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 803 GRLSSVRVVPTGGDWVRPEVVRRLRVEApgVRFAGLGGATETPVHNSIFEVTEPIPDDWTALPFGVPLPNNACRVVDDTG 882
Cdd:cd17649 209 GRPPSLRLYIFGGEALSPELLRRWLKAP--VRLFNAYGPTEATVTPLVWKCEAGAARAGASMPIGRPLGGRSAYILDADL 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 883 ADCPDWVPGEYWVSGRGIARGYRGRPDLTAERFVE----HDGRIWYRTGDLVRYWPDGTLEFVGRADHRVKISGYRVELG 958
Cdd:cd17649 287 NPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPdpfgAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELG 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 959 EVETALRRVPGVRTAVAALIAVSGESDVLAAQVCADDASVTA--EGIRQALADLVPAHMIPRHITVVERIGFTDAGKLDR 1036
Cdd:cd17649 367 EIEAALLEHPGVREAAVVALDGAGGKQLVAYVVLRAAAAQPElrAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDR 446
|
..
gi 497641516 1037 RA 1038
Cdd:cd17649 447 KA 448
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
563-1039 |
1.98e-99 |
|
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: 323.04 E-value: 1.98e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 563 AEQRPDAPAVFASSGDLSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIGVDQPRDRA 642
Cdd:cd05945 1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 643 ERILESGGvslavvcggqrlsmpvPEVVLAdilggapasteitsarvDPAALAYVLFTSGSTGEPKGVEVTHDAAMNTVE 722
Cdd:cd05945 81 REILDAAK----------------PALLIA-----------------DGDDNAYIIFTSGSTGRPKGVQISHDNLVSFTN 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 723 FIGRHFDIGPADRCLALSTLEGDISVMDVFVTLRTGGSIVVVDEVQRRDPDAWARLIDAHQVTVLHFMPGWLEMLV---E 799
Cdd:cd05945 128 WMLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADPKQLFRFLAEHGITVWVSTPSFAAMCLlspT 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 800 VGRGRLSSVRVVPTGGDWVRPEVVRRLRVEAPGVRFAGLGGATETPVHNSIFEVTEPIPDDWTALPFGVPLPNNACRVVD 879
Cdd:cd05945 208 FTPESLPSLRHFLFCGEVLPHKTARALQQRFPDARIYNTYGPTEATVAVTYIEVTPEVLDGYDRLPIGYAKPGAKLVILD 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 880 DTGADCPDWVPGEYWVSGRGIARGYRGRPDLTAERFVEHDGRIWYRTGDLVRYWPDGTLEFVGRADHRVKISGYRVELGE 959
Cdd:cd05945 288 EDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDEGQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEE 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 960 VETALRRVPGVRTAVAALIAVSGESDVLAAQV--CADDASVTAEGIRQALADLVPAHMIPRHITVVERIGFTDAGKLDRR 1037
Cdd:cd05945 368 IEAALRQVPGVKEAVVVPKYKGEKVTELIAFVvpKPGAEAGLTKAIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRK 447
|
..
gi 497641516 1038 AV 1039
Cdd:cd05945 448 AL 449
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
555-1038 |
8.21e-98 |
|
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: 318.49 E-value: 8.21e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 555 LHDGFFRQAEQRPDAPAVFASSGDLSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIG 634
Cdd:cd12115 1 LHDLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 635 VDQPRDRAERILESGGVSLAVVcggqrlsmpvpevvladilggapasteitsarvDPAALAYVLFTSGSTGEPKGVEVTH 714
Cdd:cd12115 81 PAYPPERLRFILEDAQARLVLT---------------------------------DPDDLAYVIYTSGSTGRPKGVAIEH 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 715 DAAMNTVEFIGRHFDIGPADRCLALSTLEGDISVMDVFVTLRTGGSIVVVDEVQRRdPDAWARLidahQVTVLHFMPGWL 794
Cdd:cd12115 128 RNAAAFLQWAAAAFSAEELAGVLASTSICFDLSVFELFGPLATGGKVVLADNVLAL-PDLPAAA----EVTLINTVPSAA 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 795 EMLVEVGrGRLSSVRVVPTGGDWVRPEVVRRLRVEAPGVRFAGLGGATETPVHNSIFEVTepiPDDWTALPFGVPLPNNA 874
Cdd:cd12115 203 AELLRHD-ALPASVRVVNLAGEPLPRDLVQRLYARLQVERVVNLYGPSEDTTYSTVAPVP---PGASGEVSIGRPLANTQ 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 875 CRVVDDTGADCPDWVPGEYWVSGRGIARGYRGRPDLTAERFV---EHDGRIWYRTGDLVRYWPDGTLEFVGRADHRVKIS 951
Cdd:cd12115 279 AYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLpdpFGPGARLYRTGDLVRWRPDGLLEFLGRADNQVKVR 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 952 GYRVELGEVETALRRVPGVRTAVAALIAVSGESDVLAAQVCADDAS-VTAEGIRQALADLVPAHMIPRHITVVERIGFTD 1030
Cdd:cd12115 359 GFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPGAaGLVEDLRRHLGTRLPAYMVPSRFVRLDALPLTP 438
|
....*...
gi 497641516 1031 AGKLDRRA 1038
Cdd:cd12115 439 NGKIDRSA 446
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
567-1039 |
2.14e-97 |
|
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: 317.71 E-value: 2.14e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 567 PDAPAVFASSGDLSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIGVDQPRDRAERIL 646
Cdd:cd17643 1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 647 ESGGVSLAVVcggqrlsmpvpevvladilggapasteitsarvDPAALAYVLFTSGSTGEPKGVEVTHDAAMNTVEFIGR 726
Cdd:cd17643 81 ADSGPSLLLT---------------------------------DPDDLAYVIYTSGSTGRPKGVVVSHANVLALFAATQR 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 727 HFDIGPADRCLALSTLEGDISVMDVFVTLRTGGSIVVVDEVQRRDPDAWARLIDAHQVTVLHFMPGWLEMLVEVGRG--- 803
Cdd:cd17643 128 WFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGVTVLNQTPSAFYQLVEAADRdgr 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 804 RLSSVRVVPTGGDWVRPEVVRRL--RVEAPGVRFAGLGGATETPVHNSIFEVTEPIPDDWTALPFGVPLPNNACRVVDDT 881
Cdd:cd17643 208 DPLALRYVIFGGEALEAAMLRPWagRFGLDRPQLVNMYGITETTVHVTFRPLDAADLPAAAASPIGRPLPGLRVYVLDAD 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 882 GADCPDWVPGEYWVSGRGIARGYRGRPDLTAERFVEH----DGRIWYRTGDLVRYWPDGTLEFVGRADHRVKISGYRVEL 957
Cdd:cd17643 288 GRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANpfggPGSRMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIEL 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 958 GEVETALRRVPGVRTAVAALIAVSGESDVLAAQVCADD-ASVTAEGIRQALADLVPAHMIPRHITVVERIGFTDAGKLDR 1036
Cdd:cd17643 368 GEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADDgAAADIAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDR 447
|
...
gi 497641516 1037 RAV 1039
Cdd:cd17643 448 AAL 450
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
559-1038 |
1.21e-95 |
|
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: 314.27 E-value: 1.21e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 559 FFRQAEQRPDAPAVFASSGDLSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIGVDQP 638
Cdd:cd17655 3 FEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 639 RDRAERILESGGVSLAVVCGGQRLSMPVPEVVLADILGGAPASTEITSARV-DPAALAYVLFTSGSTGEPKGVEVTHDAA 717
Cdd:cd17655 83 EERIQYILEDSGADILLTQSHLQPPIAFIGLIDLLDEDTIYHEESENLEPVsKSDDLAYVIYTSGSTGKPKGVMIEHRGV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 718 MNTVEFIGRHFDIGPADRCLALSTLEGDISVMDVFVTLRTGGSIVVVDEVQRRDPDAWARLIDAHQVTVLHFMPGWLEML 797
Cdd:cd17655 163 VNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQALTQYIRQNRITIIDLTPAHLKLL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 798 VEVGRGRLSSVRVVPTGGDWVRPEVVRRL-RVEAPGVRFAGLGGATETPVHNSIFEVtEPIPDDWTALPFGVPLPNNACR 876
Cdd:cd17655 243 DAADDSEGLSLKHLIVGGEALSTELAKKIiELFGTNPTITNAYGPTETTVDASIYQY-EPETDQQVSVPIGKPLGNTRIY 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 877 VVDDTGADCPDWVPGEYWVSGRGIARGYRGRPDLTAERFVEHD---GRIWYRTGDLVRYWPDGTLEFVGRADHRVKISGY 953
Cdd:cd17655 322 ILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPfvpGERMYRTGDLARWLPDGNIEFLGRIDHQVKIRGY 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 954 RVELGEVETALRRVPGVRTAVAalIAVSGE--SDVLAAQVCADDaSVTAEGIRQALADLVPAHMIPRHITVVERIGFTDA 1031
Cdd:cd17655 402 RIELGEIEARLLQHPDIKEAVV--IARKDEqgQNYLCAYIVSEK-ELPVAQLREFLARELPDYMIPSYFIKLDEIPLTPN 478
|
....*..
gi 497641516 1032 GKLDRRA 1038
Cdd:cd17655 479 GKVDRKA 485
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
555-1045 |
9.00e-94 |
|
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: 308.70 E-value: 9.00e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 555 LHDGFFRQAEQRPDAPAVFASSGDLSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIG 634
Cdd:cd05918 1 VHDLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 635 VDQPRDRAERILESGGVSLAVVCggqrlsmpvpevvladilggapasteitsarvDPAALAYVLFTSGSTGEPKGVEVTH 714
Cdd:cd05918 81 PSHPLQRLQEILQDTGAKVVLTS--------------------------------SPSDAAYVIFTSGSTGKPKGVVIEH 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 715 DAAMNTVEFIGRHFDIGPADRCLALSTLEGDISVMDVFVTLRTGGSIVVVDEVQRRdpDAWARLIDAHQVTVLHFMPGWL 794
Cdd:cd05918 129 RALSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLCIPSEEDRL--NDLAGFINRLRVTWAFLTPSVA 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 795 EMLvevGRGRLSSVRVVPTGGDWVRPEVVRRLrveAPGVRFAGLGGATETpvhnSIFEVTEPIPDDWTALPFGVPLPNNa 874
Cdd:cd05918 207 RLL---DPEDVPSLRTLVLGGEALTQSDVDTW---ADRVRLINAYGPAEC----TIAATVSPVVPSTDPRNIGRPLGAT- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 875 CRVVD--DTGADCPDWVPGEYWVSGRGIARGYRGRPDLTAERFVEH-----------DGRIwYRTGDLVRYWPDGTLEFV 941
Cdd:cd05918 276 CWVVDpdNHDRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDpawlkqegsgrGRRL-YRTGDLVRYNPDGSLEYV 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 942 GRADHRVKISGYRVELGEVETALRR-VPGVRTAVAALIAVSG--ESDVLAAQVCADDASVT------------------A 1000
Cdd:cd05918 355 GRKDTQVKIRGQRVELGEIEHHLRQsLPGAKEVVVEVVKPKDgsSSPQLVAFVVLDGSSSGsgdgdslflepsdefralV 434
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 497641516 1001 EGIRQALADLVPAHMIPRHITVVERIGFTDAGKLDRRAVARELES 1045
Cdd:cd05918 435 AELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRALRELAES 479
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
567-1038 |
6.01e-92 |
|
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: 302.25 E-value: 6.01e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 567 PDAPAVFASSGDLSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIGVDQPRDRAERIL 646
Cdd:cd17652 1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 647 ESGGvslavvcggqrlsmpvPEVVLADilggapasteitsarvdPAALAYVLFTSGSTGEPKGVEVTHDAAMNTVEFIGR 726
Cdd:cd17652 81 ADAR----------------PALLLTT-----------------PDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIA 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 727 HFDIGPADRCLALSTLEGDISVMDVFVTLRTGGSIVVVDEVQRRDPDAWARLIDAHQVTVLHFMPGWLEMLVEVGrgrLS 806
Cdd:cd17652 128 AFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLLREHRITHVTLPPAALAALPPDD---LP 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 807 SVRVVPTGGDWVRPEVVRRLrveAPGVRFAGLGGATETPVHNSIfevTEPIPDDwTALPFGVPLPNNACRVVDDTGADCP 886
Cdd:cd17652 205 DLRTLVVAGEACPAELVDRW---APGRRMINAYGPTETTVCATM---AGPLPGG-GVPPIGRPVPGTRVYVLDARLRPVP 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 887 DWVPGEYWVSGRGIARGYRGRPDLTAERFVEH----DGRIWYRTGDLVRYWPDGTLEFVGRADHRVKISGYRVELGEVET 962
Cdd:cd17652 278 PGVPGELYIAGAGLARGYLNRPGLTAERFVADpfgaPGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEA 357
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497641516 963 ALRRVPGVRTAVAALIAVSGESDVLAAQVC-ADDASVTAEGIRQALADLVPAHMIPRHITVVERIGFTDAGKLDRRA 1038
Cdd:cd17652 358 ALTEHPGVAEAVVVVRDDRPGDKRLVAYVVpAPGAAPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRA 434
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
555-1046 |
5.18e-91 |
|
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440087 [Multi-domain] Cd Length: 452 Bit Score: 300.19 E-value: 5.18e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 555 LHDGFFRQAEQRPDAPAVFASSGDLSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIG 634
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 635 VDQPRDRAERILESGGVSLAVVcggqrlsmpvpevvladilggapasteitsarvdpaalAYVLFTSGSTGEPKGVEVTH 714
Cdd:COG0318 81 PRLTAEELAYILEDSGARALVT--------------------------------------ALILYTSGTTGRPKGVMLTH 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 715 DAAMNTVEFIGRHFDIGPADRCLALSTLEGDIS-VMDVFVTLRTGGSIVVVDevqRRDPDAWARLIDAHQVTVLHFMPGW 793
Cdd:COG0318 123 RNLLANAAAIAAALGLTPGDVVLVALPLFHVFGlTVGLLAPLLAGATLVLLP---RFDPERVLELIERERVTVLFGVPTM 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 794 LEMLV---EVGRGRLSSVRVVPTGGDWVRPEVVRRLRvEAPGVRFAGLGGATETPVHnsifeVTEPIPDDWTALPF--GV 868
Cdd:COG0318 200 LARLLrhpEFARYDLSSLRLVVSGGAPLPPELLERFE-ERFGVRIVEGYGLTETSPV-----VTVNPEDPGERRPGsvGR 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 869 PLPNNACRVVDDTGADCPDWVPGEYWVSGRGIARGYRGRPDLTAERFveHDGriWYRTGDLVRYWPDGTLEFVGRADHRV 948
Cdd:COG0318 274 PLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAF--RDG--WLRTGDLGRLDEDGYLYIVGRKKDMI 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 949 KISGYRVELGEVETALRRVPGVRTAVAALI--AVSGESdVLAAQVCADDASVTAEGIRQALADLVPAHMIPRHITVVERI 1026
Cdd:COG0318 350 ISGGENVYPAEVEEVLAAHPGVAEAAVVGVpdEKWGER-VVAFVVLRPGAELDAEELRAFLRERLARYKVPRRVEFVDEL 428
|
490 500
....*....|....*....|
gi 497641516 1027 GFTDAGKLDRRAVARELESA 1046
Cdd:COG0318 429 PRTASGKIDRRALRERYAAG 448
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
559-951 |
1.13e-90 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 298.07 E-value: 1.13e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 559 FFRQAEQRPDAPAVFASSGD-LSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIGVDQ 637
Cdd:pfam00501 1 LERQAARTPDKTALEVGEGRrLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 638 PRDRAERILESGGVSLAVVCGGQRLSM--------------------PVPEVVLADILGGAPASTEITSARVDPAALAYV 697
Cdd:pfam00501 81 PAEELAYILEDSGAKVLITDDALKLEEllealgklevvklvlvldrdPVLKEEPLPEEAKPADVPPPPPPPPDPDDLAYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 698 LFTSGSTGEPKGVEVTHDAAMNTVEFIG----RHFDIGPADRCLALSTLEGDISV-MDVFVTLRTGGSIVVVDEVQRRDP 772
Cdd:pfam00501 161 IYTSGTTGKPKGVMLTHRNLVANVLSIKrvrpRGFGLGPDDRVLSTLPLFHDFGLsLGLLGPLLAGATVVLPPGFPALDP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 773 DAWARLIDAHQVTVLHFMPGWLEMLVEVG---RGRLSSVRVVPTGGDWVRPEVVRRLRvEAPGVRFAGLGGATETPVHNS 849
Cdd:pfam00501 241 AALLELIERYKVTVLYGVPTLLNMLLEAGapkRALLSSLRLVLSGGAPLPPELARRFR-ELFGGALVNGYGLTETTGVVT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 850 IFevtEPIPDDWTALPF-GVPLPNNACRVVDD-TGADCPDWVPGEYWVSGRGIARGYRGRPDLTAERFVEHDgriWYRTG 927
Cdd:pfam00501 320 TP---LPLDEDLRSLGSvGRPLPGTEVKIVDDeTGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDEDG---WYRTG 393
|
410 420
....*....|....*....|....
gi 497641516 928 DLVRYWPDGTLEFVGRADHRVKIS 951
Cdd:pfam00501 394 DLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
555-1038 |
4.38e-86 |
|
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: 287.41 E-value: 4.38e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 555 LHDGFFRQAEQRPDAPAVFASSGDLSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIG 634
Cdd:cd17644 2 IHQLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 635 VDQPRDRAERILESGGVSLAVVcggqrlsmpvpevvladilggapasteitsarvDPAALAYVLFTSGSTGEPKGVEVTH 714
Cdd:cd17644 82 PNYPQERLTYILEDAQISVLLT---------------------------------QPENLAYVIYTSGSTGKPKGVMIEH 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 715 DAAMNTVEFIGRHFDIGPADRCLALSTLEGDISVMDVFVTLRTGGSIVVVDEVQRRDPDAWARLIDAHQVTVLHFMPGWL 794
Cdd:cd17644 129 QSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLEDFVQYIQQWQLTVLSLPPAYW 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 795 EMLVEVGRGRL----SSVRVVPTGGDWVRPEVVRRLR-VEAPGVRFAGLGGATETPVHNSIFEVTEPIPDDWTALPFGVP 869
Cdd:cd17644 209 HLLVLELLLSTidlpSSLRLVIVGGEAVQPELVRQWQkNVGNFIQLINVYGPTEATIAATVCRLTQLTERNITSVPIGRP 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 870 LPNNACRVVDDTGADCPDWVPGEYWVSGRGIARGYRGRPDLTAERFVEH-----DGRIWYRTGDLVRYWPDGTLEFVGRA 944
Cdd:cd17644 289 IANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHpfnssESERLYKTGDLARYLPDGNIEYLGRI 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 945 DHRVKISGYRVELGEVETALRRVPGVRTAVaaLIA---VSGESDVLAAQVCADDASVTAEGIRQALADLVPAHMIPRHIT 1021
Cdd:cd17644 369 DNQVKIRGFRIELGEIEAVLSQHNDVKTAV--VIVredQPGNKRLVAYIVPHYEESPSTVELRQFLKAKLPDYMIPSAFV 446
|
490
....*....|....*..
gi 497641516 1022 VVERIGFTDAGKLDRRA 1038
Cdd:cd17644 447 VLEELPLTPNGKIDRRA 463
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
327-1134 |
6.82e-83 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 299.01 E-value: 6.82e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 327 DALFARAQA----RGFTPAMALAAGFANTLARWSTTSRFLLNVPLFGRqaLHPDVDSLVGDFTSSLLLDVDLTRANTAAA 402
Cdd:PRK05691 1958 PELAARVRAfnaqRGLTLFMTMTATLAALLYRYSGQRDLRIGAPVANR--IRPESEGLIGAFLNTQVLRCQLDGQMSVSE 2035
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 403 RAQVVQDAMRTAAAHSAYPGLAVLRDLSRHRGT------QVLAPVvftsalglgelfssdvtgqfgtPGWIISQGPQ--- 473
Cdd:PRK05691 2036 LLEQVRQTVIEGQSHQDLPFDHLVEALQPPRSAaynplfQVMCNV----------------------QRWEFQQSRQlag 2093
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 474 -----VLLDAQVTEFDGGVLV-NWDVREG--------VFPAGVIDAMfAHHIDELLRLASADEAWEAPGPPALPEAQRAV 539
Cdd:PRK05691 2094 mtveyLVNDARATKFDLNLEVtDLDGRLGccltysrdLFDEPRIARM-AEHWQNLLEALLGDPQQRLAELPLLAAAEQQQ 2172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 540 REAANGRTA--EPSGEALHDGFFRQAEQRPDAPAVFASSGDLSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQI 617
Cdd:PRK05691 2173 LLDSLAGEAgeARLDQTLHGLFAAQAARTPQAPALTFAGQTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMV 2252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 618 PALLGILSVGAVYLPIGVDQPRDRAERILESGGVSLAVvcgGQRlsmpvpevVLADILGGAPASTEITSARVDPAAL--- 694
Cdd:PRK05691 2253 VGLLAILKAGGAYVPLDPEYPLERLHYMIEDSGIGLLL---SDR--------ALFEALGELPAGVARWCLEDDAAALaay 2321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 695 --------------AYVLFTSGSTGEPKGVEVTH-DAAMNTVEFIGRhFDIGPADRCLALSTLEGDISVMDVFVTLRTGG 759
Cdd:PRK05691 2322 sdaplpflslpqhqAYLIYTSGSTGKPKGVVVSHgEIAMHCQAVIER-FGMRADDCELHFYSINFDAASERLLVPLLCGA 2400
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 760 SIVVVDEVQRrDPDAWARLIDAHQVTVLHFMPGWLEMLVE--VGRGRLSSVRVVPTGGDWVRPEVVRRLR-VEAPGVRFA 836
Cdd:PRK05691 2401 RVVLRAQGQW-GAEEICQLIREQQVSILGFTPSYGSQLAQwlAGQGEQLPVRMCITGGEALTGEHLQRIRqAFAPQLFFN 2479
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 837 GLGgATETPVHNSIFEVTEPIPDDWTALPFGVPLPNNACRVVDDTGADCPDWVPGEYWVSGRGIARGYRGRPDLTAERFV 916
Cdd:PRK05691 2480 AYG-PTETVVMPLACLAPEQLEEGAASVPIGRVVGARVAYILDADLALVPQGATGELYVGGAGLAQGYHDRPGLTAERFV 2558
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 917 ----EHDGRIWYRTGDLVRYWPDGTLEFVGRADHRVKISGYRVELGEVETALRRVPGVR-TAVAALIAVSGESDV--LAA 989
Cdd:PRK05691 2559 adpfAADGGRLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVReAVVLALDTPSGKQLAgyLVS 2638
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 990 QVCADDASVTA---EGIRQALADLVPAHMIPRHITVVERIGFTDAGKLDRRAV-ARELESAvsqsqRPGHRAPSTPLQSA 1065
Cdd:PRK05691 2639 AVAGQDDEAQAalrEALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRALpAPDPELN-----RQAYQAPRSELEQQ 2713
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497641516 1066 LATIVGDLLGRQNIGIDDDFFALGGDSVLATQAVARIRAWldAPDIMVADIFANRTVSALAAVLGAGER 1134
Cdd:PRK05691 2714 LAQIWREVLNVERVGLGDNFFELGGDSILSIQVVSRARQL--GIHFSPRDLFQHQTVQTLAAVATHSEA 2780
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
567-1039 |
1.29e-76 |
|
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: 260.48 E-value: 1.29e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 567 PDAPAVFASSGDLSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIGVDQPRDRAERIL 646
Cdd:cd17650 1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 647 ESGGVSLAVVcggqrlsmpvpevvladilggapasteitsarvDPAALAYVLFTSGSTGEPKGVEVTHDAAMNTVEFIGR 726
Cdd:cd17650 81 EDSGAKLLLT---------------------------------QPEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWRR 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 727 HFDIGPAD-RCLALSTLEGDISVMDVFVTLRTGGSIVVVDEVQRRDPDAWARLIDAHQVTVLHFMPGWLEMLVE-VGRG- 803
Cdd:cd17650 128 EYELDSFPvRLLQMASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSRITLMESTPALIRPVMAyVYRNg 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 804 -RLSSVRVVPTGGDWVRPE----VVRRLRveaPGVRFAGLGGATETPVHNSIFEVTEPIPDDWTALPFGVPLPNNACRVV 878
Cdd:cd17650 208 lDLSAMRLLIVGSDGCKAQdfktLAARFG---QGMRIINSYGVTEATIDSTYYEEGRDPLGDSANVPIGRPLPNTAMYVL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 879 DDTGADCPDWVPGEYWVSGRGIARGYRGRPDLTAERFVEH---DGRIWYRTGDLVRYWPDGTLEFVGRADHRVKISGYRV 955
Cdd:cd17650 285 DERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENpfaPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRI 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 956 ELGEVETALRRVPGVRTAVAALIAVSGESDVLAAQVCADDASVTAEgIRQALADLVPAHMIPRHITVVERIGFTDAGKLD 1035
Cdd:cd17650 365 ELGEIESQLARHPAIDEAVVAVREDKGGEARLCAYVVAAATLNTAE-LRAFLAKELPSYMIPSYYVQLDALPLTPNGKVD 443
|
....
gi 497641516 1036 RRAV 1039
Cdd:cd17650 444 RRAL 447
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
557-1041 |
7.31e-75 |
|
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: 254.93 E-value: 7.31e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 557 DGFFRQAEQRPDAPAVFASSGDLSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIGVD 636
Cdd:cd17653 1 DAFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 637 QPRDRAERILESGGVSLAvvcggqrlsmpvpevvladilggapasteITSARVDPaaLAYVLFTSGSTGEPKGVEVTHDA 716
Cdd:cd17653 81 LPSARIQAILRTSGATLL-----------------------------LTTDSPDD--LAYIIFTSGSTGIPKGVMVPHRG 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 717 AMNTVEFIGRHFDIGPADRCLALSTLEGDISVMDVFVTLRTGGSIVVVDevqrrDPDAWARLIDahQVTVLHFMPGWLEM 796
Cdd:cd17653 130 VLNYVSQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGTLVLAD-----PSDPFAHVAR--TVDALMSTPSILST 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 797 LvevGRGRLSSVRVVPTGGDWVRPEVVRRLrveAPGVRFAGLGGATETPVhNSIFEVTEPIpddwTALPFGVPLPNNACR 876
Cdd:cd17653 203 L---SPQDFPNLKTIFLGGEAVPPSLLDRW---SPGRRLYNAYGPTECTI-SSTMTELLPG----QPVTIGKPIPNSTCY 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 877 VVDDTGADCPDWVPGEYWVSGRGIARGYRGRPDLTAERFVE---HDGRIWYRTGDLVRYWPDGTLEFVGRADHRVKISGY 953
Cdd:cd17653 272 ILDADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPdpfWPGSRMYRTGDYGRWTEDGGLEFLGREDNQVKVRGF 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 954 RVELGEVE-TALRRVPGVRTAVAALIavsgeSDVLAAQVCADDASVtaEGIRQALADLVPAHMIPRHITVVERIGFTDAG 1032
Cdd:cd17653 352 RINLEEIEeVVLQSQPEVTQAAAIVV-----NGRLVAFVTPETVDV--DGLRSELAKHLPSYAVPDRIIALDSFPLTANG 424
|
....*....
gi 497641516 1033 KLDRRAVAR 1041
Cdd:cd17653 425 KVDRKALRE 433
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
556-1039 |
7.57e-75 |
|
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: 255.17 E-value: 7.57e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 556 HDGFFRQAEQRPDAPAVFASSGDLSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIGV 635
Cdd:cd17645 1 HQLFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 636 DQPRDRAERILESGGVSLAVVcggqrlsmpvpevvladilggapasteitsarvDPAALAYVLFTSGSTGEPKGVEVTHD 715
Cdd:cd17645 81 DYPGERIAYMLADSSAKILLT---------------------------------NPDDLAYVIYTSGSTGLPKGVMIEHH 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 716 AAMNTVEFIGRHFDIGPADRCLALSTLEGDISVMDVFVTLRTGGSIVVVDEVQRRDPDAWARLIDAHQVTVLHFMPGWLE 795
Cdd:cd17645 128 NLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDLDALNDYFNQEGITISFLPTGAAE 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 796 MLVEVGRgrlSSVRVVPTGGDWVRpevvrrlRVEAPGVRFAGLGGATETPVHNSIFEVTEPipddWTALPFGVPLPNNAC 875
Cdd:cd17645 208 QFMQLDN---QSLRVLLTGGDKLK-------KIERKGYKLVNNYGPTENTVVATSFEIDKP----YANIPIGKPIDNTRV 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 876 RVVDDTGADCPDWVPGEYWVSGRGIARGYRGRPDLTAERFVEH---DGRIWYRTGDLVRYWPDGTLEFVGRADHRVKISG 952
Cdd:cd17645 274 YILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHpfvPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRG 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 953 YRVELGEVETALRRVPGVRTAVAALIAVSGESDVLAAQVCADDaSVTAEGIRQALADLVPAHMIPRHITVVERIGFTDAG 1032
Cdd:cd17645 354 YRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTAPE-EIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANG 432
|
....*..
gi 497641516 1033 KLDRRAV 1039
Cdd:cd17645 433 KVDRKAL 439
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
567-1039 |
3.05e-71 |
|
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: 246.23 E-value: 3.05e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 567 PDAPAVFASSGDLSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIGVDQPRDRAERIL 646
Cdd:cd17656 2 PDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 647 ESGGVSLAVVCG--GQRLSMPVPEVVLADILGGAPASTEITSArVDPAALAYVLFTSGSTGEPKGVEVTHDAAMNTVEFI 724
Cdd:cd17656 82 LDSGVRVVLTQRhlKSKLSFNKSTILLEDPSISQEDTSNIDYI-NNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLLHFE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 725 GRHFDIGPADRCLALSTLEGDISVMDVFVTLRTGGSIVVVDEVQRRDPDAWARLIDAHQVTVLHFMPGWLEMLVEVgRGR 804
Cdd:cd17656 161 REKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNIEVVFLPVAFLKFIFSE-REF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 805 LSS----VRVVPTGGDW--VRPEVVRRLRVEapGVRFAGLGGATETPVHNS-IFEVTEPIPDdwtALPFGVPLPNNACRV 877
Cdd:cd17656 240 INRfptcVKHIITAGEQlvITNEFKEMLHEH--NVHLHNHYGPSETHVVTTyTINPEAEIPE---LPPIGKPISNTWIYI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 878 VDDTGADCPDWVPGEYWVSGRGIARGYRGRPDLTAERFVEHDGR---IWYRTGDLVRYWPDGTLEFVGRADHRVKISGYR 954
Cdd:cd17656 315 LDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFDpneRMYRTGDLARYLPDGNIEFLGRADHQVKIRGYR 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 955 VELGEVETALRRVPGVRTAVAALIAVS-GESDvLAAQVCADDAsVTAEGIRQALADLVPAHMIPRHITVVERIGFTDAGK 1033
Cdd:cd17656 395 IELGEIEAQLLNHPGVSEAVVLDKADDkGEKY-LCAYFVMEQE-LNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGK 472
|
....*.
gi 497641516 1034 LDRRAV 1039
Cdd:cd17656 473 VDRKAL 478
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
567-1038 |
2.82e-65 |
|
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: 228.44 E-value: 2.82e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 567 PDAPAVFASSGDLSYAQLRDQALAVAAALRAAG-VTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIGVDQPRDRAERI 645
Cdd:cd17648 1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAeIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 646 LESggvslavvcggqrlsmpvpevvladilggapasteiTSARV---DPAALAYVLFTSGSTGEPKGVEVTHDAAMNT-V 721
Cdd:cd17648 81 LED------------------------------------TGARVvitNSTDLAYAIYTSGTTGKPKGVLVEHGSVVNLrT 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 722 EFIGRHFDIGPAD-RCLALSTLEGDISVMDVFVTLRTGGSIVVVDEVQRRDPDAWARLIDAHQVTVLHFMPGWLEMlveV 800
Cdd:cd17648 125 SLSERYFGRDNGDeAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPDRFYAYINREKVTYLSGTPSVLQQ---Y 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 801 GRGRLSSVRVVPTGGDWVRPEVVRRLRVEAPGVRFAGLGgATETPVHNSifeVTEPIPDDWTALPFGVPLPNNACRVVDD 880
Cdd:cd17648 202 DLARLPHLKRVDAAGEEFTAPVFEKLRSRFAGLIINAYG-PTETTVTNH---KRFFPGDQRFDKSLGRPVRNTKCYVLND 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 881 TGADCPDWVPGEYWVSGRGIARGYRGRPDLTAERFVEH------------DGRIwYRTGDLVRYWPDGTLEFVGRADHRV 948
Cdd:cd17648 278 AMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFLPNpfqteqerargrNARL-YKTGDLVRWLPSGELEYLGRNDFQV 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 949 KISGYRVELGEVETALRRVPGVRTAVA-----ALIAVSGESDVLAAQVCADDASVTAEGIRQALADLVPAHMIPRHITVV 1023
Cdd:cd17648 357 KIRGQRIEPGEVEAALASYPGVRECAVvakedASQAQSRIQKYLVGYYLPEPGHVPESDLLSFLRAKLPRYMVPARLVRL 436
|
490
....*....|....*
gi 497641516 1024 ERIGFTDAGKLDRRA 1038
Cdd:cd17648 437 EGIPVTINGKLDVRA 451
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
559-1152 |
2.97e-63 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 237.37 E-value: 2.97e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 559 FFRQAEQRPDAPAVFASSGDLSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIGVDQP 638
Cdd:PRK05691 3726 FEAQVAAHPQRIAASCLDQQWSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGLP 3805
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 639 RDRAERILESGGVSLaVVCG------GQRLSMPVPEVVLADIL--------GGAPASTEITSArvdPAALAYVLFTSGST 704
Cdd:PRK05691 3806 AQRLQRIIELSRTPV-LVCSaacreqARALLDELGCANRPRLLvweevqagEVASHNPGIYSG---PDNLAYVIYTSGST 3881
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 705 GEPKGVEVTHDAAMNTVEFIGRHFDIGPADRCLALSTLEGDISVMDVFVTLRTGGSIVVVDEVQRRDPDAWARLIDAHQV 784
Cdd:PRK05691 3882 GLPKGVMVEQRGMLNNQLSKVPYLALSEADVIAQTASQSFDISVWQFLAAPLFGARVEIVPNAIAHDPQGLLAHVQAQGI 3961
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 785 TVLHFMPGWLEMLVEVGRGRLSSVR-VVPTGgDWVRPEVVRRLRVEAPGVRFAGLGGATETPVHNSIFEVTEPIPDDwTA 863
Cdd:PRK05691 3962 TVLESVPSLIQGMLAEDRQALDGLRwMLPTG-EAMPPELARQWLQRYPQIGLVNAYGPAECSDDVAFFRVDLASTRG-SY 4039
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 864 LPFGVPLPNNACRVVDDTGADCPDWVPGEYWVSGRGIARGYRGRPDLTAERFVEHD----GRIWYRTGDLVRYWPDGTLE 939
Cdd:PRK05691 4040 LPIGSPTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVPHPfgapGERLYRTGDLARRRSDGVLE 4119
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 940 FVGRADHRVKISGYRVELGEVETALRRVPGVR-TAVAALIAVSGESDV--LAAQVCADDASVTAEGIRQALADLVPAHMI 1016
Cdd:PRK05691 4120 YVGRIDHQVKIRGYRIELGEIEARLHEQAEVReAAVAVQEGVNGKHLVgyLVPHQTVLAQGALLERIKQRLRAELPDYMV 4199
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 1017 PRHITVVERIGFTDAGKLDRRAVArELEsaVSQSQRPGHRAPSTPLQSALATIVGDLLGRQNIGIDDDFFALGGDSVLAT 1096
Cdd:PRK05691 4200 PLHWLWLDRLPLNANGKLDRKALP-ALD--IGQLQSQAYLAPRNELEQTLATIWADVLKVERVGVHDNFFELGGHSLLAT 4276
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 497641516 1097 QAVARIRAWLDApDIMVADIFANRTVSALAAV---LGAGERDPGRLDQVAELYLEVIGM 1152
Cdd:PRK05691 4277 QIASRVQKALQR-NVPLRAMFECSTVEELAEYiegLAGSAIDEQKVDRLSDLMAELEGL 4334
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
694-1035 |
6.67e-62 |
|
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: 214.84 E-value: 6.67e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 694 LAYVLFTSGSTGEPKGVEVTHDAAMNTVEFIGRHFDIGPADRCLALSTLEGDISVMDVFVTLRTGGSIVVVDevqRRDPD 773
Cdd:cd04433 2 PALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLP---KFDPE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 774 AWARLIDAHQVTVLHFMPGWLEMLVEVGRGR---LSSVRVVPTGGDWVRPEVVRRLRvEAPGVRFAGLGGATETPVHNSI 850
Cdd:cd04433 79 AALELIEREKVTILLGVPTLLARLLKAPESAgydLSSLRALVSGGAPLPPELLERFE-EAPGIKLVNGYGLTETGGTVAT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 851 FEvtepiPDDWTALP--FGVPLPNNACRVVDDTGADCPDWVPGEYWVSGRGIARGYRGRPDLTAERFveHDGriWYRTGD 928
Cdd:cd04433 158 GP-----PDDDARKPgsVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVD--EDG--WYRTGD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 929 LVRYWPDGTLEFVGRADHRVKISGYRVELGEVETALRRVPGVrtAVAALIAVSGE---SDVLAAQVCADDASVTAEGIRQ 1005
Cdd:cd04433 229 LGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGV--AEAAVVGVPDPewgERVVAVVVLRPGADLDAEELRA 306
|
330 340 350
....*....|....*....|....*....|
gi 497641516 1006 ALADLVPAHMIPRHITVVERIGFTDAGKLD 1035
Cdd:cd04433 307 HVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
563-1042 |
4.89e-57 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 206.28 E-value: 4.89e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 563 AEQRPDAPAvFASSGD-LSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIGVDQPRDR 641
Cdd:PRK04813 12 AQTQPDFPA-YDYLGEkLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVDVSSPAER 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 642 AERILESGGVSLAVVCGGQRLSM-PVPEVVLADI--LGGAPASTEITSArVDPAALAYVLFTSGSTGEPKGVEVTHDaam 718
Cdd:PRK04813 91 IEMIIEVAKPSLIIATEELPLEIlGIPVITLDELkdIFATGNPYDFDHA-VKGDDNYYIIFTSGTTGKPKGVQISHD--- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 719 NTVEF---IGRHFDIGPADRCLALSTLEGDISVMDVFVTLRTGGSIVVVDEVQRRDPDAWARLIDAHQVTVLHFMPGWLE 795
Cdd:PRK04813 167 NLVSFtnwMLEDFALPEGPQFLNQAPYSFDLSVMDLYPTLASGGTLVALPKDMTANFKQLFETLPQLPINVWVSTPSFAD 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 796 M---LVEVGRGRLSSVRVVPTGGDWVRPEVVRRLRVEAPGVRFAGLGGATETPVHNSIFEVTEPIPDDWTALPFGVPLPN 872
Cdd:PRK04813 247 McllDPSFNEEHLPNLTHFLFCGEELPHKTAKKLLERFPSATIYNTYGPTEATVAVTSIEITDEMLDQYKRLPIGYAKPD 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 873 NACRVVDDTGADCPDWVPGEYWVSGRGIARGYRGRPDLTAERFVEHDGRIWYRTGDLVrYWPDGTLEFVGRADHRVKISG 952
Cdd:PRK04813 327 SPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFFTFDGQPAYHTGDAG-YLEDGLLFYQGRIDFQIKLNG 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 953 YRVELGEVETALRRVPGVRTAVAALIAVSGESDVLAAQVCADDASVTAEG-----IRQALADLVPAHMIPRHITVVERIG 1027
Cdd:PRK04813 406 YRIELEEIEQNLRQSSYVESAVVVPYNKDHKVQYLIAYVVPKEEDFEREFeltkaIKKELKERLMEYMIPRKFIYRDSLP 485
|
490
....*....|....*
gi 497641516 1028 FTDAGKLDRRAVARE 1042
Cdd:PRK04813 486 LTPNGKIDRKALIEE 500
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
561-1044 |
1.33e-49 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 185.70 E-value: 1.33e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 561 RQAEQRPDAPAVFASSGD-----LSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIGV 635
Cdd:COG0365 17 RHAEGRGDKVALIWEGEDgeertLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 636 D-QPRDRAERIlESGGVSLAVVC-GGQRLSMPVPEV-VLADILGGAP-----------------------------ASTE 683
Cdd:COG0365 97 GfGAEALADRI-EDAEAKVLITAdGGLRGGKVIDLKeKVDEALEELPslehvivvgrtgadvpmegdldwdellaaASAE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 684 ITSARVDPAALAYVLFTSGSTGEPKGVEVTHDAAMNTVEFIGR-HFDIGPADRCLALSTL-----EGDIsvmdVFVTLRT 757
Cdd:COG0365 176 FEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKyVLDLKPGDVFWCTADIgwatgHSYI----VYGPLLN 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 758 GGSIVVVDEVQR-RDPDAWARLIDAHQVTVLHFMPGWLEMLVEVG-----RGRLSSVRVVPTGGDWVRPEVVRRLRvEAP 831
Cdd:COG0365 252 GATVVLYEGRPDfPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGdeplkKYDLSSLRLLGSAGEPLNPEVWEWWY-EAV 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 832 GVRFAGLGGATETpvhNSIFEVTEPIpddwtaLP-----FGVPLPNNACRVVDDTGADCPDWVPGEYWVSGR--GIARGY 904
Cdd:COG0365 331 GVPIVDGWGQTET---GGIFISNLPG------LPvkpgsMGKPVPGYDVAVVDEDGNPVPPGEEGELVIKGPwpGMFRGY 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 905 RGRPDLTAERFVEHDGRiWYRTGDLVRYWPDGTLEFVGRADHRVKISGYRVELGEVETALRRVPGVRTAvaaliAVSGES 984
Cdd:COG0365 402 WNDPERYRETYFGRFPG-WYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEA-----AVVGVP 475
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497641516 985 D-----------VLAAQVCADDAsvTAEGIRQALADLVPAHMIPRHITVVERIGFTDAGKLDRRAVaRELE 1044
Cdd:COG0365 476 DeirgqvvkafvVLKPGVEPSDE--LAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLL-RKIA 543
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
559-1036 |
2.57e-48 |
|
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.
Pssm-ID: 341286 [Multi-domain] Cd Length: 435 Bit Score: 178.57 E-value: 2.57e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 559 FFRQAEQRPDAPAVFASSGDLSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIgvdqp 638
Cdd:cd17631 1 LRRRARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPL----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 639 rdraerilesggvslavvcgGQRLSMPVPEVVLADilggapasteiTSARVDPAALAYVLFTSGSTGEPKGVEVTHDAAM 718
Cdd:cd17631 76 --------------------NFRLTPPEVAYILAD-----------SGAKVLFDDLALLMYTSGTTGRPKGAMLTHRNLL 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 719 NTVEFIGRHFDIGPADRCLALSTL-EGDISVMDVFVTLRTGGSIVVVDEVqrrDPDAWARLIDAHQVTVLHFMPGWLEML 797
Cdd:cd17631 125 WNAVNALAALDLGPDDVLLVVAPLfHIGGLGVFTLPTLLRGGTVVILRKF---DPETVLDLIERHRVTSFFLVPTMIQAL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 798 VEVGRGR---LSSVRVVPTGGDWVRPEVVRRLrvEAPGVRFAGLGGATETPVHNSIFEvtepiPDDWTALP--FGVPLPN 872
Cdd:cd17631 202 LQHPRFAttdLSSLRAVIYGGAPMPERLLRAL--QARGVKFVQGYGMTETSPGVTFLS-----PEDHRRKLgsAGRPVFF 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 873 NACRVVDDTGADCPDWVPGEYWVSGRGIARGYRGRPDLTAERFveHDGriWYRTGDLVRYWPDGTLEFVGRADHRVKISG 952
Cdd:cd17631 275 VEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAF--RDG--WFHTGDLGRLDEDGYLYIVDRKKDMIISGG 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 953 YRVELGEVETALRRVPGVRTAvaaliAVSGESD------VLAAQVCADDASVTAEGIRQALADLVPAHMIPRHITVVERI 1026
Cdd:cd17631 351 ENVYPAEVEDVLYEHPAVAEV-----AVIGVPDekwgeaVVAVVVPRPGAELDEDELIAHCRERLARYKIPKSVEFVDAL 425
|
490
....*....|
gi 497641516 1027 GFTDAGKLDR 1036
Cdd:cd17631 426 PRNATGKILK 435
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
561-1038 |
6.98e-47 |
|
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341259 [Multi-domain] Cd Length: 468 Bit Score: 175.44 E-value: 6.98e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 561 RQAEQRPDAPAVFASSGDLSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIGVDQPRD 640
Cdd:cd05936 7 EAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 641 RAERILESGGVSlAVVCGgqrlsmpvpeVVLADILggAPASTEITSARVDPAALAYVLFTSGSTGEPKGVEVTHDAAMNT 720
Cdd:cd05936 87 ELEHILNDSGAK-ALIVA----------VSFTDLL--AAGAPLGERVALTPEDVAVLQYTSGTTGVPKGAMLTHRNLVAN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 721 VEFIGRHF--DIGPADR---CLALSTLEGDISVMDVFvtLRTGGSIVVvdeVQRRDPDAWARLIDAHQVTVLHFMPGWLE 795
Cdd:cd05936 154 ALQIKAWLedLLEGDDVvlaALPLFHVFGLTVALLLP--LALGATIVL---IPRFRPIGVLKEIRKHRVTIFPGVPTMYI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 796 MLV---EVGRGRLSSVRVVPTGGDWVRPEVVRRLRvEAPGVRFAGLGGATET-PV--HNSIFEVTEP--IpddwtalpfG 867
Cdd:cd05936 229 ALLnapEFKKRDFSSLRLCISGGAPLPVEVAERFE-ELTGVPIVEGYGLTETsPVvaVNPLDGPRKPgsI---------G 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 868 VPLPNNACRVVDDTGADCPDWVPGEYWVSGRGIARGYRGRPDLTAERFVehDGriWYRTGDLVRYWPDGTLEFVGRADHR 947
Cdd:cd05936 299 IPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFV--DG--WLRTGDIGYMDEDGYFFIVDRKKDM 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 948 VKISGYRVELGEVETALRRVPGVRTAVAALI--AVSGEsDVLAAQVCADDASVTAEGIRQALADLVPAHMIPRHITVVER 1025
Cdd:cd05936 375 IIVGGFNVYPREVEEVLYEHPAVAEAAVVGVpdPYSGE-AVKAFVVLKEGASLTEEEIIAFCREQLAGYKVPRQVEFRDE 453
|
490
....*....|...
gi 497641516 1026 IGFTDAGKLDRRA 1038
Cdd:cd05936 454 LPKSAVGKILRRE 466
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
554-1127 |
1.71e-45 |
|
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.
Pssm-ID: 274582 [Multi-domain] Cd Length: 1389 Bit Score: 179.49 E-value: 1.71e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 554 ALHDGFFRQAEQRPDAPAVFASSGDL---------SYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGIL 624
Cdd:TIGR03443 237 AIHDIFADNAEKHPDRTCVVETPSFLdpssktrsfTYKQINEASNILAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVL 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 625 SVGAV-------YLP------IGVDQPRdrAERILESGGV--SLAVVCGGQRLSM--PVPEVVLAD---ILGGAPASTEI 684
Cdd:TIGR03443 317 KAGATfsvidpaYPParqtiyLSVAKPR--ALIVIEKAGTldQLVRDYIDKELELrtEIPALALQDdgsLVGGSLEGGET 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 685 -------------TSARVDPAALAYVLFTSGSTGEPKGVEVTHDAAMNTVEFIGRHFDIGPADRCLALSTLEGDISVMDV 751
Cdd:TIGR03443 395 dvlapyqalkdtpTGVVVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFGLSENDKFTMLSGIAHDPIQRDM 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 752 FVTLRTGGSIVV--VDEVQrrDPDAWARLIDAHQVTVLHFMPGWLEMLVEVGRGRLSSVRVVPTGGDWVRPEVVRRLRVE 829
Cdd:TIGR03443 475 FTPLFLGAQLLVptADDIG--TPGRLAEWMAKYGATVTHLTPAMGQLLSAQATTPIPSLHHAFFVGDILTKRDCLRLQTL 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 830 APGVRFAGLGGATETPVHNSIFEVTePIPDDWTAL-------PFGVPLPNNACRVVD--DTGADCPDWVPGEYWVSGRGI 900
Cdd:TIGR03443 553 AENVCIVNMYGTTETQRAVSYFEIP-SRSSDSTFLknlkdvmPAGKGMKNVQLLVVNrnDRTQTCGVGEVGEIYVRAGGL 631
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 901 ARGYRGRPDLTAERFVEH---DGRIW----------------------YRTGDLVRYWPDGTLEFVGRADHRVKISGYRV 955
Cdd:TIGR03443 632 AEGYLGLPELNAEKFVNNwfvDPSHWidldkennkperefwlgprdrlYRTGDLGRYLPDGNVECCGRADDQVKIRGFRI 711
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 956 ELGEVETALRRVPGVRTAVA-------------ALIAVSGESDVLAAQVCADDASVTAEG--------------IRQALA 1008
Cdd:TIGR03443 712 ELGEIDTHLSQHPLVRENVTlvrrdkdeeptlvSYIVPQDKSDELEEFKSEVDDEESSDPvvkglikyrklikdIREYLK 791
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 1009 DLVPAHMIPRHITVVERIGFTDAGKLDRRAV----ARELESAVSQSQRPGHRAPSTPLQSALATIVGDLLGRQ--NIGID 1082
Cdd:TIGR03443 792 KKLPSYAIPTVIVPLKKLPLNPNGKVDKPALpfpdTAQLAAVAKNRSASAADEEFTETEREIRDLWLELLPNRpaTISPD 871
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 497641516 1083 DDFFALGGDSVLATQAVARIRAWLDApDIMVADIFANRTVSALAA 1127
Cdd:TIGR03443 872 DSFFDLGGHSILATRMIFELRKKLNV-ELPLGLIFKSPTIKGFAK 915
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
562-1042 |
2.45e-45 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 172.29 E-value: 2.45e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 562 QAEQRPDAPAVFASSGDLSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIGVdqpRDR 641
Cdd:PRK06187 15 GARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINI---RLK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 642 AERIL-------------ESGGVSLA--------------VVCGGQRLSMPVPEVVLADILGGAPasTEITSARVDPAAL 694
Cdd:PRK06187 92 PEEIAyilndaedrvvlvDSEFVPLLaailpqlptvrtviVEGDGPAAPLAPEVGEYEELLAAAS--DTFDFPDIDENDA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 695 AYVLFTSGSTGEPKGVEVTHDAAMNTVEFIGRHFDIGPADRCLAlstlegdisVMDVF---------VTLRTGGSIVVVD 765
Cdd:PRK06187 170 AAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLV---------IVPMFhvhawglpyLALMAGAKQVIPR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 766 EVqrrDPDAWARLIDAHQVTVLHFMPGWLEMLVEVGRGR---LSSVRVVPTGGDWVRPEVVRRLRvEAPGVRFAGLGGAT 842
Cdd:PRK06187 241 RF---DPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYfvdFSSLRLVIYGGAALPPALLREFK-EKFGIDLVQGYGMT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 843 ET-PVhNSIFEVTEPIPDDWT-ALPFGVPLPNNACRVVDDTGADCPdWVP---GEYWVSGRGIARGYRGRPDLTAERFVe 917
Cdd:PRK06187 317 ETsPV-VSVLPPEDQLPGQWTkRRSAGRPLPGVEARIVDDDGDELP-PDGgevGEIIVRGPWLMQGYWNRPEATAETID- 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 918 hDGriWYRTGDLVRYWPDGTLEFVGRADHRVKISGYRVELGEVETALRRVPGVRTAvaaliAVSGESD------VLAAQV 991
Cdd:PRK06187 394 -GG--WLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEV-----AVIGVPDekwgerPVAVVV 465
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 497641516 992 CADDASVTAEGIRQALADLVPAHMIPRHITVVERIGFTDAGKLDRRAVaRE 1042
Cdd:PRK06187 466 LKPGATLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVL-RE 515
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
570-1036 |
1.71e-43 |
|
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: 164.56 E-value: 1.71e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 570 PAVFASSGDLSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIGVD-QPRDraeriles 648
Cdd:cd05919 2 TAFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLlHPDD-------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 649 ggvslavvcggqrlsmpvpevvLADILGGAPASTEITSArvdpAALAYVLFTSGSTGEPKGVEVTHDAAMNTVEFIGRH- 727
Cdd:cd05919 74 ----------------------YAYIARDCEARLVVTSA----DDIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMAREa 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 728 FDIGPADRCLALSTLEGDISV-MDVFVTLRTGGSIVVVDEvqRRDPDAWARLIDAHQVTVLHFMP-GWLEMLVEVGRGR- 804
Cdd:cd05919 128 LGLTPGDRVFSSAKMFFGYGLgNSLWFPLAVGASAVLNPG--WPTAERVLATLARFRPTVLYGVPtFYANLLDSCAGSPd 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 805 -LSSVRVVPTGGDWVRPEVVRRLrVEAPGVRFAGLGGATETpVHnsIFEVTEPipDDWTALPFGVPLPNNACRVVDDTGA 883
Cdd:cd05919 206 aLRSLRLCVSAGEALPRGLGERW-MEHFGGPILDGIGATEV-GH--IFLSNRP--GAWRLGSTGRPVPGYEIRLVDEEGH 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 884 DCPDWVPGEYWVSGRGIARGYRGRPDLTAERFVEHdgriWYRTGDLVRYWPDGTLEFVGRADHRVKISGYRVELGEVETA 963
Cdd:cd05919 280 TIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFNGG----WYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESL 355
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497641516 964 LRRVPGVrtAVAALIAVSGESDVLAAQ---VCADDASVT---AEGIRQALADLVPAHMIPRHITVVERIGFTDAGKLDR 1036
Cdd:cd05919 356 IIQHPAV--AEAAVVAVPESTGLSRLTafvVLKSPAAPQeslARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQR 432
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
567-1040 |
2.61e-43 |
|
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: 165.56 E-value: 2.61e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 567 PDAPAVFASSGD--LSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIGVDQPRDRAER 644
Cdd:cd05926 1 PDAPALVVPGSTpaLTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 645 ILESGGVSLAVVCGG---------QRLSMPVPEVVL----------ADILGGAPASTEITSAR--VDPAALAYVLFTSGS 703
Cdd:cd05926 81 YLADLGSKLVLTPKGelgpasraaSKLGLAILELALdvgvlirapsAESLSNLLADKKNAKSEgvPLPDDLALILHTSGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 704 TGEPKGVEVTHDAAMNTVEFIGRHFDIGPADRCLALSTL---EGDISVmdVFVTLRTGGSIVVVDevqRRDPDAWARLID 780
Cdd:cd05926 161 TGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLVVMPLfhvHGLVAS--LLSTLAAGGSVVLPP---RFSASTFWPDVR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 781 AHQVTVLHFMPGWLEMLVEV----GRGRLSSVRVVPTGGDWVRPEVVRRL--RVEAPGVRFAGLggaTETpVHNSifeVT 854
Cdd:cd05926 236 DYNATWYTAVPTIHQILLNRpepnPESPPPKLRFIRSCSASLPPAVLEALeaTFGAPVLEAYGM---TEA-AHQM---TS 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 855 EPIPDdwTALPFG-VPLPNNA-CRVVDDTGADCPDWVPGEYWVSGRGIARGYRGRPDLTAERFvEHDGriWYRTGDLVRY 932
Cdd:cd05926 309 NPLPP--GPRKPGsVGKPVGVeVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAA-FKDG--WFRTGDLGYL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 933 WPDGTLEFVGRADHRVKISGYRVELGEVETALRRVPGVRTAVAalIAVS----GEsDVLAAQVCADDASVTAEGIRQALA 1008
Cdd:cd05926 384 DADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVA--FGVPdekyGE-EVAAAVVLREGASVTEEELRAFCR 460
|
490 500 510
....*....|....*....|....*....|..
gi 497641516 1009 DLVPAHMIPRHITVVERIGFTDAGKLDRRAVA 1040
Cdd:cd05926 461 KHLAAFKVPKKVYFVDELPKTATGKIQRRKVA 492
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
579-1043 |
6.09e-43 |
|
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: 163.06 E-value: 6.09e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 579 LSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPI----GVDQPRDRaeriLESGGVSLA 654
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLfsafGPEAIRDR----LENSEAKVL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 655 VVcggqrlsmpvpevvladilggapasTEITSARVDPAALAYVLFTSGSTGEPKGVEVTHDAaMNTVEFIGR-HFDIGPA 733
Cdd:cd05969 77 IT-------------------------TEELYERTDPEDPTLLHYTSGTTGTPKGVLHVHDA-MIFYYFTGKyVLDLHPD 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 734 DR--CLA-----LSTLEGdisvmdVFVTLRTGGSIVVVDEvqRRDPDAWARLIDAHQVTVLHFMPGWLEMLVEVG----- 801
Cdd:cd05969 131 DIywCTAdpgwvTGTVYG------IWAPWLNGVTNVVYEG--RFDAESWYGIIERVKVTVWYTAPTAIRMLMKEGdelar 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 802 RGRLSSVRVVPTGGDWVRPEVVRrLRVEAPGVRFAGLGGATETPVHNSIFEVTEPIpddwTALPFGVPLPNNACRVVDDT 881
Cdd:cd05969 203 KYDLSSLRFIHSVGEPLNPEAIR-WGMEVFGVPIHDTWWQTETGSIMIANYPCMPI----KPGSMGKPLPGVKAAVVDEN 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 882 GADCPDWVPGEY-----WVSgrgIARGYRGRPDLTAERFVehDGriWYRTGDLVRYWPDGTLEFVGRADHRVKISGYRVE 956
Cdd:cd05969 278 GNELPPGTKGILalkpgWPS---MFRGIWNDEERYKNSFI--DG--WYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVG 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 957 LGEVETALRRVPGVrtavaALIAVSGESDVLAAQVCADDASVTaEG--------------IRQALAdlvpAHMIPRHITV 1022
Cdd:cd05969 351 PFEVESALMEHPAV-----AEAGVIGKPDPLRGEIIKAFISLK-EGfepsdelkeeiinfVRQKLG----AHVAPREIEF 420
|
490 500
....*....|....*....|..
gi 497641516 1023 VERIGFTDAGKLDRRAV-AREL 1043
Cdd:cd05969 421 VDNLPKTRSGKIMRRVLkAKEL 442
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
580-1037 |
3.24e-41 |
|
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: 157.45 E-value: 3.24e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 580 SYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIGVDQPRDRAERILESGGVSLAVVcgg 659
Cdd:cd05934 5 TYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 660 qrlsmpvpevvladilggapasteitsarvdpaALAYVLFTSGSTGEPKGVEVTHDAAMNTVEFIGRHFDIGPADRCLA- 738
Cdd:cd05934 82 ---------------------------------DPASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGEDDVYLTv 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 739 LSTLEGDISVMDVFVTLRTGGSIVVVDevqRRDPDAWARLIDAHQVTVLHFMPGWLEMLV---EVGRGRLSSVRVVptGG 815
Cdd:cd05934 129 LPLFHINAQAVSVLAALSVGATLVLLP---RFSASRFWSDVRRYGATVTNYLGAMLSYLLaqpPSPDDRAHRLRAA--YG 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 816 DWVRPEVVRRLRvEAPGVRFAGLGGATETpvhnsIFEVTEPIPDDWTALPFGVPLPNNACRVVDDTGADCPDWVPGEYWV 895
Cdd:cd05934 204 APNPPELHEEFE-ERFGVRLLEGYGMTET-----IVGVIGPRDEPRRPGSIGRPAPGYEVRIVDDDGQELPAGEPGELVI 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 896 ---SGRGIARGYRGRPDLTAERFveHDGriWYRTGDLVRYWPDGTLEFVGRADHRVKISGYRVELGEVETALRRVPGVR- 971
Cdd:cd05934 278 rglRGWGFFKGYYNMPEATAEAM--RNG--WFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVRe 353
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497641516 972 TAVAALIAVSGESDVLAAQVCADDASVTAEGIRQALADLVPAHMIPRHITVVERIGFTDAGKLDRR 1037
Cdd:cd05934 354 AAVVAVPDEVGEDEVKAVVVLRPGETLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKA 419
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
579-1041 |
7.98e-41 |
|
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: 156.34 E-value: 7.98e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 579 LSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPI-GVDQPRDRAERIlESGGVSlAVVC 657
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLtTLLGPKDIEYRL-EAAGAK-AIVT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 658 GGQrlsmpvpevvladilggapasteitsarvDPAALayvLFTSGSTGEPKGVEVTHDAAMNTVEFIGRHFDIGP----- 732
Cdd:cd05972 79 DAE-----------------------------DPALI---YFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRPddihw 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 733 --ADRCLALSTLEGDISVMDVFVTlrtggsiVVVDEVQRRDPDAWARLIDAHQVTVLHFMPGWLEMLVEVG--RGRLSSV 808
Cdd:cd05972 127 niADPGWAKGAWSSFFGPWLLGAT-------VFVYEGPRFDAERILELLERYGVTSFCGPPTAYRMLIKQDlsSYKFSHL 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 809 RVVPTGGDWVRPEVVRRLRvEAPGVRFAGLGGATETPVHNSIFEVTEPIPDDwtalpFGVPLPNNACRVVDDTGADCPDW 888
Cdd:cd05972 200 RLVVSAGEPLNPEVIEWWR-AATGLPIRDGYGQTETGLTVGNFPDMPVKPGS-----MGRPTPGYDVAIIDDDGRELPPG 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 889 VPGEYWV--SGRGIARGYRGRPDLTAERFVEHdgriWYRTGDLVRYWPDGTLEFVGRADHRVKISGYRVELGEVETALRR 966
Cdd:cd05972 274 EEGDIAIklPPPGLFLGYVGDPEKTEASIRGD----YYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLE 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 967 VPGVrtAVAALIAVSGE---SDVLAAQVCADDAS---VTAEGIRQALADLVPAHMIPRHITVVERIGFTDAGKLdRRAVA 1040
Cdd:cd05972 350 HPAV--AEAAVVGSPDPvrgEVVKAFVVLTSGYEpseELAEELQGHVKKVLAPYKYPREIEFVEELPKTISGKI-RRVEL 426
|
.
gi 497641516 1041 R 1041
Cdd:cd05972 427 R 427
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
574-1014 |
2.38e-40 |
|
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: 156.60 E-value: 2.38e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 574 ASSGD-LSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLP-------------IGVDQPR 639
Cdd:cd05911 5 ADTGKeLTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAanpiytadelahqLKISKPK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 640 ------DRAERILES----GGVSLAVVCGGQRLSMPVPEVVLaDILGGAPASTEITSARVDPAALAYVLFTSGSTGEPKG 709
Cdd:cd05911 85 viftdpDGLEKVKEAakelGPKDKIIVLDDKPDGVLSIEDLL-SPTLGEEDEDLPPPLKDGKDDTAAILYSSGTTGLPKG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 710 VEVTHDAAMNTVEFIGRHF--DIGPADRCLALSTLEgDISVMDVFVTLRTGGSIVVVDevQRRDPDAWARLIDAHQVTVL 787
Cdd:cd05911 164 VCLSHRNLIANLSQVQTFLygNDGSNDVILGFLPLY-HIYGLFTTLASLLNGATVIIM--PKFDSELFLDLIEKYKITFL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 788 HFMPGWLEMLVE---VGRGRLSSVRVVPTGGDWVRPEVVRRLRVEAPGVRFAGLGGATETpvhNSIFEVTEPIPDDWTAL 864
Cdd:cd05911 241 YLVPPIAAALAKsplLDKYDLSSLRVILSGGAPLSKELQELLAKRFPNATIKQGYGMTET---GGILTVNPDGDDKPGSV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 865 pfGVPLPNNACRVVD-DTGADCPDWVPGEYWVSGRGIARGYRGRPDLTAERFVEhDGriWYRTGDLVRYWPDGTLEFVGR 943
Cdd:cd05911 318 --GRLLPNVEAKIVDdDGKDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDE-DG--WLHTGDIGYFDEDGYLYIVDR 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497641516 944 ADHRVKISGYRVELGEVETALRRVPGVR-TAVAAL-IAVSGESDVlAAQVCADDASVTAEGIRQALADLVPAH 1014
Cdd:cd05911 393 KKELIKYKGFQVAPAELEAVLLEHPGVAdAAVIGIpDEVSGELPR-AYVVRKPGEKLTEKEVKDYVAKKVASY 464
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
561-1038 |
1.35e-39 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 154.68 E-value: 1.35e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 561 RQAEQRPDAPAVFASSGDLSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIgvdQPR- 639
Cdd:PRK07656 13 RAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPL---NTRy 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 640 --DRAERILESGGVSLAVVCGG-QRLSMPVPE-------VVLADILGG--------------APASTEITSARVDPAALA 695
Cdd:PRK07656 90 taDEAAYILARGDAKALFVLGLfLGVDYSATTrlpalehVVICETEEDdphtekmktftdflAAGDPAERAPEVDPDDVA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 696 YVLFTSGSTGEPKGVEVTHDAAMNTVEFIGRHFDIGPADRCLAlstlegdisVMDVFVT----------LRTGGSIVVVd 765
Cdd:PRK07656 170 DILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLA---------ANPFFHVfgykagvnapLMRGATILPL- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 766 evQRRDPDAWARLIDAHQVTVLHFMPGWLEMLVEVGRGR---LSSVRVVPTGGDWVRPEVVRRLRVEAPGVRFAGLGGAT 842
Cdd:PRK07656 240 --PVFDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSaedLSSLRLAVTGAASMPVALLERFESELGVDIVLTGYGLS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 843 E-TPVhnsifeVT-EPIPDDWTALP--FGVPLPNNACRVVDDTGADCPDWVPGEYWVSGRGIARGYRGRPDLTAERfVEH 918
Cdd:PRK07656 318 EaSGV------TTfNRLDDDRKTVAgtIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAA-IDA 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 919 DGriWYRTGDLVRYWPDGTLEFVGRADHRVKISGYRVELGEVETALRRVPGVrtAVAALIAV----SGESdVLAAQVCAD 994
Cdd:PRK07656 391 DG--WLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAV--AEAAVIGVpderLGEV-GKAYVVLKP 465
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 497641516 995 DASVTAEGI----RQALADlvpaHMIPRHITVVERIGFTDAGKLDRRA 1038
Cdd:PRK07656 466 GAELTEEELiaycREHLAK----YKVPRSIEFLDELPKNATGKVLKRA 509
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
567-1035 |
5.22e-39 |
|
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: 151.86 E-value: 5.22e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 567 PDAPAV----FASSGDLSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIGVDQPRDRA 642
Cdd:cd17654 1 PDRPALiidqTTSDTTVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 643 ERILESGGVSLAVVCG--GQRLSMPVPEVVLADILGGAPasteitsarvdpaaLAYVLFTSGSTGEPKGVEVTHDAAMNT 720
Cdd:cd17654 81 LTVMKKCHVSYLLQNKelDNAPLSFTPEHRHFNIRTDEC--------------LAYVIHTSGTTGTPKIVAVPHKCILPN 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 721 VEFIGRHFDIGPADRCLALSTLEGDISVMDVFVTLRTGGSIVVVDEVQRRDPDAWARLID-AHQVTVLHFMPGWLEML-V 798
Cdd:cd17654 147 IQHFRSLFNITSEDILFLTSPLTFDPSVVEIFLSLSSGATLLIVPTSVKVLPSKLADILFkRHRITVLQATPTLFRRFgS 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 799 EVGRG----RLSSVRVVPTGGD-WVRPEVVRRLRVEAPGVRFAGLGGATETpvhnSIFEVTEPIPDDWTALPFGVPLPNN 873
Cdd:cd17654 227 QSIKStvlsATSSLRVLALGGEpFPSLVILSSWRGKGNRTRIFNIYGITEV----SCWALAYKVPEEDSPVQLGSPLLGT 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 874 ACRVVDDTGADCPDWVPGEYwVSGRGIARGYRGRPDLTaerfvehdgriWYRTGDLVRYwPDGTLEFVGRADHRVKISGY 953
Cdd:cd17654 303 VIEVRDQNGSEGTGQVFLGG-LNRVCILDDEVTVPKGT-----------MRATGDFVTV-KDGELFFLGRKDSQIKRRGK 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 954 RVELGEVETALRRVPGVRTAVAALiavsgeSDVLAAQVCADDASVTAEGIRQALADLVPAHMIPRHITVVERIGFTDAGK 1033
Cdd:cd17654 370 RINLDLIQQVIESCLGVESCAVTL------SDQQRLIAFIVGESSSSRIHKELQLTLLSSHAIPDTFVQIDKLPLTSHGK 443
|
..
gi 497641516 1034 LD 1035
Cdd:cd17654 444 VD 445
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
552-1044 |
8.54e-38 |
|
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: 149.91 E-value: 8.54e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 552 GEALHDGFFRQAEQRPDAPAVFASSGDLSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAV-- 629
Cdd:COG1021 24 GETLGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAIpv 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 630 -YLP-------------------IGVDQ-----PRDRAERILESG-GVSLAVVCGGqrlsmPVPEVVLADiLGGAPASTE 683
Cdd:COG1021 104 fALPahrraeishfaeqseavayIIPDRhrgfdYRALARELQAEVpSLRHVLVVGD-----AGEFTSLDA-LLAAPADLS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 684 ItsARVDPAALAYVLFTSGSTGEPKGVEVTHDAAMNTVEFIGRHFDIGPADRCLALSTLEGD--ISVMDVFVTLRTGGSI 761
Cdd:COG1021 178 E--PRPDPDDVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEICGLDADTVYLAALPAAHNfpLSSPGVLGVLYAGGTV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 762 VVVDEVqrrDPDAWARLIDAHQVTVLHFMPG----WLEMlVEVGRGRLSSVRVVPTGGDWVRPEVVRRLRvEAPGVRFAG 837
Cdd:COG1021 256 VLAPDP---SPDTAFPLIERERVTVTALVPPlallWLDA-AERSRYDLSSLRVLQVGGAKLSPELARRVR-PALGCTLQQ 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 838 LGGATETPVHnsifeVTEpiPDDWTALPF---GVPL-PNNACRVVDDTGADCPDWVPGEYWVSGRGIARGYRGRPDLTAE 913
Cdd:COG1021 331 VFGMAEGLVN-----YTR--LDDPEEVILttqGRPIsPDDEVRIVDEDGNPVPPGEVGELLTRGPYTIRGYYRAPEHNAR 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 914 RFVEhDGriWYRTGDLVRYWPDGTLEFVGRA-DHRV----KISGyrvelGEVETALRRVPGVRTavAALIAVsgESDVLA 988
Cdd:COG1021 404 AFTP-DG--FYRTGDLVRRTPDGYLVVEGRAkDQINrggeKIAA-----EEVENLLLAHPAVHD--AAVVAM--PDEYLG 471
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497641516 989 AQVCA----DDASVTAEGIRQALADL-VPAHMIPRHITVVERIGFTDAGKLDRRAVARELE 1044
Cdd:COG1021 472 ERSCAfvvpRGEPLTLAELRRFLRERgLAAFKLPDRLEFVDALPLTAVGKIDKKALRAALA 532
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
599-1040 |
1.69e-37 |
|
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: 147.59 E-value: 1.69e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 599 GVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIGVDQPRDRAERIL------ESGGVSLAVVCGGQRLSMPVP----- 667
Cdd:cd05922 14 GGVRGERVVLILPNRFTYIELSFAVAYAGGRLGLVFVPLNPTLKESVLrylvadAGGRIVLADAGAADRLRDALPaspdp 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 668 -EVVLADILGGAPASTEitSARVDPAALAYVLFTSGSTGEPKGVEVTHDAAMNTVEFIGRHFDIGPADRCLALSTLEGDI 746
Cdd:cd05922 94 gTVLDADGIRAARASAP--AHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDRALTVLPLSYDY 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 747 SVMDVFVTLRTGGSIVVvdEVQRRDPDAWARLIDAHQVTVLHFMPGWLEMLVEVGRG--RLSSVRVVPTGGDWVRPEVVR 824
Cdd:cd05922 172 GLSVLNTHLLRGATLVL--TNDGVLDDAFWEDLREHGATGLAGVPSTYAMLTRLGFDpaKLPSLRYLTQAGGRLPQETIA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 825 RLRVEAPGVRFAGLGGATETPVHNSIFEvTEPIPDDWTALpfGVPLPNNACRVVDDTGADCPDWVPGEYWVSGRGIARGY 904
Cdd:cd05922 250 RLRELLPGAQVYVMYGQTEATRRMTYLP-PERILEKPGSI--GLAIPGGEFEILDDDGTPTPPGEPGEIVHRGPNVMKGY 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 905 RGRPDLTAERfVEHDGRIWyrTGDLVRYWPDGTLEFVGRADHRVKISGYRVELGEVETALRRVPGVRTAVA-ALIAVSGE 983
Cdd:cd05922 327 WNDPPYRRKE-GRGGGVLH--TGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAvGLPDPLGE 403
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 497641516 984 SDVLAAqvcADDASVTAEGIRQALADLVPAHMIPRHITVVERIGFTDAGKLDRRAVA 1040
Cdd:cd05922 404 KLALFV---TAPDKIDPKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
561-1044 |
4.56e-37 |
|
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 147.77 E-value: 4.56e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 561 RQAEQRPDAPAV------FASSGDLSYAQLRDQALAVAAALRAAGvTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIG 634
Cdd:cd05931 1 RRAAARPDRPAYtflddeGGREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 635 VDQPR---DRAERILESGGVSLAVVCGGQR----------LSMPVPEVVLADILGGAPASTEiTSARVDPAALAYVLFTS 701
Cdd:cd05931 80 PPTPGrhaERLAAILADAGPRVVLTTAAALaavrafaasrPAAGTPRLLVVDLLPDTSAADW-PPPSPDPDDIAYLQYTS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 702 GSTGEPKGVEVTHDAAMNTVEFIGRHFDIGPADRC---------LALstlegdisVMDVFVTLRTGGSIVV---VDEVQR 769
Cdd:cd05931 159 GSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVvswlplyhdMGL--------IGGLLTPLYSGGPSVLmspAAFLRR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 770 rdPDAWARLIDAHQVTVlHFMPGW-LEMLVEVGRGR------LSSVRVVPTGGDWVRPEVVRR---------LRVEA--P 831
Cdd:cd05931 231 --PLRWLRLISRYRATI-SAAPNFaYDLCVRRVRDEdlegldLSSWRVALNGAEPVRPATLRRfaeafapfgFRPEAfrP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 832 G------VRFAGLGGATETPV---------HNSIFEVTEPIPDDWTALPFGVPLPNNACRVVD-DTGADCPDWVPGEYWV 895
Cdd:cd05931 308 SyglaeaTLFVSGGPPGTGPVvlrvdrdalAGRAVAVAADDPAARELVSCGRPLPDQEVRIVDpETGRELPDGEVGEIWV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 896 SGRGIARGYRGRPDLTAERF---VEHDGRIWYRTGDLVRYWpDGTLEFVGRADHRVKISGYRVELGEVETALRRV-PGVR 971
Cdd:cd05931 388 RGPSVASGYWGRPEATAETFgalAATDEGGWLRTGDLGFLH-DGELYITGRLKDLIIVRGRNHYPQDIEATAEEAhPALR 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 972 TAVAALIAVSGESDVLAAQVCA-------DDASVTAEGIRQALAD----------LVPAHMIPRhitvverigfTDAGKL 1034
Cdd:cd05931 467 PGCVAAFSVPDDGEERLVVVAEvergadpADLAAIAAAIRAAVARehgvapadvvLVRPGSIPR----------TSSGKI 536
|
570
....*....|
gi 497641516 1035 DRRAVARELE 1044
Cdd:cd05931 537 QRRACRAAYL 546
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
579-1034 |
5.91e-37 |
|
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: 145.22 E-value: 5.91e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 579 LSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIGVDQPRDRAERILESGGVSLAVVCG 658
Cdd:cd05903 2 LTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 659 GQRLSMPVPevvladilggapasteitsarvDPAALAYVLFTSGSTGEPKGVEVTHDAAMNTVEFIGRHFDIGPADRCLA 738
Cdd:cd05903 82 RFRQFDPAA----------------------MPDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGDVFLV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 739 LSTLEGDISVMDVFVTLRTGGSIVVVDevQRRDPDAWARLIDAHQVTVLHFMPGWLEML---VEVGRGRLSSVRVVPTGG 815
Cdd:cd05903 140 ASPMAHQTGFVYGFTLPLLLGAPVVLQ--DIWDPDKALALMREHGVTFMMGATPFLTDLlnaVEEAGEPLSRLRTFVCGG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 816 DWVRPEVVRRLRvEAPGVRFAGLGGATETPvhnSIFEVTEPIPDDWTALPFGVPLPNNACRVVDDTGADCPDWVPGEYWV 895
Cdd:cd05903 218 ATVPRSLARRAA-ELLGAKVCSAYGSTECP---GAVTSITPAPEDRRLYTDGRPLPGVEIKVVDDTGATLAPGVEGELLS 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 896 SGRGIARGYRGRPDLTAERFVEhdgrIWYRTGDLVRYWPDGTLEFVGRADHRVKISGYRVELGEVETALRRVPGVRTavA 975
Cdd:cd05903 294 RGPSVFLGYLDRPDLTADAAPE----GWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIE--A 367
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497641516 976 ALIAVSGESdvLAAQVCAddASVTAEGIRQALADL--------VPAHMIPRHITVVERIGFTDAGKL 1034
Cdd:cd05903 368 AVVALPDER--LGERACA--VVVTKSGALLTFDELvayldrqgVAKQYWPERLVHVDDLPRTPSGKV 430
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
559-1036 |
7.86e-37 |
|
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: 146.36 E-value: 7.86e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 559 FFRQAEQRPDAPAVFASSGDLSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIGVDQP 638
Cdd:cd05959 10 DLNLNEGRGDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 639 RDRAERILESGGVSLAVVCG------GQRLSMPVPEVVLADILGGAPA--------------STEITSARVDPAALAYVL 698
Cdd:cd05959 90 PDDYAYYLEDSRARVVVVSGelapvlAAALTKSEHTLVVLIVSGGAGPeagalllaelvaaeAEQLKPAATHADDPAFWL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 699 FTSGSTGEPKGVEVTHDAAMNTVEFIGRH-FDIGPADRCLALSTL-----EGDisvmDVFVTLRTGGSIVVVDEvqRRDP 772
Cdd:cd05959 170 YSSGSTGRPKGVVHLHADIYWTAELYARNvLGIREDDVCFSAAKLffaygLGN----SLTFPLSVGATTVLMPE--RPTP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 773 DAWARLIDAHQVTVLHFMP-GWLEMLVEVGRGR--LSSVRVVPTGGDWVRPEVVRRLRVeapgvRFA-----GLGgATET 844
Cdd:cd05959 244 AAVFKRIRRYRPTVFFGVPtLYAAMLAAPNLPSrdLSSLRLCVSAGEALPAEVGERWKA-----RFGldildGIG-STEM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 845 pVHnsIFevTEPIPDDWTALPFGVPLPNNACRVVDDTGADCPDWVPGEYWVSGRGIARGYRGRPDLTAERFVEHdgriWY 924
Cdd:cd05959 318 -LH--IF--LSNRPGRVRYGTTGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQGE----WT 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 925 RTGDLVRYWPDGTLEFVGRADHRVKISGYRVELGEVETALRRVPGVRTAvaaliAVSGESD----------VLAAQVCAD 994
Cdd:cd05959 389 RTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEA-----AVVGVEDedgltkpkafVVLRPGYED 463
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 497641516 995 DAsVTAEGIRQALADLVPAHMIPRHITVVERIGFTDAGKLDR 1036
Cdd:cd05959 464 SE-ALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQR 504
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
518-1046 |
8.16e-36 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 144.37 E-value: 8.16e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 518 ASADEAWEAPGPPALPeaqravreaangRTAEPSGEALHDGFFRQAEQRPDAPAVFASSGDLSYAQLRDQALAVAAALRA 597
Cdd:PRK05605 9 AFADKPWLQSYAPWTP------------HDLDYGDTTLVDLYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 598 AGVTAGDTIAVMGPKTAEQIPALLGILSVGAV-------YLP---------------IGVDQPRDRAERILESGGVSLAV 655
Cdd:PRK05605 77 LGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVvvehnplYTAhelehpfedhgarvaIVWDKVAPTVERLRRTTPLETIV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 656 VCG-------GQR--LSMPVP-------------------EVVLADILGGApaSTEITSARVDPAALAYVLFTSGSTGEP 707
Cdd:PRK05605 157 SVNmiaamplLQRlaLRLPIPalrkaraaltgpapgtvpwETLVDAAIGGD--GSDVSHPRPTPDDVALILYTSGTTGKP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 708 KGVEVTH-----DAAMntvefiGRHF--DIGPAD-RCLAL--------STLEGDISVMdvfvtlrTGGSIVVvdeVQRRD 771
Cdd:PRK05605 235 KGAQLTHrnlfaNAAQ------GKAWvpGLGDGPeRVLAAlpmfhaygLTLCLTLAVS-------IGGELVL---LPAPD 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 772 PDAWARLIDAHQVTVLHFMPGWLEMLVEVGRGR---LSSVRVVPTGGDWVRPEVVRRLRVEAPGVRFAGLgGATETpvhn 848
Cdd:PRK05605 299 IDLILDAMKKHPPTWLPGVPPLYEKIAEAAEERgvdLSGVRNAFSGAMALPVSTVELWEKLTGGLLVEGY-GLTET---- 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 849 SIFEVTEPIPDDWTALPFGVPLPNNACRVVD--DTGADCPDWVPGEYWVSGRGIARGYRGRPDLTAERFveHDGriWYRT 926
Cdd:PRK05605 374 SPIIVGNPMSDDRRPGYVGVPFPDTEVRIVDpeDPDETMPDGEEGELLVRGPQVFKGYWNRPEETAKSF--LDG--WFRT 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 927 GDLVRYWPDGTLEFVGRADHRVKISGYRVELGEVETALRRVPGVR-TAVAALIAVSGESDVLAAQVCADDASVTAEGIRQ 1005
Cdd:PRK05605 450 GDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEdAAVVGLPREDGSEEVVAAVVLEPGAALDPEGLRA 529
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 497641516 1006 ALADLVPAHMIPRHITVVERIGFTDAGKLDRRAVARELESA 1046
Cdd:PRK05605 530 YCREHLTRYKVPRRFYHVDELPRDQLGKVRRREVREELLEK 570
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
579-1045 |
5.54e-35 |
|
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: 141.65 E-value: 5.54e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 579 LSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIGV----DQPRDRAERI------LES 648
Cdd:cd05906 40 QSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTVpptyDEPNARLRKLrhiwqlLGS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 649 ggvslAVVCGGQRLSMPVPEVV-LADILGGAPASTEITSA--------RVDPAALAYVLFTSGSTGEPKGVEVTHDAAMN 719
Cdd:cd05906 120 -----PVVLTDAELVAEFAGLEtLSGLPGIRVLSIEELLDtaadhdlpQSRPDDLALLMLTSGSTGFPKAVPLTHRNILA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 720 TVEFIGRHFDIGPADRCLALSTLE--GDISVMDVFVTLRTGGSIVVVDEVQRRDPDAWARLIDAHQVTVLhFMPGWLEML 797
Cdd:cd05906 195 RSAGKIQHNGLTPQDVFLNWVPLDhvGGLVELHLRAVYLGCQQVHVPTEEILADPLRWLDLIDRYRVTIT-WAPNFAFAL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 798 V-------EVGRGRLSSVRVVPTGGDWVRPEVVRRL--RVEAPGVR---FAGLGGATETpVHNSIFEVTEPIPDDWTALP 865
Cdd:cd05906 274 LndlleeiEDGTWDLSSLRYLVNAGEAVVAKTIRRLlrLLEPYGLPpdaIRPAFGMTET-CSGVIYSRSFPTYDHSQALE 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 866 F---GVPLPNNACRVVDDTGADCPDWVPGEYWVSGRGIARGYRGRPDLTAERFVEhDGriWYRTGDLVrYWPDGTLEFVG 942
Cdd:cd05906 353 FvslGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTE-DG--WFRTGDLG-FLDNGNLTITG 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 943 RADHRVKISGYRVELGEVETALRRVPGVRTAVAALIAV---SGESDVLA-----AQVCADDASVTAEGIRQALADLV--- 1011
Cdd:cd05906 429 RTKDTIIVNGVNYYSHEIEAAVEEVPGVEPSFTAAFAVrdpGAETEELAiffvpEYDLQDALSETLRAIRSVVSREVgvs 508
|
490 500 510
....*....|....*....|....*....|....
gi 497641516 1012 PAHMIPRHITVVERigfTDAGKLDRRAVARELES 1045
Cdd:cd05906 509 PAYLIPLPKEEIPK---TSLGKIQRSKLKAAFEA 539
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
579-1037 |
3.96e-34 |
|
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: 136.84 E-value: 3.96e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 579 LSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIGVDQPRDRAERILESGGVSLAVVcg 658
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVV-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 659 gqrlsmpvpevvladilggapasteiTSARVDpaaLAYVLFTSGSTGEPKGVEVTHDAAMNTVEFIGRHFDIGPAD---R 735
Cdd:cd05935 80 --------------------------GSELDD---LALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSDvilA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 736 CLALSTLEGDISVMDVFVTLrtGGSIVVVdevQRRDPDAWARLIDAHQVTVLHFMPGWLEMLVEVGRGR---LSSVRVVP 812
Cdd:cd05935 131 CLPLFHVTGFVGSLNTAVYV--GGTYVLM---ARWDRETALELIEKYKVTFWTNIPTMLVDLLATPEFKtrdLSSLKVLT 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 813 TGGDWVRPEVVRRLRvEAPGVRFAGLGGATET--PVHnsifeVTEPIPDDWTALpfGVPLPNNACRVVD-DTGADCPDWV 889
Cdd:cd05935 206 GGGAPMPPAVAEKLL-KLTGLRFVEGYGLTETmsQTH-----TNPPLRPKLQCL--GIP*FGVDARVIDiETGRELPPNE 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 890 PGEYWVSGRGIARGYRGRPDLTAERFVEHDGRIWYRTGDLVRYWPDGTLEFVGRADHRVKISGYRVELGEVETALRRVPG 969
Cdd:cd05935 278 VGEIVVRGPQIFKGYWNRPEETEESFIEIKGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPA 357
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497641516 970 VRTavAALIAVSGE--SDVLAAQVCADD---ASVTAEGIRQALADLVPAHMIPRHITVVERIGFTDAGKLDRR 1037
Cdd:cd05935 358 I*E--VCVISVPDErvGEEVKAFIVLRPeyrGKVTEEDIIEWAREQMAAYKYPREVEFVDELPRSASGKILWR 428
|
|
| C_NRPS-like |
cd19066 |
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ... |
102-518 |
8.71e-34 |
|
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long, with various activities such as antibiotic, antifungal, antitumor and immunosuppression. There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380453 [Multi-domain] Cd Length: 427 Bit Score: 135.61 E-value: 8.71e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 102 PFSLAPMQHAMWVGRQENQQLGGVAGHLYVEFDGGgIDPERLRAAATALARRHPMLRVRFLP-DGTQRIAPADEFGPFPV 180
Cdd:cd19066 1 KIPLSPMQRGMWFLKKLATDPSAFNVAIEMFLTGS-LDLARLKQALDAVMERHDVLRTRFCEeAGRYEQVVLDKTVRFRI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 181 HVEDLRERSTGEAdrRLAAIRAAKSHQQLDGAVFEL---AVTLLPAERSRLHVDLDMQAADAMSYRTLMADLAALYLG-- 255
Cdd:cd19066 80 EIIDLRNLADPEA--RLLELIDQIQQTIYDLERGPLvrvALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDAae 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 256 RDLPELGYTYRQYR-HAIEAEDARPQPARDADRAWWARRLPELPDPPALPTTGGRAENQSTRRWH---WLDPHTRDALFA 331
Cdd:cd19066 158 RQKPTLPPPVGSYAdYAAWLEKQLESEAAQADLAYWTSYLHGLPPPLPLPKAKRPSQVASYEVLTlefFLRSEETKRLRE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 332 RAQARGFTPAMALAAGFANTLARWSTTSRFLLNVPLFGRqaLHPDVDSLVGDFTSSLLLDVDLTRANTAAARAQVVQDAM 411
Cdd:cd19066 238 VARESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNR--PDEAVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKEQS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 412 RTAAAHSAYPGLAVLRDLSRHRGTQ--VLAPVVFTSALGLGELFSSDVtGQFGTPGWIISQGPQVLLDAQVTE-FDGGVL 488
Cdd:cd19066 316 REAIEHQRVPFIELVRHLGVVPEAPkhPLFEPVFTFKNNQQQLGKTGG-FIFTTPVYTSSEGTVFDLDLEASEdPDGDLL 394
|
410 420 430
....*....|....*....|....*....|
gi 497641516 489 VNWDVREGVFPAGVIDAMFAHHIDELLRLA 518
Cdd:cd19066 395 LRLEYSRGVYDERTIDRFAERYMTALRQLI 424
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
599-1039 |
1.17e-33 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 137.26 E-value: 1.17e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 599 GVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIGVDQPRDRAErilesggVSLAVvcggqrlSMPVPEVVL--ADILG 676
Cdd:cd17647 41 GIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQN-------IYLGV-------AKPRGLIVIraAGVVV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 677 GaPASTEITSarvdpaalayvlFTSGSTGEPKGVEVTHDAAMNTVEFIGRHFDIGPADRCLALSTLEGDISVMDVFVTLR 756
Cdd:cd17647 107 G-PDSNPTLS------------FTSGSEGIPKGVLGRHFSLAYYFPWMAKRFNLSENDKFTMLSGIAHDPIQRDMFTPLF 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 757 TGGSIVVVDEVQRRDPDAWARLIDAHQVTVLHFMPGWLEMLVEVGRGRLSSVRVVPTGGDWVRPEVVRRLRVEAPGVRFA 836
Cdd:cd17647 174 LGAQLLVPTQDDIGTPGRLAEWMAKYGATVTHLTPAMGQLLTAQATTPFPKLHHAFFVGDILTKRDCLRLQTLAENVRIV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 837 GLGGATETPVHNSIFEVTEPIPDDW------TALPFGVPLPNNACRVVD--DTGADCPDWVPGEYWVSGRGIARGYRGRP 908
Cdd:cd17647 254 NMYGTTETQRAVSYFEVPSRSSDPTflknlkDVMPAGRGMLNVQLLVVNrnDRTQICGIGEVGEIYVRAGGLAEGYRGLP 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 909 DLTAERFVEH---DGRIW----------------------YRTGDLVRYWPDGTLEFVGRADHRVKISGYRVELGEVETA 963
Cdd:cd17647 334 ELNKEKFVNNwfvEPDHWnyldkdnnepwrqfwlgprdrlYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTH 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 964 LRRVPGVR--------------TAVAALIAV-SGESDVLAAQVCADDASVT-------------AEGIRQALADLVPAHM 1015
Cdd:cd17647 414 ISQHPLVRenitlvrrdkdeepTLVSYIVPRfDKPDDESFAQEDVPKEVSTdpivkgligyrklIKDIREFLKKRLASYA 493
|
490 500
....*....|....*....|....
gi 497641516 1016 IPRHITVVERIGFTDAGKLDRRAV 1039
Cdd:cd17647 494 IPSLIVVLDKLPLNPNGKVDKPKL 517
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
512-1047 |
6.58e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 135.55 E-value: 6.58e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 512 DELLRLASADEAWEAPGPPALPeaqravreaangRTAE-PSGE-ALHDGFFRQAEQRPDAPAVFASSGDLSYAQLRDQAL 589
Cdd:PRK06178 2 AEEAYLAELRALQQAAWPAGIP------------REPEyPHGErPLTEYLRAWARERPQRPAIIFYGHVITYAELDELSD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 590 AVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIG----------------------VDQPRDRAERILE 647
Cdd:PRK06178 70 RFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSplfrehelsyelndagaevllaLDQLAPVVEQVRA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 648 SGGV------SLAVVCGGQrLSMPVPEVVLA---------DILGGAPAST-EITSARVDPAALAYVLFTSGSTGEPKGVE 711
Cdd:PRK06178 150 ETSLrhvivtSLADVLPAE-PTLPLPDSLRAprlaaagaiDLLPALRACTaPVPLPPPALDALAALNYTGGTTGMPKGCE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 712 VTHdaamntvefigRHFdIGPADRCLALSTLEGDISVMDVF--------------VTLRTGGSIVVVdevQRRDPDAWAR 777
Cdd:PRK06178 229 HTQ-----------RDM-VYTAAAAYAVAVVGGEDSVFLSFlpefwiagenfgllFPLFSGATLVLL---ARWDAVAFMA 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 778 LIDAHQVTVLhFMP--GWLEML--VEVGRGRLSSVRVVPTGgDWVR---PEVVRRLRVEAPGVRFAGLGGATETPVHNSI 850
Cdd:PRK06178 294 AVERYRVTRT-VMLvdNAVELMdhPRFAEYDLSSLRQVRVV-SFVKklnPDYRQRWRALTGSVLAEAAWGMTETHTCDTF 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 851 fevTEPIPDDWTALPF-----GVPLPNNACRVVD-DTGADCPDWVPGEYWVSGRGIARGYRGRPDLTAERFVehDGriWY 924
Cdd:PRK06178 372 ---TAGFQDDDFDLLSqpvfvGLPVPGTEFKICDfETGELLPLGAEGEIVVRTPSLLKGYWNKPEATAEALR--DG--WL 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 925 RTGDLVRYWPDGTLEFVGRADHRVKISGYRVELGEVETALRRVPGVRTAvaaliAVSGESDVLAAQV------CADDASV 998
Cdd:PRK06178 445 HTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGS-----AVVGRPDPDKGQVpvafvqLKPGADL 519
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 497641516 999 TAEGIRQALADLVPAHMIPRhITVVERIGFTDAGKLDRRAVARELESAV 1047
Cdd:PRK06178 520 TAAALQAWCRENMAVYKVPE-IRIVDALPMTATGKVRKQDLQALAEELK 567
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
555-1039 |
2.06e-32 |
|
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.
Pssm-ID: 341247 [Multi-domain] Cd Length: 493 Bit Score: 133.02 E-value: 2.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 555 LHDGFFRQAEQRPDAPAVF--ASSGDLSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLP 632
Cdd:cd05923 3 VFEMLRRAASRAPDACAIAdpARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 633 IgvdQPRDRAERI---LESGGVSLAVVCGGqrlSMPVPEVVLADI----LGGAPASTEITSA-------RVDPAALAYVL 698
Cdd:cd05923 83 I---NPRLKAAELaelIERGEMTAAVIAVD---AQVMDAIFQSGVrvlaLSDLVGLGEPESAgpliedpPREPEQPAFVF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 699 FTSGSTGEPKGVEVTHDAAMNTVEFIG-----RHfdiGPADRCLALSTLEGDISVMDVFV-TLRTGGSIVVVDEVqrrDP 772
Cdd:cd05923 157 YTSGTTGLPKGAVIPQRAAESRVLFMStqaglRH---GRHNVVLGLMPLYHVIGFFAVLVaALALDGTYVVVEEF---DP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 773 DAWARLIDAHQVTVLHFMPGWLEMLV---EVGRGRLSSVRVVPTGGDWVRPEVVRRLRVEAPGvRFAGLGGATETpvHNS 849
Cdd:cd05923 231 ADALKLIEQERVTSLFATPTHLDALAaaaEFAGLKLSSLRHVTFAGATMPDAVLERVNQHLPG-EKVNIYGTTEA--MNS 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 850 IFEvtePIPDDWTALPFGVPLPNNACRVVDDTGADCPDWVPGEYWVSGRGIA--RGYRGRPDLTAERFveHDGriWYRTG 927
Cdd:cd05923 308 LYM---RDARTGTEMRPGFFSEVRIVRIGGSPDEALANGEEGELIVAAAADAafTGYLNQPEATAKKL--QDG--WYRTG 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 928 DLVRYWPDGTLEFVGRADHRVKISGYRVELGEVETALRRVPGVRTAVAALIAVSGESDVLAAQVCADDASVTAEGIRQ-- 1005
Cdd:cd05923 381 DVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREGTLSADELDQfc 460
|
490 500 510
....*....|....*....|....*....|....*..
gi 497641516 1006 ---ALADLvpahMIPRHITVVERIGFTDAGKLDRRAV 1039
Cdd:cd05923 461 rasELADF----KRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
578-1039 |
4.17e-32 |
|
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: 131.18 E-value: 4.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 578 DLSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIGVDQPRDRAERILESGGVSLAVVc 657
Cdd:cd05907 5 PITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFV- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 658 ggqrlsmpvpevvladilggapasteitsarVDPAALAYVLFTSGSTGEPKGVEVTHDAAMNTVEFIGRHFDIGPADRCL 737
Cdd:cd05907 84 -------------------------------EDPDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEGDRHL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 738 A---LSTLEGDIsvMDVFVTLRTGGSIVVV--DEVQRRD------------PDAWARLIDAHQVTVlhfMPGWLEMLVEv 800
Cdd:cd05907 133 SflpLAHVFERR--AGLYVPLLAGARIYFAssAETLLDDlsevrptvflavPRVWEKVYAAIKVKA---VPGLKRKLFD- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 801 gRGRLSSVRVVPTGGDWVRPEVVRrlrveapgvRFAGLG-------GATET-PVhnsifeVTEPIPDDWTALPFGVPLPN 872
Cdd:cd05907 207 -LAVGGRLRFAASGGAPLPAELLH---------FFRALGipvyegyGLTETsAV------VTLNPPGDNRIGTVGKPLPG 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 873 NACRVVDDtgadcpdwvpGEYWVSGRGIARGYRGRPDLTAERFVEhDGriWYRTGDLVRYWPDGTLEFVGRADHRVKIS- 951
Cdd:cd05907 271 VEVRIADD----------GEILVRGPNVMLGYYKNPEATAEALDA-DG--WLHTGDLGEIDEDGFLHITGRKKDLIITSg 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 952 GYRVELGEVETALRRVPGVRTAV---------AALI-----------AVSGESDVLAAQVCADDASVTAegIRQALADL- 1010
Cdd:cd05907 338 GKNISPEPIENALKASPLISQAVvigdgrpflVALIvpdpealeawaEEHGIAYTDVAELAANPAVRAE--IEAAVEAAn 415
|
490 500 510
....*....|....*....|....*....|....*..
gi 497641516 1011 --VPAHMIPRHITVVERIG------FTDAGKLDRRAV 1039
Cdd:cd05907 416 arLSRYEQIKKFLLLPEPFtiengeLTPTLKLKRPVI 452
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
568-1041 |
2.14e-31 |
|
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: 128.95 E-value: 2.14e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 568 DAPAVFASSGDLSYAQL-RDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIGVDQPRDRAERIL 646
Cdd:cd05941 1 DRIAIVDDGDSITYADLvARAARLANRLLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 647 ESGGVSLAVvcggqrlsmpvpevvladilggapasteitsarvDPAAlayVLFTSGSTGEPKGVEVTHDAAMNTVEFIGR 726
Cdd:cd05941 81 TDSEPSLVL----------------------------------DPAL---ILYTSGTTGRPKGVVLTHANLAANVRALVD 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 727 HFDIGPADR---CLALSTLEGDISVmdVFVTLRTGGSIVV-----VDEVQRRD-----------PDAWARLIDAHQvtvL 787
Cdd:cd05941 124 AWRWTEDDVllhVLPLHHVHGLVNA--LLCPLFAGASVEFlpkfdPKEVAISRlmpsitvfmgvPTIYTRLLQYYE---A 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 788 HFMPGWLEMLVEVGRGRL----SSVRVVPTGGDWVrpevvrrlrvEAPGVRFAGLGGATETPVHNSifevtEPIPDDWTA 863
Cdd:cd05941 199 HFTDPQFARAAAAERLRLmvsgSAALPVPTLEEWE----------AITGHTLLERYGMTEIGMALS-----NPLDGERRP 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 864 LPFGVPLPNNACRVVDDTGADC-PDWVPGEYWVSGRGIARGYRGRPDLTAERFVEhDGriWYRTGDLVRYWPDGTLEFVG 942
Cdd:cd05941 264 GTVGMPLPGVQARIVDEETGEPlPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTD-DG--WFKTGDLGVVDEDGYYWILG 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 943 R-ADHRVKISGYRVELGEVETALRRVPGVRTAvaaliAVSGESD------VLAAQVCADDA-SVTAEGIRQALADLVPAH 1014
Cdd:cd05941 341 RsSVDIIKSGGYKVSALEIERVLLAHPGVSEC-----AVIGVPDpdwgerVVAVVVLRAGAaALSLEELKEWAKQRLAPY 415
|
490 500
....*....|....*....|....*..
gi 497641516 1015 MIPRHITVVERIGFTDAGKLDRRAVAR 1041
Cdd:cd05941 416 KRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
548-1038 |
1.17e-30 |
|
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: 127.44 E-value: 1.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 548 AEPSGEALHDGffrqAEQRPDAPAVFASSGDLSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVG 627
Cdd:cd05920 14 DEPLGDLLARS----AARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 628 AV---YLPigvdqprdrAERILESGGVSlavvcggqRLSMPVPEVVLADILGGAPASTEITSARvDPAALAYVLFTSGST 704
Cdd:cd05920 90 AVpvlALP---------SHRRSELSAFC--------AHAEAVAYIVPDRHAGFDHRALARELAE-SIPEVALFLLSGGTT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 705 GEPKGVEVTHD----AAMNTVEFIGrhfdIGPADRCLALSTLEGD--ISVMDVFVTLRTGGSIVVVDEVqrrDPDAWARL 778
Cdd:cd05920 152 GTPKLIPRTHNdyayNVRASAEVCG----LDQDTVYLAVLPAAHNfpLACPGVLGTLLAGGRVVLAPDP---SPDAAFPL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 779 IDAHQVTVLHFMPG----WLEMLVEVGRGrLSSVRVVPTGGDWVRPEVVRRLRvEAPGVRFAGLGGATETPVHNSIFEvt 854
Cdd:cd05920 225 IEREGVTVTALVPAlvslWLDAAASRRAD-LSSLRLLQVGGARLSPALARRVP-PVLGCTLQQVFGMAEGLLNYTRLD-- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 855 epIPDDWTALPFGVPL-PNNACRVVDDTGADCPDWVPGEYWVSGRGIARGYRGRPDLTAERFVEhDGriWYRTGDLVRYW 933
Cdd:cd05920 301 --DPDEVIIHTQGRPMsPDDEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTP-DG--FYRTGDLVRRT 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 934 PDGTLEFVGRADHRVKISGYRVELGEVETALRRVPGVRTavAALIAVSGEsdVLAAQVCA----DDASVTAEGIRQALAD 1009
Cdd:cd05920 376 PDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHD--AAVVAMPDE--LLGERSCAfvvlRDPPPSAAQLRRFLRE 451
|
490 500 510
....*....|....*....|....*....|
gi 497641516 1010 L-VPAHMIPRHITVVERIGFTDAGKLDRRA 1038
Cdd:cd05920 452 RgLAAYKLPDRIEFVDSLPLTAVGKIDKKA 481
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
563-1038 |
1.29e-30 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 128.15 E-value: 1.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 563 AEQRPDAPAVFASSGDLSYAQLRDQALAVAA-ALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIgvdQPRDR 641
Cdd:PRK08314 20 ARRYPDKTAIVFYGRAISYRELLEEAERLAGyLQQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPV---NPMNR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 642 AER---ILESGGVSLAVVcgGQRL---------SMPVPEVVLADILGGAPASTEIT------------------------ 685
Cdd:PRK08314 97 EEElahYVTDSGARVAIV--GSELapkvapavgNLRLRHVIVAQYSDYLPAEPEIAvpawlraepplqalapggvvawke 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 686 ---------SARVDPAALAYVLFTSGSTGEPKGVEVTHDAAMNTVEFIGRHFDIGPADRCLA---LSTLEGDISVMDVfv 753
Cdd:PRK08314 175 alaaglappPHTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAvlpLFHVTGMVHSMNA-- 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 754 TLRTGGSIVVVdevQRRDPDAWARLIDAHQVTVLHFMPgwlEMLVE------VGRGRLSSVRVVpTGGDWVRPEVV-RRL 826
Cdd:PRK08314 253 PIYAGATVVLM---PRWDREAAARLIERYRVTHWTNIP---TMVVDflaspgLAERDLSSLRYI-GGGGAAMPEAVaERL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 827 RvEAPGVRFAGLGGATET--PVHnsifevTEPiPDDWTALPFGVPLPNNACRVVD-DTGADCPDWVPGEYWVSGRGIARG 903
Cdd:PRK08314 326 K-ELTGLDYVEGYGLTETmaQTH------SNP-PDRPKLQCLGIPTFGVDARVIDpETLEELPPGEVGEIVVHGPQVFKG 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 904 YRGRPDLTAERFVEHDGRIWYRTGDLVRYWPDGTLEFVGRADHRVKISGYRVELGEVETALRRVPGVRTA--VAALIAVS 981
Cdd:PRK08314 398 YWNRPEATAEAFIEIDGKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEAcvIATPDPRR 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 497641516 982 GESdVLAAQVCADDA--SVTAEGIRQALADLVPAHMIPRHITVVERIGFTDAGKLDRRA 1038
Cdd:PRK08314 478 GET-VKAVVVLRPEArgKTTEEEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQ 535
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
561-1045 |
3.02e-30 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 126.51 E-value: 3.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 561 RQAEQRPDAPAVFASSGDLSYAQLRDQALAVAAA-LRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIGVD--- 636
Cdd:PRK06839 10 KRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYlIYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRlte 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 637 -----QPRDRAERIL---ESGGVSLAVVCGGQRLSMPVPEVVLADILGGAPASTEITSARvDPAALAYvlfTSGSTGEPK 708
Cdd:PRK06839 90 nelifQLKDSGTTVLfveKTFQNMALSMQKVSYVQRVISITSLKEIEDRKIDNFVEKNES-ASFIICY---TSGTTGKPK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 709 GVEVTHDA----AMNTVEFIgrhfDIGPADRCLALSTLE--GDISVMdVFVTLRTGGSIVVVDevqRRDPDAWARLIDAH 782
Cdd:PRK06839 166 GAVLTQENmfwnALNNTFAI----DLTMHDRSIVLLPLFhiGGIGLF-AFPTLFAGGVIIVPR---KFEPTKALSMIEKH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 783 QVTVLHFMPGWLEMLVEV---GRGRLSSVRVVPTGGDWVRPEVVRRLrvEAPGVRFAGLGGATETPvhNSIFEVTEpipD 859
Cdd:PRK06839 238 KVTVVMGVPTIHQALINCskfETTNLQSVRWFYNGGAPCPEELMREF--IDRGFLFGQGFGMTETS--PTVFMLSE---E 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 860 DWTALP--FGVPLPNNACRVVDDTGADCPDWVPGEYWVSGRGIARGYRGRPDLTAERFveHDGriWYRTGDLVRYWPDGT 937
Cdd:PRK06839 311 DARRKVgsIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETI--QDG--WLCTGDLARVDEDGF 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 938 LEFVGRADHRVKISGYRVELGEVETALRRVPGVRTAvaaliAVSGESDV------LAAQVCADDASVTAEGIRQALADLV 1011
Cdd:PRK06839 387 VYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEV-----AVVGRQHVkwgeipIAFIVKKSSSVLIEKDVIEHCRLFL 461
|
490 500 510
....*....|....*....|....*....|....
gi 497641516 1012 PAHMIPRHITVVERIGFTDAGKLDRRAVARELES 1045
Cdd:PRK06839 462 AKYKIPKEIVFLKELPKNATGKIQKAQLVNQLKS 495
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
562-1047 |
8.42e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 124.92 E-value: 8.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 562 QAEQRPDAPAV--FASSGDLSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIGVDQPR 639
Cdd:PRK09088 4 HARLQPQRLAAvdLALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 640 DRAERILESGGVSLAVvcGGQRLSMPVPEVV-LADILGGAPASTEITSARVDPAALAYVLFTSGSTGEPKGVEVTHDAAM 718
Cdd:PRK09088 84 SELDALLQDAEPRLLL--GDDAVAAGRTDVEdLAAFIASADALEPADTPSIPPERVSLILFTSGTSGQPKGVMLSERNLQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 719 NTVEFIGRHFDIGPADRCLALSTLEGDIS-VMDVFVTLRTGGSIVVVDEVqrrDPDAWARLIDAHQVTVLHF--MPGWLE 795
Cdd:PRK09088 162 QTAHNFGVLGRVDAHSSFLCDAPMFHIIGlITSVRPVLAVGGSILVSNGF---EPKRTLGRLGDPALGITHYfcVPQMAQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 796 MLVE---VGRGRLSSVRVVPTGGdwvRPEVVRRLRVE-APGVRFAGLGGATETpvhNSIFEVT-EPIPDDWTALPFGVPL 870
Cdd:PRK09088 239 AFRAqpgFDAAALRHLTALFTGG---APHAAEDILGWlDDGIPMVDGFGMSEA---GTVFGMSvDCDVIRAKAGAAGIPT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 871 PNNACRVVDDTGADCPDWVPGEYWVSGRGIARGYRGRPDLTAERFvehDGRIWYRTGDLVRYWPDGTLEFVGRADHRVKI 950
Cdd:PRK09088 313 PTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAF---TGDGWFRTGDIARRDADGFFWVVDRKKDMFIS 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 951 SGYRVELGEVETALRRVPGVR-TAVAALI-AVSGESDVLAAqVCADDASVTAEGIRQALADLVPAHMIPRHITVVERIGF 1028
Cdd:PRK09088 390 GGENVYPAEIEAVLADHPGIReCAVVGMAdAQWGEVGYLAI-VPADGAPLDLERIRSHLSTRLAKYKVPKHLRLVDALPR 468
|
490
....*....|....*....
gi 497641516 1029 TDAGKLdRRAVARELESAV 1047
Cdd:PRK09088 469 TASGKL-QKARLRDALAAG 486
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
580-1038 |
1.32e-29 |
|
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: 124.67 E-value: 1.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 580 SYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIG-----------VDQPRDRA------ 642
Cdd:cd12119 27 TYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINprlfpeqiayiINHAEDRVvfvdrd 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 643 -----ERILESGGVSLAVVCGGQRLSMPVPEVVLA----DILGGAPASTEITsaRVDPAALAYVLFTSGSTGEPKGVEVT 713
Cdd:cd12119 107 flpllEAIAPRLPTVEHVVVMTDDAAMPEPAGVGVlayeELLAAESPEYDWP--DFDENTAAAICYTSGTTGNPKGVVYS 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 714 HDA----AMNTVEFIGrhfdigpadrcLALStlEGDiSVMDV------------FVTLRTGGSIVVVDevQRRDPDAWAR 777
Cdd:cd12119 185 HRSlvlhAMAALLTDG-----------LGLS--ESD-VVLPVvpmfhvnawglpYAAAMVGAKLVLPG--PYLDPASLAE 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 778 LIDAHQVTVLHFMPG-WLEMLVEVGR--GRLSSVRVVPTGGDWVRPEVVRRLrvEAPGVRFAGLGGATET-PVHNSIFev 853
Cdd:cd12119 249 LIEREGVTFAAGVPTvWQGLLDHLEAngRDLSSLRRVVIGGSAVPRSLIEAF--EERGVRVIHAWGMTETsPLGTVAR-- 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 854 tepIPDDWTALPF----------GVPLPNNACRVVDDTGADCPdWVP---GEYWVSGRGIARGYRGRPDLTAERFveHDG 920
Cdd:cd12119 325 ---PPSEHSNLSEdeqlalrakqGRPVPGVELRIVDDDGRELP-WDGkavGELQVRGPWVTKSYYKNDEESEALT--EDG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 921 riWYRTGDLVRYWPDGTLEFVGRADHRVKISG---YRVELgevETALRRVPGVRTavAALIAVS----GESDVLAAqVCA 993
Cdd:cd12119 399 --WLRTGDVATIDEDGYLTITDRSKDVIKSGGewiSSVEL---ENAIMAHPAVAE--AAVIGVPhpkwGERPLAVV-VLK 470
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 497641516 994 DDASVTAEGIRQALADLVPAHMIPRHITVVERIGFTDAGKLDRRA 1038
Cdd:cd12119 471 EGATVTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKA 515
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
561-1037 |
4.74e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 123.12 E-value: 4.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 561 RQAEQRPDAPAVFASSGDLSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIGVDQPRD 640
Cdd:PRK08316 19 RSARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 641 RAERILESGGVSLAVVCGGQR-------LSMPVPEVVLADILGGAPASTEITS--------------ARVDPAALAYVLF 699
Cdd:PRK08316 99 ELAYILDHSGARAFLVDPALAptaeaalALLPVDTLILSLVLGGREAPGGWLDfadwaeagsvaepdVELADDDLAQILY 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 700 TSGSTGEPKGVEVTHDAAMNtvEFIGrhfdigpadrCL-ALSTLEGDISV----------MDVFVT--LRTGGSIVVVDe 766
Cdd:PRK08316 179 TSGTESLPKGAMLTHRALIA--EYVS----------CIvAGDMSADDIPLhalplyhcaqLDVFLGpyLYVGATNVILD- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 767 vqRRDPDAWARLIDAHQVTVLhFMPG--WLEML--VEVGRGRLSSVRVVPTGGDWVRPEVVRRLRVEAPGVRFAGLGGAT 842
Cdd:PRK08316 246 --APDPELILRTIEAERITSF-FAPPtvWISLLrhPDFDTRDLSSLRKGYYGASIMPVEVLKELRERLPGLRFYNCYGQT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 843 E-TPVHnsifevTEPIPDDWTALP--FGVPLPNNACRVVDDTGADCPDWVPGEywVSGRG--IARGYRGRPDLTAERFve 917
Cdd:PRK08316 323 EiAPLA------TVLGPEEHLRRPgsAGRPVLNVETRVVDDDGNDVAPGEVGE--IVHRSpqLMLGYWDDPEKTAEAF-- 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 918 HDGriWYRTGDLVRYWPDGTLEFVGRADHRVKISGYRVELGEVETALRRVPGVrtAVAALIAVSGE---SDVLAAQVCAD 994
Cdd:PRK08316 393 RGG--WFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAV--AEVAVIGLPDPkwiEAVTAVVVPKA 468
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 497641516 995 DASVTAEGI----RQALAdlvpAHMIPRHITVVERIGFTDAGKLDRR 1037
Cdd:PRK08316 469 GATVTEDELiahcRARLA----GFKVPKRVIFVDELPRNPSGKILKR 511
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
579-1036 |
4.82e-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: 121.86 E-value: 4.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 579 LSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIGVDQPRDRAERILESGGVSLAVVCG 658
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 659 GQRlsmpvpevvladilggapasteitsARVDPAALAYvLFTSGSTGEPKGVEVTHDAAMNTVEFIGRHFDIGPADR--C 736
Cdd:cd05973 81 ANR-------------------------HKLDSDPFVM-MFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPEDSfwN 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 737 LA--------LSTLEGDISvMDVFVTLRTGGSIVvvdevqrrdPDAWaRLIDAHQVTVLHFMPGWLEMLVEVG------- 801
Cdd:cd05973 135 AAdpgwayglYYAITGPLA-LGHPTILLEGGFSV---------ESTW-RVIERLGVTNLAGSPTAYRLLMAAGaevparp 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 802 RGRLssvRVVPTGGDWVRPEVVRRLRveapgvrfAGLGgateTPVHNSI--FEVTEPIPDDWT------ALPFGVPLPNN 873
Cdd:cd05973 204 KGRL---RRVSSAGEPLTPEVIRWFD--------AALG----VPIHDHYgqTELGMVLANHHAlehpvhAGSAGRAMPGW 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 874 ACRVVDDTGADCPDWVPGEYWVSGRGIA----RGYRGRPDLTAerfvehDGRiWYRTGDLVRYWPDGTLEFVGRADHRVK 949
Cdd:cd05973 269 RVAVLDDDGDELGPGEPGRLAIDIANSPlmwfRGYQLPDTPAI------DGG-YYLTGDTVEFDPDGSFSFIGRADDVIT 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 950 ISGYRVELGEVETALRRVPGVrtAVAALIAVSGE--SDVLAAQVCADDASVTAEGIRQALADLV----PAHMIPRHITVV 1023
Cdd:cd05973 342 MSGYRIGPFDVESALIEHPAV--AEAAVIGVPDPerTEVVKAFVVLRGGHEGTPALADELQLHVkkrlSAHAYPRTIHFV 419
|
490
....*....|...
gi 497641516 1024 ERIGFTDAGKLDR 1036
Cdd:cd05973 420 DELPKTPSGKIQR 432
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
687-1043 |
2.60e-28 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 123.88 E-value: 2.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 687 ARVDPAALAYVLFTSGSTGEPKGVEVTHDAAMNTVEFIGRHFDIGPADRCLA---------------LSTLEGdISVmdV 751
Cdd:PRK08633 777 PTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSslpffhsfgltvtlwLPLLEG-IKV--V 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 752 FVTLRTGGSIVvvdevqrrdpdawARLIDAHQVTVLHFMPGWLEMLVEVGRGR---LSSVRVVPTGGDWVRPEVVRRLRv 828
Cdd:PRK08633 854 YHPDPTDALGI-------------AKLVAKHRATILLGTPTFLRLYLRNKKLHplmFASLRLVVAGAEKLKPEVADAFE- 919
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 829 EAPGVR-FAGLGgATET-PVhnsifeVTEPIPD----DWTALPF------GVPLPNNACRVVD-DTGADCPDWVPGEYWV 895
Cdd:PRK08633 920 EKFGIRiLEGYG-ATETsPV------ASVNLPDvlaaDFKRQTGskegsvGMPLPGVAVRIVDpETFEELPPGEDGLILI 992
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 896 SGRGIARGYRGRPDLTAERFVEHDGRIWYRTGDLVRYWPDGTLEFVGRADHRVKISGYRVELGEVETALRRVPGVRTAVA 975
Cdd:PRK08633 993 GGPQVMKGYLGDPEKTAEVIKDIDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKALGGEEVVF 1072
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497641516 976 ALIAVS----GESDVLAAQVCADDasvtAEGIRQALADL-VPAHMIPRHITVVERIGFTDAGKLDRRAvAREL 1043
Cdd:PRK08633 1073 AVTAVPdekkGEKLVVLHTCGAED----VEELKRAIKESgLPNLWKPSRYFKVEALPLLGSGKLDLKG-LKEL 1140
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
566-1039 |
5.08e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 120.09 E-value: 5.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 566 RPDAPAVFASSGDLSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIGVDQPRDRAERI 645
Cdd:PRK06188 25 YPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLDDHAYV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 646 LESGGVSLAVV---------------CGGQRLSMPVPEVVLA-DILGGA----PASTEITSARVDPAALAYvlfTSGSTG 705
Cdd:PRK06188 105 LEDAGISTLIVdpapfveralallarVPSLKHVLTLGPVPDGvDLLAAAakfgPAPLVAAALPPDIAGLAY---TGGTTG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 706 EPKGVEVTHDAAMNTVEFIGRHFDIGPADRCLALSTLEGDISVMdVFVTLRTGGSIVVVDEVqrrDPDAWARLIDAHQVT 785
Cdd:PRK06188 182 KPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSHAGGAF-FLPTLLRGGTVIVLAKF---DPAEVLRAIEEQRIT 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 786 VLHFMPGWLEMLVEVGRGR---LSSVRVVPTGGDWVRPEvvrRLR--VEAPGVRFAGLGGATETPVHNSIFEVTEPIPDD 860
Cdd:PRK06188 258 ATFLVPTMIYALLDHPDLRtrdLSSLETVYYGASPMSPV---RLAeaIERFGPIFAQYYGQTEAPMVITYLRKRDHDPDD 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 861 WTAL-PFGVPLPNNACRVVDDTGADCPDWVPGEYWVSGRGIARGYRGRPDLTAERFveHDGriWYRTGDLVRYWPDGTLE 939
Cdd:PRK06188 335 PKRLtSCGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAF--RDG--WLHTGDVAREDEDGFYY 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 940 FVGRADHRVKISGYRVELGEVETALRRVPGVrtAVAALIAVS----GESdVLAAQVCADDASVTAEGIRQALADLVPAHM 1015
Cdd:PRK06188 411 IVDRKKDMIVTGGFNVFPREVEDVLAEHPAV--AQVAVIGVPdekwGEA-VTAVVVLRPGAAVDAAELQAHVKERKGSVH 487
|
490 500
....*....|....*....|....
gi 497641516 1016 IPRHITVVERIGFTDAGKLDRRAV 1039
Cdd:PRK06188 488 APKQVDFVDSLPLTALGKPDKKAL 511
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
696-1037 |
1.18e-27 |
|
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: 115.94 E-value: 1.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 696 YVLFTSGSTGEPKGVEVTHD---------AAMNTVEFIGRHFDI-----GPADRCLALSTLEGDISVMDVFVTLRTGGSI 761
Cdd:cd05924 7 YILYTGGTTGMPKGVMWRQEdifrmlmggADFGTGEFTPSEDAHkaaaaAAGTVMFPAPPLMHGTGSWTAFGGLLGGQTV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 762 VVVDEvqRRDPDAWARLIDAHQVTVLHF------MPgWLEMLVEVGRGRLSSVRVVPTGGDWVRPEVVRRLRVEAPGVRF 835
Cdd:cd05924 87 VLPDD--RFDPEEVWRTIEKHKVTSMTIvgdamaRP-LIDALRDAGPYDLSSLFAISSGGALLSPEVKQGLLELVPNITL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 836 AGLGGATETpvHNSIFEVTEPIPDDwtALPFGVPLPNNAcrVVDDTGADCPDWVPGEYWVSGRG-IARGYRGRPDLTAER 914
Cdd:cd05924 164 VDAFGSSET--GFTGSGHSAGSGPE--TGPFTRANPDTV--VLDDDGRVVPPGSGGVGWIARRGhIPLGYYGDEAKTAET 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 915 FVEHDGRIWYRTGDLVRYWPDGTLEFVGRADHRVKISGYRVELGEVETALRRVPGVRTAVaaliaVSGESD-----VLAA 989
Cdd:cd05924 238 FPEVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVL-----VVGRPDerwgqEVVA 312
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 497641516 990 QVCADD-ASVTAEGIRQALADLVPAHMIPRHITVVERIGFTDAGKLDRR 1037
Cdd:cd05924 313 VVQLREgAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGKADYR 361
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
578-1043 |
2.85e-27 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 118.07 E-value: 2.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 578 DLSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPI----GVDQPRDRaeriLESGGVSL 653
Cdd:PRK04319 73 KYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLfeafMEEAVRDR----LEDSEAKV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 654 AVVCGGQRLSMPVPE------VVLADILGGAP------------ASTEITSARVDPAALAYVLFTSGSTGEPKGVEVTHD 715
Cdd:PRK04319 149 LITTPALLERKPADDlpslkhVLLVGEDVEEGpgtldfnalmeqASDEFDIEWTDREDGAILHYTSGSTGKPKGVLHVHN 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 716 aAMNTVEFIGRH-FDIGPADR--CLA-----LSTLEGdisvmdVFVTLRTGGSIVVVDEvqRRDPDAWARLIDAHQVTVL 787
Cdd:PRK04319 229 -AMLQHYQTGKYvLDLHEDDVywCTAdpgwvTGTSYG------IFAPWLNGATNVIDGG--RFSPERWYRILEDYKVTVW 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 788 HFMPGWLEMLVEVG-----RGRLSSVRVVPTGGDWVRPEVVRRlrveapGVRFAGLggatetpvhnsifevtePIPDDW- 861
Cdd:PRK04319 300 YTAPTAIRMLMGAGddlvkKYDLSSLRHILSVGEPLNPEVVRW------GMKVFGL-----------------PIHDNWw 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 862 ------------TALP-----FGVPLPNNACRVVDDTGADCPDWVPGEY-----WVSgrgIARGYRGRPDLTAERFVehD 919
Cdd:PRK04319 357 mtetggimianyPAMDikpgsMGKPLPGIEAAIVDDQGNELPPNRMGNLaikkgWPS---MMRGIWNNPEKYESYFA--G 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 920 GriWYRTGDLVRYWPDGTLEFVGRADHRVKISGYRVELGEVETALRRVPGVrtAVAALI----AVSGEsdVLAAQVCADD 995
Cdd:PRK04319 432 D--WYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAV--AEAGVIgkpdPVRGE--IIKAFVALRP 505
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 497641516 996 ASVTAEGIRQALADLV----PAHMIPRHITVVERIGFTDAGKLDRRAV-AREL 1043
Cdd:PRK04319 506 GYEPSEELKEEIRGFVkkglGAHAAPREIEFKDKLPKTRSGKIMRRVLkAWEL 558
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
697-1036 |
4.27e-27 |
|
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: 113.52 E-value: 4.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 697 VLFTSGSTGEPKGVEVTHD----AAMNTVEFIGrhfdIGPADRCLALSTLegdISVMDVFVTLRT---GGSIVVVDevqR 769
Cdd:cd17637 5 IIHTAAVAGRPRGAVLSHGnliaANLQLIHAMG----LTEADVYLNMLPL---FHIAGLNLALATfhaGGANVVME---K 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 770 RDPDAWARLIDAHQVTVLHFMPGWLEMLVEV---GRGRLSSVRVVpTGGDwvRPEVVRRLRVEAPGvRFAGLGGATETpv 846
Cdd:cd17637 75 FDPAEALELIEEEKVTLMGSFPPILSNLLDAaekSGVDLSSLRHV-LGLD--APETIQRFEETTGA-TFWSLYGQTET-- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 847 hnSIFEVTEPIPD-DWTAlpfGVPLPNNACRVVDDTGADCPDWVPGEYWVSGRGIARGYRGRPDLTAERFveHDGriWYR 925
Cdd:cd17637 149 --SGLVTLSPYRErPGSA---GRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTF--RNG--WHH 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 926 TGDLVRYWPDGTLEFVGRADHR--VKISGYRVELGEVETALRRVPGVRTAVaaLIAVS----GESdVLAAQVCADDASVT 999
Cdd:cd17637 220 TGDLGRFDEDGYLWYAGRKPEKelIKPGGENVYPAEVEKVILEHPAIAEVC--VIGVPdpkwGEG-IKAVCVLKPGATLT 296
|
330 340 350
....*....|....*....|....*....|....*..
gi 497641516 1000 AEGIRQALADLVPAHMIPRHITVVERIGFTDAGKLDR 1036
Cdd:cd17637 297 ADELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
555-978 |
9.48e-27 |
|
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: 115.80 E-value: 9.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 555 LHDGFFRQAEQRPDAPA-VFASSGD-LSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLP 632
Cdd:cd05904 7 LDSVSFLFASAHPSRPAlIDAATGRaLTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 633 IG-VDQPRDRAERILESG---------------GVSLAVVCGGQRLSMPVPEVVLADILGGAPASTEITSARvDPAALay 696
Cdd:cd05904 87 ANpLSTPAEIAKQVKDSGaklafttaelaeklaSLALPVVLLDSAEFDSLSFSDLLFEADEAEPPVVVIKQD-DVAAL-- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 697 vLFTSGSTGEPKGVEVTHD---AAMNTVEFiGRHFDIGPADRCLALSTLeGDISVMDVFV--TLRTGGSIVVvdeVQRRD 771
Cdd:cd05904 164 -LYSSGTTGRSKGVMLTHRnliAMVAQFVA-GEGSNSDSEDVFLCVLPM-FHIYGLSSFAlgLLRLGATVVV---MPRFD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 772 PDAWARLIDAHQVTVLHFMPGWLEMLV---EVGRGRLSSVRVVPTGGDWVRPEVVRRLRVEAPGVRFAGLGGATE-TPVH 847
Cdd:cd05904 238 LEELLAAIERYKVTHLPVVPPIVLALVkspIVDKYDLSSLRQIMSGAAPLGKELIEAFRAKFPNVDLGQGYGMTEsTGVV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 848 NSIFevtepiPDDWTALPF---GVPLPNNACRVVD-DTGADCPDWVPGEYWVSGRGIARGYRGRPDLTAERFVEhDGriW 923
Cdd:cd05904 318 AMCF------APEKDRAKYgsvGRLVPNVEAKIVDpETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDK-EG--W 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 497641516 924 YRTGDLVRYWPDGTLEFVGRADHRVKISGYRVELGEVETALRRVPGVrtAVAALI 978
Cdd:cd05904 389 LHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEI--LDAAVI 441
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
563-1053 |
2.23e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 115.23 E-value: 2.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 563 AEQRPDAPAVFASSGDLSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIGVDQPRDRA 642
Cdd:PRK06164 20 ARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 643 ERILESGGVSL------------------------------AVVCGG-QRLSMPVP--EVVLADILGGAPASTEITSArV 689
Cdd:PRK06164 100 AHILGRGRARWlvvwpgfkgidfaailaavppdalpplraiAVVDDAaDATPAPAPgaRVQLFALPDPAPPAAAGERA-A 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 690 DPAALAYVLFTSGSTGEPKGVEVTHDAAMNTVEFIGRHFDIGPADRCLALSTLEGDISVMDVFVTLRTGGSIVVVDEVqr 769
Cdd:PRK06164 179 DPDAGALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGFSTLLGALAGGAPLVCEPVF-- 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 770 rDPDAWARLIDAHQVTvlHFMpGWLEMLVEV-----GRGRLSSVRVV------PTGGDWVRpevvrrlRVEAPGVRFAGL 838
Cdd:PRK06164 257 -DAARTARALRRHRVT--HTF-GNDEMLRRIldtagERADFPSARLFgfasfaPALGELAA-------LARARGVPLTGL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 839 GGATETPVHNSIFEVTEPIPDDWtaLPFGVPL-PNNACRVVD-DTGADCPDWVPGEYWVSGRGIARGYRGRPDLTAERFV 916
Cdd:PRK06164 326 YGSSEVQALVALQPATDPVSVRI--EGGGRPAsPEARVRARDpQDGALLPDGESGEIEIRAPSLMRGYLDNPDATARALT 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 917 EhDGriWYRTGDLVRYWPDGTLEFVGRADHRVKISGYRVELGEVETALRRVPGVRTAVAALIAVSGESDVLAAQVCADDA 996
Cdd:PRK06164 404 D-DG--YFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGATRDGKTVPVAFVIPTDGA 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 497641516 997 SVTAEGIRQALADLVPAHMIPRHITVVERIGFTDA--GKLDRRAVARELESAVSQSQRP 1053
Cdd:PRK06164 481 SPDEAGLMAACREALAGFKVPARVQVVEAFPVTESanGAKIQKHRLREMAQARLAAERA 539
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
686-1035 |
2.47e-26 |
|
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: 114.35 E-value: 2.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 686 SARVDPAALAYVLFTSGSTGEPKGVEVTHDAAMNTVEFIGRHFDIGPADRClalstlegdISVMDVF----------VTL 755
Cdd:cd05909 141 VAPVQPDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVV---------FGALPFFhsfgltgclwLPL 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 756 RTGGSIVVvdEVQRRDPDAWARLIDAHQVTVL----HFMPGWLEmlvEVGRGRLSSVRVVPTGGDWVRPEvVRRLRVEAP 831
Cdd:cd05909 212 LSGIKVVF--HPNPLDYKKIPELIYDKKATILlgtpTFLRGYAR---AAHPEDFSSLRLVVAGAEKLKDT-LRQEFQEKF 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 832 GVRFAGLGGATET-PVhnsiFEVTEPIPDDwTALPFGVPLPNNACRVVD-DTGADCPDWVPGEYWVSGRGIARGYRGRPD 909
Cdd:cd05909 286 GIRILEGYGTTECsPV----ISVNTPQSPN-KEGTVGRPLPGMEVKIVSvETHEEVPIGEGGLLLVRGPNVMLGYLNEPE 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 910 LTAERFveHDGriWYRTGDLVRYWPDGTLEFVGRADHRVKISGYRVELGEVETALRRVPGVRTAVAAlIAVS----GESD 985
Cdd:cd05909 361 LTSFAF--GDG--WYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEILPEDNEVAV-VSVPdgrkGEKI 435
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 497641516 986 VLaaqvCADDASVTAEGIRQAL-ADLVPAHMIPRHITVVERIGFTDAGKLD 1035
Cdd:cd05909 436 VL----LTTTTDTDPSSLNDILkNAGISNLAKPSYIHQVEEIPLLGTGKPD 482
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
531-1043 |
2.62e-26 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 114.86 E-value: 2.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 531 ALPEAQRAVREAAngrtaePSGEALHDGFFRQAEQRPDAPAVFASSGDLSYAQLRDQALAVAAALRAAGVTAGDTIAVMG 610
Cdd:PRK06155 5 GAGLAARAVDPLP------PSERTLPAMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMC 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 611 PKTAEQIPALLGILSVGAVYLPIGVDQPRDRAERILESGGVSLAVV-CGGQRLSMPVPEVVLAD----ILGGAPAST--- 682
Cdd:PRK06155 79 GNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVVeAALLAALEAADPGDLPLpavwLLDAPASVSvpa 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 683 ------------EITSARVDPAALAYVLFTSGSTGEPKGVEVTHDA----AMNTVEFIGrhfdIGPAD---RCLALStle 743
Cdd:PRK06155 159 gwstaplppldaPAPAAAVQPGDTAAILYTSGTTGPSKGVCCPHAQfywwGRNSAEDLE----IGADDvlyTTLPLF--- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 744 gDISVMDVFVTLRTGGSIVVVDEvQRRDPDAWARLIdAHQVTVLHFMPGWLEMLV---EVGRGRLSSVRVVPTGGdwVRP 820
Cdd:PRK06155 232 -HTNALNAFFQALLAGATYVLEP-RFSASGFWPAVR-RHGATVTYLLGAMVSILLsqpARESDRAHRVRVALGPG--VPA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 821 EVVRRLRvEAPGVRFAGLGGATETpvhNSIFEVTEPIPDDWTAlpfGVPLPNNACRVVDDTGADCPDWVPGEYWVSGR-- 898
Cdd:PRK06155 307 ALHAAFR-ERFGVDLLDGYGSTET---NFVIAVTHGSQRPGSM---GRLAPGFEARVVDEHDQELPDGEPGELLLRADep 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 899 -GIARGYRGRPDLTaerfVEHDGRIWYRTGDLVRYWPDGTLEFVGRADHRVKISGYRVELGEVETALRRVPGVrtAVAAL 977
Cdd:PRK06155 380 fAFATGYFGMPEKT----VEAWRNLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAV--AAAAV 453
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 978 IAVS---GESDVLAAQVCADDASVT-AEGIRQALADLvPAHMIPRHITVVERIGFTDAGKLdRRAVAREL 1043
Cdd:PRK06155 454 FPVPselGEDEVMAAVVLRDGTALEpVALVRHCEPRL-AYFAVPRYVEFVAALPKTENGKV-QKFVLREQ 521
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
552-1043 |
5.32e-26 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 114.07 E-value: 5.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 552 GEA-LHDGFFRQAEQRPDAPAVFASSG-DLSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAV 629
Cdd:PRK06087 21 GDAsLADYWQQTARAMPDKIAVVDNHGaSYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 630 YLPIGVDQPRDRAERILESGGVSLAVVCGGQRLSMPVPE-------------VVLADILggAPASTEITSARV------- 689
Cdd:PRK06087 101 SVPLLPSWREAELVWVLNKCQAKMFFAPTLFKQTRPVDLilplqnqlpqlqqIVGVDKL--APATSSLSLSQIiadyepl 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 690 --DPAA----LAYVLFTSGSTGEPKGVEVTHdaamNTVEFIGRHF---------DI--GPADRCLALSTLEGDISVMDVf 752
Cdd:PRK06087 179 ttAITThgdeLAAVLFTSGTEGLPKGVMLTH----NNILASERAYcarlnltwqDVfmMPAPLGHATGFLHGVTAPFLI- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 753 vtlrtGGSIVVVDevqRRDPDAWARLIDAHQVT-VLHFMPGWLEML--VEVGRGRLSSVRVVPTGGDWVRPEVVRrlRVE 829
Cdd:PRK06087 254 -----GARSVLLD---IFTPDACLALLEQQRCTcMLGATPFIYDLLnlLEKQPADLSALRFFLCGGTTIPKKVAR--ECQ 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 830 APGVRFAGLGGATETPVHnSIFEVTEPIPddWTALPFGVPLPNNACRVVDDTGADCPDWVPGEYWVSGRGIARGYRGRPD 909
Cdd:PRK06087 324 QRGIKLLSVYGSTESSPH-AVVNLDDPLS--RFMHTDGYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 910 LTAeRFVEHDGriWYRTGDLVRYWPDGTLEFVGRADHRVKISGYRVELGEVETALRRVPGVRTavAALIAVSGESdvLAA 989
Cdd:PRK06087 401 LTA-RALDEEG--WYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHD--ACVVAMPDER--LGE 473
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497641516 990 QVCAdDASVTAEGIRQALADL--------VPAHMIPRHITVVERIGFTDAGKLDRRAVAREL 1043
Cdd:PRK06087 474 RSCA-YVVLKAPHHSLTLEEVvaffsrkrVAKYKYPEHIVVIDKLPRTASGKIQKFLLRKDI 534
|
|
| ArgR-Cyc_NRPS-like |
cd20480 |
Cyc (heterocyclization)-like domain of Vibrio anguillarum AngR and similar proteins; belongs ... |
116-521 |
7.64e-26 |
|
Cyc (heterocyclization)-like domain of Vibrio anguillarum AngR and similar proteins; belongs to the Condensation-domain family; Vibrio anguillarum AngR plays a role in regulating the expression of iron transport genes as well as in the production of the siderophore anguibactin. Cyc-domains are a type of Condensation (C) domain. Cyc-domains catalyze two separate reactions in the creation of heterocyclized peptide products in nonribosomal peptide synthesis: amide bond formation followed by intramolecular cyclodehydration between a Cys, Ser, or Thr side chain and a carbonyl carbon on the peptide backbone to form a thiazoline, oxazoline, or methyloxazoline ring. C-domains typically have a conserved HHxxxD motif at the active site; Cyc-domains have a alternative, conserved DxxxxD active site motif, mutation of the aspartate residues in this motif can abolish or diminish condensation activity. Members of this subfamily have an SxxxD motif at the active site. C-domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to Cyc-domains there are various other subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380470 [Multi-domain] Cd Length: 406 Bit Score: 111.44 E-value: 7.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 116 RQENQqlgGVAGHLYVEFDGGGIDPERLRAAATALARRHPMLRVRFLPDGTQRIAPADEFGPFPVHveDLRERSTGEADR 195
Cdd:cd20480 18 RSEQQ---SIANFIYQEFDYENISVDTLERCLTVLINHHPMLHALLSDDFYLHINSKNQIDAFAVN--DLSSASEQEAAE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 196 RLAAIRAAKSHQQlDGAVFELAVTLLPAERSRLHVDLDMQAADAMSYRTLMADLAALYLGRDLPELGYTYRQYRHAIEAE 275
Cdd:cd20480 93 QLARTRATLTKSR-SKATISVVLSLLPANKIRLHVRFNSVVVDHPSVNLFFEQLCQLLRGSLLSFLAQEQVILAHNQLVI 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 276 DARPQParDADRAWWARRLPELPDPPALPT---------TG--GRAENQSTRRWHwldphtrdALFARAQARGFTPAMAL 344
Cdd:cd20480 172 SELQST--GLSSAFWNEQILQLPSSANLPTvcepeklreTGitRRTLTLSSDKWQ--------QLVTISKQHNVTPELTL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 345 AAGFANTLARWSTTSRFLLnvplfgRQALHP--DVDSLVGDFTSSLLLDVDlTRANTAAARAQVVQDAMRTAAAHSAYPG 422
Cdd:cd20480 242 ASIFSAVLSLWGNQKDMML------RFDLNKknDVAGVIGQFTQPLLVGLS-GFGQSFLSLVKENQKHFEQAYPFRQIPI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 423 LAVLRDLSR----HRGTqvlAPVVFTSALglgelfssDVTGQFGTPGWIISQGPQVLLDAQVTEFDGGVLVNWDVREGVF 498
Cdd:cd20480 315 FDLVRQLAKlsesHRYP---ANIAFSSQL--------SGNNTLGRSGWGCRQSANTWLSLHAFISQGGLILQWDSQDALF 383
|
410 420
....*....|....*....|...
gi 497641516 499 PAGVIDAMFAHHIDELLRLASAD 521
Cdd:cd20480 384 PKDMIQDMLTSYSKLLESLSQSD 406
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
552-1034 |
1.31e-25 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 112.84 E-value: 1.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 552 GEALHDGFFRQAEQRPDAPAVFASSGD------LSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILS 625
Cdd:PRK13295 23 DRTINDDLDACVASCPDKTAVTAVRLGtgaprrFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 626 VGAVYLPIgvdQP--RDRAER-ILESGGVSLAVV----------CGGQRLSMPVPEVVLADILGG--------------- 677
Cdd:PRK13295 103 IGAVLNPL---MPifRERELSfMLKHAESKVLVVpktfrgfdhaAMARRLRPELPALRHVVVVGGdgadsfeallitpaw 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 678 --APASTEI-TSARVDPAALAYVLFTSGSTGEPKGVEVTHDAAM-NTVEFIGRhFDIGPADRCLALST---LEGDISVMD 750
Cdd:PRK13295 180 eqEPDAPAIlARLRPGPDDVTQLIYTSGTTGEPKGVMHTANTLMaNIVPYAER-LGLGADDVILMASPmahQTGFMYGLM 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 751 VFVTLrtgGSIVVVDEVQrrDPDAWARLIDAHQVTvlhFM----PGWLEML--VEVGRGRLSSVRVVPTGGDWVRPEVVR 824
Cdd:PRK13295 259 MPVML---GATAVLQDIW--DPARAAELIRTEGVT---FTmastPFLTDLTraVKESGRPVSSLRTFLCAGAPIPGALVE 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 825 RLRvEAPGVRFAGLGGATEtpvhNSIFEVTEP-IPDDWTALPFGVPLPNNACRVVDDTGADCPDWVPGEYWVSGRGIARG 903
Cdd:PRK13295 331 RAR-AALGAKIVSAWGMTE----NGAVTLTKLdDPDERASTTDGCPLPGVEVRVVDADGAPLPAGQIGRLQVRGCSNFGG 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 904 YRGRPDLTAerfveHDGRIWYRTGDLVRYWPDGTLEFVGRADHRVKISGYRVELGEVETALRRVPGVrtAVAALIAVSGE 983
Cdd:PRK13295 406 YLKRPQLNG-----TDADGWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAI--AQVAIVAYPDE 478
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 497641516 984 SdvLAAQVCA-----DDASVTAEGIRQAL-ADLVPAHMIPRHITVVERIGFTDAGKL 1034
Cdd:PRK13295 479 R--LGERACAfvvprPGQSLDFEEMVEFLkAQKVAKQYIPERLVVRDALPRTPSGKI 533
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
546-978 |
1.55e-25 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 113.27 E-value: 1.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 546 RTAEPSGEALHDGFFRQAEQRPDAPAVFASSG----DLSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALL 621
Cdd:COG1022 4 FSDVPPADTLPDLLRRRAARFPDRVALREKEDgiwqSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 622 GILSVGAVYLPIGVDQPRDRAERILESGGVSLAVVcGGQRL---------SMP-VPEVVLADILGGAPASTEIT------ 685
Cdd:COG1022 84 AILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFV-EDQEQldkllevrdELPsLRHIVVLDPRGLRDDPRLLSldella 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 686 --------------SARVDPAALAYVLFTSGSTGEPKGVEVTHDAAMNTVEFIGRHFDIGPADRCLA------------- 738
Cdd:COG1022 163 lgrevadpaelearRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSflplahvfertvs 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 739 ---------------LSTLEGD---------ISVMDVFVTLRTGgsivVVDEVQRRDP-------------DAWARLIDA 781
Cdd:COG1022 243 yyalaagatvafaesPDTLAEDlrevkptfmLAVPRVWEKVYAG----IQAKAEEAGGlkrklfrwalavgRRYARARLA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 782 HQVtvlhfMPGWLEMLVEVG--------RGRL-SSVRVVPTGGDWVRPEVVRrlrveapgvRFAGLG-------GATET- 844
Cdd:COG1022 319 GKS-----PSLLLRLKHALAdklvfsklREALgGRLRFAVSGGAALGPELAR---------FFRALGipvlegyGLTETs 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 845 PVhNSIFEVTEPIPDdwTAlpfGVPLPNNACRVVDDtgadcpdwvpGEYWVSGRGIARGYRGRPDLTAERFVEhDGriWY 924
Cdd:COG1022 385 PV-ITVNRPGDNRIG--TV---GPPLPGVEVKIAED----------GEILVRGPNVMKGYYKNPEATAEAFDA-DG--WL 445
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497641516 925 RTGDLVRYWPDGTLEFVGRADHRVKIS-GYRVELGEVETALRRVPGVRTAV---------AALI 978
Cdd:COG1022 446 HTGDIGELDEDGFLRITGRKKDLIVTSgGKNVAPQPIENALKASPLIEQAVvvgdgrpflAALI 509
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
699-1036 |
1.91e-25 |
|
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: 109.29 E-value: 1.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 699 FTSGSTGEPKGVEVTHDAAMNTVEFIGRHFDIGPADR-CLALSTLEGDISVMDVFVTLRTGGSIVVVDEVqrRDPDAWAR 777
Cdd:cd05917 9 FTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRlCIPVPLFHCFGSVLGVLACLTHGATMVFPSPS--FDPLAVLE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 778 LIDAHQVTVLHFMPgwlEMLV-EVGRGR-----LSSVRVVPTGGDWVRPEVVRRLrVEAPGVRFAGLG-GATET-PVhNS 849
Cdd:cd05917 87 AIEKEKCTALHGVP---TMFIaELEHPDfdkfdLSSLRTGIMAGAPCPPELMKRV-IEVMNMKDVTIAyGMTETsPV-ST 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 850 IFEVTEPIPDDWTALpfGVPLPNNACRVVD-DTGADCPDWVPGEYWVSGRGIARGYRGRPDLTAErfvEHDGRIWYRTGD 928
Cdd:cd05917 162 QTRTDDSIEKRVNTV--GRIMPHTEAKIVDpEGGIVPPVGVPGELCIRGYSVMKGYWNDPEKTAE---AIDGDGWLHTGD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 929 LVRYWPDGTLEFVGRADHRVKISGYRVELGEVETALRRVPGVrtAVAALIAVsgESDVLAAQVCA-----DDASVTAEGI 1003
Cdd:cd05917 237 LAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKV--SDVQVVGV--PDERYGEEVCAwirlkEGAELTEEDI 312
|
330 340 350
....*....|....*....|....*....|...
gi 497641516 1004 RQALADLVPAHMIPRHITVVERIGFTDAGKLDR 1036
Cdd:cd05917 313 KAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQK 345
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
567-1037 |
2.76e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 111.90 E-value: 2.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 567 PDAPAVFASSGDLSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVylPIGV----------- 635
Cdd:PRK07798 17 PDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAV--PVNVnyryvedelry 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 636 -------------DQPRDRAERILES-GGVSLAVVCGGQRLSMPVPEVV-LADILGGAPAsteitsARVDPAALA---YV 697
Cdd:PRK07798 95 llddsdavalvyeREFAPRVAEVLPRlPKLRTLVVVEDGSGNDLLPGAVdYEDALAAGSP------ERDFGERSPddlYL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 698 LFTSGSTGEPKGVEVTHD----AAMN-----TVEFIGRHFDI------GPADRCLALSTLEGDISVMDVFVTLRTGGSIV 762
Cdd:PRK07798 169 LYTGGTTGMPKGVMWRQEdifrVLLGgrdfaTGEPIEDEEELakraaaGPGMRRFPAPPLMHGAGQWAAFAALFSGQTVV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 763 VVDeVQRRDPDAWARLIDAHQVTVLhFMPG------WLEMLVEVGRGRLSSVRVVPTGGDWVRPEVVRRLRVEAPGVRFA 836
Cdd:PRK07798 249 LLP-DVRFDADEVWRTIEREKVNVI-TIVGdamarpLLDALEARGPYDLSSLFAIASGGALFSPSVKEALLELLPNVVLT 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 837 GLGGATETPVHNSIFEVTEPIPDDwtALPFGvplPNNACRVVDDTGADCPDWVPGEYWVSGRG-IARGYRGRPDLTAERF 915
Cdd:PRK07798 327 DSIGSSETGFGGSGTVAKGAVHTG--GPRFT---IGPRTVVLDEDGNPVEPGSGEIGWIARRGhIPLGYYKDPEKTAETF 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 916 VEHDGRIWYRTGDLVRYWPDGTLEFVGRADHRVKISGYRVELGEVETALRRVPGVRTAVaaliaVSGESD------VLAA 989
Cdd:PRK07798 402 PTIDGVRYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADAL-----VVGVPDerwgqeVVAV 476
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 497641516 990 QVCADDASVTAEGIRQALADLVPAHMIPRHITVVERIGFTDAGKLDRR 1037
Cdd:PRK07798 477 VQLREGARPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGKADYR 524
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
693-1041 |
3.31e-25 |
|
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: 107.80 E-value: 3.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 693 ALAYVLFTSGSTGEPKGVEVTHDAAMNTVEFIGRHFDIGPADRCLaLSTLEGDIS-VMDVFVTLRTGGSIVVVDEvqrrd 771
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWL-LSLPLYHVGgLAILVRSLLAGAELVLLER----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 772 pdAWARLIDAHQ--VTVLHFMPGWLEMLVE--VGRGRLSSVRVVPTGGDWVRPEVVRRLrvEAPGVRFAGLGGATETPVH 847
Cdd:cd17630 75 --NQALAEDLAPpgVTHVSLVPTQLQRLLDsgQGPAALKSLRAVLLGGAPIPPELLERA--ADRGIPLYTTYGMTETASQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 848 nsifeVTEPIPDDWTALPFGVPLPNNACRVVDDtgadcpdwvpGEYWVSGRGIARGYR--GRPDLTAErfvehDGriWYR 925
Cdd:cd17630 151 -----VATKRPDGFGRGGVGVLLPGRELRIVED----------GEIWVGGASLAMGYLrgQLVPEFNE-----DG--WFT 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 926 TGDLVRYWPDGTLEFVGRADHRVKISGYRVELGEVETALRRVPGVRTAVaaliaVSGESD-----VLAAQVCADDASVTA 1000
Cdd:cd17630 209 TKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAF-----VVGVPDeelgqRPVAVIVGRGPADPA 283
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 497641516 1001 EgIRQALADLVPAHMIPRHITVVERIGFTDAGKLDRRAVAR 1041
Cdd:cd17630 284 E-LRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRA 323
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
561-1042 |
3.33e-25 |
|
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: 111.43 E-value: 3.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 561 RQAEQRPDAPAV-----FASSGDLSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLP--- 632
Cdd:cd05970 25 AMAKEYPDKLALvwcddAGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPath 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 633 ------------------IGVDQPRDRAERI----LESGGVSLAVVCGGqrlsmPVPE------VVLADILGGAPASTEI 684
Cdd:cd05970 105 qltakdivyriesadikmIVAIAEDNIPEEIekaaPECPSKPKLVWVGD-----PVPEgwidfrKLIKNASPDFERPTAN 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 685 TSARVDPAALAYvlFTSGSTGEPKGVEvtHDAAMNTVEFIGRHF--DIGPADRCLALSTLEGDISVMDVFVTLRTGGSIV 762
Cdd:cd05970 180 SYPCGEDILLVY--FSSGTTGMPKMVE--HDFTYPLGHIVTAKYwqNVREGGLHLTVADTGWGKAVWGKIYGQWIAGAAV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 763 VVDEVQRRDPDAWARLIDAHQVTVLHFMPGWLEMLV--EVGRGRLSSVRVVPTGGDWVRPEVVRRLRvEAPGVRFAGLGG 840
Cdd:cd05970 256 FVYDYDKFDPKALLEKLSKYGVTTFCAPPTIYRFLIreDLSRYDLSSLRYCTTAGEALNPEVFNTFK-EKTGIKLMEGFG 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 841 ATETPVHNSIFEVTEPIPDDwtalpFGVPLPNNACRVVDDTGADCPDWVPGEYWV---SGR--GIARGYRGRPDLTAERF 915
Cdd:cd05970 335 QTETTLTIATFPWMEPKPGS-----MGKPAPGYEIDLIDREGRSCEAGEEGEIVIrtsKGKpvGLFGGYYKDAEKTAEVW 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 916 veHDGriWYRTGDLVRYWPDGTLEFVGRADHRVKISGYRVELGEVETALRRVPGVRTAvaaliAVSGESDVLAAQVCADD 995
Cdd:cd05970 410 --HDG--YYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLEC-----AVTGVPDPIRGQVVKAT 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 497641516 996 ASVTA-----EGIRQALADLV----PAHMIPRHITVVERIGFTDAGKLdRRAVARE 1042
Cdd:cd05970 481 IVLAKgyepsEELKKELQDHVkkvtAPYKYPRIVEFVDELPKTISGKI-RRVEIRE 535
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
566-1039 |
4.85e-25 |
|
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: 111.81 E-value: 4.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 566 RPDAPAVF-----ASSGDLSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPI----GVD 636
Cdd:cd05968 74 TRTRPALRwegedGTSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIfsgfGKE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 637 QPRDR-----AERILESGG-------VSLAVVCGGQRLSMPVPEVVLADILGGAP---------------ASTEITSARV 689
Cdd:cd05968 154 AAATRlqdaeAKALITADGftrrgreVNLKEEADKACAQCPTVEKVVVVRHLGNDftpakgrdlsydeekETAGDGAERT 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 690 DPAALAYVLFTSGSTGEPKGVEVTH-----DAAMNtvefIGRHFDIGPADRCLALSTLEGDISVMDVFVTLRTGGSIVVV 764
Cdd:cd05968 234 ESEDPLMIIYTSGTTGKPKGTVHVHagfplKAAQD----MYFQFDLKPGDLLTWFTDLGWMMGPWLIFGGLILGATMVLY 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 765 DEV-QRRDPDAWARLIDAHQVTVLHFMPGWLEMLV-----EVGRGRLSSVRVVPTGGDWVRPE-----VVRRLRVEAPGV 833
Cdd:cd05968 310 DGApDHPKADRLWRMVEDHEITHLGLSPTLIRALKprgdaPVNAHDLSSLRVLGSTGEPWNPEpwnwlFETVGKGRNPII 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 834 RFAGlggatETPVHNSIF--EVTEPIpddwTALPFGVPLPNNACRVVDDTGADCPDWVpGEY-----WVsgrGIARGYRG 906
Cdd:cd05968 390 NYSG-----GTEISGGILgnVLIKPI----KPSSFNGPVPGMKADVLDESGKPARPEV-GELvllapWP---GMTRGFWR 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 907 RPDLTAERFVEHDGRIWYRtGDLVRYWPDGTLEFVGRADHRVKISGYRVELGEVETALRRVPGVRTAVAALIA--VSGES 984
Cdd:cd05968 457 DEDRYLETYWSRFDNVWVH-GDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPhpVKGEA 535
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 497641516 985 DVLAAqVCADDASVTaEGIRQALADLVPAHM----IPRHITVVERIGFTDAGKLDRRAV 1039
Cdd:cd05968 536 IVCFV-VLKPGVTPT-EALAEELMERVADELgkplSPERILFVKDLPKTRNAKVMRRVI 592
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
568-1042 |
8.16e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 109.69 E-value: 8.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 568 DAPAVFASSGDLSYAQLRDqalavAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIGVDQ-PRDRAERIL 646
Cdd:PRK07787 15 IADAVRIGGRVLSRSDLAG-----AATAVAERVAGARRVAVLATPTLATVLAVVGALIAGVPVVPVPPDSgVAERRHILA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 647 ESGGVSLAVVCGGQRLSMPVPEVVLAdilggapASTEITSARVDPAALAYVLFTSGSTGEPKGVEVTHDAAMNTVEFIGR 726
Cdd:PRK07787 90 DSGAQAWLGPAPDDPAGLPHVPVRLH-------ARSWHRYPEPDPDAPALIVYTSGTTGPPKGVVLSRRAIAADLDALAE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 727 HFDIGPAD---RCLALSTLEGdiSVMDVFVTLRTGGSIVvvdEVQRRDPDAWARLIDAHQvTVLHFMPGWLEMLVEVGR- 802
Cdd:PRK07787 163 AWQWTADDvlvHGLPLFHVHG--LVLGVLGPLRIGNRFV---HTGRPTPEAYAQALSEGG-TLYFGVPTVWSRIAADPEa 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 803 -GRLSSVRVVPTGGDWVRPEVVRRLRvEAPGVRFAGLGGATETPVHNSIFEVTEPIPDdWTalpfGVPLPNNACRVVDDT 881
Cdd:PRK07787 237 aRALRGARLLVSGSAALPVPVFDRLA-ALTGHRPVERYGMTETLITLSTRADGERRPG-WV----GLPLAGVETRLVDED 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 882 GADCP--DWVPGEYWVSGRGIARGYRGRPDLTAERFVEhDGriWYRTGDLVRYWPDGTLEFVGR-ADHRVKISGYRVELG 958
Cdd:PRK07787 311 GGPVPhdGETVGELQVRGPTLFDGYLNRPDATAAAFTA-DG--WFRTGDVAVVDPDGMHRIVGReSTDLIKSGGYRIGAG 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 959 EVETALRRVPGVRTAvaaliAVSGESD------VLAAQVCADDasVTAEGIRQALADLVPAHMIPRHITVVERIGFTDAG 1032
Cdd:PRK07787 388 EIETALLGHPGVREA-----AVVGVPDddlgqrIVAYVVGADD--VAADELIDFVAQQLSVHKRPREVRFVDALPRNAMG 460
|
490
....*....|
gi 497641516 1033 KLDRRAVARE 1042
Cdd:PRK07787 461 KVLKKQLLSE 470
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
579-1043 |
8.69e-25 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 110.48 E-value: 8.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 579 LSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAV----YLPIG-------VDQPRdraeRILE 647
Cdd:PRK09192 50 LPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVpvplPLPMGfggresyIAQLR----GMLA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 648 SGGVSLAVvcGGQRLSMPVPEVVLAD--ILGGAPASTEITSA------RVDPAALAYVLFTSGSTGEPKGVEVTHDAAMN 719
Cdd:PRK09192 126 SAQPAAII--TPDELLPWVNEATHGNplLHVLSHAWFKALPEadvalpRPTPDDIAYLQYSSGSTRFPRGVIITHRALMA 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 720 TVEFIGRH-FDIGPADRCLALSTLEGDISVMDVFVTLRTggSIVVVDEVQRRD----PDAWARLIDAHQVTVLHFMPGWL 794
Cdd:PRK09192 204 NLRAISHDgLKVRPGDRCVSWLPFYHDMGLVGFLLTPVA--TQLSVDYLPTRDfarrPLQWLDLISRNRGTISYSPPFGY 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 795 EMLVEVGRGR------LSSVRVVPTGGDWVRPEVVRRLrVEAPG---------------------VRFAGLGGA--TETp 845
Cdd:PRK09192 282 ELCARRVNSKdlaeldLSCWRVAGIGADMIRPDVLHQF-AEAFApagfddkafmpsyglaeatlaVSFSPLGSGivVEE- 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 846 VHNSIFE---VTEPIPDDWTAL-PF---GVPLPNNACRVVDDTGADCPDWVPGEYWVSGRGIARGYRGRPDltAERFVEH 918
Cdd:PRK09192 360 VDRDRLEyqgKAVAPGAETRRVrTFvncGKALPGHEIEIRNEAGMPLPERVVGHICVRGPSLMSGYFRDEE--SQDVLAA 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 919 DGriWYRTGDLvRYWPDGTLEFVGRADHRVKISGYRVELGEVETALRRVPGVRTAVAALIAVSGESDV-LAAQV-CADDA 996
Cdd:PRK09192 438 DG--WLDTGDL-GYLLDGYLYITGRAKDLIIINGRNIWPQDIEWIAEQEPELRSGDAAAFSIAQENGEkIVLLVqCRISD 514
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 997 SVTAEGIRQALA-------------DLVPAHMIPRhitvverigfTDAGKLDrRAVAREL 1043
Cdd:PRK09192 515 EERRGQLIHALAalvrsefgveaavELVPPHSLPR----------TSSGKLS-RAKAKKR 563
|
|
| Condensation |
pfam00668 |
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ... |
105-519 |
1.45e-24 |
|
Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.
Pssm-ID: 395541 [Multi-domain] Cd Length: 454 Bit Score: 108.57 E-value: 1.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 105 LAPMQHAMWVgrqeNQQLGGVAGH----LYVEFDGGgIDPERLRAAATALARRHPMLRVRFLPDGT----QRIAPADefg 176
Cdd:pfam00668 7 LSPAQKRMWF----LEKLEPHSSAynmpAVLKLTGE-LDPERLEKALQELINRHDALRTVFIRQENgepvQVILEER--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 177 PFPVHVEDLRERSTGEADRRLAAI--RAAKSHQQLDGAVFeLAVTLLPAERSRLHVDLDMQ--AADAMSYRTLMADLAAL 252
Cdd:pfam00668 79 PFELEIIDISDLSESEEEEAIEAFiqRDLQSPFDLEKGPL-FRAGLFRIAENRHHLLLSMHhiIVDGVSLGILLRDLADL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 253 YL----GRDLPELGYT-YRQYrhAIEAEDARPQPARDADRAWWARRLPELPDPPALPTTGGRAENQS------TRRwhwL 321
Cdd:pfam00668 158 YQqllkGEPLPLPPKTpYKDY--AEWLQQYLQSEDYQKDAAYWLEQLEGELPVLQLPKDYARPADRSfkgdrlSFT---L 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 322 DPHTRDALFARAQARGFTPAMALAAGFANTLARWSTTSRFLLNVPLFGRqaLHPDVDSLVGDFTSSLLLDVDLTRANTAA 401
Cdd:pfam00668 233 DEDTEELLRKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGR--PSPDIERMVGMFVNTLPLRIDPKGGKTFS 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 402 ARAQVVQDAMRTAAAHSAYPgLAVLRDLSRHRGTQVLAP-----VVFTSALGLG---ELFSSDvTGQFGTPGWIISQGPQ 473
Cdd:pfam00668 311 ELIKRVQEDLLSAEPHQGYP-FGDLVNDLRLPRDLSRHPlfdpmFSFQNYLGQDsqeEEFQLS-ELDLSVSSVIEEEAKY 388
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 497641516 474 VlLDAQVTEFDGGVLVNWDVREGVFPAGVIDAMFAHHIDELLRLAS 519
Cdd:pfam00668 389 D-LSLTASERGGGLTIKIDYNTSLFDEETIERFAEHFKELLEQAIA 433
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
518-1034 |
1.64e-24 |
|
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: 109.97 E-value: 1.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 518 ASADEAWEAPGPPAlpeaQRAVREAANGRTAEPSGEAL---HDGFFRQAEQRPDAPAVFASSGD------LSYAQLRDQA 588
Cdd:cd17634 19 AGKILDWITPYQKV----KNTSFAPGAPSIKWFEDATLnlaANALDRHLRENGDRTAIIYEGDDtsqsrtISYRELHREV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 589 LAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPI-GVDQPRDRAERILESGGVSLAVVCGGQR------ 661
Cdd:cd17634 95 CRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIfGGFAPEAVAGRIIDSSSRLLITADGGVRagrsvp 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 662 ----------LSMPVPEVVLADILGGAP-----------------ASTEITSARVDPAALAYVLFTSGSTGEPKGVEVTH 714
Cdd:cd17634 175 lkknvddalnPNVTSVEHVIVLKRTGSDidwqegrdlwwrdliakASPEHQPEAMNAEDPLFILYTSGTTGKPKGVLHTT 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 715 DAAMNTVEFIGRH-FDIGPADRCLALStlegDISVMD-----VFVTLRTGGSIVVVDEVQRR-DPDAWARLIDAHQVTVL 787
Cdd:cd17634 255 GGYLVYAATTMKYvFDYGPGDIYWCTA----DVGWVTghsylLYGPLACGATTLLYEGVPNWpTPARMWQVVDKHGVNIL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 788 HFMPGWLEMLVEVG-----RGRLSSVRVVPTGGDWVRPEVVRRL--RVEAPGVRFAGLGGATETpvhnSIFEVTE-PIPD 859
Cdd:cd17634 331 YTAPTAIRALMAAGddaieGTDRSSLRILGSVGEPINPEAYEWYwkKIGKEKCPVVDTWWQTET----GGFMITPlPGAI 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 860 DWTALPFGVPLPNNACRVVDDTGADCPDWVPGEYWVSGR--GIARGYRGRPDltaERFVEHDGRI--WYRTGDLVRYWPD 935
Cdd:cd17634 407 ELKAGSATRPVFGVQPAVVDNEGHPQPGGTEGNLVITDPwpGQTRTLFGDHE---RFEQTYFSTFkgMYFSGDGARRDED 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 936 GTLEFVGRADHRVKISGYRVELGEVETALRRVPGVRTAvaaliAVSGESDVLAAQ-----VCADDASVTAEGIRQALADL 1010
Cdd:cd17634 484 GYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEA-----AVVGIPHAIKGQapyayVVLNHGVEPSPELYAELRNW 558
|
570 580
....*....|....*....|....*...
gi 497641516 1011 VPAHM----IPRHITVVERIGFTDAGKL 1034
Cdd:cd17634 559 VRKEIgplaTPDVVHWVDSLPKTRSGKI 586
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
561-1028 |
2.18e-24 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 109.22 E-value: 2.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 561 RQAEQRPDAPAVFA-----SSGD-----LSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVy 630
Cdd:PRK09274 14 RAAQERPDQLAVAVpggrgADGKlaydeLSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAV- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 631 lPIGVD----------------------QPRDRAERILESGGVS--LAVVCGGQRLSMPVPevVLADILGGAPAStEITS 686
Cdd:PRK09274 93 -PVLVDpgmgiknlkqclaeaqpdafigIPKAHLARRLFGWGKPsvRRLVTVGGRLLWGGT--TLATLLRDGAAA-PFPM 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 687 ARVDPAALAYVLFTSGSTGEPKGVEVTHDAAMNTVEFIGRHFDIGPADRclalstlegDISVMDVFV--TLRTGGSIVVV 764
Cdd:PRK09274 169 ADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEI---------DLPTFPLFAlfGPALGMTSVIP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 765 DEVQRR----DPDAWARLIDAHQVTVLHFMPGWLEMLVEVGRGR---LSSVRVVPTGGDWVRPEVVRRLR-VEAPGVRFA 836
Cdd:PRK09274 240 DMDPTRpatvDPAKLFAAIERYGVTNLFGSPALLERLGRYGEANgikLPSLRRVISAGAPVPIAVIERFRaMLPPDAEIL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 837 GLGGATET-PVhnSIFEVTEPIPDDW--TALPFGV----PLPNNACRVVDDTGADCPDW-----VP----GEYWVSGRGI 900
Cdd:PRK09274 320 TPYGATEAlPI--SSIESREILFATRaaTDNGAGIcvgrPVDGVEVRIIAISDAPIPEWddalrLAtgeiGEIVVAGPMV 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 901 ARGYRGRPDLTAE-RFVEHDGRIWYRTGDLVRYWPDGTLEFVGRADHRVKISGYRVELGEVETALRRVPGV-RTAVAALI 978
Cdd:PRK09274 398 TRSYYNRPEATRLaKIPDGQGDVWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVkRSALVGVG 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 497641516 979 AVSGESDVLAAQVcADDASVTAEGIRQALADLVPAHmipRHITVVERIGF 1028
Cdd:PRK09274 478 VPGAQRPVLCVEL-EPGVACSKSALYQELRALAAAH---PHTAGIERFLI 523
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
561-1137 |
3.63e-24 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 110.64 E-value: 3.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 561 RQAEQRPDAPAV--FASSGD----LSYAQLrDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLP-- 632
Cdd:PRK05691 17 RRAAQTPDRLALrfLADDPGegvvLSYRDL-DLRARTIAAALQARASFGDRAVLLFPSGPDYVAAFFGCLYAGVIAVPay 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 633 ----------------IGVDQPRdraeRILESGGVSLAVVCGGQRLSMPVPEVVLADILGGAPASTEITSArVDPAALAY 696
Cdd:PRK05691 96 ppesarrhhqerllsiIADAEPR----LLLTVADLRDSLLQMEELAAANAPELLCVDTLDPALAEAWQEPA-LQPDDIAF 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 697 VLFTSGSTGEPKGVEVTHDAAMNTVEFIGRHF--DIGPADRCLALSTLEGDISVMDVFVTLRTGGSIVVVDEVQR--RDP 772
Cdd:PRK05691 171 LQYTSGSTALPKGVQVSHGNLVANEQLIRHGFgiDLNPDDVIVSWLPLYHDMGLIGGLLQPIFSGVPCVLMSPAYflERP 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 773 DAWARLID------------AHQVTVLHFMPGWLEMLvevgrgRLSSVRVVPTGGDWVRPEVVRRLRVEAPGVRFA---- 836
Cdd:PRK05691 251 LRWLEAISeyggtisggpdfAYRLCSERVSESALERL------DLSRWRVAYSGSEPIRQDSLERFAEKFAACGFDpdsf 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 837 ----GLGGAT-------------ETPVHNSIFEVTEPIPDDWTAL-PFGVPLPNNACRVVD-DTGADCPDWVPGEYWVSG 897
Cdd:PRK05691 325 fasyGLAEATlfvsggrrgqgipALELDAEALARNRAEPGTGSVLmSCGRSQPGHAVLIVDpQSLEVLGDNRVGEIWASG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 898 RGIARGYRGRPDLTAERFVEHDGRIWYRTGDLvRYWPDGTLEFVGRADHRVKISGYRVELGEVE-TALRRVPGVRTAVAA 976
Cdd:PRK05691 405 PSIAHGYWRNPEASAKTFVEHDGRTWLRTGDL-GFLRDGELFVTGRLKDMLIVRGHNLYPQDIEkTVEREVEVVRKGRVA 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 977 LIAVS--GESDV-LAAQVCAD-DASVTAEG----IRQALADLVpaHMIPRHITVVE--RIGFTDAGKLDRRAVARELE-- 1044
Cdd:PRK05691 484 AFAVNhqGEEGIgIAAEISRSvQKILPPQAliksIRQAVAEAC--QEAPSVVLLLNpgALPKTSSGKLQRSACRLRLAdg 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 1045 SAVSQSQRPGHR--------APSTPLQSALATIVGDLLGRQNIGIDDDFFALGGDSVLATQAVARIRAWLDApDIMVADI 1116
Cdd:PRK05691 562 SLDSYALFPALQaveaaqtaASGDELQARIAAIWCEQLKVEQVAADDHFFLLGGNSIAATQVVARLRDELGI-DLNLRQL 640
|
650 660
....*....|....*....|.
gi 497641516 1117 FANRTVSALAAVLGAGERDPG 1137
Cdd:PRK05691 641 FEAPTLAAFSAAVARQLAGGG 661
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
560-1024 |
3.74e-24 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 108.04 E-value: 3.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 560 FRQAEQRPDAPAVFASSGD-LSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIGVDQP 638
Cdd:PRK07514 9 LRAAFADRDAPFIETPDGLrYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 639 RDRAERILESGGVSLaVVCGGQRLSM--------PVPEVVLADILGG-------APASTEITSARVDPAALAYVLFTSGS 703
Cdd:PRK07514 89 LAELDYFIGDAEPAL-VVCDPANFAWlskiaaaaGAPHVETLDADGTgslleaaAAAPDDFETVPRGADDLAAILYTSGT 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 704 TGEPKGVEVTHDAAMNTVEFIGRHFDIGPADRCL-ALSTLEgdisVMDVFV----TLRTGGSIVVVdevQRRDPDAwarl 778
Cdd:PRK07514 168 TGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIhALPIFH----THGLFVatnvALLAGASMIFL---PKFDPDA---- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 779 idahqvtVLHFMPgwlemlvevgrgRLSSVRVVPT------GGDWVRPEVVRRLRV----EAP-------------GVRF 835
Cdd:PRK07514 237 -------VLALMP------------RATVMMGVPTfytrllQEPRLTREAAAHMRLfisgSAPllaethrefqertGHAI 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 836 AGLGGATETPVHNSifevtEPIPDDWTALPFGVPLPNNACRVVD-DTGADCPDWVPGEYWVSGRGIARGYRGRPDLTAER 914
Cdd:PRK07514 298 LERYGMTETNMNTS-----NPYDGERRAGTVGFPLPGVSLRVTDpETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEE 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 915 FVEhDGriWYRTGDLVRYWPDGTLEFVGRADHRVKISGYRVELGEVETALRRVPGVrtAVAALIAVS----GESdVLAAQ 990
Cdd:PRK07514 373 FRA-DG--FFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGV--VESAVIGVPhpdfGEG-VTAVV 446
|
490 500 510
....*....|....*....|....*....|....
gi 497641516 991 VCADDASVTAEGIRQALADLVPAHMIPRHITVVE 1024
Cdd:PRK07514 447 VPKPGAALDEAAILAALKGRLARFKQPKRVFFVD 480
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
568-1055 |
3.78e-24 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 109.35 E-value: 3.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 568 DAPAVFASSGdLSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIGVDQPRDRAERILE 647
Cdd:PRK06060 21 DRPAFYAADV-VTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAAR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 648 SGGVSLAVVCGGQRLSMPVPEVV-LADILGGA----PASTEITSARvdpaALAYVLFTSGSTGEPKGVEVTHDAAMNTVE 722
Cdd:PRK06060 100 NTEPALVVTSDALRDRFQPSRVAeAAELMSEAarvaPGGYEPMGGD----ALAYATYTSGTTGPPKAAIHRHADPLTFVD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 723 FIGRH-FDIGPADRCLALSTLEGDISVMD-VFVTLRTGGSiVVVDEVQRRDPDAwARLIDAHQVTVLHFMPGWLEMLVEV 800
Cdd:PRK06060 176 AMCRKaLRLTPEDTGLCSARMYFAYGLGNsVWFPLATGGS-AVINSAPVTPEAA-AILSARFGPSVLYGVPNFFARVIDS 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 801 -GRGRLSSVRVVPTGGDWVRPEVVRRLRVEAPGVRFAGLGGATE---TPVHNSIfevtepipDDWTALPFGVPLPNNACR 876
Cdd:PRK06060 254 cSPDSFRSLRCVVSAGEALELGLAERLMEFFGGIPILDGIGSTEvgqTFVSNRV--------DEWRLGTLGRVLPPYEIR 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 877 VVDDTGADCPDWVPGEYWVSGRGIARGYRGRPDltaeRFVEHDGriWYRTGDLVRYWPDGTLEFVGRADHRVKISGYRVE 956
Cdd:PRK06060 326 VVAPDGTTAGPGVEGDLWVRGPAIAKGYWNRPD----SPVANEG--WLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 957 LGEVETALRRVPGV-RTAVAALIAVSGESDVLAAQVCAD----DASVTAEGIRQALADLVpAHMIPRHITVVERIGFTDA 1031
Cdd:PRK06060 400 PREVERLIIEDEAVaEAAVVAVRESTGASTLQAFLVATSgatiDGSVMRDLHRGLLNRLS-AFKVPHRFAVVDRLPRTPN 478
|
490 500 510
....*....|....*....|....*....|..
gi 497641516 1032 GKLDRRAVAR--------ELESAVSQSQRPGH 1055
Cdd:PRK06060 479 GKLVRGALRKqsptkpiwELSLTEPGSGVRAQ 510
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
545-1043 |
1.11e-23 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 107.17 E-value: 1.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 545 GRTAEP-SGEALHDGFFRQAEQRPDAPAVFASSGDL--SYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALL 621
Cdd:PRK12583 9 GGGDKPlLTQTIGDAFDATVARFPDREALVVRHQALryTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 622 GILSVGAVYLPIGVDQPRDRAERILESGGV-----------------------SLAVVCGGQRLSMPVPEVVLADILGGA 678
Cdd:PRK12583 89 ATARIGAILVNINPAYRASELEYALGQSGVrwvicadafktsdyhamlqellpGLAEGQPGALACERLPELRGVVSLAPA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 679 PAS-----TEITSA--RVDPAALAY------------VLFTSGSTGEPKGVEVTHDAAMNTVEFIGRHFDIGPADR-CLA 738
Cdd:PRK12583 169 PPPgflawHELQARgeTVSREALAErqasldrddpinIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRlCVP 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 739 LSTLEGDISVMDVFVTLRTGGSIVVVDEvqRRDPDAWARLIDAHQVTVLHFMPG-WLEMLVEVGRGR--LSSVRVVPTGG 815
Cdd:PRK12583 249 VPLYHCFGMVLANLGCMTVGACLVYPNE--AFDPLATLQAVEEERCTALYGVPTmFIAELDHPQRGNfdLSSLRTGIMAG 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 816 DWVRPEVVRRLRVE--APGVRFAglGGATETPVHNSIFEVTEPIPDDWTALpfGVPLPNNACRVVDDTGADCPDWVPGEY 893
Cdd:PRK12583 327 APCPIEVMRRVMDEmhMAEVQIA--YGMTETSPVSLQTTAADDLERRVETV--GRTQPHLEVKVVDPDGATVPRGEIGEL 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 894 WVSGRGIARGYRGRPDLTAERfVEHDGriWYRTGDLVRYWPDGTLEFVGRADHRVKISGYRVELGEVETALRRVPGVrtA 973
Cdd:PRK12583 403 CTRGYSVMKGYWNNPEATAES-IDEDG--WMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAV--A 477
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497641516 974 VAALIAVSGE---SDVLAAQVCADDASVTAEGIRQALADLVPAHMIPRHITVVERIGFTDAGKLdRRAVAREL 1043
Cdd:PRK12583 478 DVQVFGVPDEkygEEIVAWVRLHPGHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKV-QKFRMREI 549
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
693-1036 |
1.19e-23 |
|
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: 103.25 E-value: 1.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 693 ALAYVLFTSGSTGEPKGVEVTHDAAMNTVEfIGRH-FDIGPADRCLALSTLEGDISVMDVFVTLRTGGSIVVvdevQRR- 770
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERSWIESFV-CNEDlFNISGEDAILAPGPLSHSLFLYGAISALYLGGTFIG----QRKf 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 771 DPDAWARLIDAHQVTVLHFMPGWLEMLVEVGRgRLSSVRVVPTGGDWVRPEVVRRLRVEAPGVRFAGLGGATETPVhnsi 850
Cdd:cd17633 76 NPKSWIRKINQYNATVIYLVPTMLQALARTLE-PESKIKSIFSSGQKLFESTKKKLKNIFPKANLIEFYGTSELSF---- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 851 feVTEPIPDD-WTALPFGVPLPNNACRVVDDTGAdcpdwVPGEYWVSGRGIARGYrgrpdlTAERFVEHDGriWYRTGDL 929
Cdd:cd17633 151 --ITYNFNQEsRPPNSVGRPFPNVEIEIRNADGG-----EIGKIFVKSEMVFSGY------VRGGFSNPDG--WMSVGDI 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 930 VRYWPDGTLEFVGRADHRVKISGYRVELGEVETALRRVPGVRTAVAALIAVSGESDVLAAQVCADdaSVTAEGIRQALAD 1009
Cdd:cd17633 216 GYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYSGD--KLTYKQLKRFLKQ 293
|
330 340
....*....|....*....|....*..
gi 497641516 1010 LVPAHMIPRHITVVERIGFTDAGKLDR 1036
Cdd:cd17633 294 KLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
599-1038 |
1.56e-23 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 105.21 E-value: 1.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 599 GVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPigvdqprdraerilesggvsLAVVCGGQRLsmpvpEVVLADilggA 678
Cdd:cd05971 27 GLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVP--------------------LFALFGPEAL-----EYRLSN----S 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 679 PASTEITSARVDPAalaYVLFTSGSTGEPKGVEVTHDAAMNTVEFIGRHFDIGPADRCLALSTLE-GDI-SVMDVFVTLR 756
Cdd:cd05971 78 GASALVTDGSDDPA---LIIYTSGTTGPPKGALHAHRVLLGHLPGVQFPFNLFPRDGDLYWTPADwAWIgGLLDVLLPSL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 757 TGGSIVVVDEVQRRDPDAWARLIDAHQVTVLHFMPGWLEMLVEVGRGRLS---SVRVVPTGGDWVRPEVVRRLRvEAPGV 833
Cdd:cd05971 155 YFGVPVLAHRMTKFDPKAALDLMSRYGVTTAFLPPTALKMMRQQGEQLKHaqvKLRAIATGGESLGEELLGWAR-EQFGV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 834 RFAGLGGATETPVHNSIFEVTEPIPDDwtalPFGVPLPNNACRVVDDTGADCPdwvPGEywVSGRGIAR-------GYRG 906
Cdd:cd05971 234 EVNEFYGQTECNLVIGNCSALFPIKPG----SMGKPIPGHRVAIVDDNGTPLP---PGE--VGEIAVELpdpvaflGYWN 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 907 RPDLTAERFVEHdgriWYRTGDLVRYWPDGTLEFVGRADHRVKISGYRVELGEVETALRRVPGVRTAVAALI--AVSGES 984
Cdd:cd05971 305 NPSATEKKMAGD----WLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIpdPIRGEI 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 497641516 985 ----DVLAAQVCADDAsvTAEGIRQALADLVPAHMIPRHITVVERIGFTDAGKLDRRA 1038
Cdd:cd05971 381 vkafVVLNPGETPSDA--LAREIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRRE 436
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
690-1036 |
2.84e-23 |
|
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: 102.72 E-value: 2.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 690 DPAAlayVLFTSGSTGEPKGVEVTHDAAMNTVEFIGRH-FDIGPADRCLALSTLEGDISVMDVFVTLRTGGSIVVVDEvq 768
Cdd:cd17635 2 DPLA---VIFTSGTTGEPKAVLLANKTFFAVPDILQKEgLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGE-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 769 RRDPDAWARLIDAHQVTVLHFMPGWLEMLVEVGRGRLS---SVRVVPTGGDwvrpevvrrlRVEAPGVRFAGLGGATETP 845
Cdd:cd17635 77 NTTYKSLFKILTTNAVTTTCLVPTLLSKLVSELKSANAtvpSLRLIGYGGS----------RAIAADVRFIEATGLTNTA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 846 VHNSIFEVTE----PIPDDWTAL-PFGVPLPNNACRVVDDTGADCPDWVPGEYWVSGRGIARGYRGRPDLTAERFVEHdg 920
Cdd:cd17635 147 QVYGLSETGTalclPTDDDSIEInAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLIDG-- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 921 riWYRTGDLVRYWPDGTLEFVGRADHRVKISGYRVELGEVETALRRVPGVRTAVAALI--AVSGESDVLAAQVCADDASV 998
Cdd:cd17635 225 --WVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEIsdEEFGELVGLAVVASAELDEN 302
|
330 340 350
....*....|....*....|....*....|....*...
gi 497641516 999 TAEGIRQALADLVPAHMIPRHITVVERIGFTDAGKLDR 1036
Cdd:cd17635 303 AIRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
697-1035 |
6.59e-23 |
|
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: 101.22 E-value: 6.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 697 VLFTSGSTGEPKGVEVTHDA--AMNTVEFIGRhfDIGPADRCLALSTLEGDISVMDVFVTLRTGGSIVVVdevQRRDPDA 774
Cdd:cd17636 5 AIYTAAFSGRPNGALLSHQAllAQALVLAVLQ--AIDEGTVFLNSGPLFHIGTLMFTLATFHAGGTNVFV---RRVDAEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 775 WARLIDAHQVTVLHFMPGWLEMLVEVGRGR---LSSVRVVPTGGDWVRPEVVRrlrvEAPGVRfaGLGGATETpvhnsif 851
Cdd:cd17636 80 VLELIEAERCTHAFLLPPTIDQIVELNADGlydLSSLRSSPAAPEWNDMATVD----TSPWGR--KPGGYGQT------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 852 EVTEPIPDDWTALP----FGVPLPNNACRVVDDTGADCPDWVPGEYWVSGRGIARGYRGRPDLTAERFVehDGriWYRTG 927
Cdd:cd17636 147 EVMGLATFAALGGGaiggAGRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTR--GG--WHHTN 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 928 DLVRYWPDGTLEFVGRADHRVKISGYRVELGEVETALRRVPGVRTavAALIAVSGE---SDVLAAQVCADDASVTAEGIR 1004
Cdd:cd17636 223 DLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVAD--AAVIGVPDPrwaQSVKAIVVLKPGASVTEAELI 300
|
330 340 350
....*....|....*....|....*....|.
gi 497641516 1005 QALADLVPAHMIPRHITVVERIGFTDAGKLD 1035
Cdd:cd17636 301 EHCRARIASYKKPKSVEFADALPRTAGGADD 331
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
559-1044 |
6.32e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 101.27 E-value: 6.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 559 FFRQAEQR-PDAPAVFASSGDLSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIGVDQ 637
Cdd:PRK07470 12 FLRQAARRfPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 638 PRDRAERILESGGVSlAVVCGGQ--------RLSMPVPEVVLAdiLGGAPASTEITS-------ARVDPAALAY-----V 697
Cdd:PRK07470 92 TPDEVAYLAEASGAR-AMICHADfpehaaavRAASPDLTHVVA--IGGARAGLDYEAlvarhlgARVANAAVDHddpcwF 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 698 LFTSGSTGEPKGVEVTHdAAMNTVefIGRHF-DIGP----ADRCLALSTLEGDISVMDVFVTLRTGGSIVVVDEvqRRDP 772
Cdd:PRK07470 169 FFTSGTTGRPKAAVLTH-GQMAFV--ITNHLaDLMPgtteQDASLVVAPLSHGAGIHQLCQVARGAATVLLPSE--RFDP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 773 DAWARLIDAHQVTVLHFMPGWLEMLVE---VGRGRLSSVR-VVPTGGDWVRPEVVRRLRVEAPG-VRFAGLGGATET-PV 846
Cdd:PRK07470 244 AEVWALVERHRVTNLFTVPTILKMLVEhpaVDRYDHSSLRyVIYAGAPMYRADQKRALAKLGKVlVQYFGLGEVTGNiTV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 847 HNSIFEVTEPIPDDWTAlPFGVPLPNNACRVVDDTGADCPDWVPGEYWVSGRGIARGYRGRPDLTAERFVehDGriWYRT 926
Cdd:PRK07470 324 LPPALHDAEDGPDARIG-TCGFERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAFR--DG--WFRT 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 927 GDLVRYWPDGTLEFVGRADHRVKISGYRVELGEVETALRRVPGVrTAVAAL---IAVSGESDVlAAQVCADDASVTAEGI 1003
Cdd:PRK07470 399 GDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAV-SEVAVLgvpDPVWGEVGV-AVCVARDGAPVDEAEL 476
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 497641516 1004 RQALADLVPAHMIPRHITVVERIGFTDAGKLDRRAVARELE 1044
Cdd:PRK07470 477 LAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVREELE 517
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
563-1044 |
1.21e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 99.96 E-value: 1.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 563 AEQRPDAPAVFASSGDLSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIGVDQPRDRA 642
Cdd:PRK06145 12 ARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 643 ERILESGGVSLAVVcgGQRLSMPV----PEVVL-----ADI----LGGAPASTEITSArvdPAALAYVLFTSGSTGEPKG 709
Cdd:PRK06145 92 AYILGDAGAKLLLV--DEEFDAIValetPKIVIdaaaqADSrrlaQGGLEIPPQAAVA---PTDLVRLMYTSGTTDRPKG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 710 VEVTHDaamntvEFIGRHFD------IGPADRCLALSTLEgDISVMDV--FVTLRTGGSIVVVDEVqrrDPDAWARLIDA 781
Cdd:PRK06145 167 VMHSYG------NLHWKSIDhvialgLTASERLLVVGPLY-HVGAFDLpgIAVLWVGGTLRIHREF---DPEAVLAAIER 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 782 HQVTVLHFMPGWLEMLVEV---GRGRLSSVRVVPTGGDWVRPEVVRRLRVEAPGVRFAGLGGATETPVHNSIFEVTEPIP 858
Cdd:PRK06145 237 HRLTCAWMAPVMLSRVLTVpdrDRFDLDSLAWCIGGGEKTPESRIRDFTRVFTRARYIDAYGLTETCSGDTLMEAGREIE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 859 DDWTAlpfGVPLPNNACRVVDDTGADCPDWVPGEYWVSGRGIARGYRGRPDLTAERFVEHdgriWYRTGDLVRYWPDGTL 938
Cdd:PRK06145 317 KIGST---GRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGD----WFRSGDVGYLDEEGFL 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 939 EFVGRADHRVKISGYRVELGEVETALRRVPGVRTAvaaliAVSGESD------VLAAQVCADDASVTAEGIRQALADLVP 1012
Cdd:PRK06145 390 YLTDRKKDMIISGGENIASSEVERVIYELPEVAEA-----AVIGVHDdrwgerITAVVVLNPGATLTLEALDRHCRQRLA 464
|
490 500 510
....*....|....*....|....*....|..
gi 497641516 1013 AHMIPRHITVVERIGFTDAGKLDRRAVARELE 1044
Cdd:PRK06145 465 SFKVPRQLKVRDELPRNPSGKVLKRVLRDELN 496
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
579-1014 |
3.33e-21 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 98.30 E-value: 3.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 579 LSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVylPIGVDQPRDRAERilesggvslavvcg 658
Cdd:cd05910 3 LSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAV--PVLIDPGMGRKNL-------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 659 GQRLSMPVPEVVLADILGGapasteitsarvDPAAlayVLFTSGSTGEPKGVEVTHDAAMNTVEFIGRHFDIGPADRCLA 738
Cdd:cd05910 67 KQCLQEAEPDAFIGIPKAD------------EPAA---ILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEVDLA 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 739 LSTLegdISVMDVFVTLRTggsivVVDEVQ-----RRDPDAWARLIDAHQVTVLHFMPGWLEMLVEVGRG---RLSSVRV 810
Cdd:cd05910 132 TFPL---FALFGPALGLTS-----VIPDMDptrpaRADPQKLVGAIRQYGVSIVFGSPALLERVARYCAQhgiTLPSLRR 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 811 VPTGGDWVRPEVVRRLR-VEAPGVRFAGLGGATET-PV----HNSIFEVTEPIPDDWTALPFGVPLPNNACRVVDDTGAD 884
Cdd:cd05910 204 VLSAGAPVPIALAARLRkMLSDEAEILTPYGATEAlPVssigSRELLATTTAATSGGAGTCVGRPIPGVRVRIIEIDDEP 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 885 ---------CPDWVPGEYWVSGRGIARGYRGRPDLTA-ERFVEHDGRIWYRTGDLVRYWPDGTLEFVGRADHRVKISGYR 954
Cdd:cd05910 284 iaewddtleLPRGEIGEITVTGPTVTPTYVNRPVATAlAKIDDNSEGFWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGT 363
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497641516 955 VELGEVETALRRVPGV-RTAVAALIAVSGESDVLAAQVCADDASVTAEgIRQALADLVPAH 1014
Cdd:cd05910 364 LYTEPVERVFNTHPGVrRSALVGVGKPGCQLPVLCVEPLPGTITPRAR-LEQELRALAKDY 423
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
597-1043 |
3.58e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 98.91 E-value: 3.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 597 AAGVTAGDTIAVMGPKTAEQIPALLGI-LSVGAVYLpigVDQPRDRA---------ERILESGGVSLAVVcgGQRLSMPV 666
Cdd:PRK07768 48 AAGVGPGDAVAVLAGAPVEIAPTAQGLwMRGASLTM---LHQPTPRTdlavwaedtLRVIGMIGAKAVVV--GEPFLAAA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 667 PE--------VVLADILGGAPASTEITsarvDPAALAYVLFTSGSTGEPKGVEVTHD------AAMntveFIGRHFDIGp 732
Cdd:PRK07768 123 PVleekgirvLTVADLLAADPIDPVET----GEDDLALMQLTSGSTGSPKAVQITHGnlyanaEAM----FVAAEFDVE- 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 733 ADRCLALSTLEGDISVMDVF-VTLRTGGSIVVVDEVQ-RRDPDAWARLIDAHQVTVLhFMPGW--------LEMLVEVGR 802
Cdd:PRK07768 194 TDVMVSWLPLFHDMGMVGFLtVPMYFGAELVKVTPMDfLRDPLLWAELISKYRGTMT-AAPNFayallarrLRRQAKPGA 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 803 GRLSSVRVVPTGGDWVRPEVVRRLrVEApGVRFaGLG--------GATETPVHNSI------FEVTEPIPDDWTALPFGV 868
Cdd:PRK07768 273 FDLSSLRFALNGAEPIDPADVEDL-LDA-GARF-GLRpeailpayGMAEATLAVSFspcgagLVVDEVDADLLAALRRAV 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 869 P---------------LPNNACRVVDDTGADCPDWVPGEYWVSGRGIARGYrgrpdLTAERFVE-HDGRIWYRTGDLVRY 932
Cdd:PRK07768 350 PatkgntrrlatlgppLPGLEVRVVDEDGQVLPPRGVGVIELRGESVTPGY-----LTMDGFIPaQDADGWLDTGDLGYL 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 933 WPDGTLEFVGRADHRVKISGYRVELGEVETALRRVPGVRTAVAALI----AVSGESDVLAAQVCADDASVTAEGIRQALA 1008
Cdd:PRK07768 425 TEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVRPGNAVAVrldaGHSREGFAVAVESNAFEDPAEVRRIRHQVA 504
|
490 500 510
....*....|....*....|....*....|....*....
gi 497641516 1009 DLVPAH--MIPRHITVVE--RIGFTDAGKLdRRAVAREL 1043
Cdd:PRK07768 505 HEVVAEvgVRPRNVVVLGpgSIPKTPSGKL-RRANAAEL 542
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
569-1040 |
3.96e-21 |
|
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: 97.93 E-value: 3.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 569 APAVFASSGDLSYAQLRDQALAVAAALRAAGVTA-GDTIAVMGPKTAEQIPALLGILSVGAVYLPIGVDQPRDRAERILE 647
Cdd:cd05958 1 RTCLRSPEREWTYRDLLALANRIANVLVGELGIVpGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 648 SGGVSLAVvCGGQrlsmpvpevvladilggapasteiTSARVDPAALAyvlFTSGSTGEPKGVEVTHDAAMNTVEFIGRH 727
Cdd:cd05958 81 KARITVAL-CAHA------------------------LTASDDICILA---FTSGTTGAPKATMHFHRDPLASADRYAVN 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 728 -FDIGPADRCLALSTLegdisvmdvFVTLRTGGSIVVVDEV-------QRRDPDAWARLIDAHQVTVLHFMPGWLEMLVE 799
Cdd:cd05958 133 vLRLREDDRFVGSPPL---------AFTFGLGGVLLFPFGVgasgvllEEATPDLLLSAIARYKPTVLFTAPTAYRAMLA 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 800 VGRGR---LSSVRVVPTGGDWVRPEVVRRLRvEAPGVRFAGLGGATETpVHnsIFevTEPIPDDWTALPFGVPLPNNACR 876
Cdd:cd05958 204 HPDAAgpdLSSLRKCVSAGEALPAALHRAWK-EATGIPIIDGIGSTEM-FH--IF--ISARPGDARPGATGKPVPGYEAK 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 877 VVDDTGADCPDWVPGEYWVSGrgiARGYRGRPDLTAERFVEHDgriWYRTGDLVRYWPDGTLEFVGRADHRVKISGYRVE 956
Cdd:cd05958 278 VVDDEGNPVPDGTIGRLAVRG---PTGCRYLADKRQRTYVQGG---WNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIA 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 957 LGEVETALRRVPGVrtAVAALIAVSGESD--VLAAQVCADDASVTAEGIRQALADLVPAHMI----PRHITVVERIGFTD 1030
Cdd:cd05958 352 PPEVEDVLLQHPAV--AECAVVGHPDESRgvVVKAFVVLRPGVIPGPVLARELQDHAKAHIApykyPRAIEFVTELPRTA 429
|
490
....*....|
gi 497641516 1031 AGKLDRRAVA 1040
Cdd:cd05958 430 TGKLQRFALR 439
|
|
| SgcC5_NRPS-like |
cd19539 |
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ... |
154-521 |
1.74e-20 |
|
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- bond forming activity and similar C-domains of modular NRPSs; SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. This subfamily also includes similar C-domains of modular NRPSs such as Penicillium chrysogenum N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase PCBAB. Condensation (C) domains of NRPSs normally catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380462 [Multi-domain] Cd Length: 427 Bit Score: 95.52 E-value: 1.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 154 HPMLRVRFLPDGT----QRIAPADEfgpfpvHVEDLRERSTGEADRRLAAIRAAKSHQqldGAVFELAVT------LLPA 223
Cdd:cd19539 52 HEALRTLLVRDDGgvprQEILPPGP------APLEVRDLSDPDSDRERRLEELLRERE---SRGFDLDEEppiravLGRF 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 224 ERSRLHVDLDMQ--AADAMSYRTLMADLAALYLGR------DLPELGYTYRQYrhAIEAEDARPQPARDADRAWWARRLP 295
Cdd:cd19539 123 DPDDHVLVLVAHhtAFDAWSLDVFARDLAALYAARrkgpaaPLPELRQQYKEY--AAWQREALAAPRAAELLDFWRRRLR 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 296 ELpDPPALPTTGGR-AENQSTRRWH--WLDPHTRDALFARAQARGFTPAMALAAGFANTLARWSTTSRFLLNVPLFGRQa 372
Cdd:cd19539 201 GA-EPTALPTDRPRpAGFPYPGADLrfELDAELVAALRELAKRARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRN- 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 373 lHPDVDSLVGDFTSSLLLDVDLTRANTAAARAQVVQDAMRTAAAHSAYP------GLAVLRDLSRHrGTQVLAPVVFTSA 446
Cdd:cd19539 279 -HPRFESTVGFFVNLLPLRVDVSDCATFRDLIARVRKALVDAQRHQELPfqqlvaELPVDRDAGRH-PLVQIVFQVTNAP 356
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497641516 447 LGLGELFSsdvtGQFGTPGWIISQGPQVLLDAQVTEFDGGVLVNWDVREGVFPAGVIDAmFAHHIDELLRLASAD 521
Cdd:cd19539 357 AGELELAG----GLSYTEGSDIPDGAKFDLNLTVTEEGTGLRGSLGYATSLFDEETIQG-FLADYLQVLRQLLAN 426
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
867-1037 |
1.77e-20 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 96.76 E-value: 1.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 867 GVPLPNNACRVVDDTGADCPDWVPGEYWVSGRGIARGYRGRPDLTAERFvEHDGriWYRTGDLVRYWPDGTLEFVGRADH 946
Cdd:PRK05677 381 GIPVPSTLCKVIDDDGNELPLGEVGELCVKGPQVMKGYWQRPEATDEIL-DSDG--WLKTGDIALIQEDGYMRIVDRKKD 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 947 RVKISGYRVELGEVETALRRVPGVRTAVAalIAV----SGESdVLAAQVCADDASVTAEGIRQALADLVPAHMIPRHITV 1022
Cdd:PRK05677 458 MILVSGFNVYPNELEDVLAALPGVLQCAA--IGVpdekSGEA-IKVFVVVKPGETLTKEQVMEHMRANLTGYKVPKAVEF 534
|
170
....*....|....*
gi 497641516 1023 VERIGFTDAGKLDRR 1037
Cdd:PRK05677 535 RDELPTTNVGKILRR 549
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
690-994 |
2.03e-20 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.
Pssm-ID: 341250 [Multi-domain] Cd Length: 545 Bit Score: 96.52 E-value: 2.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 690 DPAALAYVLFTSGSTGEPKGVEVTHDAAMNTV----EFIGRHFDIGPADRCLALSTLEGDISVMDVFVTLRTGGSI---- 761
Cdd:cd05927 112 KPEDLATICYTSGTTGNPKGVMLTHGNIVSNVagvfKILEILNKINPTDVYISYLPLAHIFERVVEALFLYHGAKIgfys 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 762 ----VVVDEVQRRDPDA-------WARLIDAHQVTVLH--FMPGWL-EMLVEVGRGRLSS-------------------- 807
Cdd:cd05927 192 gdirLLLDDIKALKPTVfpgvprvLNRIYDKIFNKVQAkgPLKRKLfNFALNYKLAELRSgvvraspfwdklvfnkikqa 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 808 ----VRVVPTGGDWVRPEVVRRLRVeAPGVRFAGLGGATETPVHNSIFEvtepiPDDWTALPFGVPLPNNACRVVD--DT 881
Cdd:cd05927 272 lggnVRLMLTGSAPLSPEVLEFLRV-ALGCPVLEGYGQTECTAGATLTL-----PGDTSVGHVGGPLPCAEVKLVDvpEM 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 882 GADCPDWVP-GEYWVSGRGIARGYRGRPDLTAERFVEhDGriWYRTGDLVRYWPDGTLEFVGRADHRVKIS-GYRVELGE 959
Cdd:cd05927 346 NYDAKDPNPrGEVCIRGPNVFSGYYKDPEKTAEALDE-DG--WLHTGDIGEWLPNGTLKIIDRKKNIFKLSqGEYVAPEK 422
|
330 340 350
....*....|....*....|....*....|....*..
gi 497641516 960 VETALrrvpgVRTAVAALIAVSGES--DVLAAQVCAD 994
Cdd:cd05927 423 IENIY-----ARSPFVAQIFVYGDSlkSFLVAIVVPD 454
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
547-1040 |
4.77e-20 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 95.34 E-value: 4.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 547 TAEPSGEALHDGFF----RQAEQRPDAPAVFASSGD--LSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPAL 620
Cdd:PRK05852 6 GAAPMASDFGPRIAdlveVAATRLPEAPALVVTADRiaISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 621 LGILSVGAVYLPIG----VDQPRDRAER------ILESGGVS-----------LAVVCGGQR-LSMPVPEVVLADILGGA 678
Cdd:PRK05852 86 LAASRADLVVVPLDpalpIAEQRVRSQAagarvvLIDADGPHdraepttrwwpLTVNVGGDSgPSGGTLSVHLDAATEPT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 679 PASTEITSARVDPAalaYVLFTSGSTGEPKGVEVTHDAAMNTVEFIGRHFDIGPADRCLALSTL-EGDISVMDVFVTLRT 757
Cdd:PRK05852 166 PATSTPEGLRPDDA---MIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLyHGHGLIAALLATLAS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 758 GGSIVVVDEVQRRDPDAWARLIDAHqVTVLHFMPGWLEMLVE------VGRGRlSSVRVVPTGGDWVRPEVVRRLRVE-- 829
Cdd:PRK05852 243 GGAVLLPARGRFSAHTFWDDIKAVG-ATWYTAVPTIHQILLEraatepSGRKP-AALRFIRSCSAPLTAETAQALQTEfa 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 830 APGVRFAGLGGATETPVHNSI--FEVTEPiPDDWTALPFGVPLPNnaCRVVDDTGADCPDWVPGEYWVSGRGIARGYRGR 907
Cdd:PRK05852 321 APVVCAFGMTEATHQVTTTQIegIGQTEN-PVVSTGLVGRSTGAQ--IRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGD 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 908 PDLTAERFVehDGriWYRTGDLVRYWPDGTLEFVGRADHRVKISGYRVELGEVETALRRVPGVRTAVAALI--AVSGESd 985
Cdd:PRK05852 398 PTITAANFT--DG--WLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVpdQLYGEA- 472
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 497641516 986 VLAAQVCADDASVTAEGIRQALADLVPAHMIPRHITVVERIGFTDAGKLDRRAVA 1040
Cdd:PRK05852 473 VAAVIVPRESAPPTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAVA 527
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
561-1024 |
1.00e-19 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.
Pssm-ID: 341283 [Multi-domain] Cd Length: 486 Bit Score: 93.90 E-value: 1.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 561 RQAEQRPDAPAVFASSGDLSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIGVDQPRD 640
Cdd:cd12118 12 RAAAVYPDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 641 RAERILESGGvslavvcggqrlsmpvPEVVLAD--------ILGGAPASTEITSA-RVDPAALAYvlfTSGSTGEPKGVE 711
Cdd:cd12118 92 EIAFILRHSE----------------AKVLFVDrefeyedlLAEGDPDFEWIPPAdEWDPIALNY---TSGTTGRPKGVV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 712 VTHDAAM-NTVEFIGRHfdiGPADRCLALSTLegdisvmDVF----------VTLRtGGSIVVVDEVqrrDPDAWARLID 780
Cdd:cd12118 153 YHHRGAYlNALANILEW---EMKQHPVYLWTL-------PMFhcngwcfpwtVAAV-GGTNVCLRKV---DAKAIYDLIE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 781 AHQVTvlHF--MPGWLEMLV---EVGRGRLSSVRVVPTGGdwVRPEVVRRLRVEAPGVRFAGLGGATET--PVhnsifeV 853
Cdd:cd12118 219 KHKVT--HFcgAPTVLNMLAnapPSDARPLPHRVHVMTAG--APPPAAVLAKMEELGFDVTHVYGLTETygPA------T 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 854 TEPIPDDWTALPF----------GVPLPN-NACRVVDDTGADCpdwVP------GEYWVSGRGIARGYRGRPDLTAERFv 916
Cdd:cd12118 289 VCAWKPEWDELPTeerarlkarqGVRYVGlEEVDVLDPETMKP---VPrdgktiGEIVFRGNIVMKGYLKNPEATAEAF- 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 917 eHDGriWYRTGDLVRYWPDGTLEFVGRADHrVKIS-GYRVELGEVETALRRVPGVRTavAALIAVS----GESdvlaaqV 991
Cdd:cd12118 365 -RGG--WFHSGDLAVIHPDGYIEIKDRSKD-IIISgGENISSVEVEGVLYKHPAVLE--AAVVARPdekwGEV------P 432
|
490 500 510
....*....|....*....|....*....|....*...
gi 497641516 992 CA-----DDASVTAEGIRQALADLVPAHMIPRHITVVE 1024
Cdd:cd12118 433 CAfvelkEGAKVTEEEIIAFCREHLAGFMVPKTVVFGE 470
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
550-1037 |
1.19e-19 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 94.28 E-value: 1.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 550 PSGEALHDGFFRQAEQRPDAPAVF-ASSGD-LSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVG 627
Cdd:PLN02246 20 PNHLPLHDYCFERLSEFSDRPCLIdGATGRvYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 628 AV-------YLP-------------IGVDQPR--DRAERILESGGVSLAVVCGGQRLSMPVPEVVLADilGGAPASTEIT 685
Cdd:PLN02246 100 AVtttanpfYTPaeiakqakasgakLIITQSCyvDKLKGLAEDDGVTVVTIDDPPEGCLHFSELTQAD--ENELPEVEIS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 686 SarVDPAALAYvlfTSGSTGEPKGVEVTHDAAMNTV--EFIGR--HFDIGPADRCL---------ALStlegdiSVMdvF 752
Cdd:PLN02246 178 P--DDVVALPY---SSGTTGLPKGVMLTHKGLVTSVaqQVDGEnpNLYFHSDDVILcvlpmfhiySLN------SVL--L 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 753 VTLRTGGSIVVvdeVQRRDPDAWARLIDAHQVTVLHFMPGWLEMLV---EVGRGRLSSVRVVPTGGDWVRPEVVRRLRVE 829
Cdd:PLN02246 245 CGLRVGAAILI---MPKFEIGALLELIQRHKVTIAPFVPPIVLAIAkspVVEKYDLSSIRMVLSGAAPLGKELEDAFRAK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 830 APGVRFAGLGGATET-PVHN-SIFEVTEPIPDDWTALpfGVPLPNNACRVVD-DTGADCPDWVPGEYWVSGRGIARGYRG 906
Cdd:PLN02246 322 LPNAVLGQGYGMTEAgPVLAmCLAFAKEPFPVKSGSC--GTVVRNAELKIVDpETGASLPRNQPGEICIRGPQIMKGYLN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 907 RPDLTAeRFVEHDGriWYRTGDLVRYWPDGTLEFVGRADHRVKISGYRVELGEVETALRRVPGVrtAVAALIA----VSG 982
Cdd:PLN02246 400 DPEATA-NTIDKDG--WLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSI--ADAAVVPmkdeVAG 474
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 497641516 983 ESDVlAAQVCADDASVTAEGIRQALADLVPAHMIPRHITVVERIGFTDAGKLDRR 1037
Cdd:PLN02246 475 EVPV-AFVVRSNGSEITEDEIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRK 528
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
579-968 |
1.49e-19 |
|
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341295 [Multi-domain] Cd Length: 468 Bit Score: 93.19 E-value: 1.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 579 LSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIGVDQPRDRAERILESGGVSLAVVcg 658
Cdd:cd17640 6 ITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALVV-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 659 gqrlsmpvpevvladilggapasteitsaRVDPAALAYVLFTSGSTGEPKGVEVTHDAAMNTVEFIGRHFDIGPADRCLA 738
Cdd:cd17640 84 -----------------------------ENDSDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQPGDRFLS 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 739 L---------------------------STLEGD---------ISVMDVFVTLRTGgsivVVDEVQRRDPdawarlidaH 782
Cdd:cd17640 135 IlpiwhsyersaeyfifacgcsqaytsiRTLKDDlkrvkphyiVSVPRLWESLYSG----IQKQVSKSSP---------I 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 783 QVTVLHFmpgwlemLVEVGRgrlssVRVVPTGGDWVRPEVVRRLrvEAPGVRFAGLGGATET-PVhnsifeVTEPIPDDW 861
Cdd:cd17640 202 KQFLFLF-------FLSGGI-----FKFGISGGGALPPHVDTFF--EAIGIEVLNGYGLTETsPV------VSARRLKCN 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 862 TALPFGVPLPNNACRVVD-DTGADCPDWVPGEYWVSGRGIARGYRGRPDLTAErFVEHDGriWYRTGDLVRYWPDGTLEF 940
Cdd:cd17640 262 VRGSVGRPLPGTEIKIVDpEGNVVLPPGEKGIVWVRGPQVMKGYYKNPEATSK-VLDSDG--WFNTGDLGWLTCGGELVL 338
|
410 420
....*....|....*....|....*....
gi 497641516 941 VGRA-DHRVKISGYRVELGEVETALRRVP 968
Cdd:cd17640 339 TGRAkDTIVLSNGENVEPQPIEEALMRSP 367
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
550-1050 |
4.31e-19 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 92.35 E-value: 4.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 550 PSGEALHDGFFRQAEQRPDAPA-VFASSGD-LSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVG 627
Cdd:PLN02330 25 PDKLTLPDFVLQDAELYADKVAfVEAVTGKaVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 628 AVYLPIGVDQPRDRAERILESGGVSLAVVCG---GQRLSMPVPEVVLADI-LGGAPASTEITSA-----------RVDPA 692
Cdd:PLN02330 105 GVFSGANPTALESEIKKQAEAAGAKLIVTNDtnyGKVKGLGLPVIVLGEEkIEGAVNWKELLEAadragdtsdneEILQT 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 693 ALAYVLFTSGSTGEPKGVEVTHdaaMNTV-EFIGRHFDIGPaDRCLALSTLeGDISVMDV-------FVTLRTGGSIVVV 764
Cdd:PLN02330 185 DLCALPFSSGTTGISKGVMLTH---RNLVaNLCSSLFSVGP-EMIGQVVTL-GLIPFFHIygitgicCATLRNKGKVVVM 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 765 DEVQRRdpdAWARLIDAHQVTVLHFMPGWLEMLVE---VGRGRLS--SVRVVPTGGDWVRPEVVRRLRVEAPGVRFAGLG 839
Cdd:PLN02330 260 SRFELR---TFLNALITQEVSFAPIVPPIILNLVKnpiVEEFDLSklKLQAIMTAAAPLAPELLTAFEAKFPGVQVQEAY 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 840 GATEtpvhNSIFEVTEPIPDDWTAL----PFGVPLPNNACRVVD-DTGADCPDWVPGEYWVSGRGIARGYRGRPDLTAeR 914
Cdd:PLN02330 337 GLTE----HSCITLTHGDPEKGHGIakknSVGFILPNLEVKFIDpDTGRSLPKNTPGELCVRSQCVMQGYYNNKEETD-R 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 915 FVEHDGriWYRTGDLVRYWPDGTLEFVGRADHRVKISGYRVELGEVETALRRVPGVRTAVAALIAVSGESDVLAAQVCAD 994
Cdd:PLN02330 412 TIDEDG--WLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVIN 489
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 497641516 995 -DASVTAEGIRQALADLVPAHMIPRHITVVERIGFTDAGKLDRRAVARELESAVSQS 1050
Cdd:PLN02330 490 pKAKESEEDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKEKMLSINKAN 546
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
605-1048 |
5.29e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 91.76 E-value: 5.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 605 TIAVMGPKTAEQIPALLGILSVGAVYLPIGVDQPRD-RAERILESggvSLAVVCGGQRLSMPVPEV---------VLADI 674
Cdd:PRK07638 52 TIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDeLKERLAIS---NADMIVTERYKLNDLPDEegrvieideWKRMI 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 675 LGGAPASTEITSARVDPAalaYVLFTSGSTGEPKGVEVTHDAAMNTVEFIGRHFDIGPADRCLALSTLEGDISVMDVFVT 754
Cdd:PRK07638 129 EKYLPTYAPIENVQNAPF---YMGFTSGSTGKPKAFLRAQQSWLHSFDCNVHDFHMKREDSVLIAGTLVHSLFLYGAIST 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 755 LRTGGSIVVVDEVQRRDPDAWarlIDAHQVTVLHFMPGWLEMLVEVGRGRLSSVRVVPTGGDWvRPEVVRRLRVEAPGVR 834
Cdd:PRK07638 206 LYVGQTVHLMRKFIPNQVLDK---LETENISVMYTVPTMLESLYKENRVIENKMKIISSGAKW-EAEAKEKIKNIFPYAK 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 835 FAGLGGATETPVhnsifeVTEPIPDDWTALP--FGVPLPNNACRVVDDTGADCPDWVPGEYWVSGRGIARGYRGRPDLTA 912
Cdd:PRK07638 282 LYEFYGASELSF------VTALVDEESERRPnsVGRPFHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGYIIGGVLAR 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 913 ERFVEHdgriWYRTGDLVRYWPDGTLEFVGRADHRVKISGYRVELGEVETALRRVPGVRTAVAALIAVS--GESDVLAAq 990
Cdd:PRK07638 356 ELNADG----WMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSywGEKPVAII- 430
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 497641516 991 vcadDASVTAEGIRQALADLVPAHMIPRHITVVERIGFTDAGKLDRRAVARELESAVS 1048
Cdd:PRK07638 431 ----KGSATKQQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAKSWIENQEK 484
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
566-1048 |
8.58e-19 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 91.44 E-value: 8.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 566 RPDAPAVF-ASSG-DLSYAQLRDQALAVAA-ALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIG-VDQPRDR 641
Cdd:PLN02574 52 HNGDTALIdSSTGfSISYSELQPLVKSMAAgLYHVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNpSSSLGEI 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 642 AERILE-SGGVSLAV---VCGGQRLSMPV---PEVV-LADILGGAPASTEITSARVDPAA--------LAYVLFTSGSTG 705
Cdd:PLN02574 132 KKRVVDcSVGLAFTSpenVEKLSPLGVPVigvPENYdFDSKRIEFPKFYELIKEDFDFVPkpvikqddVAAIMYSSGTTG 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 706 EPKGVEVTHDAAMNTVEFIGRhFDIG----PADRCLALSTLEG-DISVMDVFVT--LRTGGSIVVVdevQRRDPDAWARL 778
Cdd:PLN02574 212 ASKGVVLTHRNLIAMVELFVR-FEASqyeyPGSDNVYLAALPMfHIYGLSLFVVglLSLGSTIVVM---RRFDASDMVKV 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 779 IDAHQVTVLHFMPGWLEMLVEVGRGR----LSSVRVVPTGGDWVRPEVVRRLRVEAPGVRFAGLGGATE-TPVHNSIFEv 853
Cdd:PLN02574 288 IDRFKVTHFPVVPPILMALTKKAKGVcgevLKSLKQVSCGAAPLSGKFIQDFVQTLPHVDFIQGYGMTEsTAVGTRGFN- 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 854 TEPIpDDWTALpfGVPLPNNACRVVD-DTGADCPDWVPGEYWVSGRGIARGYRGRPDLTAERFVEhDGriWYRTGDLVRY 932
Cdd:PLN02574 367 TEKL-SKYSSV--GLLAPNMQAKVVDwSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDK-DG--WLRTGDIAYF 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 933 WPDGTLEFVGRADHRVKISGYRVELGEVETALRRVPGVRTavAALIAV----SGESDVlAAQVCADDASVTAEGIRQALA 1008
Cdd:PLN02574 441 DEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIID--AAVTAVpdkeCGEIPV-AFVVRRQGSTLSQEAVINYVA 517
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 497641516 1009 DLVPAHMIPRHITVVERIGFTDAGKLDRRAVARELESAVS 1048
Cdd:PLN02574 518 KQVAPYKKVRKVVFVQSIPKSPAGKILRRELKRSLTNSVS 557
|
|
| COG4908 |
COG4908 |
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ... |
105-340 |
1.56e-18 |
|
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];
Pssm-ID: 443936 [Multi-domain] Cd Length: 243 Bit Score: 86.25 E-value: 1.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 105 LAPMQHAMWVGRQENQqlggvAGHLYVEFD-GGGIDPERLRAAATALARRHPMLRVRF-LPDGT--QRIAPAdefGPFPV 180
Cdd:COG4908 1 LSPAQKRFLFLEPGSN-----AYNIPAVLRlEGPLDVEALERALRELVRRHPALRTRFvEEDGEpvQRIDPD---ADLPL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 181 HVEDLRERSTGEADRRLAAIRAAKSHQQLD---GAVFELAVTLLPAERSRLHVDLDMQAADAMSYRTLMADLAALY---- 253
Cdd:COG4908 73 EVVDLSALPEPEREAELEELVAEEASRPFDlarGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYaall 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 254 LGRD--LPELGYTYRQYrhAIEAEDARPQPARDADRAWWARRLPELPDPPALPTTGGRAENQSTR---RWHWLDPHTRDA 328
Cdd:COG4908 153 EGEPppLPELPIQYADY--AAWQRAWLQSEALEKQLEYWRQQLAGAPPVLELPTDRPRPAVQTFRgatLSFTLPAELTEA 230
|
250
....*....|..
gi 497641516 329 LFARAQARGFTP 340
Cdd:COG4908 231 LKALAKAHGATV 242
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
697-1034 |
4.26e-18 |
|
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.
Pssm-ID: 341293 [Multi-domain] Cd Length: 330 Bit Score: 86.79 E-value: 4.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 697 VLFTSGSTGEPKGVEVTHDAAMNTVEFIGRHFDIGPADRCLALSTLEGDISV-MDVFVTLRTGGSIVvvdEVQRRDPDAW 775
Cdd:cd17638 5 IMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFFHTFGYkAGIVACLLTGATVV---PVAVFDVDAI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 776 ARLIDAHQVTVLhfmPG----WLEMLVEVGR--GRLSSVRVVPTGGDWVRPEVVRRLRVEAPGVRFAGLGGATETPVhns 849
Cdd:cd17638 82 LEAIERERITVL---PGpptlFQSLLDHPGRkkFDLSSLRAAVTGAATVPVELVRRMRSELGFETVLTAYGLTEAGV--- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 850 ifeVTEPIPDD---WTALPFGVPLPNNACRVVDDtgadcpdwvpGEYWVSGRGIARGYRGRPDLTAERfVEHDGriWYRT 926
Cdd:cd17638 156 ---ATMCRPGDdaeTVATTCGRACPGFEVRIADD----------GEVLVRGYNVMQGYLDDPEATAEA-IDADG--WLHT 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 927 GDLVRYWPDGTLEFVGRADHRVKISGYRVELGEVETALRRVPGVrtAVAALIAVSGES--------DVLAAQVCADDASV 998
Cdd:cd17638 220 GDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGV--AQVAVIGVPDERmgevgkafVVARPGVTLTEEDV 297
|
330 340 350
....*....|....*....|....*....|....*.
gi 497641516 999 TAEgIRQALADlvpaHMIPRHITVVERIGFTDAGKL 1034
Cdd:cd17638 298 IAW-CRERLAN----YKVPRFVRFLDELPRNASGKV 328
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
561-1057 |
5.30e-18 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 89.24 E-value: 5.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 561 RQAEQRPDAPAV--------FASSGDLSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYlP 632
Cdd:PRK07529 33 RAAARHPDAPALsflldadpLDRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAGIAN-P 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 633 IGVDQPRDRAERILESGGVSLAV-------------VCGGQRLSMPVPEVVLADILG--GAPASTEITSARVDPAA---- 693
Cdd:PRK07529 112 INPLLEPEQIAELLRAAGAKVLVtlgpfpgtdiwqkVAEVLAALPELRTVVEVDLARylPGPKRLAVPLIRRKAHArild 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 694 -----------------------LAYVLFTSGSTGEPKGVEVTHDAAMNTVEFIGRHFDIGPADRCLALSTLegdISVMD 750
Cdd:PRK07529 192 fdaelarqpgdrlfsgrpigpddVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDTVFCGLPL---FHVNA 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 751 VFVTLRT----GGSIVVVDEVQRRDPDAWAR---LIDAHQVTVLHFMPGWLEML--VEVGRGRLSSVRVVPTGGDWVRPE 821
Cdd:PRK07529 269 LLVTGLAplarGAHVVLATPQGYRGPGVIANfwkIVERYRINFLSGVPTVYAALlqVPVDGHDISSLRYALCGAAPLPVE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 822 VVRRLRvEAPGVRFAGLGGATETPVHNSIFEVTEPIPDDWTalpfGVPLPNNACRVV--DDTGA---DCPDWVPGEYWVS 896
Cdd:PRK07529 349 VFRRFE-AATGVRIVEGYGLTEATCVSSVNPPDGERRIGSV----GLRLPYQRVRVVilDDAGRylrDCAVDEVGVLCIA 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 897 GRGIARGYrgrpdLTAE--RFVEHDGRiWYRTGDLVRYWPDGTLEFVGRADHRVKISGYRVELGEVETALRRVPGVrtav 974
Cdd:PRK07529 424 GPNVFSGY-----LEAAhnKGLWLEDG-WLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAV---- 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 975 aALIAVSGESDVLAAQV-CA-----DDASVTAEGIRQALADLVPAH-MIPRHITVVERIGFTDAGK-----LDRRAVARE 1042
Cdd:PRK07529 494 -ALAAAVGRPDAHAGELpVAyvqlkPGASATEAELLAFARDHIAERaAVPKHVRILDALPKTAVGKifkpaLRRDAIRRV 572
|
570
....*....|....*
gi 497641516 1043 LESAVSQSQRPGHRA 1057
Cdd:PRK07529 573 LRAALRDAGVEAEVV 587
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
867-1050 |
1.16e-17 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 88.19 E-value: 1.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 867 GVPLPNNACRVVDDTGADCPDWVPGEYWVSGRGIARGYRGRPDLTAErfVEHDGriWYRTGDLVRYWPDGTLEFVGRADH 946
Cdd:PRK08974 381 GLPVPSTEIKLVDDDGNEVPPGEPGELWVKGPQVMLGYWQRPEATDE--VIKDG--WLATGDIAVMDEEGFLRIVDRKKD 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 947 RVKISGYRVELGEVETALRRVPGVRTAVAALIA--VSGEsdVLAAQVCADDASVTAEGIRQALADLVPAHMIPRHITVVE 1024
Cdd:PRK08974 457 MILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPseVSGE--AVKIFVVKKDPSLTEEELITHCRRHLTGYKVPKLVEFRD 534
|
170 180
....*....|....*....|....*.
gi 497641516 1025 RIGFTDAGKLDRRAVARELESAVSQS 1050
Cdd:PRK08974 535 ELPKSNVGKILRRELRDEARAKVDNK 560
|
|
| LCL_NRPS-like |
cd19531 |
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ... |
154-432 |
1.18e-17 |
|
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. Streptomyces globisporus SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.
Pssm-ID: 380454 [Multi-domain] Cd Length: 427 Bit Score: 87.03 E-value: 1.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 154 HPMLRVRF-LPDGT--QRIAPAdefGPFPVHVEDLRERSTGEADRRLAAIRAAKSHQqldgaVFELA------VTLLpae 224
Cdd:cd19531 52 HEALRTTFvEVDGEpvQVILPP---LPLPLPVVDLSGLPEAEREAEAQRLAREEARR-----PFDLArgpllrATLL--- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 225 rsRLHVD-----LDMQ--AADAMSYRTLMADLAALYLGR------DLPELGYTYRQY----RHAIEAEdarpqpARDADR 287
Cdd:cd19531 121 --RLGEDehvllLTMHhiVSDGWSMGVLLRELAALYAAFlagrpsPLPPLPIQYADYavwqREWLQGE------VLERQL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 288 AWWARRLPELPDPPALPTTGGRAENQSTR--RWHW-LDPHTRDALFARAQARGFTPAMALAAGFANTLARWSTTSRFLLN 364
Cdd:cd19531 193 AYWREQLAGAPPVLELPTDRPRPAVQSFRgaRVRFtLPAELTAALRALARREGATLFMTLLAAFQVLLHRYSGQDDIVVG 272
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497641516 365 VPLFGRQalHPDVDSLVGDFTSSLLLDVDLTRANTAAARAQVVQDAMRTAAAHSAYP------GLAVLRDLSRH 432
Cdd:cd19531 273 TPVAGRN--RAELEGLIGFFVNTLVLRTDLSGDPTFRELLARVRETALEAYAHQDLPfeklveALQPERDLSRS 344
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
562-1044 |
1.58e-17 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 86.94 E-value: 1.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 562 QAEQRPDAPAVFASSGDLSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIGVdqpR-D 640
Cdd:PRK03640 11 RAFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNT---RlS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 641 RAERI--LESGGVSLAVVCGG-QRLSMPVPEVVLADILGGAPASTEITSArVDPAALAYVLFTSGSTGEPKGVEVTHD-- 715
Cdd:PRK03640 88 REELLwqLDDAEVKCLITDDDfEAKLIPGISVKFAELMNGPKEEAEIQEE-FDLDEVATIMYTSGTTGKPKGVIQTYGnh 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 716 --AAMNTVEFIGRHFDigpaDRCLA---------LSTLegdisvmdvFVTLRTGGSIVVVdevQRRDPDAWARLIDAHQV 784
Cdd:PRK03640 167 wwSAVGSALNLGLTED----DCWLAavpifhisgLSIL---------MRSVIYGMRVVLV---EKFDAEKINKLLQTGGV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 785 TVLHFMPGWLE-MLVEVGRGRL-SSVRVVPTGG---DWVRPEVVRRLRVeaPGVRFAGLggaTETPvhNSIfeVTEPiPD 859
Cdd:PRK03640 231 TIISVVSTMLQrLLERLGEGTYpSSFRCMLLGGgpaPKPLLEQCKEKGI--PVYQSYGM---TETA--SQI--VTLS-PE 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 860 DwtAL----PFGVPLPNNACRVVDDtGADCPDWVPGEYWVSGRGIARGYRGRPDLTAERFveHDGriWYRTGDLVRYWPD 935
Cdd:PRK03640 301 D--ALtklgSAGKPLFPCELKIEKD-GVVVPPFEEGEIVVKGPNVTKGYLNREDATRETF--QDG--WFKTGDIGYLDEE 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 936 GTLEFVGRADHRVkISGyrvelGE------VETALRRVPGVRTAVaaliaVSGESD-----VLAAQVCAdDASVTAEGIR 1004
Cdd:PRK03640 374 GFLYVLDRRSDLI-ISG-----GEniypaeIEEVLLSHPGVAEAG-----VVGVPDdkwgqVPVAFVVK-SGEVTEEELR 441
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 497641516 1005 QALADLVPAHMIPRHITVVERIGFTDAGKLDRRAVARELE 1044
Cdd:PRK03640 442 HFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQLVE 481
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
576-1037 |
4.04e-17 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 85.91 E-value: 4.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 576 SGD--LSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIGVDQPRDRAERILESGGVSl 653
Cdd:PRK12406 7 SGDrrRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGAR- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 654 aVVCGGQRLSMPVPEVVLADI-LGGAPASTEITSA-RVDPAAL---------------------------AYVLFTSGST 704
Cdd:PRK12406 86 -VLIAHADLLHGLASALPAGVtVLSVPTPPEIAAAyRISPALLtppagaidwegwlaqqepydgppvpqpQSMIYTSGTT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 705 GEPKGVE---VTHDAAMNTVEFIGRHFDIGPADRCLalstLEGDI--SVMDVF--VTLRTGGSIVVvdeVQRRDPDAWAR 777
Cdd:PRK12406 165 GHPKGVRraaPTPEQAAAAEQMRALIYGLKPGIRAL----LTGPLyhSAPNAYglRAGRLGGVLVL---QPRFDPEELLQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 778 LIDAHQVTVLHFMPGW---LEMLVEVGRGR--LSSVRVVPTGGDWVRPEVVRRLrVEAPGVRFAGLGGATETPVhnsife 852
Cdd:PRK12406 238 LIERHRITHMHMVPTMfirLLKLPEEVRAKydVSSLRHVIHAAAPCPADVKRAM-IEWWGPVIYEYYGSTESGA------ 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 853 VTEPIPDDWTALP--FGVPLPNNACRVVDDTGADCPDWVPGEYWVSGRGIAR-GYRGRPDLTAErfVEHDGriWYRTGDL 929
Cdd:PRK12406 311 VTFATSEDALSHPgtVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDfTYHNKPEKRAE--IDRGG--FITSGDV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 930 VRYWPDGTLEFVGRADHRVKISGYRVELGEVETALRRVPGVRTAVAALIAVSGESDVLAAQVCAD-DASVTAEGIRQALA 1008
Cdd:PRK12406 387 GYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQpGATLDEADIRAQLK 466
|
490 500
....*....|....*....|....*....
gi 497641516 1009 DLVPAHMIPRHITVVERIGFTDAGKLDRR 1037
Cdd:PRK12406 467 ARLAGYKVPKHIEIMAELPREDSGKIFKR 495
|
|
| AcpA |
COG3433 |
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ... |
9-82 |
5.85e-17 |
|
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442659 [Multi-domain] Cd Length: 295 Bit Score: 82.88 E-value: 5.85e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497641516 9 EDIRAEVAELLGVDADAVQPGSNLIGQGLDSIRIMTLAGRWRRQGIAVDFATLAETPTVEAWAELVNAGKPSAD 82
Cdd:COG3433 222 EELRADVAELLGVDPEEIDPDDNLFDLGLDSIRLMQLVERWRKAGLDVSFADLAEHPTLAAWWALLAAAQAAAA 295
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
579-973 |
7.40e-17 |
|
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: 84.54 E-value: 7.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 579 LSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLP----IGVDQPRDRAERilesGGvslA 654
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPattlLTPDDLRDRVDR----GG---A 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 655 VVCggqrlsmpvpevvladilggapASTEITSARvDPAALayvLFTSGSTGEPKGVEVTHDA----AMNTVEFIGrhfdI 730
Cdd:cd05974 74 VYA----------------------AVDENTHAD-DPMLL---YFTSGTTSKPKLVEHTHRSypvgHLSTMYWIG----L 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 731 GPADRCLALSTLEGDISVMDVFVTLRTGGSIVVVDEVQRRDPDAWARLIDAHQVTVLHFMPGWLEMLVEVGRGRLS-SVR 809
Cdd:cd05974 124 KPGDVHWNISSPGWAKHAWSCFFAPWNAGATVFLFNYARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQQDLASFDvKLR 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 810 VVPTGGDWVRPEVVRRLRvEAPGVRFAGLGGATETP--VHNSIFEVTEPipddwtaLPFGVPLPNNACRVVDDTGADCPD 887
Cdd:cd05974 204 EVVGAGEPLNPEVIEQVR-RAWGLTIRDGYGQTETTalVGNSPGQPVKA-------GSMGRPLPGYRVALLDPDGAPATE 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 888 wvpGEYWV---SGR--GIARGYRGRPDLTAErfVEHDGriWYRTGDLVRYWPDGTLEFVGRADHRVKISGYRVELGEVET 962
Cdd:cd05974 276 ---GEVALdlgDTRpvGLMKGYAGDPDKTAH--AMRGG--YYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELES 348
|
410
....*....|.
gi 497641516 963 ALRRVPGVRTA 973
Cdd:cd05974 349 VLIEHPAVAEA 359
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
683-1037 |
7.52e-17 |
|
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.
Pssm-ID: 341238 [Multi-domain] Cd Length: 411 Bit Score: 84.32 E-value: 7.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 683 EITSARVDPAALAYVLFTSGSTGEPKGVEVT---HDA-AMNTVEFIGRHFDigpaDRCLALSTL--EGDISVMdvFVTLR 756
Cdd:cd05912 68 QLKDSDVKLDDIATIMYTSGTTGKPKGVQQTfgnHWWsAIGSALNLGLTED----DNWLCALPLfhISGLSIL--MRSVI 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 757 TGGSIVVVDevqRRDPDAWARLIDAHQVTVLHFMPGWLEMLVEV-GRGRLSSVRVVPTGGDWVRPEVVRRlrVEAPGVRF 835
Cdd:cd05912 142 YGMTVYLVD---KFDAEQVLHLINSGKVTIISVVPTMLQRLLEIlGEGYPNNLRCILLGGGPAPKPLLEQ--CKEKGIPV 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 836 AGLGGATETpvhNSIFeVTEPIPDDWTAL-PFGVPLPNNACRVVDDTGadcPDWVPGEYWVSGRGIARGYRGRPDLTAER 914
Cdd:cd05912 217 YQSYGMTET---CSQI-VTLSPEDALNKIgSAGKPLFPVELKIEDDGQ---PPYEVGEILLKGPNVTKGYLNRPDATEES 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 915 FVehDGriWYRTGDLVRYWPDGTLEFVGRADHRVKISGYRVELGEVETALRRVPGVRTAvaaliAVSGESDVLAAQV-CA 993
Cdd:cd05912 290 FE--NG--WFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEA-----GVVGIPDDKWGQVpVA 360
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 497641516 994 ---DDASVTAEGIRQALADLVPAHMIPRHITVVERIGFTDAGKLDRR 1037
Cdd:cd05912 361 fvvSERPISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRH 407
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
561-1060 |
9.91e-17 |
|
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: 85.44 E-value: 9.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 561 RQAEQ-RPDAPAVFASSG------DLSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVY-LP 632
Cdd:cd05967 58 RHVEAgRGDQIALIYDSPvtgterTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHsVV 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 633 IGVDQPRDRAERI--------------LESGGV-----------SLAVVCGG-----QRLSMPVpevVLADILGGAPAST 682
Cdd:cd05967 138 FGGFAAKELASRIddakpklivtascgIEPGKVvpykplldkalELSGHKPHhvlvlNRPQVPA---DLTKPGRDLDWSE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 683 EITSA-RVDPAALA-----YVLFTSGSTGEPKGV-------EVTHDAAMNTVefigrhFDIGPADRCLALStlegDIS-V 748
Cdd:cd05967 215 LLAKAePVDCVPVAatdplYILYTSGTTGKPKGVvrdngghAVALNWSMRNI------YGIKPGDVWWAAS----DVGwV 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 749 MD----VFVTLRTGGSIVVVD--EVQRRDPDAWARLIDAHQVTVLHFMPgwlemlvevgrgrlSSVRVV---PTGGDWVR 819
Cdd:cd05967 285 VGhsyiVYGPLLHGATTVLYEgkPVGTPDPGAFWRVIEKYQVNALFTAP--------------TAIRAIrkeDPDGKYIK 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 820 PEVVRRLRV--------EAPGVRFAGlgGATETPVHNSIFEvTE---PIpddwTALPFG------------VPLPNNACR 876
Cdd:cd05967 351 KYDLSSLRTlflagerlDPPTLEWAE--NTLGVPVIDHWWQ-TEtgwPI----TANPVGleplpikagspgKPVPGYQVQ 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 877 VVDDTGADCPDWVPGEYWVSGR---GIARGYRGRPdltaERFVE---HDGRIWYRTGDLVRYWPDGTLEFVGRADHRVKI 950
Cdd:cd05967 424 VLDEDGEPVGPNELGNIVIKLPlppGCLLTLWKND----ERFKKlylSKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINV 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 951 SGYRVELGEVETALRRVPGVrtAVAALIAVSGE---SDVLAAQVCADDASVTAEGIRQALADLVPAHMIP----RHITVV 1023
Cdd:cd05967 500 AGHRLSTGEMEESVLSHPAV--AECAVVGVRDElkgQVPLGLVVLKEGVKITAEELEKELVALVREQIGPvaafRLVIFV 577
|
570 580 590
....*....|....*....|....*....|....*..
gi 497641516 1024 ERIGFTDAGKLDRRAVArelesAVSQSQRPGhrAPST 1060
Cdd:cd05967 578 KRLPKTRSGKILRRTLR-----KIADGEDYT--IPST 607
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
560-1033 |
1.05e-16 |
|
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: 85.40 E-value: 1.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 560 FRQAEQrPDAPAVFASSG----DLSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIGV 635
Cdd:cd05943 77 LRHADA-DDPAAIYAAEDgertEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSP 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 636 D-------------QPR---------------DRAERILE--------SGGVSLAVVCGGQR--LSMPVPEVVLADILGG 677
Cdd:cd05943 156 DfgvpgvldrfgqiEPKvlfavdaytyngkrhDVREKVAElvkglpslLAVVVVPYTVAAGQpdLSKIAKALTLEDFLAT 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 678 APAStEITSARVDPAALAYVLFTSGSTGEPKGveVTHDAAMNTVEFI---GRHFDIGPADRCLALST---------LEGd 745
Cdd:cd05943 236 GAAG-ELEFEPLPFDHPLYILYSSGTTGLPKC--IVHGAGGTLLQHLkehILHCDLRPGDRLFYYTTcgwmmwnwlVSG- 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 746 isvmdvfvtLRTGGSIVVVDEVQ-RRDPDAWARLIDAHQVTVLHFMPGWLEMLVEVG-----RGRLSSVRVV-------- 811
Cdd:cd05943 312 ---------LAVGATIVLYDGSPfYPDTNALWDLADEEGITVFGTSAKYLDALEKAGlkpaeTHDLSSLRTIlstgsplk 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 812 PTGGDWVRPEVvrrlrveAPGVRFAGLGGATETpvhNSIFEVTEPIpddwtaLPFG-----VPLPNNACRVVDDTGADCP 886
Cdd:cd05943 383 PESFDYVYDHI-------KPDVLLASISGGTDI---ISCFVGGNPL------LPVYrgeiqCRGLGMAVEAFDEEGKPVW 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 887 DwVPGEYwVSGRGIAR---GYRGRPDLTAER---FVEHDGrIWyRTGDLVRYWPDGTLEFVGRADHRVKISGYRVELGEV 960
Cdd:cd05943 447 G-EKGEL-VCTKPFPSmpvGFWNDPDGSRYRaayFAKYPG-VW-AHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEI 522
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497641516 961 ETALRRVPGVRTA-VAALIAVSGESDVLAAQVCADDASVT---AEGIRQAL-ADLVPAHmIPRHITVVERIGFTDAGK 1033
Cdd:cd05943 523 YRVVEKIPEVEDSlVVGQEWKDGDERVILFVKLREGVELDdelRKRIRSTIrSALSPRH-VPAKIIAVPDIPRTLSGK 599
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
561-1034 |
1.21e-16 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 84.83 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 561 RQAEQRPDAPAVFASSGDLSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIGVD-QPR 639
Cdd:PRK07786 25 RHALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRlTPP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 640 DRAERILESGG------VSLAVVCGGQRLSMPVPEVVLadILGGAPAS------TEITSARVDPAAL-------AYVLFT 700
Cdd:PRK07786 105 EIAFLVSDCGAhvvvteAALAPVATAVRDIVPLLSTVV--VAGGSSDDsvlgyeDLLAEAGPAHAPVdipndspALIMYT 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 701 SGSTGEPKGVEVTHD--AAMNTVEFIGRHFDIGpADRCLALSTLEGDISVMDVFVTLRTGGSIvVVDEVQRRDPDAWARL 778
Cdd:PRK07786 183 SGTTGRPKGAVLTHAnlTGQAMTCLRTNGADIN-SDVGFVGVPLFHIAGIGSMLPGLLLGAPT-VIYPLGAFDPGQLLDV 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 779 IDAHQVTVLHFMPG-WLEMLVEVG-RGRLSSVRVVPTGGDWVRPEVVRRLRVEAPGVRFAGLGGATETPVHNSIFEVTEP 856
Cdd:PRK07786 261 LEAEKVTGIFLVPAqWQAVCAEQQaRPRDLALRVLSWGAAPASDTLLRQMAATFPEAQILAAFGQTEMSPVTCMLLGEDA 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 857 IPDDWTAlpfGVPLPNNACRVVDDTGADCPDWVPGEYWVSGRGIARGYRGRPDLTAERFveHDGriWYRTGDLVRYWPDG 936
Cdd:PRK07786 341 IRKLGSV---GKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAF--AGG--WFHSGDLVRQDEEG 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 937 TLEFVGRADHRVKISGYRVELGEVETALRRVPGVRTavAALIAVS----GESDVLAAQVCADDASVTAEGIRQALADLVP 1012
Cdd:PRK07786 414 YVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVE--VAVIGRAdekwGEVPVAVAAVRNDDAALTLEDLAEFLTDRLA 491
|
490 500
....*....|....*....|..
gi 497641516 1013 AHMIPRHITVVERIGFTDAGKL 1034
Cdd:PRK07786 492 RYKHPKALEIVDALPRNPAGKV 513
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
867-1037 |
1.36e-16 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 84.49 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 867 GVPLPNNACRVVDDTGADCPDWVPGEYWVSGRGIARGYRGRPDLTAERFvehDGRIWYRTGDLVRYWPDGTLEFVGRADH 946
Cdd:PRK12492 389 GIPVPGTALKVIDDDGNELPLGERGELCIKGPQVMKGYWQQPEATAEAL---DAEGWFKTGDIAVIDPDGFVRIVDRKKD 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 947 RVKISGYRVELGEVETALRRVPGVrtAVAALIAVSGESDVLAAQ--VCADDASVTAEGIRQALADLVPAHMIPRHITVVE 1024
Cdd:PRK12492 466 LIIVSGFNVYPNEIEDVVMAHPKV--ANCAAIGVPDERSGEAVKlfVVARDPGLSVEELKAYCKENFTGYKVPKHIVLRD 543
|
170
....*....|...
gi 497641516 1025 RIGFTDAGKLDRR 1037
Cdd:PRK12492 544 SLPMTPVGKILRR 556
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
678-1042 |
2.11e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 83.96 E-value: 2.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 678 APASTEITSARVDPAALAYVLFTSGSTGEPKGVEVTHDAAMNTVEFIGRHFDIGPADRC-LALSTLEGDISVMDVFVTLR 756
Cdd:PRK07867 138 AHRDAEPPFRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDDVCyVSMPLFHSNAVMAGWAVALA 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 757 TGGSIVVvdevqRRDPDAWARLIDAHQ--VTVLHFMPGWLEMLV---EVGRGRLSSVRVV--PTGGDWVRPEVVRRLrve 829
Cdd:PRK07867 218 AGASIAL-----RRKFSASGFLPDVRRygATYANYVGKPLSYVLatpERPDDADNPLRIVygNEGAPGDIARFARRF--- 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 830 apGVRFAGLGGATETPVhnsIFEVTEPIPDDwtALpfGVPLPNNAcrVVD-DTGADCPdwvPGEYW-------------- 894
Cdd:PRK07867 290 --GCVVVDGFGSTEGGV---AITRTPDTPPG--AL--GPLPPGVA--IVDpDTGTECP---PAEDAdgrllnadeaigel 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 895 --VSGRGIARGYRGRPDLTAERFveHDGRIWyrTGDLVRYWPDGTLEFVGRADHRVKISGYRVELGEVETALRRVPG-VR 971
Cdd:PRK07867 356 vnTAGPGGFEGYYNDPEADAERM--RGGVYW--SGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDaTE 431
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497641516 972 TAVAALIAVSGESDVLAAQVCADDASVTAEGIRQALA---DLVPAhMIPRHITVVERIGFTDAGKLDRRAVARE 1042
Cdd:PRK07867 432 VAVYAVPDPVVGDQVMAALVLAPGAKFDPDAFAEFLAaqpDLGPK-QWPSYVRVCAELPRTATFKVLKRQLSAE 504
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
579-1004 |
2.18e-16 |
|
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: 83.26 E-value: 2.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 579 LSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIgvdqprdraerilesggvslavvcg 658
Cdd:cd05914 8 LTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPI------------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 659 gqrLSMPVPEVVlADILGGAPASTEITSarvDPAALAYVLFTSGSTGEPKGVEVTHDAAMNTVEFIGRHFDIGPADRCLA 738
Cdd:cd05914 63 ---LAEFTADEV-HHILNHSEAKAIFVS---DEDDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGKGDKILS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 739 LSTLEGDISVMDVFVT-LRTGGSIVVVDEVqrrdPDAWARLIDAHQVTVLHFMPGWLEM--------------------- 796
Cdd:cd05914 136 ILPLHHIYPLTFTLLLpLLNGAHVVFLDKI----PSAKIIALAFAQVTPTLGVPVPLVIekifkmdiipkltlkkfkfkl 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 797 ----------------LVEVGRGRLssvRVVPTGGDWVRPEVVRRLRveAPGVRFAGLGGATET-PVhnsifeVTEPIPD 859
Cdd:cd05914 212 akkinnrkirklafkkVHEAFGGNI---KEFVIGGAKINPDVEEFLR--TIGFPYTIGYGMTETaPI------ISYSPPN 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 860 DWTALPFGVPLPNNACRVVDDTgadcPDWVPGEYWVSGRGIARGYRGRPDLTAERFVEhDGriWYRTGDLVRYWPDGTLE 939
Cdd:cd05914 281 RIRLGSAGKVIDGVEVRIDSPD----PATGEGEIIVRGPNVMKGYYKNPEATAEAFDK-DG--WFHTGDLGKIDAEGYLY 353
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497641516 940 FVGRADHR-VKISGYRVELGEVETALRRVPGVrtaVAALIAVSGESDVLAAQVCADDASVTAEGIR 1004
Cdd:cd05914 354 IRGRKKEMiVLSSGKNIYPEEIEAKINNMPFV---LESLVVVQEKKLVALAYIDPDFLDVKALKQR 416
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
693-1041 |
2.43e-16 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 82.02 E-value: 2.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 693 ALAYVLFTSGSTGEPKGVEVTHDA----AMNTVEFIGrhfdiGPADRCLALSTLEgdISVMDVFV-TLRTGGSIVVVDEV 767
Cdd:PRK07824 36 DVALVVATSGTTGTPKGAMLTAAAltasADATHDRLG-----GPGQWLLALPAHH--IAGLQVLVrSVIAGSEPVELDVS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 768 QRRDPDAWARLIDA----HQVTVLHFMPGWLEMLVEVGRGRLSSVRVVPTGGDWVRPEVVRRlrVEAPGVRFAGLGGATE 843
Cdd:PRK07824 109 AGFDPTALPRAVAElgggRRYTSLVPMQLAKALDDPAATAALAELDAVLVGGGPAPAPVLDA--AAAAGINVVRTYGMSE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 844 TP---VHNsifevtepipddwtalpfGVPLPNNACRVVDdtgadcpdwvpGEYWVSGRGIARGYRGRPDLTAerFVEHDg 920
Cdd:PRK07824 187 TSggcVYD------------------GVPLDGVRVRVED-----------GRIALGGPTLAKGYRNPVDPDP--FAEPG- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 921 riWYRTGDLVRYwPDGTLEFVGRADHRVKISGYRVELGEVETALRRVPGVRTAvaaliAVSGESD------VLAAQVCAD 994
Cdd:PRK07824 235 --WFRTDDLGAL-DDGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADC-----AVFGLPDdrlgqrVVAAVVGDG 306
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 497641516 995 DASVTAEGIRQALADLVPAHMIPRHITVVERIGFTDAGKLDRRAVAR 1041
Cdd:PRK07824 307 GPAPTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVR 353
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
558-1037 |
2.44e-16 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 83.65 E-value: 2.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 558 GFFRQAEQRPDAPAVFASSGDLSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGA--VYLPIGV 635
Cdd:PRK13382 48 GFAIAAQRCPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGAdiLLLNTSF 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 636 DQPRDRA-------------ERILESGGVSLAVVCGGQRLS--MPVPEVVLADILGGAPASTEITSArvdPAALAYVLFT 700
Cdd:PRK13382 128 AGPALAEvvtregvdtviydEEFSATVDRALADCPQATRIVawTDEDHDLTVEVLIAAHAGQRPEPT---GRKGRVILLT 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 701 SGSTGEPKGVEVTHDAamntvefigrhfDIGPADRCLALSTLEGDISVMDV--------FVTLRTGGSIVVVDEVQRR-D 771
Cdd:PRK13382 205 SGTTGTPKGARRSGPG------------GIGTLKAILDRTPWRAEEPTVIVapmfhawgFSQLVLAASLACTIVTRRRfD 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 772 PDAWARLIDAHQVTVLHFMPGWLEMLVEV---GRGRLS--SVRVVPTGGDWVRPEVVRRLrVEAPGVRFAGLGGATETPV 846
Cdd:PRK13382 273 PEATLDLIDRHRATGLAVVPVMFDRIMDLpaeVRNRYSgrSLRFAAASGSRMRPDVVIAF-MDQFGDVIYNNYNATEAGM 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 847 hnsifeVTEPIPDDWTALP--FGVPLPNNACRVVDDTGADCPDWVPGEYWVSGRGIARGYRgrPDLTAERfveHDGRIwy 924
Cdd:PRK13382 352 ------IATATPADLRAAPdtAGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGYT--SGSTKDF---HDGFM-- 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 925 RTGDLVRYWPDGTLEFVGRADHRVKISGYRVELGEVETALRRVPGVrtAVAALIAVSGES--DVLAA-QVCADDASVTAE 1001
Cdd:PRK13382 419 ASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDV--AEAAVIGVDDEQygQRLAAfVVLKPGASATPE 496
|
490 500 510
....*....|....*....|....*....|....*.
gi 497641516 1002 GIRQALADLVPAHMIPRHITVVERIGFTDAGKLDRR 1037
Cdd:PRK13382 497 TLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRR 532
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
563-1037 |
1.08e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 81.51 E-value: 1.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 563 AEQRPDAPAVFASSGDLSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGA--VYLPIGVDQPR- 639
Cdd:PRK07788 59 ARRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGAriILLNTGFSGPQl 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 640 -------------------DRAERILESGGVSLAVVCGGQRLSMPVPEV-VLADILggapASTEITSARVDPAALAYVLF 699
Cdd:PRK07788 139 aevaaregvkalvyddeftDLLSALPPDLGRLRAWGGNPDDDEPSGSTDeTLDDLI----AGSSTAPLPKPPKPGGIVIL 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 700 TSGSTGEPKGVevthdaamntvefigrhfdigPADRCLALSTLEGDISVmdvfVTLRTGGSIVVVDE------------- 766
Cdd:PRK07788 215 TSGTTGTPKGA---------------------PRPEPSPLAPLAGLLSR----VPFRAGETTLLPAPmfhatgwahltla 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 767 -------VQRR--DPDAWARLIDAHQVTVLHFMPGWLEMLVEVG---RGR--LSSVRVVPTGGDWVRPEVVRRLrVEAPG 832
Cdd:PRK07788 270 malgstvVLRRrfDPEATLEDIAKHKATALVVVPVMLSRILDLGpevLAKydTSSLKIIFVSGSALSPELATRA-LEAFG 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 833 VRFAGLGGATETPVhnsifeVTEPIPDDWTALPFGVPLPNNACRVV--DDTGADCPDWVPGEYWVSGRGIARGYR-GRPD 909
Cdd:PRK07788 349 PVLYNLYGSTEVAF------ATIATPEDLAEAPGTVGRPPKGVTVKilDENGNEVPRGVVGRIFVGNGFPFEGYTdGRDK 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 910 LTAERFVEhdgriwyrTGDLVRYWPDGTLEFVGRADHRVKISGYRVELGEVETALRRVPGVRTAvaaliAVSGESDV--- 986
Cdd:PRK07788 423 QIIDGLLS--------SGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEA-----AVIGVDDEefg 489
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 497641516 987 --LAAQVC-ADDASVTAEGIRQALADLVPAHMIPRHITVVERIGFTDAGKLDRR 1037
Cdd:PRK07788 490 qrLRAFVVkAPGAALDEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKR 543
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
599-1044 |
2.21e-15 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 80.59 E-value: 2.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 599 GVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPiGVDQ--PRD--------RAERILESGGV-----SLAVVCGGQRLS 663
Cdd:cd05928 63 GLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIP-GTIQltAKDilyrlqasKAKCIVTSDELapevdSVASECPSLKTK 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 664 MPVPE------VVLADILGGA-PASTEITSARVDPAAlayVLFTSGSTGEPKGVEVTHDAAMNTVEFIGRHF-DIGPADR 735
Cdd:cd05928 142 LLVSEksrdgwLNFKELLNEAsTEHHCVETGSQEPMA---IYFTSGTTGSPKMAEHSHSSLGLGLKVNGRYWlDLTASDI 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 736 CLALSTLEGDISVMDVFVTLRTGGSIVVVDEVQRRDPDAWARLIDAHQVTVLHFMPGWLEMLVE--VGRGRLSSVRVVPT 813
Cdd:cd05928 219 MWNTSDTGWIKSAWSSLFEPWIQGACVFVHHLPRFDPLVILKTLSSYPITTFCGAPTVYRMLVQqdLSSYKFPSLQHCVT 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 814 GGDWVRPEVVRRLRVEApGVRFAGLGGATETPVHNSIFEVTEPIPDDwtalpFGVPLPNNACRVVDDTGADCPDWVPGEY 893
Cdd:cd05928 299 GGEPLNPEVLEKWKAQT-GLDIYEGYGQTETGLICANFKGMKIKPGS-----MGKASPPYDVQIIDDNGNVLPPGTEGDI 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 894 WVSGR-----GIARGYRGRPDLTAERFVehdgRIWYRTGDLVRYWPDGTLEFVGRADHRVKISGYRVELGEVETALRRVP 968
Cdd:cd05928 373 GIRVKpirpfGLFSGYVDNPEKTAATIR----GDFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHP 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 969 GVrtAVAALIA----VSGES----DVLAAQVCADDASVTAEGIRQALADLVPAHMIPRHITVVERIGFTDAGKLdRRAVA 1040
Cdd:cd05928 449 AV--VESAVVSspdpIRGEVvkafVVLAPQFLSHDPEQLTKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKI-QRNEL 525
|
....
gi 497641516 1041 RELE 1044
Cdd:cd05928 526 RDKE 529
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
529-1040 |
2.87e-15 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 80.04 E-value: 2.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 529 PPALPEAQRAVREAANGrtaepsGEALHDGFFRQAEQRPDAPAVFASSGDLSYAQLRDQALAVAAALRAAGVTAGDTIAV 608
Cdd:PRK13383 17 PPSPRAVLRLLREASRG------GTNPYTLLAVTAARWPGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 609 MGPKTAEQIPALLGILSVGAVYLPIGVDQPRDRAERILESGGVSLA---------VVCGGQRLSMPVPEVVLADILGGAP 679
Cdd:PRK13383 91 MCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAALRAHHISTVvadnefaerIAGADDAVAVIDPATAGAEESGGRP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 680 ASTeiTSARVdpaalayVLFTSGSTGEPKGVE---VTHDAAMNTVEFIGRHFDIGPADRCLALSTLEGdISVMDVFVTLR 756
Cdd:PRK13383 171 AVA--APGRI-------VLLTSGTTGKPKGVPrapQLRSAVGVWVTILDRTRLRTGSRISVAMPMFHG-LGLGMLMLTIA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 757 TGGSIVVvdevqRRDPDAWARLIDA--HQVTVLHFMPGWLEMLVEV-----GRGRLSSVRVVPTGGDWVRPEVVRRLrVE 829
Cdd:PRK13383 241 LGGTVLT-----HRHFDAEAALAQAslHRADAFTAVPVVLARILELpprvrARNPLPQLRVVMSSGDRLDPTLGQRF-MD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 830 APGVRFAGLGGATETPVHnsifevTEPIPDDWTALPFGVPLPNNAC--RVVDDTGADCPDWVPGEYWVSGrgiargyrgr 907
Cdd:PRK13383 315 TYGDILYNGYGSTEVGIG------ALATPADLRDAPETVGKPVAGCpvRILDRNNRPVGPRVTGRIFVGG---------- 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 908 pDLTAERFVEHDGRI----WYRTGDLVRYWPDGTLEFVGRADHRVKISGYRVELGEVETALRRVPGVrtAVAALIAVSGE 983
Cdd:PRK13383 379 -ELAGTRYTDGGGKAvvdgMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAV--ADNAVIGVPDE 455
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 984 --SDVLAAQVCADDAS-VTAEGIRQALADLVPAHMIPRHITVVERIGFTDAGKLDRRAVA 1040
Cdd:PRK13383 456 rfGHRLAAFVVLHPGSgVDAAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKELP 515
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
694-1045 |
8.02e-15 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that 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: 341234 [Multi-domain] Cd Length: 499 Bit Score: 78.68 E-value: 8.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 694 LAYVLFTSGSTGEPKGVEVTHDAAMNTVEFIGRHFDIGPADRCLALSTLEGDISVMDVFVTLRTGGS---IVVVDEVQRR 770
Cdd:cd05908 108 LAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMnqyLMPTRLFIRR 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 771 dPDAWARLIDAHQVTVL---HFMPGWL------EMLVEVGrgrLSSVRVVPTGGDWVRPEVVRRLR-------------- 827
Cdd:cd05908 188 -PILWLKKASEHKATIVsspNFGYKYFlktlkpEKANDWD---LSSIRMILNGAEPIDYELCHEFLdhmskyglkrnail 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 828 -----VEAP-GVRFAGLGGATETPVHNSIF--------EVTEPIPDDWTALPFGVPLPNNACRVVDDTGADCPDWVPGEY 893
Cdd:cd05908 264 pvyglAEASvGASLPKAQSPFKTITLGRRHvthgepepEVDKKDSECLTFVEVGKPIDETDIRICDEDNKILPDGYIGHI 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 894 WVSGRGIARGYRGRPDLTAERFVEhDGriWYRTGDL--VRywpDGTLEFVGRADHRVKISGYRVELGEVETALRRVPGVR 971
Cdd:cd05908 344 QIRGKNVTPGYYNNPEATAKVFTD-DG--WLKTGDLgfIR---NGRLVITGREKDIIFVNGQNVYPHDIERIAEELEGVE 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 972 TAVAALIAVSGEsdvlaaQVCADDASVTAEGiRQALADLVP-AHMIPRH-----------ITVVERIGFTDAGKLDRRAV 1039
Cdd:cd05908 418 LGRVVACGVNNS------NTRNEEIFCFIEH-RKSEDDFYPlGKKIKKHlnkrggwqineVLPIRRIPKTTSGKVKRYEL 490
|
....*.
gi 497641516 1040 ARELES 1045
Cdd:cd05908 491 AQRYQS 496
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
580-1037 |
8.33e-15 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 78.57 E-value: 8.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 580 SYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIGVDQPRDRAERILESGGVSLaVVCGG 659
Cdd:PRK08008 39 SYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASL-LVTSA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 660 QRLSM----------PVPEVVLADILGGA-PASTEITSAR-VDPAALAY-----------VLFTSGSTGEPKGVEVTHda 716
Cdd:PRK08008 118 QFYPMyrqiqqedatPLRHICLTRVALPAdDGVSSFTQLKaQQPATLCYapplstddtaeILFTSGTTSRPKGVVITH-- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 717 amNTVEFIGRHFDIGPADRclalstlEGDI--SVMDVF----------VTLRTGGSIVVVDEVQRRdpdAWARLIDAHQV 784
Cdd:PRK08008 196 --YNLRFAGYYSAWQCALR-------DDDVylTVMPAFhidcqctaamAAFSAGATFVLLEKYSAR---AFWGQVCKYRA 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 785 TVLHFMPgwleMLVEVgrgrLSSVRVVPTGGDWVRPEVVRRLRV---------EAPGVRFAGLGGATETpvhnsIFEVTE 855
Cdd:PRK08008 264 TITECIP----MMIRT----LMVQPPSANDRQHCLREVMFYLNLsdqekdafeERFGVRLLTSYGMTET-----IVGIIG 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 856 PIPDD---WTALpfGVPLPNNACRVVDDTGADCPDWVPGEYW---VSGRGIARGYRGRPDLTAERFvEHDGriWYRTGDL 929
Cdd:PRK08008 331 DRPGDkrrWPSI--GRPGFCYEAEIRDDHNRPLPAGEIGEICikgVPGKTIFKEYYLDPKATAKVL-EADG--WLHTGDT 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 930 VRYWPDGTLEFVGRADHRVKISGYRVELGEVETALRRVPGVRTAvaaliAVSGESDVLAAQ------VCADDASVTAEGI 1003
Cdd:PRK08008 406 GYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDI-----VVVGIKDSIRDEaikafvVLNEGETLSEEEF 480
|
490 500 510
....*....|....*....|....*....|....
gi 497641516 1004 RQALADLVPAHMIPRHITVVERIGFTDAGKLDRR 1037
Cdd:PRK08008 481 FAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKK 514
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
561-1037 |
9.95e-15 |
|
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.
Pssm-ID: 341270 [Multi-domain] Cd Length: 608 Bit Score: 78.76 E-value: 9.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 561 RQAEQRPDAPAVF--ASSGD----LSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPI- 633
Cdd:cd05966 61 RHLKERGDKVAIIweGDEPDqsrtITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVf 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 634 GVDQPRDRAERILESGGVSLAVVCGGQRLSMPVPEVVLAD-ILGGAP-------------------------------AS 681
Cdd:cd05966 141 AGFSAESLADRINDAQCKLVITADGGYRGGKVIPLKEIVDeALEKCPsvekvlvvkrtggevpmtegrdlwwhdlmakQS 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 682 TEITSARVDPAALAYVLFTSGSTGEPKGVEVTHD-----AAMnTVEFIgrhFDIGPADR--CLAlstlegDISVMdvfvt 754
Cdd:cd05966 221 PECEPEWMDSEDPLFILYTSGSTGKPKGVVHTTGgyllyAAT-TFKYV---FDYHPDDIywCTA------DIGWI----- 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 755 lrTGGSIVV-------VDEVQRR------DPDAWARLIDAHQVTVLHFMPGWLEMLVEVG-----RGRLSSVRVVPTGGD 816
Cdd:cd05966 286 --TGHSYIVygplangATTVMFEgtptypDPGRYWDIVEKHKVTIFYTAPTAIRALMKFGdewvkKHDLSSLRVLGSVGE 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 817 WVRPEVVRRLRveapgvRFAGLGGAtetpvhnsifevtePIPDDW----------TALPFGVPL-PNNACR--------V 877
Cdd:cd05966 364 PINPEAWMWYY------EVIGKERC--------------PIVDTWwqtetggimiTPLPGATPLkPGSATRpffgiepaI 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 878 VDDTGADCPDWVPGeYWVSGR---GIARGYRGRPdltaERFVE-----HDGriWYRTGDLVRYWPDGTLEFVGRADHRVK 949
Cdd:cd05966 424 LDEEGNEVEGEVEG-YLVIKRpwpGMARTIYGDH----ERYEDtyfskFPG--YYFTGDGARRDEDGYYWITGRVDDVIN 496
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 950 ISGYRVELGEVETALRRVPGVrtAVAALIA----VSGEsdVLAAQVCADDASVTAEGIRQALADLVpAHMI-----PRHI 1020
Cdd:cd05966 497 VSGHRLGTAEVESALVAHPAV--AEAAVVGrphdIKGE--AIYAFVTLKDGEEPSDELRKELRKHV-RKEIgpiatPDKI 571
|
570
....*....|....*..
gi 497641516 1021 TVVERIGFTDAGKLDRR 1037
Cdd:cd05966 572 QFVPGLPKTRSGKIMRR 588
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
561-1051 |
1.55e-14 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 78.13 E-value: 1.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 561 RQAEQRPDAPAVFASSG--DLSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIGVDQP 638
Cdd:PRK05857 22 EQARQQPEAIALRRCDGtsALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 639 RDRAERILESGGVSLAVVCGGQRL-SMPVPEVVLA------DILGGAPAS----------TEITSARVDPAALayvLFTS 701
Cdd:PRK05857 102 IAAIERFCQITDPAAALVAPGSKMaSSAVPEALHSipviavDIAAVTRESehsldaaslaGNADQGSEDPLAM---IFTS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 702 GSTGEPKGV-----------EVTHDAAMNTVEFIGRHFDIGPadrcLALSTLEGdisVMDVFVTLRTGGSIVVVDEvqrr 770
Cdd:PRK05857 179 GTTGEPKAVllanrtffavpDILQKEGLNWVTWVVGETTYSP----LPATHIGG---LWWILTCLMHGGLCVTGGE---- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 771 DPDAWARLIDAHQVTVLHFMPGWLEMLV---EVGRGRLSSVRVVPTGGDWVRPEVVRRlrVEAPGVRFAGLGGATET--- 844
Cdd:PRK05857 248 NTTSLLEILTTNAVATTCLVPTLLSKLVselKSANATVPSLRLVGYGGSRAIAADVRF--IEATGVRTAQVYGLSETgct 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 845 ----PVHNSIFEVTEpipddwtALPFGVPLPNNACRVVDDTGAD--CPDWVP----GEYWVSGRGIARGYRGRPDLTAER 914
Cdd:PRK05857 326 alclPTDDGSIVKIE-------AGAVGRPYPGVDVYLAATDGIGptAPGAGPsasfGTLWIKSPANMLGYWNNPERTAEV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 915 FVEHdgriWYRTGDLVRYWPDGTLEFVGRADHRVKISGYRVELGEVETALRRVPGVRTAVAALI------AVSGESDVLA 988
Cdd:PRK05857 399 LIDG----WVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIpdeefgALVGLAVVAS 474
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497641516 989 AQVcadDASVTAEgirqaLADLVPAH--------MIPRHITVVERIGFTDAGKLDRRAVARELESAVSQSQ 1051
Cdd:PRK05857 475 AEL---DESAARA-----LKHTIAARfrresepmARPSTIVIVTDIPRTQSGKVMRASLAAAATADKARVV 537
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
553-1042 |
2.17e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 77.77 E-value: 2.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 553 EALHDGFFRQAEQRPDAPAVFASSGDLSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYL- 631
Cdd:PRK06710 24 QPLHKYVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVq 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 632 --PIGVD-----QPRDRAERILESGGVSLAVVCGGQRLS-------------MPVPEVVL--------ADILGGAPASTE 683
Cdd:PRK06710 104 tnPLYTEreleyQLHDSGAKVILCLDLVFPRVTNVQSATkiehvivtriadfLPFPKNLLypfvqkkqSNLVVKVSESET 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 684 I-----------TSARV--DPAA-LAYVLFTSGSTGEPKGVEVTH-DAAMNTVEFIGRHFDIGPADRC----LALSTLEG 744
Cdd:PRK06710 184 IhlwnsvekevnTGVEVpcDPENdLALLQYTGGTTGFPKGVMLTHkNLVSNTLMGVQWLYNCKEGEEVvlgvLPFFHVYG 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 745 DISVMDVfvTLRTGGSIVVVDEVqrrDPDAWARLIDAHQVTVLHFMPGWLEMLVE---VGRGRLSSVRVVPTGGDWVRPE 821
Cdd:PRK06710 264 MTAVMNL--SIMQGYKMVLIPKF---DMKMVFEAIKKHKVTLFPGAPTIYIALLNsplLKEYDISSIRACISGSAPLPVE 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 822 VVRRLRVEAPGVRFAGLGGATETPVHNSIFEVTEPIPDDwtalpFGVPLPNNACRVVD-DTGADCPDWVPGEYWVSGRGI 900
Cdd:PRK06710 339 VQEKFETVTGGKLVEGYGLTESSPVTHSNFLWEKRVPGS-----IGVPWPDTEAMIMSlETGEALPPGEIGEIVVKGPQI 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 901 ARGYRGRPDLTAErfVEHDGriWYRTGDLVRYWPDGTLEFVGRADHRVKISGYRVELGEVETALRRVPGVRTAVAALI-- 978
Cdd:PRK06710 414 MKGYWNKPEETAA--VLQDG--WLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVpd 489
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497641516 979 AVSGESdVLAAQVCADDASVTAEGIRQALADLVPAHMIPRHITVVERIGFTDAGKLDRRAVARE 1042
Cdd:PRK06710 490 PYRGET-VKAFVVLKEGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVLIEE 552
|
|
| starter-C_NRPS |
cd19533 |
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ... |
104-522 |
2.65e-14 |
|
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. While standard C-domains catalyze peptide bond formation between two amino acids, an initial, ('starter') C-domain may instead acylate an amino acid with a fatty acid. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380456 [Multi-domain] Cd Length: 419 Bit Score: 76.64 E-value: 2.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 104 SLAPMQHAMWVGrqenQQLGGVAGHL----YVEFDGGgIDPERLRAAATALARRHPMLRVRF-LPDGT--QRIapaDEFG 176
Cdd:cd19533 3 PLTSAQRGVWFA----EQLDPEGSIYnlaeYLEITGP-VDLAVLERALRQVIAEAETLRLRFtEEEGEpyQWI---DPYT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 177 PFPVHVEDLRerstGEADRRLAA---IRAAKSHQ-QLDGAV-FELAVTLLPAERSRLHVDLDMQAADAMSYRTLMADLAA 251
Cdd:cd19533 75 PVPIRHIDLS----GDPDPEGAAqqwMQEDLRKPlPLDNDPlFRHALFTLGDNRHFWYQRVHHIVMDGFSFALFGQRVAE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 252 LYL----GRDLPElgYTYRQYRHAIEAEDA-RPQPARDADRAWWARRLPELPDPPALPTTGGRAENQSTRRWHWLDPHTR 326
Cdd:cd19533 151 IYTallkGRPAPP--APFGSFLDLVEEEQAyRQSERFERDRAFWTEQFEDLPEPVSLARRAPGRSLAFLRRTAELPPELT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 327 DALFARAQARGFTPAMALAAGFANTLARWSTTSRFLLNVPLFGR---QALHpdvdsLVGDFTSSLLLDVDLTRANTAAAR 403
Cdd:cd19533 229 RTLLEAAEAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGRlgaAARQ-----TPGMVANTLPLRLTVDPQQTFAEL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 404 AQVVQDAMRTAAAHSAYPGLAVLRDLSRHRGTQVLA-PVVFTSALGLGELFsSDVTGQFGTpgwiISQGPQVLLDAQVTE 482
Cdd:cd19533 304 VAQVSRELRSLLRHQRYRYEDLRRDLGLTGELHPLFgPTVNYMPFDYGLDF-GGVVGLTHN----LSSGPTNDLSIFVYD 378
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 497641516 483 FD--GGVLVNWDVREGVFPAGVIdAMFAHHIDELLRLASADE 522
Cdd:cd19533 379 RDdeSGLRIDFDANPALYSGEDL-ARHQERLLRLLEEAAADP 419
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
663-970 |
3.42e-14 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.
Pssm-ID: 341294 [Multi-domain] Cd Length: 507 Bit Score: 76.87 E-value: 3.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 663 SMPVpeVVLADILGG---------APASTEITSARvdPAALAYVLFTSGSTGEPKGVEVTHD---AAMNTVEFIGRHFdI 730
Cdd:cd17639 54 NIPI--VTVYATLGEdalihslneTECSAIFTDGK--PDDLACIMYTSGSTGNPKGVMLTHGnlvAGIAGLGDRVPEL-L 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 731 GPADRCLALSTLEGDISVMDVFVTLRTGGSI------VVVDEVQRR-DPDAWArlidaHQVTVLHFMP--------GWLE 795
Cdd:cd17639 129 GPDDRYLAYLPLAHIFELAAENVCLYRGGTIgygsprTLTDKSKRGcKGDLTE-----FKPTLMVGVPaiwdtirkGVLA 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 796 MLVEVGR-----------GRLSSVRVVPTGGDWVRpEVVRRLRvEAPG--VRFAGLGGA--------------------- 841
Cdd:cd17639 204 KLNPMGGlkrtlfwtayqSKLKALKEGPGTPLLDE-LVFKKVR-AALGgrLRYMLSGGAplsadtqeflnivlcpviqgy 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 842 --TETpVHNSIFEvtepIPDDWTALPFGVPLPNNACRVVD------DTGADCPDwvpGEYWVSGRGIARGYRGRPDLTAE 913
Cdd:cd17639 282 glTET-CAGGTVQ----DPGDLETGRVGPPLPCCEIKLVDweeggySTDKPPPR---GEILIRGPNVFKGYYKNPEKTKE 353
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 497641516 914 RFvehDGRIWYRTGDLVRYWPDGTLEFVGRADHRVKIS-GYRVELGEVETALRRVPGV 970
Cdd:cd17639 354 AF---DGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQnGEYIALEKLESIYRSNPLV 408
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
694-1041 |
6.10e-14 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 74.82 E-value: 6.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 694 LAYVLFTSGSTGEPKGVEVTHDAAMNTVEFIGRHFDIGPADRCL-ALSTLEGDISVMDVFVTLRTGGSIVVVDEVQRRDP 772
Cdd:cd05944 4 VAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLcGLPLFHVNGSVVTLLTPLASGAHVVLAGPAGYRNP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 773 ----DAWaRLIDAHQVTVLHFMPGWLEMLVEVGRGR-LSSVRVVPTGGDWVRPEVVRRLRvEAPGVRFAGLGGATE-TPV 846
Cdd:cd05944 84 glfdNFW-KLVERYRITSLSTVPTVYAALLQVPVNAdISSLRFAMSGAAPLPVELRARFE-DATGLPVVEGYGLTEaTCL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 847 HNSIFEVTEPIPDDwtalpFGVPLPNNACRVVDDTGA-----DC-PDWVpGEYWVSGRGIARGYrgrpdLTAERFVEHDG 920
Cdd:cd05944 162 VAVNPPDGPKRPGS-----VGLRLPYARVRIKVLDGVgrllrDCaPDEV-GEICVAGPGVFGGY-----LYTEGNKNAFV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 921 R-IWYRTGDLVRYWPDGTLEFVGRADHRVKISGYRVELGEVETALRRVPGVrtavaALIAVSGESDVLAAQV-CA----- 993
Cdd:cd05944 231 AdGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAV-----AFAGAVGQPDAHAGELpVAyvqlk 305
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 497641516 994 DDASVTAEGIRQALADLVPAH-MIPRHITVVERIGFTDAGKLDRRAVAR 1041
Cdd:cd05944 306 PGAVVEEEELLAWARDHVPERaAVPKHIEVLEELPVTAVGKVFKPALRA 354
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
699-1033 |
8.35e-14 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 75.62 E-value: 8.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 699 FTSGSTGEPKGVEVTHDAAMNTVEFIGRHFDIGPADR---------CLALstlegdisVMDVFVTLRTGGSIVVVdeVQR 769
Cdd:PRK08315 206 YTSGTTGFPKGATLTHRNILNNGYFIGEAMKLTEEDRlcipvplyhCFGM--------VLGNLACVTHGATMVYP--GEG 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 770 RDPDAWARLIDAHQVTVLHFMPG-WLEMLVEVGRGR--LSSVRvvpTG---GDWVRPEVVRRL--RVEAPGVRFAGlgGA 841
Cdd:PRK08315 276 FDPLATLAAVEEERCTALYGVPTmFIAELDHPDFARfdLSSLR---TGimaGSPCPIEVMKRVidKMHMSEVTIAY--GM 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 842 TET-PVhnsifeVTEPIPDDwtalPF-------GVPLPNNACRVVD-DTGADCPDWVPGEYWVSGRGIARGYRGRPDLTA 912
Cdd:PRK08315 351 TETsPV------STQTRTDD----PLekrvttvGRALPHLEVKIVDpETGETVPRGEQGELCTRGYSVMKGYWNDPEKTA 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 913 ERfVEHDGriWYRTGDLVRYWPDGTLEFVGradhRVK---ISG----Y-RvelgEVETALRRVPGVRTavAALIAVS--- 981
Cdd:PRK08315 421 EA-IDADG--WMHTGDLAVMDEEGYVNIVG----RIKdmiIRGgeniYpR----EIEEFLYTHPKIQD--VQVVGVPdek 487
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 497641516 982 -GEsdvlaaQVCA-----DDASVTAEGIRQALADLVPAHMIPRHITVVERIGFTDAGK 1033
Cdd:PRK08315 488 yGE------EVCAwiilrPGATLTEEDVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGK 539
|
|
| E_NRPS |
cd19534 |
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
102-386 |
1.22e-13 |
|
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Epimerization (E) domains of nonribosomal peptide synthetases (NRPS) flip the chirality of the end amino acid of a peptide being manufactured by the NRPS. E-domains are homologous to the Condensation (C) domains. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Specialized tailoring NRPS domains such as E-domains greatly increase the range of possible peptide products created by the NRPS machinery. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the E-domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380457 [Multi-domain] Cd Length: 428 Bit Score: 74.60 E-value: 1.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 102 PFSLAPMQHamWVGRQE-------NQQLggvagHLYVEfdgGGIDPERLRAAATALARRHPMLRVRFLPDG---TQRIAP 171
Cdd:cd19534 1 EVPLTPIQR--WFFEQNlagrhhfNQSV-----LLRVP---QGLDPDALRQALRALVEHHDALRMRFRREDggwQQRIRG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 172 ADEfGPFPVHVEDLRErSTGEADRRLAAIRAAKSHQQLDGAVFELAVTLLPAERSRLHVDLDMQAADAMSYRTLMADLAA 251
Cdd:cd19534 71 DVE-ELFRLEVVDLSS-LAQAAAIEALAAEAQSSLDLEEGPLLAAALFDGTDGGDRLLLVIHHLVVDGVSWRILLEDLEA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 252 LY---LGRDLPELGYT--YRQYrhAIEAEDARPQPARDADRAWWARRLPelPDPPALP----TTGGRAENQSTRrwhwLD 322
Cdd:cd19534 149 AYeqaLAGEPIPLPSKtsFQTW--AELLAEYAQSPALLEELAYWRELPA--ADYWGLPkdpeQTYGDARTVSFT----LD 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497641516 323 PHTRDALFARAQARGFT-PAMALAAGFANTLARWSTTSRFLLNVPLFGRQALHPDVD--SLVGDFTS 386
Cdd:cd19534 221 EEETEALLQEANAAYRTeINDLLLAALALAFQDWTGRAPPAIFLEGHGREEIDPGLDlsRTVGWFTS 287
|
|
| AcpA |
COG3433 |
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ... |
865-1136 |
1.80e-13 |
|
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442659 [Multi-domain] Cd Length: 295 Bit Score: 72.48 E-value: 1.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 865 PFGVPLPNNACRVVDDTGADCPDWVPGEYWVSGRGIARGYRGRPDLTAERFVEHDGRIW----------YRTGDLVRYWP 934
Cdd:COG3433 13 PDEPPPVIPPAIVQARALLLIVDLQGYFGGFGGEGGLLGAGLLLRIRLLAAAARAPFIPvpypaqpgrqADDLRLLLRRG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 935 DGTLEFVGRADHRVKISGYRVELGEVETALRRVPGVRTAVAALIAVSGESDVLAAQVCADDASVTAEGIRQALADLVPAH 1014
Cdd:COG3433 93 LGPGGGLERLVQQVVIRAERGEEEELLLVLRAAAVVRVAVLAALRGAGVGLLLIVGAVAALDGLAAAAALAALDKVPPDV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 1015 MIPRHITVVERIGFTDAGKLDRRAVARELESAVSQSQRPGHRAPSTPLQSALATIVGDLLG--RQNIGIDDDFFALGGDS 1092
Cdd:COG3433 173 VAASAVVALDALLLLALKVVARAAPALAAAEALLAAASPAPALETALTEEELRADVAELLGvdPEEIDPDDNLFDLGLDS 252
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 497641516 1093 VLATQAVARIRAwlDAPDIMVADIFANRTVSALAAVLGAGERDP 1136
Cdd:COG3433 253 IRLMQLVERWRK--AGLDVSFADLAEHPTLAAWWALLAAAQAAA 294
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
603-1037 |
2.90e-13 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 74.14 E-value: 2.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 603 GDTIAVMGPKTAEQIPALLGILSVGAVYLPIG-VDQPRDRAERILESGGVSLAVVCG-----GQRLS-MPVPEVV---LA 672
Cdd:PRK08751 76 GDRVALMMPNCLQYPIATFGVLRAGLTVVNVNpLYTPRELKHQLIDSGASVLVVIDNfgttvQQVIAdTPVKQVIttgLG 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 673 DILGGAPAST---------------------------------EITSARVDPAALAYVLFTSGSTGEPKGVEVTHD---A 716
Cdd:PRK08751 156 DMLGFPKAALvnfvvkyvkklvpeyringairfrealalgrkhSMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRnlvA 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 717 AMNTV-EFIGRHFDIGPADRCL--ALSTLEGDISVMDVFVTLRTGGSIVVVDevQRRDPDAWARLIDAHQVTV------- 786
Cdd:PRK08751 236 NMQQAhQWLAGTGKLEEGCEVVitALPLYHIFALTANGLVFMKIGGCNHLIS--NPRDMPGFVKELKKTRFTAftgvntl 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 787 ---LHFMPGWLEMlvevgrgRLSSVRVVPTGGDWVRPEVVRRLRvEAPGVRFAGLGGATETPVHNSIFEVTEPipdDWTA 863
Cdd:PRK08751 314 fngLLNTPGFDQI-------DFSSLKMTLGGGMAVQRSVAERWK-QVTGLTLVEAYGLTETSPAACINPLTLK---EYNG 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 864 lPFGVPLPNNACRVVDDTGADCPDWVPGEYWVSGRGIARGYRGRPDLTAErFVEHDGriWYRTGDLVRYWPDGTLEFVGR 943
Cdd:PRK08751 383 -SIGLPIPSTDACIKDDAGTVLAIGEIGELCIKGPQVMKGYWKRPEETAK-VMDADG--WLHTGDIARMDEQGFVYIVDR 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 944 ADHRVKISGYRVELGEVETALRRVPGVRTAVAALIAVSGESDVLAAQVCADDASVTAEGIRQALADLVPAHMIPRHITVV 1023
Cdd:PRK08751 459 KKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVIVKKDPALTAEDVKAHARANLTGYKQPRIIEFR 538
|
490
....*....|....
gi 497641516 1024 ERIGFTDAGKLDRR 1037
Cdd:PRK08751 539 KELPKTNVGKILRR 552
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
693-1043 |
3.82e-13 |
|
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341297 [Multi-domain] Cd Length: 532 Bit Score: 73.33 E-value: 3.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 693 ALAYVLFTSGSTGEPKGVEVTHdaaMNTVEFIGRHFD------IGPADRCLALSTLEGDISVMDVFVTLRTGGSIVVVde 766
Cdd:cd17642 185 QVALIMNSSGSTGLPKGVQLTH---KNIVARFSHARDpifgnqIIPDTAILTVIPFHHGFGMFTTLGYLICGFRVVLM-- 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 767 vQRRDPDAWARLIDAHQVTVLHFMPGWLEMLVE---VGRGRLSSVRVVPTGGDWVRPEV---VRRlRVEAPGVRfAGLGg 840
Cdd:cd17642 260 -YKFEEELFLRSLQDYKVQSALLVPTLFAFFAKstlVDKYDLSNLHEIASGGAPLSKEVgeaVAK-RFKLPGIR-QGYG- 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 841 ATETpvhNSIFEVTePIPDDWTAlPFGVPLPNNACRVVD-DTGADCPDWVPGEYWVSGRGIARGYRGRPDLTAErFVEHD 919
Cdd:cd17642 336 LTET---TSAILIT-PEGDDKPG-AVGKVVPFFYAKVVDlDTGKTLGPNERGELCVKGPMIMKGYVNNPEATKA-LIDKD 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 920 GriWYRTGDLVRYWPDGTLEFVGRADHRVKISGYRVELGEVETALRRVPGVRTAvaaliAVSGESDVLAAQ------VCA 993
Cdd:cd17642 410 G--WLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDA-----GVAGIPDEDAGElpaavvVLE 482
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 497641516 994 DDASVTAEGIRQALADLV-PAHMIPRHITVVERIGFTDAGKLDRRAVaREL 1043
Cdd:cd17642 483 AGKTMTEKEVMDYVASQVsTAKRLRGGVKFVDEVPKGLTGKIDRRKI-REI 532
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
578-951 |
5.75e-13 |
|
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341255 [Multi-domain] Cd Length: 508 Bit Score: 72.89 E-value: 5.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 578 DLSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIGVDQPRDRAERILESGGVSL---- 653
Cdd:cd05932 6 EFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKAlfvg 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 654 ---------AVVCGG-QRLSMPVPEVVLA-----DILGGAPASTEITsaRVDPAALAYVLFTSGSTGEPKGVEVTHDAAM 718
Cdd:cd05932 86 klddwkamaPGVPEGlISISLPPPSAANCqyqwdDLIAQHPPLEERP--TRFPEQLATLIYTSGTTGQPKGVMLTFGSFA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 719 NTVEFIGRHFDIGPADRCLALSTLEGDISVMDVFVTLRTGGSIVV--------VDEVQRRDPDAW---ARLIDAHQVTVL 787
Cdd:cd05932 164 WAAQAGIEHIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVAfaesldtfVEDVQRARPTLFfsvPRLWTKFQQGVQ 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 788 HFMPgwlemlvevgRGRLSSVRVVPTGGDWVRPEVVRRLRVEApgVRFAGLGGAtetPVHNSIFE----VTEPIPDDW-- 861
Cdd:cd05932 244 DKIP----------QQKLNLLLKIPVVNSLVKRKVLKGLGLDQ--CRLAGCGSA---PVPPALLEwyrsLGLNILEAYgm 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 862 --------TALPF-------GVPLPNNACRVVDDtgadcpdwvpGEYWVSGRGIARGYRGRPDLTAERFVEhDGriWYRT 926
Cdd:cd05932 309 tenfayshLNYPGrdkigtvGNAGPGVEVRISED----------GEILVRSPALMMGYYKDPEATAEAFTA-DG--FLRT 375
|
410 420
....*....|....*....|....*
gi 497641516 927 GDLVRYWPDGTLEFVGRADHRVKIS 951
Cdd:cd05932 376 GDKGELDADGNLTITGRVKDIFKTS 400
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
925-1037 |
5.95e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 72.38 E-value: 5.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 925 RTGDLvRYWP-DGTLEFVGRADHRVKISGYRVELGEVETALRRVPGVRTAVA--ALIAVSGEsdVLAAQVCADDASVTAE 1001
Cdd:PRK08308 294 FTKDL-GYKSeRGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVyrGKDPVAGE--RVKAKVISHEEIDPVQ 370
|
90 100 110
....*....|....*....|....*....|....*.
gi 497641516 1002 gIRQALADLVPAHMIPRHITVVERIGFTDAGKLDRR 1037
Cdd:PRK08308 371 -LREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRK 405
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
571-1037 |
1.02e-12 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 71.86 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 571 AVFASSGD-LSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIGVDQPRDRAERILESG 649
Cdd:PRK08276 3 VIMAPSGEvVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 650 G-----VS--LAVVCGGQRLSMPVPEVVLADILGGAPASTEITSARV--------DPAALAYVLFTSGSTGEPKGV--EV 712
Cdd:PRK08276 83 GakvliVSaaLADTAAELAAELPAGVPLLLVVAGPVPGFRSYEEALAaqpdtpiaDETAGADMLYSSGTTGRPKGIkrPL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 713 TH----DAAMNTVEFIGRHFDIGPADRCLALSTLEgDISVMDVFVTLRTGGSIVVVDEvqRRDPDAWARLIDAHQVTVLH 788
Cdd:PRK08276 163 PGldpdEAPGMMLALLGFGMYGGPDSVYLSPAPLY-HTAPLRFGMSALALGGTVVVME--KFDAEEALALIERYRVTHSQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 789 FMPgwlEMLV-------EVgRGR--LSSVRVVPTGGDWVRPEVVRRLrVEAPGvrfaglggatetPVHNSIFEVTEPI-- 857
Cdd:PRK08276 240 LVP---TMFVrmlklpeEV-RARydVSSLRVAIHAAAPCPVEVKRAM-IDWWG------------PIIHEYYASSEGGgv 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 858 ----PDDWTALPFGVPLPNNA-CRVVDDTGADCPDWVPGEYWVSGRGIARGYRGRPDLTAERFVEHDgriWYRTGDLVRY 932
Cdd:PRK08276 303 tvitSEDWLAHPGSVGKAVLGeVRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARNPHG---WVTVGDVGYL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 933 WPDGTLEFVGRADHRVkISGyrvelG------EVETALRRVPGVrtAVAALIAVS----GESDVLAAQV--CADDASVTA 1000
Cdd:PRK08276 380 DEDGYLYLTDRKSDMI-ISG-----GvniypqEIENLLVTHPKV--ADVAVFGVPdeemGERVKAVVQPadGADAGDALA 451
|
490 500 510
....*....|....*....|....*....|....*..
gi 497641516 1001 EGIRQALADLVPAHMIPRHITVVERIGFTDAGKLDRR 1037
Cdd:PRK08276 452 AELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKR 488
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
566-1039 |
1.56e-12 |
|
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: 71.25 E-value: 1.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 566 RPDAPAVFASSGDLSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIGVDQPRDRAERI 645
Cdd:cd05929 5 DLDRAQVFHQRRLLLLDVYSIALNRNARAAAAEGVWIADGVYIYLINSILTVFAAAAAWKCGACPAYKSSRAPRAEACAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 646 LESGGvsLAVVCGgqRLSMPVPEVVLADILGGAPASTEITSARVdpAALAYVLFTSGSTGEPKGVEVTHDAAMNTVE-FI 724
Cdd:cd05929 85 IEIKA--AALVCG--LFTGGGALDGLEDYEAAEGGSPETPIEDE--AAGWKMLYSGGTTGRPKGIKRGLPGGPPDNDtLM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 725 GRHFDIGP--ADRCLALSTLEGDISVMDVFVTLRTGGSIVVVdevQRRDPDAWARLIDAHQVTVLHFMPGW---LEMLVE 799
Cdd:cd05929 159 AAALGFGPgaDSVYLSPAPLYHAAPFRWSMTALFMGGTLVLM---EKFDPEEFLRLIERYRVTFAQFVPTMfvrLLKLPE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 800 VGRGR--LSSVR-VVPTGGdwVRPEVVRRLRVEAPGVRFAGLGGATE---TPVHNSifevtepipDDWTALP--FGVPLP 871
Cdd:cd05929 236 AVRNAydLSSLKrVIHAAA--PCPPWVKEQWIDWGGPIIWEYYGGTEgqgLTIING---------EEWLTHPgsVGRAVL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 872 NNACrVVDDTGADCPDWVPGEYWVSGrGIARGYRGRPDLTAERFVEHDgriWYRTGDLVRYWPDGTLEFVGRADHRVKIS 951
Cdd:cd05929 305 GKVH-ILDEDGNEVPPGEIGEVYFAN-GPGFEYTNDPEKTAAARNEGG---WSTLGDVGYLDEDGYLYLTDRRSDMIISG 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 952 GYRVELGEVETALRRVPGVRTAVAALIAVSGESDVLAAQV----CADDASVTAEGIRQALADLVPAHMIPRHITVVERIG 1027
Cdd:cd05929 380 GVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVqpapGADAGTALAEELIAFLRDRLSRYKCPRSIEFVAELP 459
|
490
....*....|..
gi 497641516 1028 FTDAGKLDRRAV 1039
Cdd:cd05929 460 RDDTGKLYRRLL 471
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
561-1046 |
1.80e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 71.52 E-value: 1.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 561 RQAEQRPDAPAVFASSGDLSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIGVdqpRD 640
Cdd:PRK08162 26 RAAEVYPDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNT---RL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 641 RAERI---LESGGVSLAVV--------------CGGQRLsmPVPEVVLADILGGAPAST---EITSARVDPA-------- 692
Cdd:PRK08162 103 DAASIafmLRHGEAKVLIVdtefaevarealalLPGPKP--LVIDVDDPEYPGGRFIGAldyEAFLASGDPDfawtlpad 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 693 -----ALAYvlfTSGSTGEPKGVeVTHD--AAMNTVEFIgRHFDIGPadRCLALSTLEgdisvmdVF----------VTL 755
Cdd:PRK08162 181 ewdaiALNY---TSGTTGNPKGV-VYHHrgAYLNALSNI-LAWGMPK--HPVYLWTLP-------MFhcngwcfpwtVAA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 756 RTGGSIVvvdeVQRRDPDAWARLIDAHQVTVLHFMPGWLEMLV----EVGRGRLSSVRVVPTGGDwvrPEVVRRLRVEAP 831
Cdd:PRK08162 247 RAGTNVC----LRKVDPKLIFDLIREHGVTHYCGAPIVLSALInapaEWRAGIDHPVHAMVAGAA---PPAAVIAKMEEI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 832 GVRFAGLGGATETPVHNSIFEVTepipDDWTALPF----------GVPLP-NNACRVVD-DTGADcpdwVP------GEY 893
Cdd:PRK08162 320 GFDLTHVYGLTETYGPATVCAWQ----PEWDALPLderaqlkarqGVRYPlQEGVTVLDpDTMQP----VPadgetiGEI 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 894 WVSGRGIARGYRGRPDLTAERFveHDGriWYRTGDLVRYWPDGTLEFVGRADHrVKISGyrvelG------EVETALRRV 967
Cdd:PRK08162 392 MFRGNIVMKGYLKNPKATEEAF--AGG--WFHTGDLAVLHPDGYIKIKDRSKD-IIISG-----GenissiEVEDVLYRH 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 968 PGVrtAVAALIAVS----GESDvlaaqvCA-----DDASVTAEGIRQALADLVPAHMIPRHITVVErIGFTDAGKLDR-- 1036
Cdd:PRK08162 462 PAV--LVAAVVAKPdpkwGEVP------CAfvelkDGASATEEEIIAHCREHLAGFKVPKAVVFGE-LPKTSTGKIQKfv 532
|
570
....*....|.
gi 497641516 1037 -RAVARELESA 1046
Cdd:PRK08162 533 lREQAKSLKAI 543
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
552-1038 |
4.01e-12 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 70.40 E-value: 4.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 552 GEALHDGFFRQAEqrPDAPAVFASSGDLSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAE---QIPALL--GILSV 626
Cdd:PRK10946 24 DLPLTDILTRHAA--SDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEfyiTFFALLklGVAPV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 627 GAVY------LPIGVDQ--PR----DRAERILESGGV--SLAVVCggqrlsmPVPEVVLadiLGGAPASTEITSARVDPA 692
Cdd:PRK10946 102 NALFshqrseLNAYASQiePAlliaDRQHALFSDDDFlnTLVAEH-------SSLRVVL---LLNDDGEHSLDDAINHPA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 693 A-----------LAYVLFTSGSTGEPKGVEVTHD----AAMNTVEFIG-----RHFDIGPADRCLALSTlEGDISVmdvf 752
Cdd:PRK10946 172 EdftatpspadeVAFFQLSGGSTGTPKLIPRTHNdyyySVRRSVEICGftpqtRYLCALPAAHNYPMSS-PGALGV---- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 753 vtLRTGGSIVVVdevqrRDPDAWA--RLIDAHQVTVLHFMPG----WLEMLVEVG-RGRLSSVRVVPTGGDWVRPEVVRR 825
Cdd:PRK10946 247 --FLAGGTVVLA-----PDPSATLcfPLIEKHQVNVTALVPPavslWLQAIAEGGsRAQLASLKLLQVGGARLSETLARR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 826 LRVEApGVRFAGLGGATETPVHNSIFEvtepIPDDWTALPFGVPL-PNNACRVVDDTGADCPDWVPGEYWVSGRGIARGY 904
Cdd:PRK10946 320 IPAEL-GCQLQQVFGMAEGLVNYTRLD----DSDERIFTTQGRPMsPDDEVWVADADGNPLPQGEVGRLMTRGPYTFRGY 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 905 RGRPDLTAERFvehDGRIWYRTGDLVRYWPDGTLEFVGRADHRVKISGYRVELGEVETALRRVPGVrtAVAALIAVsgES 984
Cdd:PRK10946 395 YKSPQHNASAF---DANGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAV--IHAALVSM--ED 467
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497641516 985 DVLAAQVCAddASVTAEGIR----------QALADlvpaHMIPRHITVVERIGFTDAGKLDRRA 1038
Cdd:PRK10946 468 ELMGEKSCA--FLVVKEPLKavqlrrflreQGIAE----FKLPDRVECVDSLPLTAVGKVDKKQ 525
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
599-1042 |
4.75e-12 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 69.77 E-value: 4.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 599 GVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIGVDqprdraerilesggvslavvcggqrlsmpvpevvladiLGGA 678
Cdd:cd05937 27 GVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYN--------------------------------------LSGD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 679 PA--STEITSAR---VDPAALAYVLFTSGSTGEPKGVEVTHDAAMNTVEFIGRHFDIGPADR---CLALstLEGDISVMD 750
Cdd:cd05937 69 PLihCLKLSGSRfviVDPDDPAILIYTSGTTGLPKAAAISWRRTLVTSNLLSHDLNLKNGDRtytCMPL--YHGTAAFLG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 751 VFVTLRTGGSIVVVDEVQRRDpdAWARLIDAhQVTVLHFMPgwlemlvEVGRGRLS----------SVRVVptGGDWVRP 820
Cdd:cd05937 147 ACNCLMSGGTLALSRKFSASQ--FWKDVRDS-GATIIQYVG-------ELCRYLLStppspydrdhKVRVA--WGNGLRP 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 821 EVVRRLR----VEAPGVRFAGLGGATETPVHNSifevtepipDDWTA-------------LPFGVPL----PNNACRVVD 879
Cdd:cd05937 215 DIWERFRerfnVPEIGEFYAATEGVFALTNHNV---------GDFGAgaighhglirrwkFENQVVLvkmdPETDDPIRD 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 880 D-TG--ADCPDWVPGEYWV----SGRGIARGYRGRPDLTAERFVE---HDGRIWYRTGDLVRYWPDGTLEFVGRADHRVK 949
Cdd:cd05937 286 PkTGfcVRAPVGEPGEMLGrvpfKNREAFQGYLHNEDATESKLVRdvfRKGDIYFRTGDLLRQDADGRWYFLDRLGDTFR 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 950 ISGYRVELGEVETALRRVPGVRTAVAALIAVSGESDVLAAQVCA--DDASVTAEGIRQALADL----VPAHMIPRHITVV 1023
Cdd:cd05937 366 WKSENVSTTEVADVLGAHPDIAEANVYGVKVPGHDGRAGCAAITleESSAVPTEFTKSLLASLarknLPSYAVPLFLRLT 445
|
490
....*....|....*....
gi 497641516 1024 ERIGFTDAGKLDRRAVARE 1042
Cdd:cd05937 446 EEVATTDNHKQQKGVLRDE 464
|
|
| DCL_NRPS |
cd19543 |
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ... |
105-424 |
6.04e-12 |
|
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor; The DCL-type Condensation (C) domain catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. This domain is D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains in addition to the LCL- and DCL-types such as starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380465 [Multi-domain] Cd Length: 423 Bit Score: 69.15 E-value: 6.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 105 LAPMQHAMWVGRQENQQLGgvaghLYVE---FD-GGGIDPERLRAAATALARRHPMLRVRFLPDGTQR---IAPADefGP 177
Cdd:cd19543 4 LSPMQEGMLFHSLLDPGSG-----AYVEqmvITlEGPLDPDRFRAAWQAVVDRHPILRTSFVWEGLGEplqVVLKD--RK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 178 FPVHVEDLRERSTGEADRRLAAIRAAKSHQQLD---GAVFELAVTLLPAERSRL-----HVDLdmqaaDAMSYRTLMADL 249
Cdd:cd19543 77 LPWRELDLSHLSEAEQEAELEALAEEDRERGFDlarAPLMRLTLIRLGDDRYRLvwsfhHILL-----DGWSLPILLKEL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 250 AALYLGR---DLPELGYT--YRQYRHAIEAEDarpqpaRDADRAWWARRLPELPDPPALPTTGGRAENQSTRR---WHWL 321
Cdd:cd19543 152 FAIYAALgegQPPSLPPVrpYRDYIAWLQRQD------KEAAEAYWREYLAGFEEPTPLPKELPADADGSYEPgevSFEL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 322 DPHTRDALFARAQARGFTPAMALAAGFANTLARWSTTSRFLLNVPLFGRQALHPDVDSLVGDFTSSLLLDVDLTRANTAA 401
Cdd:cd19543 226 SAELTARLQELARQHGVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGRPAELPGIETMVGLFINTLPVRVRLDPDQTVL 305
|
330 340
....*....|....*....|...
gi 497641516 402 ARAQVVQDAMRTAAAHSaYPGLA 424
Cdd:cd19543 306 ELLKDLQAQQLELREHE-YVPLY 327
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
667-1048 |
1.62e-11 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 68.84 E-value: 1.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 667 PEVVLADILGG--APASTEITSARVDPAALAYVLFTSGSTGEPKGVEVTHDAAMNTVEFIGRHFDIGPADRCLalstleg 744
Cdd:PRK06814 766 AQIGLADKIKGllAGRFPLVYFCNRDPDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPEDKVF------- 838
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 745 diSVMDVFVTL-RTGGSIV-VVDEVQ----------RRDPDawarLIDAHQVTVLH----FMPGWLEMLVEVGrgrLSSV 808
Cdd:PRK06814 839 --NALPVFHSFgLTGGLVLpLLSGVKvflypsplhyRIIPE----LIYDTNATILFgtdtFLNGYARYAHPYD---FRSL 909
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 809 RVVPTGGDWVRPEVvRRLRVEAPGVRFAGLGGATE--------TPVHNSIFEVtepipddwtalpfGVPLPNNACRVVDD 880
Cdd:PRK06814 910 RYVFAGAEKVKEET-RQTWMEKFGIRILEGYGVTEtapvialnTPMHNKAGTV-------------GRLLPGIEYRLEPV 975
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 881 TGADcpdwVPGEYWVSGRGIARGYrgrpdLTAER--FVEHDGRIWYRTGDLVRYWPDGTLEFVGRADHRVKISGYRVELG 958
Cdd:PRK06814 976 PGID----EGGRLFVRGPNVMLGY-----LRAENpgVLEPPADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLA 1046
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 959 EVETALRRV-PGVRTAVAALI-AVSGESDVLaaqvCADDASVT-AEGIRQALADLVPAHMIPRHITVVERIGFTDAGKLD 1035
Cdd:PRK06814 1047 AVEELAAELwPDALHAAVSIPdARKGERIIL----LTTASDATrAAFLAHAKAAGASELMVPAEIITIDEIPLLGTGKID 1122
|
410
....*....|...
gi 497641516 1036 RRAVARELESAVS 1048
Cdd:PRK06814 1123 YVAVTKLAEEAAA 1135
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
529-739 |
1.73e-11 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 68.36 E-value: 1.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 529 PPALPEAQRAVREAANGRTAEPSGEA-LHDGFFRQAEQRPDAPAVFASSGDLSYAQLRDQALAVAAALRAAGVTAGDTIA 607
Cdd:PRK08279 12 PRRLPDLPGILRGLKRTALITPDSKRsLGDVFEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 608 VMGPKTAEQIPALLGILSVGAVY-----------LP--IGVDQPR------DRAERILESGG-VSLAV---VCGGQRLSM 664
Cdd:PRK08279 92 LLMENRPEYLAAWLGLAKLGAVVallntqqrgavLAhsLNLVDAKhlivgeELVEAFEEARAdLARPPrlwVAGGDTLDD 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497641516 665 PVPEVVLADILGGAPASTEITSARVDPAALAYVLFTSGSTGEPKGVEVTHDAAMNTVEFIGRHFDIGPADR---CLAL 739
Cdd:PRK08279 172 PEGYEDLAAAAAGAPTTNPASRSGVTAKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDVlycCLPL 249
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
563-1037 |
2.89e-11 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 67.41 E-value: 2.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 563 AEQRPDAPAV-FASSGD-LSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIGVDQPRD 640
Cdd:PRK13391 7 AQTTPDKPAViMASTGEvVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 641 RAERILESGGVSLAVVCGGQR-----LSMPVPEVVLADILGGAPASTEITsaRVDPAALAY-------------VLFTSG 702
Cdd:PRK13391 87 EAAYIVDDSGARALITSAAKLdvaraLLKQCPGVRHRLVLDGDGELEGFV--GYAEAVAGLpatpiadeslgtdMLYSSG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 703 STGEPKGV-----EVTHDAAMNTVEFIGRHFDIGPADRCLALSTLEGDISVMDVFVTLRTGGSIVVVDevqRRDPDAWAR 777
Cdd:PRK13391 165 TTGRPKGIkrplpEQPPDTPLPLTAFLQRLWGFRSDMVYLSPAPLYHSAPQRAVMLVIRLGGTVIVME---HFDAEQYLA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 778 LIDAHQVTVLHFMPG-WLEMLV--EVGRGR--LSSVRVVPTGGDWVRPEVVRRLrveapgVRFAGlggatetPVHNSIFE 852
Cdd:PRK13391 242 LIEEYGVTHTQLVPTmFSRMLKlpEEVRDKydLSSLEVAIHAAAPCPPQVKEQM------IDWWG-------PIIHEYYA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 853 VTEPI------PDDWTALP-------FGVPlpnnacRVVDDTGADCPDWVPGEYWVSGrGIARGYRGRPDLTAERFVEHD 919
Cdd:PRK13391 309 ATEGLgftacdSEEWLAHPgtvgramFGDL------HILDDDGAELPPGEPGTIWFEG-GRPFEYLNDPAKTAEARHPDG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 920 GriWYRTGDLVRYWPDGTLEFVGRADHRVKISGYRVELGEVETALRRVPGVrtAVAALIAVSGE---SDVLAAQVCAD-- 994
Cdd:PRK13391 382 T--WSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKV--ADAAVFGVPNEdlgEEVKAVVQPVDgv 457
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 497641516 995 --DASVTAEGI---RQALAdlvpAHMIPRHITVVERIGFTDAGKLDRR 1037
Cdd:PRK13391 458 dpGPALAAELIafcRQRLS----RQKCPRSIDFEDELPRLPTGKLYKR 501
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
599-1059 |
7.23e-11 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 66.34 E-value: 7.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 599 GVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIGVDQPRDRAERILESGGVSLAVV---CGGQ--RLSMPVPEVVLAD 673
Cdd:PRK05620 60 GITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIVAdprLAEQlgEILKECPCVRAVV 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 674 ILGGAPASTEITSAR-----------------------VDPAALAYVLFTSGSTGEPKGVEVTHDA----AMN--TVEfi 724
Cdd:PRK05620 140 FIGPSDADSAAAHMPegikvysyealldgrstvydwpeLDETTAAAICYSTGTTGAPKGVVYSHRSlylqSLSlrTTD-- 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 725 grHFDIGPADRCLALSTLEGDISVMDVFVTLRTGGSIVVVDEvqRRDPDAWARLIDAHQVTVLHFMPG-WLEMLVEVGRG 803
Cdd:PRK05620 218 --SLAVTHGESFLCCVPIYHVLSWGVPLAAFMSGTPLVFPGP--DLSAPTLAKIIATAMPRVAHGVPTlWIQLMVHYLKN 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 804 --RLSSVRVVPTGGDWVRPEVVRrLRVEAPGVRFAGLGGATETpvhNSIFEVTEPipddwtalPFGVPLPNNAC------ 875
Cdd:PRK05620 294 ppERMSLQEIYVGGSAVPPILIK-AWEERYGVDVVHVWGMTET---SPVGTVARP--------PSGVSGEARWAyrvsqg 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 876 --------RVVDD----TGADCP--------DWVPGEYWVS----GRGIARGYRGRP-DLTAERFVEhDGriWYRTGDLV 930
Cdd:PRK05620 362 rfpasleyRIVNDgqvmESTDRNegeiqvrgNWVTASYYHSpteeGGGAASTFRGEDvEDANDRFTA-DG--WLRTGDVG 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 931 RYWPDGTLEFVGRADHRVKISGYRVELGEVETALRRVPGVRTAvaALIAVSGESDV---LAAQVCADDAS---VTAEGIR 1004
Cdd:PRK05620 439 SVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVEC--AVIGYPDDKWGerpLAVTVLAPGIEptrETAERLR 516
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 497641516 1005 QALADLVPAHMIPRHITVVERIGFTDAGKLDR---RAVARELESAVSQSQRPGHRAPS 1059
Cdd:PRK05620 517 DQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKkdlRQHLADGDFEIIKLKGPGESGES 574
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
600-1061 |
1.09e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 65.91 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 600 VTA-GDTIAVMGPKTAEQIPALLGILSVGAVYLPIGVDQPRDRAER------------ILESGGVSLAV------VCGGQ 660
Cdd:PRK07769 75 VTKpGDRVAILAPQNLDYLIAFFGALYAGRIAVPLFDPAEPGHVGRlhavlddctpsaILTTTDSAEGVrkffraRPAKE 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 661 RlsmpvPEVVLADILggaPASTEITSARVDPA--ALAYVLFTSGSTGEPKGVEVTHDAAMNTVEFIGRHFDIGPADRCLA 738
Cdd:PRK07769 155 R-----PRVIAVDAV---PDEVGATWVPPEANedTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEGQEGDRGVS 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 739 LSTLEGDISVMDVFVTLRTGGSIVVVDevqrrdPDAWARlidahqvtvlhfMPG-WLEMLVEVGRGR------------- 804
Cdd:PRK07769 227 WLPFFHDMGLITVLLPALLGHYITFMS------PAAFVR------------RPGrWIRELARKPGGTggtfsaapnfafe 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 805 ----------------LSSVRVVPTGGDWVRPEVVRRLRvEApgvrFA-------------GLGGAT----ETPVHNS-- 849
Cdd:PRK07769 289 haaarglpkdgeppldLSNVKGLLNGSEPVSPASMRKFN-EA----FApyglpptaikpsyGMAEATlfvsTTPMDEEpt 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 850 -IF---------EVTEPIPDDWTALPF----GVPLPNNACRVVDDTGADCPDWVPGEYWVSGRGIARGYRGRPDLTAERF 915
Cdd:PRK07769 364 vIYvdrdelnagRFVEVPADAPNAVAQvsagKVGVSEWAVIVDPETASELPDGQIGEIWLHGNNIGTGYWGKPEETAATF 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 916 ---------------VEHDGRiWYRTGDLVRYWpDGTLEFVGRADHRVKISGYRVELGEVE-TALRRVPGVRTAVAALIA 979
Cdd:PRK07769 444 qnilksrlseshaegAPDDAL-WVRTGDYGVYF-DGELYITGRVKDLVIIDGRNHYPQDLEyTAQEATKALRTGYVAAFS 521
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 980 V-----------------------SGESDVLAAQVCA----DDASVTAEGIRQALAD----------LVPAHMIPRhitv 1022
Cdd:PRK07769 522 VpanqlpqvvfddshaglkfdpedTSEQLVIVAERAPgahkLDPQPIADDIRAAIAVrhgvtvrdvlLVPAGSIPR---- 597
|
570 580 590
....*....|....*....|....*....|....*....
gi 497641516 1023 verigfTDAGKLDRRAVARELesaVSQSQRPGHRAPSTP 1061
Cdd:PRK07769 598 ------TSSGKIARRACRAAY---LDGSLRSGYGQPAFP 627
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
675-1046 |
1.85e-10 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 64.82 E-value: 1.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 675 LGGAPASTEITSArvdPAALAYVLFTSGSTGEPKGVEVTHDA----AMNTVEFIGrhfdIGPADRCLALSTL--EGDISv 748
Cdd:PLN02860 158 RALGTTELDYAWA---PDDAVLICFTSGTTGRPKGVTISHSAlivqSLAKIAIVG----YGEDDVYLHTAPLchIGGLS- 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 749 mDVFVTLRTGGSIVVVDEVqrrdpDAWARL--IDAHQVTVLHFMPGWLEMLVEVGRGRLS-----SVRVVPTGGDWVRPE 821
Cdd:PLN02860 230 -SALAMLMVGACHVLLPKF-----DAKAALqaIKQHNVTSMITVPAMMADLISLTRKSMTwkvfpSVRKILNGGGSLSSR 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 822 VVRRLRVEAPGVRFAGLGGATET-------PVHNSIFE-------VTEPIPDDWTALPFGV----PLPNNACRVvddtGA 883
Cdd:PLN02860 304 LLPDAKKLFPNAKLFSAYGMTEAcssltfmTLHDPTLEspkqtlqTVNQTKSSSVHQPQGVcvgkPAPHVELKI----GL 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 884 DCPDWVpGEYWVSGRGIARGYRGRPDLTAERFVEHdgrIWYRTGDLVRYWPDGTLEFVGRADHRVKISGYRVELGEVETA 963
Cdd:PLN02860 380 DESSRV-GRILTRGPHVMLGYWGQNSETASVLSND---GWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAV 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 964 LRRVPGVRTAVAALIAVSGESDVLAAQV-------CADDASVTAEGIRQALADLVPAH---------MIPRHITVVER-I 1026
Cdd:PLN02860 456 LSQHPGVASVVVVGVPDSRLTEMVVACVrlrdgwiWSDNEKENAKKNLTLSSETLRHHcreknlsrfKIPKLFVQWRKpF 535
|
410 420
....*....|....*....|
gi 497641516 1027 GFTDAGKLDRRAVARELESA 1046
Cdd:PLN02860 536 PLTTTGKIRRDEVRREVLSH 555
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
678-1037 |
2.22e-10 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 64.78 E-value: 2.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 678 APASTEITSARVDPAALAYVLFTSGSTGEPKGVEvtHD-------AAMnTVEFIgrhFDIGPADR--CLAlstlegdisv 748
Cdd:PRK00174 231 AGASDECEPEPMDAEDPLFILYTSGSTGKPKGVL--HTtggylvyAAM-TMKYV---FDYKDGDVywCTA---------- 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 749 mDV-FVT---------LRTGGSIVVVDEVQRR-DPDAWARLIDAHQVTVLHFMPGWLEMLVEVGRG-----RLSSVRVVP 812
Cdd:PRK00174 295 -DVgWVTghsyivygpLANGATTLMFEGVPNYpDPGRFWEVIDKHKVTIFYTAPTAIRALMKEGDEhpkkyDLSSLRLLG 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 813 TGGDWVRPE-------VVRRLRVeapgvrfaglggatetpvhnsifevtePIPDDW----------TALPFGVPL-PNNA 874
Cdd:PRK00174 374 SVGEPINPEawewyykVVGGERC---------------------------PIVDTWwqtetggimiTPLPGATPLkPGSA 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 875 CR--------VVDDTGADCPDWVPGeYWVSGR---GIARGYRGRPdltaERFVE-----HDGriWYRTGDLVRYWPDGTL 938
Cdd:PRK00174 427 TRplpgiqpaVVDEEGNPLEGGEGG-NLVIKDpwpGMMRTIYGDH----ERFVKtyfstFKG--MYFTGDGARRDEDGYY 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 939 EFVGRADHRVKISGYRVELGEVETALRRVPGVRTAvaaliAVSGESDVLAAQ-VCA-----DDASVTAEgIRQALADLVp 1012
Cdd:PRK00174 500 WITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEA-----AVVGRPDDIKGQgIYAfvtlkGGEEPSDE-LRKELRNWV- 572
|
410 420 430
....*....|....*....|....*....|
gi 497641516 1013 AHMI-----PRHITVVERIGFTDAGKLDRR 1037
Cdd:PRK00174 573 RKEIgpiakPDVIQFAPGLPKTRSGKIMRR 602
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
563-716 |
2.37e-10 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 64.12 E-value: 2.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 563 AEQRPDAPAVFASSGDLSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIGVDQPRDRA 642
Cdd:PRK09029 13 AQVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLL 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497641516 643 ERILESGGVSLAVVCGGQRLSMPVPEVVLAdilggapASTEITSARVDPAALAYVLFTSGSTGEPKGVEVTHDA 716
Cdd:PRK09029 93 EELLPSLTLDFALVLEGENTFSALTSLHLQ-------LVEGAHAVAWQPQRLATMTLTSGSTGLPKAAVHTAQA 159
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
867-1038 |
3.83e-10 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 63.99 E-value: 3.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 867 GVPLPNNACRVVD-DTGADCPDWVPGEYWVSGRGIARGYRGRPDLTAERFV----------EH-----DGRIWYRTGDLV 930
Cdd:PRK12476 405 GQVARSQWAVIVDpDTGAELPDGEVGEIWLHGDNIGRGYWGRPEETERTFGaklqsrlaegSHadgaaDDGTWLRTGDLG 484
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 931 RYWpDGTLEFVGRADHRVKISGYRVELGEVE-TALRRVPGVRTAVAALIAVSGESD---VLAAQVCA----DDASVTAEG 1002
Cdd:PRK12476 485 VYL-DGELYITGRIADLIVIDGRNHYPQDIEaTVAEASPMVRRGYVTAFTVPAEDNerlVIVAERAAgtsrADPAPAIDA 563
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 497641516 1003 IRQALAD----------LVPAHMIPRhitvverigfTDAGKLDRRA 1038
Cdd:PRK12476 564 IRAAVSRrhglavadvrLVPAGAIPR----------TTSGKLARRA 599
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
579-974 |
4.20e-10 |
|
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: 63.53 E-value: 4.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 579 LSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIGVDQprdRAErilesggvslavvcg 658
Cdd:cd05940 4 LTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNL---RGE--------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 659 gqrlsmpvpevVLADILGgapasteITSARVDPAALAYVLFTSGSTGEPKGVEVTHDAAMNTVEFIGRHFDIGPADR--- 735
Cdd:cd05940 66 -----------SLAHCLN-------VSSAKHLVVDAALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGGALPSDVlyt 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 736 CLALSTLEGDIsvMDVFVTLRTGGSIVVVDEVQRRdpDAWARLIdAHQVTVLHFMPGWLEMLVEVGRG---RLSSVRVVp 812
Cdd:cd05940 128 CLPLYHSTALI--VGWSACLASGATLVIRKKFSAS--NFWDDIR-KYQATIFQYIGELCRYLLNQPPKpteRKHKVRMI- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 813 tGGDWVRPEVVRRL--RVEAPgvRFAGLGGATETpvhNS----IFEVTEPIPDDWTALPFGVPLpnnacRVVD---DTGA 883
Cdd:cd05940 202 -FGNGLRPDIWEEFkeRFGVP--RIAEFYAATEG---NSgfinFFGKPGAIGRNPSLLRKVAPL-----ALVKydlESGE 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 884 ----------DCPDWVPGEYW--VSGRGIARGYRGRPDLTAE--RFVEHDGRIWYRTGDLVRYWPDGTLEFVGRADHRVK 949
Cdd:cd05940 271 pirdaegrciKVPRGEPGLLIsrINPLEPFDGYTDPAATEKKilRDVFKKGDAWFNTGDLMRLDGEGFWYFVDRLGDTFR 350
|
410 420
....*....|....*....|....*
gi 497641516 950 ISGYRVELGEVETALRRVPGVRTAV 974
Cdd:cd05940 351 WKGENVSTTEVAAVLGAFPGVEEAN 375
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
689-964 |
8.21e-10 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 62.91 E-value: 8.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 689 VDPAALAYVLFTSGSTGEPKGVEVTHDAAMNTVEFIGRHFDigPADRCLALSTLEG----DISVMDVFVTLrtgGSIVVV 764
Cdd:PRK06334 180 KDPEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFS--PKEDDVMMSFLPPfhayGFNSCTLFPLL---SGVPVV 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 765 DEVQRRDPDAWARLIDAHQVTVLHFMPGWLEMLVEVGRGR---LSSVRVVPTGGDWVRPEVVRRLRVEAPGVRFAGLGGA 841
Cdd:PRK06334 255 FAYNPLYPKKIVEMIDEAKVTFLGSTPVFFDYILKTAKKQescLPSLRFVVIGGDAFKDSLYQEALKTFPHIQLRQGYGT 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 842 TE-TPVhnsIFEVTEPIPDDWTALpfGVPLPNNACRVV-DDTGADCPDWVPGEYWVSGRGIARGYRGRPDltAERFVEHD 919
Cdd:PRK06334 335 TEcSPV---ITINTVNSPKHESCV--GMPIRGMDVLIVsEETKVPVSSGETGLVLTRGTSLFSGYLGEDF--GQGFVELG 407
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 497641516 920 GRIWYRTGDLVRYWPDGTLEFVGRADHRVKISGYRVELGEVETAL 964
Cdd:PRK06334 408 GETWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESIL 452
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
565-822 |
1.24e-09 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 62.51 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 565 QRPDAPAVFASSGD-----LSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVY--------- 630
Cdd:PRK03584 96 RRDDRPAIIFRGEDgprreLSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLGAIWsscspdfgv 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 631 -------------LPIGVD------QPRDRAERILE--SGGVSLAVVC-----GGQRLSMPVPEVVL-ADILGGAPAStE 683
Cdd:PRK03584 176 qgvldrfgqiepkVLIAVDgyryggKAFDRRAKVAElrAALPSLEHVVvvpylGPAAAAAALPGALLwEDFLAPAEAA-E 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 684 ITSARVDPAALAYVLFTSGSTGEPK-------GVEVTHDAAMntvefiGRHFDIGPADRCLALST--------LEGdisv 748
Cdd:PRK03584 255 LEFEPVPFDHPLWILYSSGTTGLPKcivhghgGILLEHLKEL------GLHCDLGPGDRFFWYTTcgwmmwnwLVS---- 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 749 mdvfvTLRTGGSIVVVD-EVQRRDPDAWARLIDAHQVTVLHFMPGWLEMLVEVG-----RGRLSSVRVV--------PTG 814
Cdd:PRK03584 325 -----GLLVGATLVLYDgSPFYPDPNVLWDLAAEEGVTVFGTSAKYLDACEKAGlvpgeTHDLSALRTIgstgsplpPEG 399
|
....*...
gi 497641516 815 GDWVRPEV 822
Cdd:PRK03584 400 FDWVYEHV 407
|
|
| LCL_NRPS-like |
cd19540 |
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ... |
154-438 |
1.96e-09 |
|
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.
Pssm-ID: 380463 [Multi-domain] Cd Length: 433 Bit Score: 61.28 E-value: 1.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 154 HPMLRVRF-LPDGT--QRIAPADEFGPfPVHVEDLRErstGEADRRLAAiraakshqqLDGAVFELAVTL--------LP 222
Cdd:cd19540 52 HESLRTVFpEDDGGpyQVVLPAAEARP-DLTVVDVTE---DELAARLAE---------AARRGFDLTAELplrarlfrLG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 223 AERSRLHVDLDMQAADAMSYRTLMADLAALYLGR------DLPELGYTYRQY----RHAIEAEDarpQPARDADR--AWW 290
Cdd:cd19540 119 PDEHVLVLVVHHIAADGWSMAPLARDLATAYAARragrapDWAPLPVQYADYalwqRELLGDED---DPDSLAARqlAYW 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 291 ARRLPELPDPPALPTTGGRAENQSTR---RWHWLDPHTRDALFARAQARGFTPAMALAAGFANTLARWSTTSRFLLNVPL 367
Cdd:cd19540 196 RETLAGLPEELELPTDRPRPAVASYRggtVEFTIDAELHARLAALAREHGATLFMVLHAALAVLLSRLGAGDDIPIGTPV 275
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497641516 368 FGRqaLHPDVDSLVGDFTSSLLLDVDLTRANTAAARAQVVQDAMRTAAAHSAYP------GLAVLRDLSRHRGTQVL 438
Cdd:cd19540 276 AGR--GDEALDDLVGMFVNTLVLRTDVSGDPTFAELLARVRETDLAAFAHQDVPferlveALNPPRSTARHPLFQVM 350
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
867-1037 |
2.06e-09 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 61.57 E-value: 2.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 867 GVPLPNNACRVVDDTGADCPDWVPGEYWVSGRGIARGYRGRPDLTAeRFVEHDGriWYRTGDLVRYWPDGTLEFVGRADH 946
Cdd:PRK07059 383 GLPLPSTEVSIRDDDGNDLPLGEPGEICIRGPQVMAGYWNRPDETA-KVMTADG--FFRTGDVGVMDERGYTKIVDRKKD 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 947 RVKISGYRVELGEVETALRRVPGVRTavAALIAV----SGEsdVLAAQVCADDASVTAEGIRQALADLVPAHMIPRHITV 1022
Cdd:PRK07059 460 MILVSGFNVYPNEIEEVVASHPGVLE--VAAVGVpdehSGE--AVKLFVVKKDPALTEEDVKAFCKERLTNYKRPKFVEF 535
|
170
....*....|....*
gi 497641516 1023 VERIGFTDAGKLDRR 1037
Cdd:PRK07059 536 RTELPKTNVGKILRR 550
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
562-1034 |
2.09e-09 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 61.56 E-value: 2.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 562 QAEQRPDAPAVF-ASSGD-LSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIGVDQPR 639
Cdd:PRK13390 6 HAQIAPDRPAVIvAETGEqVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 640 DRAERILESGGVSLAVVCGG-----QRLSMPVPeVVLAdiLGG---APASTEITSARVDPAAL-----AYVLFTSGSTGE 706
Cdd:PRK13390 86 PEADYIVGDSGARVLVASAAldglaAKVGADLP-LRLS--FGGeidGFGSFEAALAGAGPRLTeqpcgAVMLYSSGTTGF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 707 PKGVEvthdaamntVEFIGRHFDiGPADRCLALSTLEGDISVMDVFVT---------LR-------TGGSIVVvdeVQRR 770
Cdd:PRK13390 163 PKGIQ---------PDLPGRDVD-APGDPIVAIARAFYDISESDIYYSsapiyhaapLRwcsmvhaLGGTVVL---AKRF 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 771 DPDAWARLIDAHQVTVLHFMPGWLEMLVEVG-----RGRLSSVRVVPTGG------------DWVRPEVVRRLrveapgv 833
Cdd:PRK13390 230 DAQATLGHVERYRITVTQMVPTMFVRLLKLDadvrtRYDVSSLRAVIHAAapcpvdvkhamiDWLGPIVYEYY------- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 834 rfaglggaTETPVHNSIFeVTEPipdDWTALPFGVPLPN-NACRVVDDTGADCPDWVPGEYWVSGRGIARGYRGRPDLTA 912
Cdd:PRK13390 303 --------SSTEAHGMTF-IDSP---DWLAHPGSVGRSVlGDLHICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTA 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 913 ErfVEHDGR-IWYRTGDLVRYWPDGTLEFVGRADHRVKISGYRVELGEVETALRRVPGVRTavaalIAVSGESDV-LAAQ 990
Cdd:PRK13390 371 A--AQHPAHpFWTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHD-----VAVIGVPDPeMGEQ 443
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 497641516 991 VCAddASVTAEGIR------QALADLVPAHM----IPRHITVVERIGFTDAGKL 1034
Cdd:PRK13390 444 VKA--VIQLVEGIRgsdelaRELIDYTRSRIahykAPRSVEFVDELPRTPTGKL 495
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
563-943 |
3.38e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 60.73 E-value: 3.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 563 AEQRPD-----------APAVFASSgdLSYAQLRDQALAVAAALRAAGVTaGDTIAVMGPKTAEQIPALLGILSVGAVYL 631
Cdd:PRK05850 11 ASLQPDdaaftfidyeqDPAGVAET--LTWSQLYRRTLNVAEELRRHGST-GDRAVILAPQGLEYIVAFLGALQAGLIAV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 632 PIGVDQPRDRAER------------ILESGGVSLAVV-CGGQRLSMPVPEVVLADILGgAPASTEITSARVDPAALAYVL 698
Cdd:PRK05850 88 PLSVPQGGAHDERvsavlrdtspsvVLTTSAVVDDVTeYVAPQPGQSAPPVIEVDLLD-LDSPRGSDARPRDLPSTAYLQ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 699 FTSGSTGEPKGVEVTHDAAMNTVE-----FIGRHFDIGPADRCLaLSTLE--GDISVM-DVFVTLRTGGSIVVVDEV--- 767
Cdd:PRK05850 167 YTSGSTRTPAGVMVSHRNVIANFEqlmsdYFGDTGGVPPPDTTV-VSWLPfyHDMGLVlGVCAPILGGCPAVLTSPVafl 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 768 QRrdPDAWARLIDAHQVTV-----LHF-----------MPGwLEmlvevgrgrLSSVRVVPTGGDWVRPEVVRRLrVEap 831
Cdd:PRK05850 246 QR--PARWMQLLASNPHAFsaapnFAFelavrktsdddMAG-LD---------LGGVLGIISGSERVHPATLKRF-AD-- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 832 gvRFA-------------GLGGATetpVHNSIFEVTEP-------------------IPDDWTAL-PFGVPlPNNACRVV 878
Cdd:PRK05850 311 --RFApfnlretairpsyGLAEAT---VYVATREPGQPpesvrfdyeklsaghakrcETGGGTPLvSYGSP-RSPTVRIV 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497641516 879 D-DTGADCPDWVPGEYWVSGRGIARGYRGRPDLTAERFvehDGRI-----------WYRTGDLVRYWpDGTLEFVGR 943
Cdd:PRK05850 385 DpDTCIECPAGTVGEIWVHGDNVAAGYWQKPEETERTF---GATLvdpspgtpegpWLRTGDLGFIS-EGELFIVGR 457
|
|
| PP-binding |
pfam00550 |
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
1064-1124 |
6.26e-09 |
|
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.
Pssm-ID: 425746 [Multi-domain] Cd Length: 62 Bit Score: 53.34 E-value: 6.26e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497641516 1064 SALATIVGDLLGR--QNIGIDDDFFALGGDSVLATQAVARIRAWLDaPDIMVADIFANRTVSA 1124
Cdd:pfam00550 1 ERLRELLAEVLGVpaEEIDPDTDLFDLGLDSLLAVELIARLEEEFG-VEIPPSDLFEHPTLAE 62
|
|
| PP-binding |
pfam00550 |
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
9-69 |
1.05e-08 |
|
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.
Pssm-ID: 425746 [Multi-domain] Cd Length: 62 Bit Score: 52.57 E-value: 1.05e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497641516 9 EDIRAEVAELLGVDADAVQPGSNLIGQGLDSIRIMTLAGRWRRQ-GIAVDFATLAETPTVEA 69
Cdd:pfam00550 1 ERLRELLAEVLGVPAEEIDPDTDLFDLGLDSLLAVELIARLEEEfGVEIPPSDLFEHPTLAE 62
|
|
| AcpP |
COG0236 |
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ... |
1057-1129 |
2.09e-08 |
|
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440006 [Multi-domain] Cd Length: 80 Bit Score: 52.16 E-value: 2.09e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497641516 1057 APSTPLQSALATIVGDLLG--RQNIGIDDDFFA-LGGDSVLATQAVARIRAWLDApDIMVADIFANRTVSALAAVL 1129
Cdd:COG0236 1 MPREELEERLAEIIAEVLGvdPEEITPDDSFFEdLGLDSLDAVELIAALEEEFGI-ELPDTELFEYPTVADLADYL 75
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
690-1043 |
2.10e-08 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 58.49 E-value: 2.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 690 DPAALAYvlfTSGSTGEPKGVEVTHDAA-MNTVE-FIGRHFDIGPAdRCLALSTLEGDISVMDVFVTLRtGGSIVVVDEV 767
Cdd:PLN03102 187 DPISLNY---TSGTTADPKGVVISHRGAyLSTLSaIIGWEMGTCPV-YLWTLPMFHCNGWTFTWGTAAR-GGTSVCMRHV 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 768 QRrdPDAWARlIDAHQVTVLHFMPGWLEMLVEVGRGRLS----SVRVVpTGGDwvRPEVVRRLRVEAPGVRFAGLGGATE 843
Cdd:PLN03102 262 TA--PEIYKN-IEMHNVTHMCCVPTVFNILLKGNSLDLSprsgPVHVL-TGGS--PPPAALVKKVQRLGFQVMHAYGLTE 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 844 TpvhnsifevTEPI-----PDDWTALPFGVPL---PNNACRV-----VDDTGADCPDWVP------GEYWVSGRGIARGY 904
Cdd:PLN03102 336 A---------TGPVlfcewQDEWNRLPENQQMelkARQGVSIlgladVDVKNKETQESVPrdgktmGEIVIKGSSIMKGY 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 905 RGRPDLTAERFvEHDgriWYRTGDLVRYWPDGTLEFVGRADHRVKISGYRVELGEVETALRRVPGV-RTAVAAL------ 977
Cdd:PLN03102 407 LKNPKATSEAF-KHG---WLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVlETAVVAMphptwg 482
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497641516 978 -------IAVSGESDVLAAQvcadDASVTAEG--IRQALADLvPAHMIPRHITVVERIGFTDAGKLDR---RAVAREL 1043
Cdd:PLN03102 483 etpcafvVLEKGETTKEDRV----DKLVTRERdlIEYCRENL-PHFMCPRKVVFLQELPKNGNGKILKpklRDIAKGL 555
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
580-998 |
2.62e-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: 58.20 E-value: 2.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 580 SYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIGVDQPRDRAERILESGGVSLaVVCGG 659
Cdd:cd17641 13 TWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARV-VIAED 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 660 QR-------LSMPVPEVV--------------------LADILGGA-------PASTEITSARVDPAALAYVLFTSGSTG 705
Cdd:cd17641 92 EEqvdklleIADRIPSVRyviycdprgmrkyddprlisFEDVVALGraldrrdPGLYEREVAAGKGEDVAVLCTTSGTTG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 706 EPKGVEVTHDAAMNTvEFIGRHFD-IGPADRCLALSTLE--GDiSVMDVFVTLRTGGSIVVVDEVQRRDPD--------- 773
Cdd:cd17641 172 KPKLAMLSHGNFLGH-CAAYLAADpLGPGDEYVSVLPLPwiGE-QMYSVGQALVCGFIVNFPEEPETMMEDlreigptfv 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 774 -------------AWARLIDA---HQVTVLHFMPGWLEMLVEVGRGR--------------------------LSSVRVV 811
Cdd:cd17641 250 llpprvwegiaadVRARMMDAtpfKRFMFELGMKLGLRALDRGKRGRpvslwlrlaswladallfrplrdrlgFSRLRSA 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 812 PTGGDWVRPEVVRRLRveAPGVRFAGLGGATETPVHNSIFEVTEPIPDDwtalpFGVPLPNNACRVVDDtgadcpdwvpG 891
Cdd:cd17641 330 ATGGAALGPDTFRFFH--AIGVPLKQLYGQTELAGAYTVHRDGDVDPDT-----VGVPFPGTEVRIDEV----------G 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 892 EYWVSGRGIARGYRGRPDLTAERFVEhDGriWYRTGDLVRYWPDGTLEFVGRADHRVKIS-GYRVELGEVETALRRVPGV 970
Cdd:cd17641 393 EILVRSPGVFVGYYKNPEATAEDFDE-DG--WLHTGDAGYFKENGHLVVIDRAKDVGTTSdGTRFSPQFIENKLKFSPYI 469
|
490 500
....*....|....*....|....*...
gi 497641516 971 RTAVaaliAVSGESDVLAAQVCADDASV 998
Cdd:cd17641 470 AEAV----VLGAGRPYLTAFICIDYAIV 493
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
605-1046 |
3.28e-08 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 57.47 E-value: 3.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 605 TIAVMGPKTAEQIPALLGILSVG-AVYL---PIGVDQPRDRAERILE---SGGVSLAVVCGG--QRLSMPVPEVVLADI- 674
Cdd:PRK05851 56 AVGLVGEPTVELVAAIQGAWLAGaAVSIlpgPVRGADDGRWADATLTrfaGIGVRTVLSHGShlERLRAVDSSVTVHDLa 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 675 -LGGAPASTEITSArvDPAALAYVLFTSGSTGEPKGVEVTHDAAMNTVEFIGRHFDIGPA-DRCLALSTLEGDISVMDVF 752
Cdd:PRK05851 136 tAAHTNRSASLTPP--DSGGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVGLDAAtDVGCSWLPLYHDMGLAFLL 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 753 VTLRTGGSIvvvdevqrrdpdaWARLIDAHQVTVLHfmpgWLEMLVE---------------VGR-GR------LSSVRV 810
Cdd:PRK05851 214 TAALAGAPL-------------WLAPTTAFSASPFR----WLSWLSDsratltaapnfaynlIGKyARrvsdvdLGALRV 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 811 VPTGGDWVRPEVVRRLRVEAPGVRFAGLGGATETPVHNSIFEVTEPIP------DDWTALP---------FGVPLPNNAC 875
Cdd:PRK05851 277 ALNGGEPVDCDGFERFATAMAPFGFDAGAAAPSYGLAESTCAVTVPVPgiglrvDEVTTDDgsgarrhavLGNPIPGMEV 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 876 RVV-DDTGADCPDWVPGEYWVSGRGIARGYRGRPDLtaerfvEHDGriWYRTGDLvRYWPDGTLEFVGRADHRVKISGYR 954
Cdd:PRK05851 357 RISpGDGAAGVAGREIGEIEIRGASMMSGYLGQAPI------DPDD--WFPTGDL-GYLVDGGLVVCGRAKELITVAGRN 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 955 VELGEVETALRRVPGVRT-AVAALIAVSGESD---VLAAQ-VCADDASVTAEGIRQALAD--LVPAHMI-------PRhi 1020
Cdd:PRK05851 428 IFPTEIERVAAQVRGVREgAVVAVGTGEGSARpglVIAAEfRGPDEAGARSEVVQRVASEcgVVPSDVVfvapgslPR-- 505
|
490 500
....*....|....*....|....*.
gi 497641516 1021 tvverigfTDAGKLDRRAVARELESA 1046
Cdd:PRK05851 506 --------TSSGKLRRLAVKRSLEAA 523
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
577-983 |
3.44e-08 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 57.60 E-value: 3.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 577 GDLSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIGVDQPRDR-AERIL--------- 646
Cdd:PLN02654 119 ASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESlAQRIVdckpkvvit 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 647 ------------------------ESGGVSLAVVCGGQRLS---------MPVPEVVLADILGGAPASTEITsaRVDPAA 693
Cdd:PLN02654 199 cnavkrgpktinlkdivdaaldesAKNGVSVGICLTYENQLamkredtkwQEGRDVWWQDVVPNYPTKCEVE--WVDAED 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 694 LAYVLFTSGSTGEPKGVEVTHDAAMNTVEFIGRH-FDIGPADrcLALSTLEGDISVMDVFVTL--RTGGSIVVVDEVQRR 770
Cdd:PLN02654 277 PLFLLYTSGSTGKPKGVLHTTGGYMVYTATTFKYaFDYKPTD--VYWCTADCGWITGHSYVTYgpMLNGATVLVFEGAPN 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 771 DPDA---WaRLIDAHQVTVLHFMPGWLEMLVE-----VGRGRLSSVRVVPTGGDWVRPEVVRRlrveapgvrFAGLGGAT 842
Cdd:PLN02654 355 YPDSgrcW-DIVDKYKVTIFYTAPTLVRSLMRdgdeyVTRHSRKSLRVLGSVGEPINPSAWRW---------FFNVVGDS 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 843 ETPVHNSIFEvTE-------PIPDDWTALPFGVPLPNNACR--VVDDTGADCPDWVPGEYWVSGR--GIARGYRGRPD-L 910
Cdd:PLN02654 425 RCPISDTWWQ-TEtggfmitPLPGAWPQKPGSATFPFFGVQpvIVDEKGKEIEGECSGYLCVKKSwpGAFRTLYGDHErY 503
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497641516 911 TAERFVEHDGriWYRTGDLVRYWPDGTLEFVGRADHRVKISGYRVELGEVETALRRVPgvRTAVAALIAVSGE 983
Cdd:PLN02654 504 ETTYFKPFAG--YYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHP--QCAEAAVVGIEHE 572
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
580-1039 |
4.00e-08 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 57.45 E-value: 4.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 580 SYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIG-----------VDQPRDRA------ 642
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNprlfpeqiawiINHAEDRVvitdlt 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 643 -----ERILESGGVSLAVVCGGQRLSMPVPE----VVLADILGGAPASTEITSarVDPAALAYVLFTSGSTGEPKGV--- 710
Cdd:PRK06018 121 fvpilEKIADKLPSVERYVVLTDAAHMPQTTlknaVAYEEWIAEADGDFAWKT--FDENTAAGMCYTSGTTGDPKGVlys 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 711 ---EVTHDAAMNTVEFIGrhfdIGPADRCLALSTLEGDISVMDVFVTLRTGGSIVVVDevQRRDPDAWARLIDAHQVTVL 787
Cdd:PRK06018 199 hrsNVLHALMANNGDALG----TSAADTMLPVVPLFHANSWGIAFSAPSMGTKLVMPG--AKLDGASVYELLDTEKVTFT 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 788 HFMPG-WLEML--VEVGRGRLSSVRVVPTGGDWVRPEVVRRLRVEAPGVRFAglGGATETPVHNSIFEVTEPIPD----- 859
Cdd:PRK06018 273 AGVPTvWLMLLqyMEKEGLKLPHLKMVVCGGSAMPRSMIKAFEDMGVEVRHA--WGMTEMSPLGTLAALKPPFSKlpgda 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 860 --DWTAL----PFGVPLpnnacRVVDDTGADCPdW---VPGEYWVSGRGIARGYRGRPDltaeRFVEHDGriWYRTGDLV 930
Cdd:PRK06018 351 rlDVLQKqgypPFGVEM-----KITDDAGKELP-WdgkTFGRLKVRGPAVAAAYYRVDG----EILDDDG--FFDTGDVA 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 931 RYWPDGTLEFVGRADHRVKISGYRVELGEVETALRRVPGVrtAVAALIAVS----GESDVLAAQVcADDASVTAEGIRQA 1006
Cdd:PRK06018 419 TIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKV--AEAAVIGVYhpkwDERPLLIVQL-KPGETATREEILKY 495
|
490 500 510
....*....|....*....|....*....|...
gi 497641516 1007 LADLVPAHMIPRHITVVERIGFTDAGKLDRRAV 1039
Cdd:PRK06018 496 MDGKIAKWWMPDDVAFVDAIPHTATGKILKTAL 528
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
897-1042 |
6.28e-08 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 56.57 E-value: 6.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 897 GRGIARGYRGRPDLTAERFveHDGriWYRTGDLVRYWPDGTLEFVGRADHRVKISGYRVELGEVETALRRVPGV-RTAVA 975
Cdd:PRK13388 359 GAGFFEGYYNNPEATAERM--RHG--MYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAInRVAVY 434
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 976 ALIAVSGESDVLAAQVCADDASVTAEGIRQALA---DLvPAHMIPRHITVVERIGFTDAGKLDRRAVARE 1042
Cdd:PRK13388 435 AVPDERVGDQVMAALVLRDGATFDPDAFAAFLAaqpDL-GTKAWPRYVRIAADLPSTATNKVLKRELIAQ 503
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
867-1017 |
9.34e-08 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 56.39 E-value: 9.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 867 GVPLPNNACRV--VDDTGADCPDWVP-GEYWVSGRGIARGYRGRPDLTAERFVehDGriWYRTGDLVRYWPDGTLEFVGR 943
Cdd:PLN02861 439 GVPMTTIEARLesVPEMGYDALSDVPrGEICLRGNTLFSGYHKRQDLTEEVLI--DG--WFHTGDIGEWQPNGAMKIIDR 514
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497641516 944 ADHRVKIS-GYRVELGEVETALRRVPGVrtavaALIAVSGES--DVLAAQVCADdasvtaegiRQALADLVPAHMIP 1017
Cdd:PLN02861 515 KKNIFKLSqGEYVAVENLENTYSRCPLI-----ASIWVYGNSfeSFLVAVVVPD---------RQALEDWAANNNKT 577
|
|
| DCL_NRPS-like |
cd19536 |
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ... |
105-521 |
1.22e-07 |
|
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal fungal CT domains and Dual Epimerization/Condensation (E/C) domains; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type [D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L))], which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380459 [Multi-domain] Cd Length: 419 Bit Score: 55.53 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 105 LAPMQHAMwVGRQENQQLGGVAGHLYVEFDGGGIDPERLRAAATALARRHPMLRVRFLPDGTQR-----IAPADefgpFP 179
Cdd:cd19536 4 LSSLQEGM-LFHSLLNPGGSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFIEDGLGQpvqvvHRQAQ----VP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 180 VHVEDLRERSTgeadrRLAAIRAAKSHQQ-----LDGAVFELAVTLLPAERSR--LHVDLDMQAADAMSYRTLMADLAAL 252
Cdd:cd19536 79 VTELDLTPLEE-----QLDPLRAYKEETKirrfdLGRAPLVRAALVRKDERERflLVISDHHSILDGWSLYLLVKEILAV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 253 YLG-RDLPELGYTYRQ-YRHAIEAEdaRPQPARDADRAWWARRLP--ELPDPPALPTTGGRAENQstrRWHWLDPHTRDA 328
Cdd:cd19536 154 YNQlLEYKPLSLPPAQpYRDFVAHE--RASIQQAASERYWREYLAgaTLATLPALSEAVGGGPEQ---DSELLVSVPLPV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 329 LF-ARAQARGFTPAMALAAGFANTLARWSTTSRFLLNVPLFGRQALHPDVDSLVGDFTSSLLLDVDLTRANTAAARAQvV 407
Cdd:cd19536 229 RSrSLAKRSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEETTGAERLLGLFLNTLPLRVTLSEETVEDLLKR-A 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 408 QDAMRTAAAHSAYPglavLRDLSRHRGTQVLapvvFTSALGLgelfsSDVTGQFGTPGWIISQGP-QVLLDAQV------ 480
Cdd:cd19536 308 QEQELESLSHEQVP----LADIQRCSEGEPL----FDSIVNF-----RHFDLDFGLPEWGSDEGMrRGLLFSEFksnydv 374
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 497641516 481 ---TEFDGG-VLVNWDVREGVFPAGVIDAMFAHHIDELLRLASAD 521
Cdd:cd19536 375 nlsVLPKQDrLELKLAYNSQVLDEEQAQRLAAYYKSAIAELATAP 419
|
|
| C_PKS-NRPS |
cd20483 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
154-384 |
1.89e-07 |
|
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHXXXD motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380471 [Multi-domain] Cd Length: 430 Bit Score: 54.96 E-value: 1.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 154 HPMLRVRFL---PDGTQRiaPADEFGpFPVHVEDLrersTGEADRRLAAIRAAKSHQQL-----DGAVFELAVTLLPAER 225
Cdd:cd20483 52 HEVLRTAYFegdDFGEQQ--VLDDPS-FHLIVIDL----SEAADPEAALDQLVRNLRRQeldieEGEVIRGWLVKLPDEE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 226 SRLHVDLDMQAADAMSYRTLMADLAALY----LGRDL---PELGYTYRQYrhAIEAEDARPQPARDADRAWWARRLPELP 298
Cdd:cd20483 125 FALVLASHHIAWDRGSSKSIFEQFTALYdalrAGRDLatvPPPPVQYIDF--TLWHNALLQSPLVQPLLDFWKEKLEGIP 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 299 DPPA-LP--TTGGRAENQSTRRWHW--LDPhtrdALFAR-----AQArGFTPAMALAAGFANTLARWSTTSRFLLNVPLF 368
Cdd:cd20483 203 DASKlLPfaKAERPPVKDYERSTVEatLDK----ELLARmkricAQH-AVTPFMFLLAAFRAFLYRYTEDEDLTIGMVDG 277
|
250
....*....|....*.
gi 497641516 369 GRQalHPDVDSLVGDF 384
Cdd:cd20483 278 DRP--HPDFDDLVGFF 291
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
691-951 |
3.01e-07 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 54.82 E-value: 3.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 691 PAALAYVLFTSGSTGEPKGVEVTHDAAMNTVefigRHFDigpadrcLALSTLEGDISVMDVFVTL--------------- 755
Cdd:PLN02430 219 PLDICTIMYTSGTSGDPKGVVLTHEAVATFV----RGVD-------LFMEQFEDKMTHDDVYLSFlplahildrmieeyf 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 756 -RTGGSI--------VVVDEVQRRDPDAWA-------RLIDAHQVTVLHFMP--------------GWL----------- 794
Cdd:PLN02430 288 fRKGASVgyyhgdlnALRDDLMELKPTLLAgvprvfeRIHEGIQKALQELNPrrrlifnalykyklAWMnrgyshkkasp 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 795 --EMLV------EVGrGRLssvRVVPTGGDWVRPEVVRRLRVEAPGVRFAGLGgATETpvhnsIFEVTEPIPDDWTAL-P 865
Cdd:PLN02430 368 maDFLAfrkvkaKLG-GRL---RLLISGGAPLSTEIEEFLRVTSCAFVVQGYG-LTET-----LGPTTLGFPDEMCMLgT 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 866 FGVPLPNNACRV--VDDTGADcPDWVP--GEYWVSGRGIARGYRGRPDLTAErfVEHDGriWYRTGDLVRYWPDGTLEFV 941
Cdd:PLN02430 438 VGAPAVYNELRLeeVPEMGYD-PLGEPprGEICVRGKCLFSGYYKNPELTEE--VMKDG--WFHTGDIGEILPNGVLKII 512
|
330
....*....|
gi 497641516 942 GRADHRVKIS 951
Cdd:PLN02430 513 DRKKNLIKLS 522
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
561-1001 |
4.14e-07 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 54.28 E-value: 4.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 561 RQAEQRPDAPAVFASSGD------LSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPI- 633
Cdd:PRK12582 57 KWAAEAPDRPWLAQREPGhgqwrkVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVs 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 634 -----------------GVDQPR----------DRAERILESGGVSLAVVCGgqrLSMPVPEVVLADILGGAP-ASTEIT 685
Cdd:PRK12582 137 payslmshdhaklkhlfDLVKPRvvfaqsgapfARALAALDLLDVTVVHVTG---PGEGIASIAFADLAATPPtAAVAAA 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 686 SARVDPAALAYVLFTSGSTGEPKGVEVTHD------AAMNTV------EFIGRHFDIGPADRCLAlstleGDISvmdvFV 753
Cdd:PRK12582 214 IAAITPDTVAKYLFTSGSTGMPKAVINTQRmmcaniAMQEQLrprepdPPPPVSLDWMPWNHTMG-----GNAN----FN 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 754 TLRTGGSIVVVDEvQRRDPDAWARLIDA-HQV--TVLHFMPGWLEMLVE-------VGRGRLSSVRVVPTGGDWVRPEVV 823
Cdd:PRK12582 285 GLLWGGGTLYIDD-GKPLPGMFEETIRNlREIspTVYGNVPAGYAMLAEamekddaLRRSFFKNLRLMAYGGATLSDDLY 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 824 RR---LRVEAPGVR--FAGLGGATET-PVHNSIFEVTEPIpddwtALpFGVPLPNNACRVVddtgadcPDWVPGEYWVSG 897
Cdd:PRK12582 364 ERmqaLAVRTTGHRipFYTGYGATETaPTTTGTHWDTERV-----GL-IGLPLPGVELKLA-------PVGDKYEVRVKG 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 898 RGIARGYRGRPDLTAERFVEHDgriWYRTGDLVRYW----PDGTLEFVGRADHRVKI-SGYRVELGEVETALRRV--PGV 970
Cdd:PRK12582 431 PNVTPGYHKDPELTAAAFDEEG---FYRLGDAARFVdpddPEKGLIFDGRVAEDFKLsTGTWVSVGTLRPDAVAAcsPVI 507
|
490 500 510
....*....|....*....|....*....|....*.
gi 497641516 971 RTAVAA-----LIAVSGESDVLAAQVCADDASVTAE 1001
Cdd:PRK12582 508 HDAVVAgqdraFIGLLAWPNPAACRQLAGDPDAAPE 543
|
|
| C_NRPS-like |
cd19537 |
Condensation family domain with an atypical active site motif; Condensation (C) domains of ... |
154-417 |
6.63e-07 |
|
Condensation family domain with an atypical active site motif; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily typically have a non-canonical conserved SHXXXDX(14)Y motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380460 [Multi-domain] Cd Length: 395 Bit Score: 52.96 E-value: 6.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 154 HPMLRVRFL--PDGTQRIapadeFGPFPVHVE-----DLRErstgEADR-----RLAAIRAAKSHQQLdgavfeLAVTll 221
Cdd:cd19537 52 HRILRSRYVprDGGLRRS-----YSSSPPRVQrvdtlDVWK----EINRpfdleREDPIRVFISPDTL------LVVM-- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 222 paerSrlHVdldmqAADAMSYRTLMADLAALYLGRDLPELGYTYrqyrhaieAEDARP-QPARDADRAWWARRLPELPDP 300
Cdd:cd19537 115 ----S--HI-----ICDLTTLQLLLREVSAAYNGKLLPPVRREY--------LDSTAWsRPASPEDLDFWSEYLSGLPLL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 301 PALPTTGGRAENQSTRRWHwLDPHTRDALFARAQARGFTP-AMALAAGFAnTLARWSTTSRFLLNVPLFGRQalHPDVDS 379
Cdd:cd19537 176 NLPRRTSSKSYRGTSRVFQ-LPGSLYRSLLQFSTSSGITLhQLALAAVAL-ALQDLSDRTDIVLGAPYLNRT--SEEDME 251
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 497641516 380 LVGdftssLLLD-------VDLTRANTAAARAQVVQDAMRTAAAH 417
Cdd:cd19537 252 TVG-----LFLEplpirirFPSSSDASAADFLRAVRRSSQAALAH 291
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
691-964 |
1.21e-06 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 52.81 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 691 PAALAYVLFTSGSTGEPKGVEVTH-------DAAMNTVEfigrhfDIGPADRCLA------LSTLEGDISVMDVFVTLRT 757
Cdd:PLN02387 249 PNDIAVIMYTSGSTGLPKGVMMTHgnivatvAGVMTVVP------KLGKNDVYLAylplahILELAAESVMAAVGAAIGY 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 758 GGSIVVVD---EVQR-RDPDAwarliDAHQVTVLHFMPGWLE------------------MLVEVG-RGRLSSVRvvptg 814
Cdd:PLN02387 323 GSPLTLTDtsnKIKKgTKGDA-----SALKPTLMTAVPAILDrvrdgvrkkvdakgglakKLFDIAyKRRLAAIE----- 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 815 GDWV---RPE-------VVRRLRVEAPG-VRFAGLGGA------------------------TETPVHNSIFEvtepiPD 859
Cdd:PLN02387 393 GSWFgawGLEkllwdalVFKKIRAVLGGrIRFMLSGGAplsgdtqrfiniclgapigqgyglTETCAGATFSE-----WD 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 860 DWTALPFGVPLPNNACRVVDdtgadcpdWVPGEYWVSGRGIARG--YRGRPDLTAERF-----------VEHDGRIWYRT 926
Cdd:PLN02387 468 DTSVGRVGPPLPCCYVKLVS--------WEEGGYLISDKPMPRGeiVIGGPSVTLGYFknqektdevykVDERGMRWFYT 539
|
330 340 350
....*....|....*....|....*....|....*....
gi 497641516 927 GDLVRYWPDGTLEFVGRADHRVKIS-GYRVELGEVETAL 964
Cdd:PLN02387 540 GDIGQFHPDGCLEIIDRKKDIVKLQhGEYVSLGKVEAAL 578
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
529-714 |
1.95e-06 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 52.19 E-value: 1.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 529 PPALPEAQRAVREAANG----RTAEPSGEA---LHDGFFRQAEQRPDAPAVFASSGD-----LSYAQLRDQALAVAAALR 596
Cdd:PRK08180 8 PVAFAPPAVEVERRADGtiylRSAEPLGDYprrLTDRLVHWAQEAPDRVFLAERGADggwrrLTYAEALERVRAIAQALL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 597 AAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIG--------------------------VD--QPRDRAERILES 648
Cdd:PRK08180 88 DRGLSAERPLMILSGNSIEHALLALAAMYAGVPYAPVSpayslvsqdfgklrhvlelltpglvfADdgAAFARALAAVVP 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497641516 649 GGVSLAVVCGGQRLSMPVPevvLADILGGAP-ASTEITSARVDPAALAYVLFTSGSTGEPKGVEVTH 714
Cdd:PRK08180 168 ADVEVVAVRGAVPGRAATP---FAALLATPPtAAVDAAHAAVGPDTIAKFLFTSGSTGLPKAVINTH 231
|
|
| AcpP |
COG0236 |
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ... |
9-76 |
2.08e-06 |
|
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440006 [Multi-domain] Cd Length: 80 Bit Score: 46.77 E-value: 2.08e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 9 EDIRAEVAELLGVDADAVQPGSNLIGQ-GLDSIRIMTLAGRWRRQ-GIAVDFATLAETPTVEAWAELVNA 76
Cdd:COG0236 8 ERLAEIIAEVLGVDPEEITPDDSFFEDlGLDSLDAVELIAALEEEfGIELPDTELFEYPTVADLADYLEE 77
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
891-1043 |
5.21e-06 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 50.61 E-value: 5.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 891 GEYWVSGRGIARGYRGRPDLTAERFVEHdgriWYRTGDLVRYWPDGTLEFVGRADHRVKISGYRVELGEVETALRRVPGV 970
Cdd:PLN02479 403 GEIVMRGNMVMKGYLKNPKANEEAFANG----WFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAV 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 971 RTA--VAALIAVSGESD----VLAAQVCADDASVTAEGIRQALADLVPAHMIPRHItVVERIGFTDAGKLDR---RAVAR 1041
Cdd:PLN02479 479 LEAsvVARPDERWGESPcafvTLKPGVDKSDEAALAEDIMKFCRERLPAYWVPKSV-VFGPLPKTATGKIQKhvlRAKAK 557
|
..
gi 497641516 1042 EL 1043
Cdd:PLN02479 558 EM 559
|
|
| LCL_NRPS |
cd19538 |
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ... |
236-393 |
5.56e-06 |
|
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.
Pssm-ID: 380461 [Multi-domain] Cd Length: 432 Bit Score: 50.34 E-value: 5.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 236 AADAMSYRTLMADLAALYLGR------DLPELGYTYRQY-----RHAIEAEDARPQPARDADraWWARRLPELPDPPALP 304
Cdd:cd19538 132 AADGWSLAPLTRDLSKAYRARckgeapELAPLPVQYADYalwqqELLGDESDPDSLIARQLA--YWKKQLAGLPDEIELP 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 305 TTGGRAENQSTRRWHW---LDPHTRDALFARAQARGFTPAMALAAGFANTLARWSTTSRFLLNVPLFGRQALhpDVDSLV 381
Cdd:cd19538 210 TDYPRPAESSYEGGTLtfeIDSELHQQLLQLAKDNNVTLFMVLQAGFAALLTRLGAGTDIPIGSPVAGRNDD--SLEDLV 287
|
170
....*....|..
gi 497641516 382 GDFTSSLLLDVD 393
Cdd:cd19538 288 GFFVNTLVLRTD 299
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
691-1035 |
6.88e-06 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 50.48 E-value: 6.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 691 PAALAYVLFTSGSTGEPKGVEVTHDAAMNTVEFIGRHFDIGPADRCL-ALSTLEGDISVMDVFVTLRTGGSIV------- 762
Cdd:PRK08043 364 PEDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRFMsALPLFHSFGLTVGLFTPLLTGAEVFlypsplh 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 763 --VVDEvqrrdpdawarLIDAHQVTVLHfmpGWLEMLVEVGR-------GRLssvRVVPTGGDWVRpEVVRRLRVEAPGV 833
Cdd:PRK08043 444 yrIVPE-----------LVYDRNCTVLF---GTSTFLGNYARfanpydfARL---RYVVAGAEKLQ-ESTKQLWQDKFGL 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 834 RFAGLGGATE-TPVhnsifeVTEPIPDDWTALPFGVPLPNNACRVVDDTGADcpdwVPGEYWVSGRGIARGY-Rgrpdlt 911
Cdd:PRK08043 506 RILEGYGVTEcAPV------VSINVPMAAKPGTVGRILPGMDARLLSVPGIE----QGGRLQLKGPNIMNGYlR------ 569
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 912 aerfVEHDGRI---------------WYRTGDLVRYWPDGTLEFVGRADHRVKISGYRVELGEVET-ALRRVP-GVRTAV 974
Cdd:PRK08043 570 ----VEKPGVLevptaenargemergWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlALGVSPdKQHATA 645
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497641516 975 AALIAVSGESDVLAAQvcadDASVTAEG-IRQALADLVPAHMIPRHITVVERIGFTDAGKLD 1035
Cdd:PRK08043 646 IKSDASKGEALVLFTT----DSELTREKlQQYAREHGVPELAVPRDIRYLKQLPLLGSGKPD 703
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
561-1054 |
7.98e-06 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 49.95 E-value: 7.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 561 RQAEQRPDAPAVFASSGD------LSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVY-LPI 633
Cdd:PRK10524 61 RHLAKRPEQLALIAVSTEtdeertYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIHsVVF 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 634 GVDQPRDRAERILESGGVSLAVVCGGQRLSMPVP-----------------EVVLADiLGGAPAsTEITSARVDPAAL-- 694
Cdd:PRK10524 141 GGFASHSLAARIDDAKPVLIVSADAGSRGGKVVPykplldeaialaqhkprHVLLVD-RGLAPM-ARVAGRDVDYATLra 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 695 -----------------AYVLFTSGSTGEPKGVE-------VTHDAAMNTVefigrhFDIGPADRCLALStlegDI---- 746
Cdd:PRK10524 219 qhlgarvpvewlesnepSYILYTSGTTGKPKGVQrdtggyaVALATSMDTI------FGGKAGETFFCAS----DIgwvv 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 747 --SVMdVFVTLRTGGSIVVVDEVQRRdPDA--WARLIDAHQVTVLHFMPGWLEMLVE-----VGRGRLSSVRVV------ 811
Cdd:PRK10524 289 ghSYI-VYAPLLAGMATIMYEGLPTR-PDAgiWWRIVEKYKVNRMFSAPTAIRVLKKqdpalLRKHDLSSLRALflagep 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 812 ---PTgGDWVRpevvrrlrvEAPGVRFAGLGGATET--PVHnSIFEVTEPIPDDWTAlPfGVPLPNNACRVVDD-TGADC 885
Cdd:PRK10524 367 ldePT-ASWIS---------EALGVPVIDNYWQTETgwPIL-AIARGVEDRPTRLGS-P-GVPMYGYNVKLLNEvTGEPC 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 886 PdwvPGEywvsgRGIArGYRG-----------RPDltaERFV----EHDGRIWYRTGDLVRYWPDGTLEFVGRADHRVKI 950
Cdd:PRK10524 434 G---PNE-----KGVL-VIEGplppgcmqtvwGDD---DRFVktywSLFGRQVYSTFDWGIRDADGYYFILGRTDDVINV 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 951 SGYRVELGEVETALRRVPGVrtavaALIAVSGESDVLAAQV-----CADDASVTAEG---------IRQALADLVPAHMI 1016
Cdd:PRK10524 502 AGHRLGTREIEESISSHPAV-----AEVAVVGVKDALKGQVavafvVPKDSDSLADRearlalekeIMALVDSQLGAVAR 576
|
570 580 590
....*....|....*....|....*....|....*...
gi 497641516 1017 PRHITVVERIGFTDAGKLDRRAVArelesAVSQSQRPG 1054
Cdd:PRK10524 577 PARVWFVSALPKTRSGKLLRRAIQ-----AIAEGRDPG 609
|
|
| CT_NRPS-like |
cd19542 |
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ... |
107-447 |
9.04e-06 |
|
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike bacterial NRPS, which typically have specialized terminal thioesterase (TE) domains to cyclize peptide products, many fungal NRPSs employ a terminal condensation-like (CT) domain to produce macrocyclic peptidyl products (e.g. cyclosporine and echinocandin). Domains in this subfamily (which includes both terminal and non-terminal domains) typically have a non-canonical conserved [SN]HxxxDx(14)Y motif at their active site compared to the standard Condensation (C) domain active site motif (HHxxxD). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380464 [Multi-domain] Cd Length: 401 Bit Score: 49.61 E-value: 9.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 107 PMQHAMwVGRQENQQLGGVAgHLYVEFDGGgIDPERLRAAATALARRHPMLRVRFLPDGTQriapadefGPF-------- 178
Cdd:cd19542 6 PMQEGM-LLSQLRSPGLYFN-HFVFDLDSS-VDVERLRNAWRQLVQRHDILRTVFVESSAE--------GTFlqvvlksl 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 179 --PVHVEDLRERSTGEADRRLaairaaKSHQQLDGAVFeLAVTLLPAERSRLHVDLDMQAA--DAMSYRTLMADLAALYL 254
Cdd:cd19542 75 dpPIEEVETDEDSLDALTRDL------LDDPTLFGQPP-HRLTLLETSSGEVYLVLRISHAlyDGVSLPIILRDLAAAYN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 255 GR-DLPELGY-TYRQYRHAIEAEDArpqpardadRAWWARRL---PELPDPPALPTTGGRAENQSTRRwhwldphTRDAL 329
Cdd:cd19542 148 GQlLPPAPPFsDYISYLQSQSQEES---------LQYWRKYLqgaSPCAFPSLSPKRPAERSLSSTRR-------SLAKL 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 330 FARAQARGFTPAMALAAGFANTLARWSTTSRFLLNVPLFGRQALHPDVDSLVGDFTSSLLLDVDLTRANTAAARAQVVQD 409
Cdd:cd19542 212 EAFCASLGVTLASLFQAAWALVLARYTGSRDVVFGYVVSGRDLPVPGIDDIVGPCINTLPVRVKLDPDWTVLDLLRQLQQ 291
|
330 340 350
....*....|....*....|....*....|....*...
gi 497641516 410 AMRTAAAHSAYPglavLRDLsRHRGTQVLAPVVFTSAL 447
Cdd:cd19542 292 QYLRSLPHQHLS----LREI-QRALGLWPSGTLFNTLV 324
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
698-973 |
9.21e-06 |
|
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341256 [Multi-domain] Cd Length: 596 Bit Score: 49.66 E-value: 9.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 698 LFTSGSTGEPKGVEVTHDAAMNTVEFIGRHFDIGPADR-------CLALSTLEGDIsvMDVFVTLRTGGSIVVVD----- 765
Cdd:cd05933 156 IYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLRPATVgqesvvsYLPLSHIAAQI--LDIWLPIKVGGQVYFAQpdalk 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 766 --------EVQ----------------------------RRDPDAWARLIDAHQVTVL------HFMP-GWLEMLVeVGR 802
Cdd:cd05933 234 gtlvktlrEVRptafmgvprvwekiqekmkavgaksgtlKRKIASWAKGVGLETNLKLmggespSPLFyRLAKKLV-FKK 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 803 GR----LSSVRVVPTGGDWVRPEVVRR-LRVEAPGVRFAGLggaTETP-VHnsifevTEPIPDDWTALPFGVPLPnnACR 876
Cdd:cd05933 313 VRkalgLDRCQKFFTGAAPISRETLEFfLSLNIPIMELYGM---SETSgPH------TISNPQAYRLLSCGKALP--GCK 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 877 V-VDDTGADCpdwvPGEYWVSGRGIARGYRGRPDLTaERFVEHDGriWYRTGDLVRYWPDGTLEFVGRADHRVKISGyrv 955
Cdd:cd05933 382 TkIHNPDADG----IGEICFWGRHVFMGYLNMEDKT-EEAIDEDG--WLHSGDLGKLDEDGFLYITGRIKELIITAG--- 451
|
330 340
....*....|....*....|....*
gi 497641516 956 elGE------VETALR-RVPGVRTA 973
Cdd:cd05933 452 --GEnvppvpIEDAVKkELPIISNA 474
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
561-1039 |
9.48e-06 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 49.74 E-value: 9.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 561 RQAEQRPDAPAVFASSGD-----LSYAQLRDQALAVAAALRAAGVTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPI-- 633
Cdd:cd05921 3 HWARQAPDRTWLAEREGNggwrrVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVsp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 634 ----------------GVDQPR----------DRAERILESGGVSLAVVCGG--QRLSMPVPEVVLADILGGAPASteit 685
Cdd:cd05921 83 ayslmsqdlaklkhlfELLKPGlvfaqdaapfARALAAIFPLGTPLVVSRNAvaGRGAISFAELAATPPTAAVDAA---- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 686 SARVDPAALAYVLFTSGSTGEPKGVEVTHDA-AMNTVEFIGRHFDIGPADRCLALS-----TLEGDISVMdvfVTLRTGG 759
Cdd:cd05921 159 FAAVGPDTVAKFLFTSGSTGLPKAVINTQRMlCANQAMLEQTYPFFGEEPPVLVDWlpwnhTFGGNHNFN---LVLYNGG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 760 SIVVVDevQRRDPDAWARLIDAHQ--VTVLHFM-PGWLEMLVEVGRGR-------LSSVRVVPTGGDWVRPEV---VRRL 826
Cdd:cd05921 236 TLYIDD--GKPMPGGFEETLRNLReiSPTVYFNvPAGWEMLVAALEKDealrrrfFKRLKLMFYAGAGLSQDVwdrLQAL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 827 RVEAPG--VRFAGLGGATETPvhNSIFEVTEPipddwTALP--FGVPLPNNACRVVDdtgadcpdwVPGEYWVSGRG--I 900
Cdd:cd05921 314 AVATVGerIPMMAGLGATETA--PTATFTHWP-----TERSglIGLPAPGTELKLVP---------SGGKYEVRVKGpnV 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 901 ARGYRGRPDLTAERFVEhDGriWYRTGDLVRYW----PDGTLEFVGRADHRVKI-SGYRVELGEVETALRRV--PGVRTA 973
Cdd:cd05921 378 TPGYWRQPELTAQAFDE-EG--FYCLGDAAKLAdpddPAKGLVFDGRVAEDFKLaSGTWVSVGPLRARAVAAcaPLVHDA 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 974 VaalIAVSGESDV-------------LAAQVCADDASVTA-EGIRQALADLVPAHM---------IPRHITVVERIGF-- 1028
Cdd:cd05921 455 V---VAGEDRAEVgalvfpdllacrrLVGLQEASDAEVLRhAKVRAAFRDRLAALNgeatgsssrIARALLLDEPPSIdk 531
|
570
....*....|....
gi 497641516 1029 ---TDAGKLDRRAV 1039
Cdd:cd05921 532 geiTDKGYINQRAV 545
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
518-1009 |
1.43e-05 |
|
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: 49.38 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 518 ASADEAWEAPGPPALPEAQ--------RAVREAANGRTAEP-SGEALHDGFFRQAEQRPDApavfassgdlSYAQLRDQA 588
Cdd:cd17632 8 APLEAVTEAIRRPGLRLAQiiatvmtgYADRPALGQRATELvTDPATGRTTLRLLPRFETI----------TYAELWERV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 589 LAVAAALRAAG-VTAGDTIAVMGPKTAEQIPALLGILSVGAVYLPIGVDQPRDRAERIL--------------------- 646
Cdd:cd17632 78 GAVAAAHDPEQpVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILaeteprllavsaehldlavea 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 647 --ESGGVSLAVVCGGQR----------------LSMPVPEVVL---ADILGGAPASTEITSArVDPAALAYVLFTSGSTG 705
Cdd:cd17632 158 vlEGGTPPRLVVFDHRPevdahraalesarerlAAVGIPVTTLtliAVRGRDLPPAPLFRPE-PDDDPLALLIYTSGSTG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 706 EPKGVEVTHdaamNTVEFIGRHFDIGPADRCLA--------LSTLEGDISvmdVFVTLRTGGSIVVVDEvqrrdPDAWAR 777
Cdd:cd17632 237 TPKGAMYTE----RLVATFWLKVSSIQDIRPPAsitlnfmpMSHIAGRIS---LYGTLARGGTAYFAAA-----SDMSTL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 778 LIDAHQV--TVLHFMPGWLEMLVEVGRGRLSSVRVVPTGGDWVRPEVVRRLRVEAPGVRFAG--LGGATETPVHNSIFEV 853
Cdd:cd17632 305 FDDLALVrpTELFLVPRVCDMLFQRYQAELDRRSVAGADAETLAERVKAELRERVLGGRLLAavCGSAPLSAEMKAFMES 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 854 T--EPIPDDWTALPFGVPLPNNACR---VVDDTGADCPD---------WVPGEYWVSGRGIARGYRGRPDLTAERFVEhD 919
Cdd:cd17632 385 LldLDLHDGYGSTEAGAVILDGVIVrppVLDYKLVDVPElgyfrtdrpHPRGELLVKTDTLFPGYYKRPEVTAEVFDE-D 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 920 GriWYRTGDLV-RYWPDgTLEFVGRADHRVKIS-GYRVELGEVETALRRVPGVRTavaalIAVSGESD---VLAAQVCAD 994
Cdd:cd17632 464 G--FYRTGDVMaELGPD-RLVYVDRRNNVLKLSqGEFVTVARLEAVFAASPLVRQ-----IFVYGNSErayLLAVVVPTQ 535
|
570
....*....|....*..
gi 497641516 995 DA--SVTAEGIRQALAD 1009
Cdd:cd17632 536 DAlaGEDTARLRAALAE 552
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
691-972 |
1.48e-05 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 49.25 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 691 PAALAYVLFTSGSTGEPKGVEVTHDAAMNTVEFIGRhfdigpadrclALSTLEGDISVMDVFVT---------------- 754
Cdd:PLN02614 222 KSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIR-----------LLKSANAALTVKDVYLSylplahifdrvieecf 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 755 LRTGGSI--------VVVDEVQRRDPD---AWARLIDAHQVTVLHFMPG------------------------------- 792
Cdd:PLN02614 291 IQHGAAIgfwrgdvkLLIEDLGELKPTifcAVPRVLDRVYSGLQKKLSDggflkkfvfdsafsykfgnmkkgqshveasp 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 793 WLEMLV--EVGRGRLSSVRVVPTGGDWVRPEVVRRLRVEAPGVRFAGLGgATETPVHNSIfevtePIPDDWTAL-PFGVP 869
Cdd:PLN02614 371 LCDKLVfnKVKQGLGGNVRIILSGAAPLASHVESFLRVVACCHVLQGYG-LTESCAGTFV-----SLPDELDMLgTVGPP 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 870 LPNNACRV--VDDTGADCPDWVP-GEYWVSGRGIARGYRGRPDLTAERFVehDGriWYRTGDLVRYWPDGTLEFVGRADH 946
Cdd:PLN02614 445 VPNVDIRLesVPEMEYDALASTPrGEICIRGKTLFSGYYKREDLTKEVLI--DG--WLHTGDVGEWQPNGSMKIIDRKKN 520
|
330 340
....*....|....*....|....*..
gi 497641516 947 RVKIS-GYRVELGEVETALRRVPGVRT 972
Cdd:PLN02614 521 IFKLSqGEYVAVENIENIYGEVQAVDS 547
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
16-386 |
1.83e-05 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 49.19 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 16 AELLGVDAdaVQPGSNLIGQGLDSIRIMTLAGRWRRQGIAVDFATLAETPTVEAWAELVNAGKPSAdrpaepadapADAG 95
Cdd:PRK12316 1028 QDVLGVER--VGLDDNFFELGGDSIVSIQVVSRARQAGIQLSPRDLFQHQTIRSLALVAKAGQATA----------ADQG 1095
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 96 R-SGEdepFSLAPMQHAMWV----GRQE-NQQLGGVAGHlyvefdggGIDPERLRAAATALARRHPMLRVRFLP-DGTQR 168
Cdd:PRK12316 1096 PaSGE---VALAPVQRWFFEqaipQRQHwNQSLLLQARQ--------PLDPDRLGRALERLVAHHDALRLRFREeDGGWQ 1164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 169 IAPADefgpfPVHVEDLRERSTGEADRRLAAIRAAKSHQQLD-GAVFELAVTLLPAERSRLHVDLDMQAADAMSYRTLMA 247
Cdd:PRK12316 1165 QAYAA-----PQAGEVLWQRQAASEEELLALCEEAQRSLDLEqGPLLRALLVDMADGSQRLLLVIHHLVVDGVSWRILLE 1239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 248 DLAALY--LGRDLPELGYTY-----RQYRHAieaedarpqPARDADRAWWARRLPELPDppALPT---TGGRAENQSTRR 317
Cdd:PRK12316 1240 DLQRAYadLDADLPARTSSYqawarRLHEHA---------GARAEELDYWQAQLEDAPH--ELPCenpDGALENRHERKL 1308
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497641516 318 WHWLDP-HTRDAL-FARAQARGFTPAMALAAgFANTLARWSTTSRFLLNVPLFGRQALHPDVD--SLVGDFTS 386
Cdd:PRK12316 1309 ELRLDAeRTRQLLqEAPAAYRTQVNDLLLTA-LARVTCRWSGQASVLVQLEGHGREDLFEDIDlsRTVGWFTS 1380
|
|
| FUM14_C_NRPS-like |
cd19545 |
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ... |
238-382 |
2.63e-05 |
|
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond forming Fusarium verticillioides FUM14 protein; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) typically catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. However, some C-domains have ester-bond forming activity. This subfamily includes Fusarium verticillioides FUM14 (also known as NRPS8), a bi-domain protein with an ester-bond forming NRPS C-domain, which catalyzes linkages between an aminoacyl/peptidyl-PCP donor and a hydroxyl-containing acceptor. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. FUM14 has an altered active site motif DHTHCD instead of the typical HHxxxD motif seen in other subfamily members. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380467 [Multi-domain] Cd Length: 395 Bit Score: 48.06 E-value: 2.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 238 DAMSYRTLMADLAALYLGRDLPELGYtYRQYRHAIEAEDarpqpaRDADRAWWARRL--------PELPDPPALPTTGGR 309
Cdd:cd19545 126 DGWSLPLILRQVLAAYQGEPVPQPPP-FSRFVKYLRQLD------DEAAAEFWRSYLagldpavfPPLPSSRYQPRPDAT 198
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497641516 310 AEnqstRRWHWLDPHTRdalfaraqarGFTPAMALAAGFANTLARWSTTSRFLLNVPLFGRQALHPDVDSLVG 382
Cdd:cd19545 199 LE----HSISLPSSASS----------GVTLATVLRAAWALVLSRYTGSDDVVFGVTLSGRNAPVPGIEQIVG 257
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
10-517 |
3.91e-05 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 48.41 E-value: 3.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 10 DIRAEVAELLGVDADavqpgSNLIGQGLDSIRIMTLAGRWRRQGIAVDFATLAETPTVEAWAELVNAGKPSAdrpaepad 89
Cdd:PRK12316 3563 AIWADVLKLEQVGLT-----DNFFELGGDSIISLQVVSRARQAGIRFTPKDLFQHQTIQGLARVARVGGGVA-------- 3629
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 90 aPADAGRSGED--EPFSLAPMQHAMWVGRQENQQLggvaghlyVEFDGGGIDPERLRAAATALARRHPMLRVRFLPDG-- 165
Cdd:PRK12316 3630 -VDQGPVSGETllLPIQQQFFEEPVPERHHWNQSL--------LLKPREALDAAALEAALQALVEHHDALRLRFVEDAgg 3700
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 166 -TQRIAPADEfgpfPVHVEDLRERSTGEADRRLAAiRAAKSHQQLDGAVFELAVTLLPAERSRLHVDLDMQAADAMSYRT 244
Cdd:PRK12316 3701 wTAEHLPVEL----GGALLWRAELDDAEELERLGE-EAQRSLDLADGPLLRALLATLADGSQRLLLVIHHLVVDGVSWRI 3775
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 245 LMADLAALY----LGR--DLPELGYTYRQYrhAIEAEDARPQPARDADRAWWARRLPELPDP-PALPTTGGRAENQSTRR 317
Cdd:PRK12316 3776 LLEDLQQAYqqllQGEapRLPAKTSSFKAW--AERLQEHARGEALKAELAYWQEQLQGVSSElPCDHPQGALQNRHAASV 3853
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 318 WHWLDPHTRDALFARAQARGFTPAM-ALAAGFANTLARWSTTSRFLLNVPLFGRQALHPDVD--SLVGDFTSslLLDVDL 394
Cdd:PRK12316 3854 QTRLDRELTRRLLQQAPAAYRTQVNdLLLTALARVVCRWTGEASALVQLEGHGREDLFADIDlsRTVGWFTS--LFPVRL 3931
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 395 TRANTAAARAQVVQDAMRtaAAHSAYPGLAVLRDLSRHRGTQVLA--PVVFTSALGLGELFSS-DVTGQFGTP---GWII 468
Cdd:PRK12316 3932 SPVEDLGASIKAIKEQLR--AIPNKGIGFGLLRYLGDEESRRTLAglPVPRITFNYLGQFDGSfDEEMALFVPageSAGA 4009
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 497641516 469 SQGPQVLLDAQVT----EFDGGVLVNWDVREGVFPAGVIDAMFAHHIDELLRL 517
Cdd:PRK12316 4010 EQSPDAPLDNWLSlngrVYGGELSLDWTFSREMFEEATIQRLADDYAAELTAL 4062
|
|
| C_PKS-NRPS |
cd19532 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
154-304 |
7.92e-05 |
|
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHxxxD motif, a few such as Monascus pilosus lovastatin nonaketide synthase MokA have a non-canonical HRxxxD motif in the C-domain and are unable to catalyze amide-bond formation. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380455 [Multi-domain] Cd Length: 421 Bit Score: 46.68 E-value: 7.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 154 HPMLRVRFLPDG-----TQRIAPAdefgpFPVHVEDLRERSTGEADRrlaAIRAAKSHqqldgaVFELA------VTLL- 221
Cdd:cd19532 52 HEALRTCFFTDPedgepMQGVLAS-----SPLRLEHVQISDEAEVEE---EFERLKNH------VYDLEsgetmrIVLLs 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 222 -PAERSRL-----HVdldmqAADAMSYRTLMADLAALYLGRDLPELGYTYRQY----RHAIEaedarpQPARDADRAWWA 291
Cdd:cd19532 118 lSPTEHYLifgyhHI-----AMDGVSFQIFLRDLERAYNGQPLLPPPLQYLDFaarqRQDYE------SGALDEDLAYWK 186
|
170
....*....|....
gi 497641516 292 RRLPELPDP-PALP 304
Cdd:cd19532 187 SEFSTLPEPlPLLP 200
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
924-1024 |
9.45e-05 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 46.30 E-value: 9.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 924 YRTGDLVRYWPD----GT----LEFV-GRADHRVKISGYRVELGEVETALRRVPGVRTAVAALIAVSGESDVLAAQVCAD 994
Cdd:COG1541 297 YRTGDLTRLLPEpcpcGRthprIGRIlGRADDMLIIRGVNVFPSQIEEVLLRIPEVGPEYQIVVDREGGLDELTVRVELA 376
|
90 100 110
....*....|....*....|....*....|.
gi 497641516 995 DAsVTAEGIRQALADLVPAH-MIPRHITVVE 1024
Cdd:COG1541 377 PG-ASLEALAEAIAAALKAVlGLRAEVELVE 406
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
810-951 |
6.46e-04 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 43.94 E-value: 6.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 810 VVPTGGDWVRPEVVRRLRVEApGVRFAGLGGATETpvhnsifevTEPI----PDDWTALPFGVPL-PNNACRVVDDTGAD 884
Cdd:PTZ00342 465 VILNGGGKLSPKIAEELSVLL-NVNYYQGYGLTET---------TGPIfvqhADDNNTESIGGPIsPNTKYKVRTWETYK 534
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497641516 885 CPDWVP-GEYWVSGRGIARGYRGRPDLTAERFVeHDGriWYRTGDLVRYWPDGTLEFVGRADHRVKIS 951
Cdd:PTZ00342 535 ATDTLPkGELLIKSDSIFSGYFLEKEQTKNAFT-EDG--YFKTGDIVQINKNGSLTFLDRSKGLVKLS 599
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
291-841 |
2.65e-03 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 42.17 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 291 ARRLPELPDPPalpttggraenqstrrwhwldphtrdalFARAQARGFTPAMALAAGFANTLARWSTTSRFLLNVPLFGR 370
Cdd:COG3321 857 GRRRVPLPTYP----------------------------FQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAAL 908
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 371 QALHPDVDSLVGDFTSSLLLDVDLTRANTAAARAQVVQDAMRTAAAHSAYPGLAVLRDLSRHRGTQVLAPVVFTSALGLG 450
Cdd:COG3321 909 LALAAAAAAALALAAAALAALLALVALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAA 988
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 451 ELFSSDVTGQFGTPGWIISQGPQVLLDAQVTEFDGGVLVNWDVREGVFPAGVIDAMFAHHIDELLRLASADEAWEAPGPP 530
Cdd:COG3321 989 AAAAAAALAAAAALALLAAAALLLAAAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAAL 1068
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 531 ALPEAQRAVREAANGRTAEPSGEALHDGFFRQAEQRPDAPAVFASSGDLSYAQLRDQALAVAAALRAAGVTAGDTIAVMG 610
Cdd:COG3321 1069 LLLAALAELALAAAALALAAALAAAALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAA 1148
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 611 PKTAEQIPALLGILSVGAVYLPIGVDQPRDRAERILESGGVSLAVVCGGQRLSMPVPEVVLADILGGAPASTEITSARVD 690
Cdd:COG3321 1149 ALALAAAAAALAAALAAALLAAAALLLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAA 1228
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 691 PAALAYVLFTSGSTGEPKGVEVTHDAAMNTVEFIGRHFDIGPADRCLALSTLEGDISVMDVFVTLRTGGSIVVVDEVQRR 770
Cdd:COG3321 1229 AAAALALLALAAAAAAVAALAAAAAALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAA 1308
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497641516 771 DPDAWARLIDAHQVTVLHFMPGWLEMLVEVGRGRLSSVRVVPTGGDWVRPEVVRRLRVEAPGVRFAGLGGA 841
Cdd:COG3321 1309 AAAAAAAAAAAALAAALLAAALAALAAAVAAALALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALALA 1379
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
959-1033 |
2.92e-03 |
|
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: 37.52 E-value: 2.92e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497641516 959 EVETALRRVPGVRTA--VAALIAVSGESdVLAAQVCADDASVTAEGIRQALADLVPAHMIPRHITVVERIGFTDAGK 1033
Cdd:pfam13193 1 EVESALVSHPAVAEAavVGVPDELKGEA-PVAFVVLKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
926-1039 |
8.64e-03 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 39.98 E-value: 8.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497641516 926 TGDLVRYWPDGTLEFVGRADHRVKISGYRVELGEVETALRRvpgvrTAVAALIAVSGESD-----VLAAQVCADDASVTA 1000
Cdd:PRK07445 328 TDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILA-----TGLVQDVCVLGLPDphwgeVVTAIYVPKDPSISL 402
|
90 100 110
....*....|....*....|....*....|....*....
gi 497641516 1001 EGIRQALADLVPAHMIPRHITVVERIGFTDAGKLDRRAV 1039
Cdd:PRK07445 403 EELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQL 441
|
|
| |
