|
Name |
Accession |
Description |
Interval |
E-value |
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
64-1343 |
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: 682.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 64 LVPDRAHRHDPFPVTDVQAAYLLGRGETFAYGGVACHGYGELVYpELDPERMTAAWRALIARHDMLRAVVEADGAQRVLA 143
Cdd:COG1020 11 PAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLV-AALLLLAALLARRRRALRTRLRTRAGRPVQVIQPV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 144 EVPPFEVPVIDLTG---RPEAVVDAAVSAVRAEMDHLVHTPDRWPLFAARITRADHRTVLHVSIDFLIADFISVQVVLDE 220
Cdd:COG1020 90 VAAPLPVVVLLVDLealAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLLLAELLRL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 221 LHRLYHRPDEPLPPLEITFRDYQLAERAVRDSPRHERDKQWWLARVDELPAAPELPTV-ARPADSEGRFRRWETRLSSQV 299
Cdd:COG1020 170 YLAAYAGAPLPLPPLPIQYADYALWQREWLQGEELARQLAYWRQQLAGLPPLLELPTDrPRPAVQSYRGARVSFRLPAEL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 300 WEGLRQRAGRHGVSPSGAVLAAFSDTIAAYSRRSRFTLDITLLNRApvHDQVNALVGDFTSVDLLAVDADPTRRFDERAR 379
Cdd:COG1020 250 TAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRP--RPELEGLVGFFVNTLPLRVDLSGDPSFAELLA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 380 DLQAQLWEDLDHRSFSGIEVMREIAR-RQGAEAALFPVVFTsAIGITSAGAAADGAPLGELgYGISQTPQVWIDCQNIER 458
Cdd:COG1020 328 RVRETLLAAYAHQDLPFERLVEELQPeRDLSRNPLFQVMFV-LQNAPADELELPGLTLEPL-ELDSGTAKFDLTLTVVET 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 459 DGGLVSNWDVREEVFPPGVVDDMFAAYDAVLHRLAGDDAAWTGTGHPDPPEATRDRRAETNRTQAPVPAGM-LHDRVVLQ 537
Cdd:COG1020 406 GDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQLLAEWNATAAPYPADAtLHELFEAQ 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 538 ALSTPDRPAVVAADRTLDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVDTSQPAARR 617
Cdd:COG1020 486 AARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERL 565
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 618 RTILTNAGIRCALTQSGVDRNGWAEGLRLLDVDLLGTGQ--PQPVEGSGDPEELAYVIHTSGSTGSPKGVMINHRGAVNT 695
Cdd:COG1020 566 AYMLEDAGARLVLTQSALAARLPELGVPVLALDALALAAepATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNL 645
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 696 VLDINDRFGVGPDDRVLGLSNLGFDLSVYDVFGPLSVGGAVVLPDPQRRGDPSHWADLVGTHGVTVWNSVPAQLQMlhdy 775
Cdd:COG1020 646 LAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLLRA---- 721
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 776 LVSATATVPDGLRLAMLSGDWIPVALPDQIRARVPGLRIVSLGGATEASIWSIWYPIEQVDPEWRSIPYGRPLTNQSFHV 855
Cdd:COG1020 722 LLDAAPEALPSLRLVLVGGEALPPELVRRWRARLPGARLVNLYGPTETTVDSTYYEVTPPDADGGSVPIGRPIANTRVYV 801
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 856 LDAALRPRPDLVSGELYIGGVGLAVGYLNDRERTAERFVVHP--QTGERLYRTGDLGRYLPDGTIEFLGREDLQVKIRGY 933
Cdd:COG1020 802 LDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPfgFPGARLYRTGDLARWLPDGNLEFLGRADDQVKIRGF 881
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 934 RIELAEIEAALGGHPAVAGAVVVVDGDTPLERRLAAFVEPAGRPVTAAQAEHDQAALRQL-----GVDACVDADSTLTGV 1008
Cdd:COG1020 882 RIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLALALLLPpymvpAAVVLLLPLPLTGNG 961
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 1009 DRERYLAYAHRLDD-----VALPAMVDAFRAAGLFAAGSRHPLADLLDTAHVASRHHRLVRRWLRALTDAGLLDRDTDGR 1083
Cdd:COG1020 962 KLDRLALPAPAAAAaaaaaAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLLFL 1041
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 1084 YGLTPAGAAADTDAGWREVEQLADAEDRELLDYFRASTAHLPALLRGEDDPLALLFPQGRVDVSQGLYERTLFNRWANEA 1163
Cdd:COG1020 1042 AAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLALLLAL 1121
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 1164 AAALVRRIAEQRIEPGALRVLEVGAGAGGTTAAVLAALDGYEVDYLATDLSPFFLGELRTRFGDRPGLRLEAVDIDRDLA 1243
Cdd:COG1020 1122 LAALRARRAVRQEGPRLRLLVALAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLLLLLLLLLLLL 1201
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 1244 GQGLSPNSFDVVVAGDVLHASADVGRALDRLREVLAPQGWLVACEMTRDHHQIMTSLELLVRVDEATADFTDLRRGTEQV 1323
Cdd:COG1020 1202 LLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAALLALALALLALALLLLALALLLP 1281
|
1290 1300
....*....|....*....|
gi 1860141834 1324 FLDRRSWLEVLGAAGAAQPL 1343
Cdd:COG1020 1282 ALARARAARTARALALLLLL 1301
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
542-989 |
0e+00 |
|
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: 610.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 542 PDRPAVVAADRTLDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVDTSQPAARRRTIL 621
Cdd:cd12114 1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 622 TNAGIRCALTQSGVDRNGWAEGLRLLDVDLLGTGQPQPVEGSGDPEELAYVIHTSGSTGSPKGVMINHRGAVNTVLDIND 701
Cdd:cd12114 81 ADAGARLVLTDGPDAQLDVAVFDVLILDLDALAAPAPPPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTILDINR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 702 RFGVGPDDRVLGLSNLGFDLSVYDVFGPLSVGGAVVLPDPQRRGDPSHWADLVGTHGVTVWNSVPAQLQMLHDYLVSATA 781
Cdd:cd12114 161 RFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDPAHWAELIERHGVTLWNSVPALLEMLLDVLEAAQA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 782 TvPDGLRLAMLSGDWIPVALPDQIRARVPGLRIVSLGGATEASIWSIWYPIEQVDPEWRSIPYGRPLTNQSFHVLDAALR 861
Cdd:cd12114 241 L-LPSLRLVLLSGDWIPLDLPARLRALAPDARLISLGGATEASIWSIYHPIDEVPPDWRSIPYGRPLANQRYRVLDPRGR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 862 PRPDLVSGELYIGGVGLAVGYLNDRERTAERFVVHPqTGERLYRTGDLGRYLPDGTIEFLGREDLQVKIRGYRIELAEIE 941
Cdd:cd12114 320 DCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHP-DGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIE 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1860141834 942 AALGGHPaVAGAVVVVDGDTPLERRLAAFVEPAGRPVTAAQAEHDQAA 989
Cdd:cd12114 399 AALQAHP-GVARAVVVVLGDPGGKRLAAFVVPDNDGTPIAPDALRAFL 445
|
|
| Cyc_NRPS |
cd19535 |
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
74-496 |
2.03e-180 |
|
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: 548.63 E-value: 2.03e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 74 PFPVTDVQAAYLLGRGETFAYGGVACHGYGELVYPELDPERMTAAWRALIARHDMLRAVVEADGAQRVLAEVPPFEVPVI 153
Cdd:cd19535 1 PFPLTDVQYAYWIGRQDDQELGGVGCHAYLEFDGEDLDPDRLERAWNKLIARHPMLRAVFLDDGTQQILPEVPWYGITVH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 154 DLTGRPEAVVDAAVSAVRAEMDHLVHTPDRWPLFAARITR-ADHRTVLHVSIDFLIADFISVQVVLDELHRLYHRPDEPL 232
Cdd:cd19535 81 DLRGLSEEEAEAALEELRERLSHRVLDVERGPLFDIRLSLlPEGRTRLHLSIDLLVADALSLQILLRELAALYEDPGEPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 233 PPLEITFRDYQLAERAVRDSpRHERDKQWWLARVDELPAAPELPTVARPAD-SEGRFRRWETRLSSQVWEGLRQRAGRHG 311
Cdd:cd19535 161 PPLELSFRDYLLAEQALRET-AYERARAYWQERLPTLPPAPQLPLAKDPEEiKEPRFTRREHRLSAEQWQRLKERARQHG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 312 VSPSGAVLAAFSDTIAAYSRRSRFTLDITLLNRAPVHDQVNALVGDFTSVDLLAVDADPTRRFDERARDLQAQLWEDLDH 391
Cdd:cd19535 240 VTPSMVLLTAYAEVLARWSGQPRFLLNLTLFNRLPLHPDVNDVVGDFTSLLLLEVDGSEGQSFLERARRLQQQLWEDLDH 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 392 RSFSGIEVMREIARRQGAEAALFPVVFTSAIGITSAGAAADgAPLGELGYGISQTPQVWIDCQNIERDGGLVSNWDVREE 471
Cdd:cd19535 320 SSYSGVVVVRRLLRRRGGQPVLAPVVFTSNLGLPLLDEEVR-EVLGELVYMISQTPQVWLDHQVYEEDGGLLLNWDAVDE 398
|
410 420
....*....|....*....|....*
gi 1860141834 472 VFPPGVVDDMFAAYDAVLHRLAGDD 496
Cdd:cd19535 399 LFPEGMLDDMFDAYVRLLERLADDD 423
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
542-992 |
1.18e-139 |
|
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: 440.04 E-value: 1.18e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 542 PDRPAVVAADRTLDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVDTSQPAARRRTIL 621
Cdd:cd05930 1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 622 TNAGIRCALTqsgvdrngwaeglrlldvdllgtgqpqpvegsgDPEELAYVIHTSGSTGSPKGVMINHRGAVNTVLDIND 701
Cdd:cd05930 81 EDSGAKLVLT---------------------------------DPDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQE 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 702 RFGVGPDDRVLGLSNLGFDLSVYDVFGPLSVGGAVVLPDPQRRGDPSHWADLVGTHGVTVWNSVPAQLQMLHDYLVSATA 781
Cdd:cd05930 128 AYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSLLRLLLQELELAAL 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 782 TvpdGLRLAMLSGDWIPVALPDQIRARVPGLRIVSLGGATEASIWSIWYPIEQVDPEWRSIPYGRPLTNQSFHVLDAALR 861
Cdd:cd05930 208 P---SLRLVLVGGEALPPDLVRRWRELLPGARLVNLYGPTEATVDATYYRVPPDDEEDGRVPIGRPIPNTRVYVLDENLR 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 862 PRPDLVSGELYIGGVGLAVGYLNDRERTAERFVVHP-QTGERLYRTGDLGRYLPDGTIEFLGREDLQVKIRGYRIELAEI 940
Cdd:cd05930 285 PVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPfGPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEI 364
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1860141834 941 EAALGGHPAVAGAVVVVDGDTPLERRLAAFVEPAGRPVTaaqaehDQAALRQ 992
Cdd:cd05930 365 EAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGGEL------DEEELRA 410
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
556-948 |
3.52e-139 |
|
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: 437.08 E-value: 3.52e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 556 YAELLGRAAGVAEAL-TAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVDTSQPAARRRTILTNAGIRCALTQSG 634
Cdd:TIGR01733 2 YRELDERANRLARHLrAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDSA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 635 V--DRNGWAEGLRLLDVDLLGTGQPQPVEGSGD----PEELAYVIHTSGSTGSPKGVMINHRGAVNTVLDINDRFGVGPD 708
Cdd:TIGR01733 82 LasRLAGLVLPVILLDPLELAALDDAPAPPPPDapsgPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDPD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 709 DRVLGLSNLGFDLSVYDVFGPLSVGGAVVLPDP-QRRGDPSHWADLVGTHGVTVWNSVPAQLQMlhdyLVSATATVPDGL 787
Cdd:TIGR01733 162 DRVLQFASLSFDASVEEIFGALLAGATLVVPPEdEERDDAALLAALIAEHPVTVLNLTPSLLAL----LAAALPPALASL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 788 RLAMLSGDWIPVALPDQIRARVPGLRIVSLGGATEASIWSIWYPIEQVDPEW-RSIPYGRPLTNQSFHVLDAALRPRPDL 866
Cdd:TIGR01733 238 RLVILGGEALTPALVDRWRARGPGARLINLYGPTETTVWSTATLVDPDDAPReSPVPIGRPLANTRLYVLDDDLRPVPVG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 867 VSGELYIGGVGLAVGYLNDRERTAERFVVHP---QTGERLYRTGDLGRYLPDGTIEFLGREDLQVKIRGYRIELAEIEAA 943
Cdd:TIGR01733 318 VVGELYIGGPGVARGYLNRPELTAERFVPDPfagGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAA 397
|
....*
gi 1860141834 944 LGGHP 948
Cdd:TIGR01733 398 LLRHP 402
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
109-994 |
1.63e-119 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 420.72 E-value: 1.63e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 109 ELDPERMTAAWRALIARHDMLRAVVEADG---AQRVLAEVPpFEVPVIDLTGRPEAVVDAAVSAVRAEMDHLVHTPDRWP 185
Cdd:PRK12467 83 ELDVSALRRAFDALVARHESLRTRFVQDEegfRQVIDASLS-LTIPLDDLANEQGRARESQIEAYINEEVARPFDLANGP 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 186 LFAARITR-ADHRTVLHVSIDFLIADFISVQVVLDELHRLY----HRPDEPLPPLEITFRDYQLAERAVRDSPRHERDKQ 260
Cdd:PRK12467 162 LLRVRLLRlADDEHVLVVTLHHIISDGWSMRVLVEELVQLYsaysQGREPSLPALPIQYADYAIWQRSWLEAGERERQLA 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 261 WWLARVDELPAAPELPT-VARPADSEGRFRRWETRLSSQVWEGLRQRAGRHGVSPSGAVLAAFSDTIAAYSRRSRFTLDI 339
Cdd:PRK12467 242 YWQEQLGGEHTVLELPTdRPRPAVPSYRGARLRVDLPQALSAGLKALAQREGVTLFMVLLASFQTLLHRYSGQSDIRIGV 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 340 TLLNRAPVhdQVNALVGDFTSVDLLAVDADPTRRFDE-----RARDLQAQLWEDLDHRSFsgIEVMReiARRQGAEAALF 414
Cdd:PRK12467 322 PNANRNRV--ETERLIGFFVNTQVLKAEVDPQASFLEllqqvKRTALGAQAHQDLPFEQL--VEALQ--PERSLSHSPLF 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 415 PVVF----TSAIGITSAGAAADGAPLGELGYGiSQTPQVWIDCQNIERDGGLVSNWDVREEVFPPGVVDDMFAAYDAVLH 490
Cdd:PRK12467 396 QVMFnhqnTATGGRDREGAQLPGLTVEELSWA-RHTAQFDLALDTYESAQGLWAAFTYATDLFEATTIERLATHWRNLLE 474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 491 RLAGDDAAWTGTGHPDPPEATRDRRAETNRTQAPVPAGMLHDRVVLQALSTPDRPAVVAADRTLDYAELLGRAAGVAEAL 570
Cdd:PRK12467 475 AIVAEPRRRLGELPLLDAEERARELVRWNAPATEYAPDCVHQLIEAQARQHPERPALVFGEQVLSYAELNRQANRLAHVL 554
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 571 TAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVDTSQPAARRRTILTNAGIRCALTQS-GVDRNGWAEGLRLLDV 649
Cdd:PRK12467 555 IAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQShLLAQLPVPAGLRSLCL 634
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 650 DLLGtgqpQPVEGSG--------DPEELAYVIHTSGSTGSPKGVMINHRGAVNTVLDINDRFGVGPDDRVLGLSNLGFDL 721
Cdd:PRK12467 635 DEPA----DLLCGYSghnpevalDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDL 710
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 722 SVYDVFGPLSVGGAVVLPDPQRRGDPSHWADLVGTHGVTVWNSVPAQLQMLhdyLVSATATVPDGLRLAMLSGDWIPVAL 801
Cdd:PRK12467 711 GVTELFGALASGATLHLLPPDCARDAEAFAALMADQGVTVLKIVPSHLQAL---LQASRVALPRPQRALVCGGEALQVDL 787
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 802 PDQIRARVPGLRIVSLGGATEASIWSIWYPIEQVDPEWRSIPYGRPLTNQSFHVLDAALRPRPDLVSGELYIGGVGLAVG 881
Cdd:PRK12467 788 LARVRALGPGARLINHYGPTETTVGVSTYELSDEERDFGNVPIGQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLARG 867
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 882 YLNDRERTAERFVVHP--QTGERLYRTGDLGRYLPDGTIEFLGREDLQVKIRGYRIELAEIEAALGGHPAVAGAVVVVDG 959
Cdd:PRK12467 868 YHRRPALTAERFVPDPfgADGGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQP 947
|
890 900 910
....*....|....*....|....*....|....*
gi 1860141834 960 DTPlERRLAAFVEPAGRPVTAAQAEHDQAALRQLG 994
Cdd:PRK12467 948 GDA-GLQLVAYLVPAAVADGAEHQATRDELKAQLR 981
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
531-991 |
2.64e-117 |
|
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: 380.08 E-value: 2.64e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 531 HDRVVLQALSTPDRPAVVAADRTLDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVDT 610
Cdd:cd17646 1 HALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 611 SQPAARRRTILTNAGIRCALTQSG-VDRNGWAEGLRLLDVDLLGTGQPQPVEGSGDPEELAYVIHTSGSTGSPKGVMINH 689
Cdd:cd17646 81 GYPADRLAYMLADAGPAVVLTTADlAARLPAGGDVALLGDEALAAPPATPPLVPPRPDNLAYVIYTSGSTGRPKGVMVTH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 690 RGAVNTVLDINDRFGVGPDDRVLGLSNLGFDLSVYDVFGPLSVGGAVVLPDPQRRGDPSHWADLVGTHGVTVWNSVPAql 769
Cdd:cd17646 161 AGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRDPAYLAALIREHGVTTCHFVPS-- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 770 qMLHDYLVSATATVPDGLRLAMLSGDWIPVALPDQIRARvPGLRIVSLGGATEASIWSIWYPIEQVDPEwRSIPYGRPLT 849
Cdd:cd17646 239 -MLRVFLAEPAAGSCASLRRVFCSGEALPPELAARFLAL-PGAELHNLYGPTEAAIDVTHWPVRGPAET-PSVPIGRPVP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 850 NQSFHVLDAALRPRPDLVSGELYIGGVGLAVGYLNDRERTAERFVVHP-QTGERLYRTGDLGRYLPDGTIEFLGREDLQV 928
Cdd:cd17646 316 NTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPfGPGSRMYRTGDLARWRPDGALEFLGRSDDQV 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1860141834 929 KIRGYRIELAEIEAALGGHPAVAGAVVVVDGDTPLERRLAAFVEPAgrpvtAAQAEHDQAALR 991
Cdd:cd17646 396 KIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPA-----AGAAGPDTAALR 453
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
537-992 |
9.67e-117 |
|
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: 378.08 E-value: 9.67e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 537 QALSTPDRPAVVAADRTLDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVDTSQPAAR 616
Cdd:cd12117 6 QAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAER 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 617 RRTILTNAGIRCALTQSGVDRNGWAEGLRLLDVDLLGTGQPQPVEGSGDPEELAYVIHTSGSTGSPKGVMINHRGAVNTV 696
Cdd:cd12117 86 LAFMLADAGAKVLLTDRSLAGRAGGLEVAVVIDEALDAGPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVAVTHRGVVRLV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 697 LDINDRfGVGPDDRVLGLSNLGFDLSVYDVFGPLSVGGAVVLPDPQRRGDPSHWADLVGTHGVTVWNSVPAQLQMLHDYL 776
Cdd:cd12117 166 KNTNYV-TLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPDALGALIAEEGVTVLWLTAALFNQLADED 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 777 VSATAtvpdGLRLAMLSGDWIPVALPDQIRARVPGLRIVSLGGATEASIWSIWYPIEQVDPEWRSIPYGRPLTNQSFHVL 856
Cdd:cd12117 245 PECFA----GLRELLTGGEVVSPPHVRRVLAACPGLRLVNGYGPTENTTFTTSHVVTELDEVAGSIPIGRPIANTRVYVL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 857 DAALRPRPDLVSGELYIGGVGLAVGYLNDRERTAERFVVHP-QTGERLYRTGDLGRYLPDGTIEFLGREDLQVKIRGYRI 935
Cdd:cd12117 321 DEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPfGPGERLYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRI 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1860141834 936 ELAEIEAALGGHPAVAGAVVVVDGDTPLERRLAAFVEPAGrpvtAAQAEHDQAALRQ 992
Cdd:cd12117 401 ELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVAEG----ALDAAELRAFLRE 453
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
107-991 |
1.57e-108 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 386.05 E-value: 1.57e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 107 YPELDPERMTAAWRALIARHDMLRAV-VEADG-AQRVLAEVPP--FEVPVIDLTGRPEAVVDAAVSAVRAEMDHLvhtpD 182
Cdd:PRK12467 1148 KGPLDIEALERSFDALVARHESLRTTfVQEDGrTRQVIHPVGSltLEEPLLLAADKDEAQLKVYVEAEARQPFDL----E 1223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 183 RWPLFAARITR-ADHRTVLHVSIDFLIADFISVQVVLDELHRLY--HRPDEP--LPPLEITFRDYQLAERAVRDSPRHER 257
Cdd:PRK12467 1224 QGPLLRVGLLRlAADEHVLVLTLHHIVSDGWSMQVLVDELVALYaaYSQGQSlqLPALPIQYADYAVWQRQWMDAGERAR 1303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 258 DKQWWLARVDELPAAPELPT-VARPADSEGRFRRWETRLSSQVWEGLRQRAGRHGVSPSGAVLAAFSDTIAAYSRRSRFT 336
Cdd:PRK12467 1304 QLAYWKAQLGGEQPVLELPTdRPRPAVQSHRGARLAFELPPALAEGLRALARREGVTLFMLLLASFQTLLHRYSGQDDIR 1383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 337 LDITLLNRApvHDQVNALVGDFTSVDLLAVDADPTRRFDE-----RARDLQAQLWEDLDHRSFsgIEVMReiARRQGAEA 411
Cdd:PRK12467 1384 VGVPIANRN--RAETEGLIGFFVNTQVLRAEVDGQASFQQllqqvKQAALEAQAHQDLPFEQL--VEALQ--PERSLSHS 1457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 412 ALFPVVFTSAIGITSAGAAADGAPLGELGYGiSQTPQVWIDCQNIERDGGLVSNWDVREEVFPPGVVDDMFAAYDAVLHR 491
Cdd:PRK12467 1458 PLFQVMFNHQRDDHQAQAQLPGLSVESLSWE-SQTAQFDLTLDTYESSEGLQASLTYATDLFEASTIERLAGHWLNLLQG 1536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 492 LAGDDAAWTGTGHPDPPEATRDRRAETNRTQAPVPAG-MLHDRVVLQALSTPDRPAVVAADRTLDYAELLGRAAGVAEAL 570
Cdd:PRK12467 1537 LVADPERRLGELDLLDEAERRQILEGWNATHTGYPLArLVHQLIEDQAAATPEAVALVFGEQELTYGELNRRANRLAHRL 1616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 571 TAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVDTSQPAARRRTILTNAGIRCALTQSGV-DRNGWAEGLRLLDV 649
Cdd:PRK12467 1617 IALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQSHLqARLPLPDGLRSLVL 1696
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 650 D-----LLGTGQPQPvEGSGDPEELAYVIHTSGSTGSPKGVMINHRGAVNTVLDINDRFGVGPDDRVLGLSNLGFDLSVY 724
Cdd:PRK12467 1697 DqeddwLEGYSDSNP-AVNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSFAFDVSVW 1775
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 725 DVFGPLSVGGAVVLPDPQRRGDPSHWADLVGTHGVTVWNSVPAQLQMLHDylVSATATVPDGLRLAMLSGDWIPVALPDQ 804
Cdd:PRK12467 1776 ELFWPLINGARLVIAPPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQ--MDEQVEHPLSLRRVVCGGEALEVEALRP 1853
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 805 IRARVPGLRIVSLGGATEASIWSIWYPIEQVDPEWR-SIPYGRPLTNQSFHVLDAALRPRPDLVSGELYIGGVGLAVGYL 883
Cdd:PRK12467 1854 WLERLPDTGLFNLYGPTETAVDVTHWTCRRKDLEGRdSVPIGQPIANLSTYILDASLNPVPIGVAGELYLGGVGLARGYL 1933
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 884 NDRERTAERFVVHP--QTGERLYRTGDLGRYLPDGTIEFLGREDLQVKIRGYRIELAEIEAALGGHPAVAGAVVVVDGDt 961
Cdd:PRK12467 1934 NRPALTAERFVADPfgTVGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQDG- 2012
|
890 900 910
....*....|....*....|....*....|
gi 1860141834 962 PLERRLAAFVEPAGRPVTAaqAEHDQAALR 991
Cdd:PRK12467 2013 ANGKQLVAYVVPTDPGLVD--DDEAQVALR 2040
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
109-948 |
9.13e-106 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 377.76 E-value: 9.13e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 109 ELDPERMTAAWRALIARHDMLRAVVEAdGAQRVLAEVP---PFEVPVIDLTGRPEAVVDAAVSAVRAEMDHLVHTPDRWP 185
Cdd:PRK12316 83 PLDRQALERAFASLVQRHETLRTVFPR-GADDSLAQVPldrPLEVEFEDCSGLPEAEQEARLRDEAQRESLQPFDLCEGP 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 186 LFAARITR-ADHRTVLHVSIDFLIADFISVQVVLDELHRLY---HRPDEP-LPPLEITFRDYQLAERAVRDSPRHERDKQ 260
Cdd:PRK12316 162 LLRVRLLRlGEEEHVLLLTLHHIVSDGWSMNVLIEEFSRFYsayATGAEPgLPALPIQYADYALWQRSWLEAGEQERQLE 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 261 WWLARVDELPAAPELPT-VARPADSEGRFRRWETRLSSQVWEGLRQRAGRHGVSPSGAVLAAFSDTIAAYSRRSRFTLDI 339
Cdd:PRK12316 242 YWRAQLGEEHPVLELPTdHPRPAVPSYRGSRYEFSIDPALAEALRGTARRQGLTLFMLLLGAFNVLLHRYSGQTDIRVGV 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 340 TLLNRAPVhdQVNALVGDFTSVDLLAVDADPTRRFDERARDLQ-----AQLWEDLD-HRSFSGIEVMREIArrqgaEAAL 413
Cdd:PRK12316 322 PIANRNRA--EVEGLIGFFVNTQVLRSVFDGRTRVATLLAGVKdtvlgAQAHQDLPfERLVEALKVERSLS-----HSPL 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 414 FPVVFTSAIGITSAGAA--ADGAPLGELGYGiSQTPQVWIDCQNIERDGGLVSNWDVREEVFPPGVVDDMFAAYDAVLHR 491
Cdd:PRK12316 395 FQVMYNHQPLVADIEALdtVAGLEFGQLEWK-SRTTQFDLTLDTYEKGGRLHAALTYATDLFEARTVERMARHWQNLLRG 473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 492 LAGDDAAWTGtghpDPPEATRDRRAET----NRTQA--PVPAGMlHDRVVLQALSTPDRPAVVAADRTLDYAELLGRAAG 565
Cdd:PRK12316 474 MVENPQARVD----ELPMLDAEERGQLvegwNATAAeyPLQRGV-HRLFEEQVERTPEAPALAFGEETLDYAELNRRANR 548
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 566 VAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVDTSQPAARRRTILTNAGIRCALTQSGVDRN-GWAEGL 644
Cdd:PRK12316 549 LAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQSHLGRKlPLAAGV 628
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 645 RLLDVDLLGT---GQP-QPVEGSGDPEELAYVIHTSGSTGSPKGVMINHRGAVNTVLDINDRFGVGPDDRVLGLSNLGFD 720
Cdd:PRK12316 629 QVLDLDRPAAwleGYSeENPGTELNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFD 708
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 721 LSVYDVFGPLSVGGAVVLPDPQRRGDPSHWADLVGTHGVTVWNSVPAQLQ-MLHDYLVSATATvpdgLRLAMLSGDWIPV 799
Cdd:PRK12316 709 VSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQaFLQDEDVASCTS----LRRIVCSGEALPA 784
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 800 ALPDQIRARVPGLRIVSLGGATEASI-WSIWYPIEQVDpewRSIPYGRPLTNQSFHVLDAALRPRPDLVSGELYIGGVGL 878
Cdd:PRK12316 785 DAQEQVFAKLPQAGLYNLYGPTEAAIdVTHWTCVEEGG---DSVPIGRPIANLACYILDANLEPVPVGVLGELYLAGRGL 861
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1860141834 879 AVGYLNDRERTAERFVVHP-QTGERLYRTGDLGRYLPDGTIEFLGREDLQVKIRGYRIELAEIEAALGGHP 948
Cdd:PRK12316 862 ARGYHGRPGLTAERFVPSPfVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHP 932
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
542-990 |
5.95e-105 |
|
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: 5.95e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 542 PDRPAVVAADRTLDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVDTSQPAARRRTIL 621
Cdd:cd12116 1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 622 TNAGIRCALTQSGVDRNGWAEGLRLLDVDLLGTGQPQPVEGSGDPEELAYVIHTSGSTGSPKGVMINHRGAVNTVLDIND 701
Cdd:cd12116 81 EDAEPALVLTDDALPDRLPAGLPVLLLALAAAAAAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSMRE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 702 RFGVGPDDRVLGLSNLGFDLSVYDVFGPLSVGGAVVLPDPQRRGDPSHWADLVGTHGVTVWNSVPAQLQMlhdyLVSATA 781
Cdd:cd12116 161 RLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHSITVMQATPATWRM----LLDAGW 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 782 TVPDGLRlAMLSGDWIPVALPDQIRARVPglRIVSLGGATEASIWSIWYPIEqvdPEWRSIPYGRPLTNQSFHVLDAALR 861
Cdd:cd12116 237 QGRAGLT-ALCGGEALPPDLAARLLSRVG--SLWNLYGPTETTIWSTAARVT---AAAGPIPIGRPLANTQVYVLDAALR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 862 PRPDLVSGELYIGGVGLAVGYLNDRERTAERFVVHPQT--GERLYRTGDLGRYLPDGTIEFLGREDLQVKIRGYRIELAE 939
Cdd:cd12116 311 PVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAgpGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGE 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1860141834 940 IEAALGGHPaVAGAVVVVDGDTPLERRLAAFVEPAGRPV--TAAQAEHDQAAL 990
Cdd:cd12116 391 IEAALAAHP-GVAQAAVVVREDGGDRRLVAYVVLKAGAApdAAALRAHLRATL 442
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
537-992 |
2.65e-101 |
|
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: 334.70 E-value: 2.65e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 537 QALSTPDRPAVVAADRTLDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVDTSQPAAR 616
Cdd:cd17651 4 QAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 617 RRTILTNAGIRCALTQSGVDrnGWAEGLRLLDVDLLGTGQPQPVEGSGDPE----ELAYVIHTSGSTGSPKGVMINHRGA 692
Cdd:cd17651 84 LAFMLADAGPVLVLTHPALA--GELAVELVAVTLLDQPGAAAGADAEPDPAldadDLAYVIYTSGSTGRPKGVVMPHRSL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 693 VNTVLDINDRFGVGPDDRVLGLSNLGFDLSVYDVFGPLSVGGAVVLPDPQRRGDPSHWADLVGTHGVTVWNSVPAQLQML 772
Cdd:cd17651 162 ANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPPALAAWLDEQRISRVFLPTVALRAL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 773 HDYLVSATATVPDgLRLAMLSGDWIPV-ALPDQIRARVPGLRIVSLGGATEASIWSIWYPIEQVDPEWRSIPYGRPLTNQ 851
Cdd:cd17651 242 AEHGRPLGVRLAA-LRYLLTGGEQLVLtEDLREFCAGLPGLRLHNHYGPTETHVVTALSLPGDPAAWPAPPPIGRPIDNT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 852 SFHVLDAALRPRPDLVSGELYIGGVGLAVGYLNDRERTAERFVVHPQ-TGERLYRTGDLGRYLPDGTIEFLGREDLQVKI 930
Cdd:cd17651 321 RVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFvPGARMYRTGDLARWLPDGELEFLGRADDQVKI 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1860141834 931 RGYRIELAEIEAALGGHPAVAGAVVVVDGDTPLERRLAAFVEPagrpvtAAQAEHDQAALRQ 992
Cdd:cd17651 401 RGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVG------DPEAPVDAAELRA 456
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
542-991 |
3.89e-101 |
|
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: 332.30 E-value: 3.89e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 542 PDRPAVVAADRTLDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVDTSQPAARRRTIL 621
Cdd:cd17652 1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 622 TNAGIRCALTQsgvdrngwaeglrlldvdllgtgqpqpvegsgdPEELAYVIHTSGSTGSPKGVMINHRGAVNTVLDIND 701
Cdd:cd17652 81 ADARPALLLTT---------------------------------PDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIA 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 702 RFGVGPDDRVLGLSNLGFDLSVYDVFGPLSVGGAVVLPDPQRRGDPSHWADLVGTHGVTVWNSVPAQLQMLhdylvsATA 781
Cdd:cd17652 128 AFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLLREHRITHVTLPPAALAAL------PPD 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 782 TVPDGLRLaMLSGDWIPVALpdqIRARVPGLRIVSLGGATEASIWSIWYpieQVDPEWRSIPYGRPLTNQSFHVLDAALR 861
Cdd:cd17652 202 DLPDLRTL-VVAGEACPAEL---VDRWAPGRRMINAYGPTETTVCATMA---GPLPGGGVPPIGRPVPGTRVYVLDARLR 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 862 PRPDLVSGELYIGGVGLAVGYLNDRERTAERFVVHP--QTGERLYRTGDLGRYLPDGTIEFLGREDLQVKIRGYRIELAE 939
Cdd:cd17652 275 PVPPGVPGELYIAGAGLARGYLNRPGLTAERFVADPfgAPGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGE 354
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1860141834 940 IEAALGGHPAVAGAVVVVDGDTPLERRLAAFVEPAGRPVTAAQAEHDQAALR 991
Cdd:cd17652 355 VEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPGAAPTAAELRAHLAER 406
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
530-990 |
5.09e-101 |
|
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: 332.36 E-value: 5.09e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 530 LHDRVVLQALSTPDRPAVVAADRTLDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVD 609
Cdd:cd12115 1 LHDLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 610 TSQPAARRRTILTNAGIRCALTqsgvdrngwaeglrlldvdllgtgqpqpvegsgDPEELAYVIHTSGSTGSPKGVMINH 689
Cdd:cd12115 81 PAYPPERLRFILEDAQARLVLT---------------------------------DPDDLAYVIYTSGSTGRPKGVAIEH 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 690 RGAVNTVLDINDRFGVGPDDRVLGLSNLGFDLSVYDVFGPLSVGGAVVLPDpqrrgDPSHWADLVGTHGVTVWNSVPAQL 769
Cdd:cd12115 128 RNAAAFLQWAAAAFSAEELAGVLASTSICFDLSVFELFGPLATGGKVVLAD-----NVLALPDLPAAAEVTLINTVPSAA 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 770 qmlhDYLVSATAtVPDGLRLAMLSGDWIPVALPDQIRARVPGLRIVSLGGATEASIWSIWYPIEQVDPEWRSIpyGRPLT 849
Cdd:cd12115 203 ----AELLRHDA-LPASVRVVNLAGEPLPRDLVQRLYARLQVERVVNLYGPSEDTTYSTVAPVPPGASGEVSI--GRPLA 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 850 NQSFHVLDAALRPRPDLVSGELYIGGVGLAVGYLNDRERTAERFVVHPQ-TGERLYRTGDLGRYLPDGTIEFLGREDLQV 928
Cdd:cd12115 276 NTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFgPGARLYRTGDLVRWRPDGLLEFLGRADNQV 355
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1860141834 929 KIRGYRIELAEIEAALGGHPAVAGAVVVVDGDTPLERRLAAFV--EPAGRPVTAAQAEHDQAAL 990
Cdd:cd12115 356 KVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIvaEPGAAGLVEDLRRHLGTRL 419
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
537-948 |
5.51e-98 |
|
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: 325.44 E-value: 5.51e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 537 QALSTPDRPAVVAADRTLDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVDTSQPAAR 616
Cdd:cd17655 6 QAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEER 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 617 RRTILTNAGIRCALTQSGVDRNGWAEGLRLLDVDllGTGQPQP---VEGSGDPEELAYVIHTSGSTGSPKGVMINHRGAV 693
Cdd:cd17655 86 IQYILEDSGADILLTQSHLQPPIAFIGLIDLLDE--DTIYHEEsenLEPVSKSDDLAYVIYTSGSTGKPKGVMIEHRGVV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 694 NTVLDINDRFGVGPDDRVLGLSNLGFDLSVYDVFGPLSVGGAVVLPDPQRRGDPSHWADLVGTHGVTVWNSVPAQLQMLh 773
Cdd:cd17655 164 NLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQALTQYIRQNRITIIDLTPAHLKLL- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 774 dylVSATATVPDGLRLAMLSGDWIPVALPDQIRARV-PGLRIVSLGGATE----ASIWsiwypieQVDPEWR---SIPYG 845
Cdd:cd17655 243 ---DAADDSEGLSLKHLIVGGEALSTELAKKIIELFgTNPTITNAYGPTEttvdASIY-------QYEPETDqqvSVPIG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 846 RPLTNQSFHVLDAALRPRPDLVSGELYIGGVGLAVGYLNDRERTAERFVVHP-QTGERLYRTGDLGRYLPDGTIEFLGRE 924
Cdd:cd17655 313 KPLGNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPfVPGERMYRTGDLARWLPDGNIEFLGRI 392
|
410 420
....*....|....*....|....
gi 1860141834 925 DLQVKIRGYRIELAEIEAALGGHP 948
Cdd:cd17655 393 DHQVKIRGYRIELGEIEARLLQHP 416
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
110-973 |
6.20e-98 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 352.72 E-value: 6.20e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 110 LDPERMTAAWRALIARHDMLRA--VVEADGAQRVLAEVPPFEVPVIDLTGRPEAVVDAAVSAVRAEMDHLVhtpdRWPLF 187
Cdd:PRK12316 2637 LDQAALEQAFDALVLRHETLRTrfVEVGEQTRQVILPNMSLRIVLEDCAGVADAAIRQRVAEEIQRPFDLA----RGPLL 2712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 188 AARITR-ADHRTVLHVSIDFLIADFISVQVVLDELHRLYHRPDE----PLPPLEITFRDYQLAERAVRDSPRHERDKQWW 262
Cdd:PRK12316 2713 RVRLLAlDGQEHVLVITQHHIVSDGWSMQVMVDELVQAYAGARRgeqpTLPPLPLQYADYAAWQRAWMDSGEGARQLDYW 2792
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 263 LARVDELPAAPELPT-VARPADSEGRFRRWETRLSSQVWEGLRQRAGRHGVSPSGAVLAAFSDTIAAYSRRSRFTLDITL 341
Cdd:PRK12316 2793 RERLGGEQPVLELPLdRPRPALQSHRGARLDVALDVALSRELLALARREGVTLFMLLLASFQVLLHRYSGQSDIRVGVPI 2872
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 342 LNRAPVhdQVNALVGDFTSVDLLAVDADPTRRFDERARDLQAQLWEDLDHRSFSGIEVMREIAR-RQGAEAALFPVVFTS 420
Cdd:PRK12316 2873 ANRNRA--ETERLIGFFVNTQVLRAQVDAQLAFRDLLGQVKEQALGAQAHQDLPFEQLVEALQPeRSLSHSPLFQVMYNH 2950
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 421 AIGitSAGAAADGAPLGELGYGISQTPQVWIDCQNIERDGGLVSNWDVREEVFPPGVVDDMFAAYDAVLHRLAGDDAAWT 500
Cdd:PRK12316 2951 QSG--ERAAAQLPGLHIESFAWDGAATQFDLALDTWESAEGLGASLTYATDLFDARTVERLARHWQNLLRGMVENPQRSV 3028
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 501 GTGHPDPPEATRDRRAETNRTQAPVP-AGMLHDRVVLQALSTPDRPAVVAADRTLDYAELLGRAAGVAEALTAAGCRRQE 579
Cdd:PRK12316 3029 DELAMLDAEERGQLLEAWNATAAEYPlERGVHRLFEEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDV 3108
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 580 LVAVVMDRGWEQVVAVLGALLAGCVYVPVDTSQPAARRRTILTNAGIRCALTQSGVdRNGWAEGLRLLDVDLLGTG-QPQ 658
Cdd:PRK12316 3109 LVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQSHL-RLPLAQGVQVLDLDRGDENyAEA 3187
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 659 PVEGSGDPEELAYVIHTSGSTGSPKGVMINHRGAVNTVLDINDRFGVGPDDRVLGLSNLGFDLSVYDVFGPLSVGGAVVL 738
Cdd:PRK12316 3188 NPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVL 3267
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 739 PDPQRRGDPSHWADLVGTHGVTVWNSVPAQLQMLhdyLVSATATVPDGLRLAMLSGDWIPvalPDQIRARVPGLRIVSLG 818
Cdd:PRK12316 3268 AGPEDWRDPALLVELINSEGVDVLHAYPSMLQAF---LEEEDAHRCTSLKRIVCGGEALP---ADLQQQVFAGLPLYNLY 3341
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 819 GATEASIWSIWYPIeqVDPEWRSIPYGRPLTNQSFHVLDAALRPRPDLVSGELYIGGVGLAVGYLNDRERTAERFVVHP- 897
Cdd:PRK12316 3342 GPTEATITVTHWQC--VEEGKDAVPIGRPIANRACYILDGSLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPf 3419
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1860141834 898 QTGERLYRTGDLGRYLPDGTIEFLGREDLQVKIRGYRIELAEIEAALGGHPAVAGAVVVVDGDtpleRRLAAFVEP 973
Cdd:PRK12316 3420 VPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAVDG----RQLVAYVVP 3491
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
537-973 |
2.19e-97 |
|
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: 322.85 E-value: 2.19e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 537 QALSTPDRPAVVAADRTLDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVDTSQPAAR 616
Cdd:cd17644 9 QVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLDPNYPQER 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 617 RRTILTNAGIRCALTQsgvdrngwaeglrlldvdllgtgqpqpvegsgdPEELAYVIHTSGSTGSPKGVMINHRGAVNTV 696
Cdd:cd17644 89 LTYILEDAQISVLLTQ---------------------------------PENLAYVIYTSGSTGKPKGVMIEHQSLVNLS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 697 LDINDRFGVGPDDRVLGLSNLGFDLSVYDVFGPLSVGGAVVLPDPQRRGDPSHWADLVGTHGVTVWNSVPAQLQMLHDYL 776
Cdd:cd17644 136 HGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLEDFVQYIQQWQLTVLSLPPAYWHLLVLEL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 777 VSATATVPDGLRLAMLSGDWIPVALPDQIRARV-PGLRIVSLGGATEASIWSIWYPIEQVDPEWR-SIPYGRPLTNQSFH 854
Cdd:cd17644 216 LLSTIDLPSSLRLVIVGGEAVQPELVRQWQKNVgNFIQLINVYGPTEATIAATVCRLTQLTERNItSVPIGRPIANTQVY 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 855 VLDAALRPRPDLVSGELYIGGVGLAVGYLNDRERTAERFVVHP---QTGERLYRTGDLGRYLPDGTIEFLGREDLQVKIR 931
Cdd:cd17644 296 ILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPfnsSESERLYKTGDLARYLPDGNIEYLGRIDNQVKIR 375
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1860141834 932 GYRIELAEIEAALGGHPAVAGAVVVVDGDTPLERRLAAFVEP 973
Cdd:cd17644 376 GFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIVP 417
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
542-992 |
5.26e-96 |
|
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: 318.16 E-value: 5.26e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 542 PDRPAVVAADRTLDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVDTSQPAARRRTIL 621
Cdd:cd17649 1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 622 TNAGIRCALTQsgvdrngwaeglrlldvdllgtgqpqpvegsgDPEELAYVIHTSGSTGSPKGVMINHrGAVNTVLD-IN 700
Cdd:cd17649 81 EDSGAGLLLTH--------------------------------HPRQLAYVIYTSGSTGTPKGVAVSH-GPLAAHCQaTA 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 701 DRFGVGPDDRVLGLSNLGFDLSVYDVFGPLSVGGAVVLPDPQRRGDPSHWADLVGTHGVTVWNSVPAQLQMLHDYLVSAT 780
Cdd:cd17649 128 ERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGVTVLDLPPAYLQQLAEEADRTG 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 781 ATVPDGLRLAMLSGDWIPVALpdQIRARVPGLRIVSLGGATEASIWSIWYPIEQVDPE-WRSIPYGRPLTNQSFHVLDAA 859
Cdd:cd17649 208 DGRPPSLRLYIFGGEALSPEL--LRRWLKAPVRLFNAYGPTEATVTPLVWKCEAGAARaGASMPIGRPLGGRSAYILDAD 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 860 LRPRPDLVSGELYIGGVGLAVGYLNDRERTAERFVVHP--QTGERLYRTGDLGRYLPDGTIEFLGREDLQVKIRGYRIEL 937
Cdd:cd17649 286 LNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPfgAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIEL 365
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1860141834 938 AEIEAALGGHPaVAGAVVVVDGDTPLERRLAAFVEPAGRPVTAAQAEHDQAALRQ 992
Cdd:cd17649 366 GEIEAALLEHP-GVREAAVVALDGAGGKQLVAYVVLRAAAAQPELRAQLRTALRA 419
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
542-993 |
1.34e-94 |
|
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: 314.25 E-value: 1.34e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 542 PDRPAVVAADRTLDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVDTSQPAARRRTIL 621
Cdd:cd17643 1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 622 TNAGIRCALTqsgvdrngwaeglrlldvdllgtgqpqpvegsgDPEELAYVIHTSGSTGSPKGVMINHRGAVNTVLDIND 701
Cdd:cd17643 81 ADSGPSLLLT---------------------------------DPDDLAYVIYTSGSTGRPKGVVVSHANVLALFAATQR 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 702 RFGVGPDDRVLGLSNLGFDLSVYDVFGPLSVGGAVVLPDPQRRGDPSHWADLVGTHGVTVWNSVPAQLQMLHDYLVSATa 781
Cdd:cd17643 128 WFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGVTVLNQTPSAFYQLVEAADRDG- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 782 TVPDGLRLAMLSGDWIPVAL--PDQIRARVPGLRIVSLGGATEASIWSIWYPIEQVD-PEWRSIPYGRPLTNQSFHVLDA 858
Cdd:cd17643 207 RDPLALRYVIFGGEALEAAMlrPWAGRFGLDRPQLVNMYGITETTVHVTFRPLDAADlPAAAASPIGRPLPGLRVYVLDA 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 859 ALRPRPDLVSGELYIGGVGLAVGYLNDRERTAERFVVHPQT--GERLYRTGDLGRYLPDGTIEFLGREDLQVKIRGYRIE 936
Cdd:cd17643 287 DGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFGgpGSRMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIE 366
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1860141834 937 LAEIEAALGGHPAVAGAVVVVDGDTPLERRLAAFVepagrpVTAAQAEHDQAALRQL 993
Cdd:cd17643 367 LGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYV------VADDGAAADIAELRAL 417
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
537-931 |
2.74e-94 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 311.94 E-value: 2.74e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 537 QALSTPDRPAV-VAADRTLDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVDTSQPAA 615
Cdd:pfam00501 4 QAARTPDKTALeVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 616 RRRTILTNAGIRCALTQSG---------------------VDRNGWAEGLRLLDVDLLGTGQPQPVEgSGDPEELAYVIH 674
Cdd:pfam00501 84 ELAYILEDSGAKVLITDDAlkleellealgklevvklvlvLDRDPVLKEEPLPEEAKPADVPPPPPP-PPDPDDLAYIIY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 675 TSGSTGSPKGVMINHRGAVNTVLDI----NDRFGVGPDDRVLGLSNLGFDLSV-YDVFGPLSVGGAVVLPDPQRRGDPSH 749
Cdd:pfam00501 163 TSGTTGKPKGVMLTHRNLVANVLSIkrvrPRGFGLGPDDRVLSTLPLFHDFGLsLGLLGPLLAGATVVLPPGFPALDPAA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 750 WADLVGTHGVTVWNSVPAQLQMLHDYLVSATATVPdGLRLAMLSGDWIPVALPDQIRARVPGlRIVSLGGATEASIWSIW 829
Cdd:pfam00501 243 LLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLS-SLRLVLSGGAPLPPELARRFRELFGG-ALVNGYGLTETTGVVTT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 830 YPIEqvDPEWRSIP-YGRPLTNQSFHVLDAA-LRPRPDLVSGELYIGGVGLAVGYLNDRERTAERFVVhpqtgERLYRTG 907
Cdd:pfam00501 321 PLPL--DEDLRSLGsVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDE-----DGWYRTG 393
|
410 420
....*....|....*....|....
gi 1860141834 908 DLGRYLPDGTIEFLGREDLQVKIR 931
Cdd:pfam00501 394 DLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
109-948 |
8.05e-94 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 333.55 E-value: 8.05e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 109 ELDPERMTAAWRALIARHDMLRA-VVEADGA--QRVLAEVPPFEVPVIDLTGRPEAVVDAAVSAVRAEMDHLVHTPDRWP 185
Cdd:PRK10252 41 ELDAPLLARAVVAGLAEADTLRMrFTEDNGEvwQWVDPALTFPLPEIIDLRTQPDPHAAAQALMQADLQQDLRVDSGKPL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 186 LFAARITRADHRTVLHVSIDFLIADFISVQVVLDELHRLY-------HRPDEPLPPLEITFRDYQlaerAVRDSPRHERD 258
Cdd:PRK10252 121 VFHQLIQLGDNRWYWYQRYHHLLVDGFSFPAITRRIAAIYcawlrgePTPASPFTPFADVVEEYQ----RYRASEAWQRD 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 259 KQWWLARVDELPAAPEL---PTVARPADSegRFRRWETRLSSQVwegLRQRAGRHGVSPSGAVLAAFSdtiAAYSRRSRF 335
Cdd:PRK10252 197 AAFWAEQRRQLPPPASLspaPLPGRSASA--DILRLKLEFTDGA---FRQLAAQASGVQRPDLALALV---ALWLGRLCG 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 336 TLDITL-------LNRAPVhdQVNALVgdfTSVDLLAVDADPTRRFDERARDLQAQLWEDLDHRSFSGIEVMREIARRQG 408
Cdd:PRK10252 269 RMDYAAgfifmrrLGSAAL--TATGPV---LNVLPLRVHIAAQETLPELATRLAAQLKKMRRHQRYDAEQIVRDSGRAAG 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 409 AEAALFPVV----------FTSAIGITSAGAAAdgaPLGELGYGISqtpqvwidcqnIERDGGLVSNWDVREEVFPPGVV 478
Cdd:PRK10252 344 DEPLFGPVLnikvfdyqldFPGVQAQTHTLATG---PVNDLELALF-----------PDEHGGLSIEILANPQRYDEATL 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 479 DDMFAAYDAVLHRLAGDDAAWTGtghpDPPEAT---RDRRAETNRTQAPVPAGMLHDRVVLQALSTPDRPAVVAADRTLD 555
Cdd:PRK10252 410 IAHAERLKALIAQFAADPALLCG----DVDILLpgeYAQLAQVNATAVEIPETTLSALVAQQAAKTPDAPALADARYQFS 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 556 YAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVDTSQPAARRRTILTNAGIRCALTQSGV 635
Cdd:PRK10252 486 YREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTADQ 565
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 636 -DRNGWAEGLRLLDVDLLGTGQPQPVEGSGDPEELAYVIHTSGSTGSPKGVMINHRGAVNTVLDINDRFGVGPDDRVLGL 714
Cdd:PRK10252 566 lPRFADVPDLTSLCYNAPLAPQGAAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTADDVVLQK 645
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 715 SNLGFDLSVYDVFGPLSVGGAVVLPDPQRRGDPSHWADLVGTHGVTVWNSVPAQLQMLHDYLVSATATVPDG-LRLAMLS 793
Cdd:PRK10252 646 TPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTTHFVPSMLAAFVASLTPEGARQSCAsLRQVFCS 725
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 794 GDWIPVALPDQIRARVpGLRIVSLGGATEASIWSIWYPI---EQVDPEWRSIPYGRPLTNQSFHVLDAALRPRPDLVSGE 870
Cdd:PRK10252 726 GEALPADLCREWQQLT-GAPLHNLYGPTEAAVDVSWYPAfgeELAAVRGSSVPIGYPVWNTGLRILDARMRPVPPGVAGD 804
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1860141834 871 LYIGGVGLAVGYLNDRERTAERFVVHP-QTGERLYRTGDLGRYLPDGTIEFLGREDLQVKIRGYRIELAEIEAALGGHP 948
Cdd:PRK10252 805 LYLTGIQLAQGYLGRPDLTASRFIADPfAPGERMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALP 883
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
110-992 |
4.15e-93 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 337.31 E-value: 4.15e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 110 LDPERMTAAWRALIARHDMLRA-VVEADGAQRVLAEV-PPFEVPVIDLTGRPEAVVDAAVSAVRAEMDHLVHTPDRWPLF 187
Cdd:PRK12316 4136 LDVERFRAAWQAALDRHDVLRSgFVWQGELGRPLQVVhKQVSLPFAELDWRGRADLQAALDALAAAERERGFDLQRAPLL 4215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 188 AARITR-ADHRTVLHVSIDFLIADFISVQVVLDELHRLYhrPDEPLPPLEITFRDYqLAERAVRDSPRHERDKQWWLARV 266
Cdd:PRK12316 4216 RLVLVRtAEGRHHLIYTNHHILMDGWSNSQLLGEVLERY--SGRPPAQPGGRYRDY-IAWLQRQDAAASEAFWREQLAAL 4292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 267 DELPAAPELPTVA--RPADSEGRFRRwetRLSSQVWEGLRQRAGRHGVSPSGAVLAAFSDTIAAYSRRSRFTLDITLLNR 344
Cdd:PRK12316 4293 DEPTRLAQAIARAdlRSANGYGEHVR---ELDATATARLREFARTQRVTLNTLVQAAWLLLLQRYTGQDTVAFGATVAGR 4369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 345 APVHDQVNALVGDFTSVDLLAVDADPTRRFDERARDLQAQLWEDLDHRSFSGIEVMREiaRRQGAEAaLFPVVFTSAiGI 424
Cdd:PRK12316 4370 PAELPGIEGQIGLFINTLPVIATPRAQQSVVEWLQQVQRQNLALREHEHTPLYEIQRW--AGQGGEA-LFDSLLVFE-NY 4445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 425 TSAGAAADGAPLGeLGYGISQTPQVWIDCQNIERDGG--LVSNWDVREEVFPPGVVDDMFAAYDAVLHRLAGDDAAWTGT 502
Cdd:PRK12316 4446 PVSEALQQGAPGG-LRFGEVTNHEQTNYPLTLAVGLGetLSLQFSYDRGHFDAATIERLARHLTNLLEAMAEDPQRRLGE 4524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 503 GHPDPPEATRDRRAETNRTQAPVPAG-MLHDRVVLQALSTPDRPAVVAADRTLDYAELLGRAAGVAEALTAAGCRRQELV 581
Cdd:PRK12316 4525 LQLLEKAEQQRIVALWNRTDAGYPATrCVHQLVAERARMTPDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLV 4604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 582 AVVMDRGWEQVVAVLGALLAGCVYVPVDTSQPAARRRTILTNAGIRCALTQSGV-DRNGWAEGLRLLDVDLLGTGQPQPV 660
Cdd:PRK12316 4605 GIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALLLTQSHLlQRLPIPDGLASLALDRDEDWEGFPA 4684
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 661 EGSG---DPEELAYVIHTSGSTGSPKGVMINHRGAVNTVLDINDRFGVGPDDRVLGLSNLGFDLSVYDVFGPLSVGGAVV 737
Cdd:PRK12316 4685 HDPAvrlHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVV 4764
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 738 LPDPQRRgDPSHWADLVGTHGVTVWNSVPAQLQMLHDYlvSATATVPDGLRLAMLSGDWIPVALPDQIRARVPGLRIVSL 817
Cdd:PRK12316 4765 IRDDSLW-DPERLYAEIHEHRVTVLVFPPVYLQQLAEH--AERDGEPPSLRVYCFGGEAVAQASYDLAWRALKPVYLFNG 4841
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 818 GGATEASIWSIWYPIEQVDPEWRS-IPYGRPLTNQSFHVLDAALRPRPDLVSGELYIGGVGLAVGYLNDRERTAERFVVH 896
Cdd:PRK12316 4842 YGPTETTVTVLLWKARDGDACGAAyMPIGTPLGNRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPD 4921
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 897 P--QTGERLYRTGDLGRYLPDGTIEFLGREDLQVKIRGYRIELAEIEAALGGHPAVAGAVVVVDGDtPLERRLAAFVEPA 974
Cdd:PRK12316 4922 PfgAPGGRLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEG-AVGKQLVGYVVPQ 5000
|
890
....*....|....*...
gi 1860141834 975 GRPVtaAQAEHDQAALRQ 992
Cdd:PRK12316 5001 DPAL--ADADEAQAELRD 5016
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
109-948 |
4.42e-92 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 334.06 E-value: 4.42e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 109 ELDPERMTAAWRALIARHDMLRAV-VEADGA--QRVLAEvPPFEVPVIDLTGRPEAVVDAAVSAVRAEMDHLVHTPDRWP 185
Cdd:PRK05691 709 ELDEAALRASFQRLVERHESLRTRfYERDGValQRIDAQ-GEFALQRIDLSDLPEAEREARAAQIREEEARQPFDLEKGP 787
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 186 LFAARITR-ADHRTVLHVSIDFLIADFISVQVVLDELHRLYHRPDE----PLPPLEITFRDYQLAERAVRDSPRHERDKQ 260
Cdd:PRK05691 788 LLRVTLVRlDDEEHQLLVTLHHIVADGWSLNILLDEFSRLYAAACQgqtaELAPLPLGYADYGAWQRQWLAQGEAARQLA 867
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 261 WWLARV-DELPAAPELPTVARPADSEGRFRRWETRLSSQVWEGLRQRAGRHGVSPSGAVLAAFSDTIAAYSRRSRFTLDI 339
Cdd:PRK05691 868 YWKAQLgDEQPVLELATDHPRSARQAHSAARYSLRVDASLSEALRGLAQAHQATLFMVLLAAFQALLHRYSGQGDIRIGV 947
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 340 TLLNRAPVHDQvnALVGDFTSVDLLAVDADPTRRFDE-----RARDLQAQLWEDLDhrsfsgIEVMREiARRQGAEAALF 414
Cdd:PRK05691 948 PNANRPRLETQ--GLVGFFINTQVLRAQLDGRLPFTAllaqvRQATLGAQAHQDLP------FEQLVE-ALPQAREQGLF 1018
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 415 PVVFTSAIGITSAGAAADGAPLGELGYGiSQTPQVWIDCQNIE-RDGGLVSNWDVREEVFPPGVVDDMFAAYDAVLHRLA 493
Cdd:PRK05691 1019 QVMFNHQQRDLSALRRLPGLLAEELPWH-SREAKFDLQLHSEEdRNGRLTLSFDYAAELFDAATIERLAEHFLALLEQVC 1097
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 494 GDDAAWTGtghpDPP---EATRDRRAETNRTQAPVPAGMLHDRVVLQALSTPDRPAVVAADRTLDYAELLGRAAGVAEAL 570
Cdd:PRK05691 1098 EDPQRALG----DVQlldAAERAQLAQWGQAPCAPAQAWLPELLNEQARQTPERIALVWDGGSLDYAELHAQANRLAHYL 1173
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 571 TAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVDTSQPAARRRTILTNAGIRCALTQSGV-DRNGWAEGLRLLDV 649
Cdd:PRK05691 1174 RDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQSHLlERLPQAEGVSAIAL 1253
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 650 DLLGT----GQPQPVEGSGDpeELAYVIHTSGSTGSPKGVMINHRGAVNTVLDINDRFGVGPDDRVLGLSNLGFDLSVYD 725
Cdd:PRK05691 1254 DSLHLdswpSQAPGLHLHGD--NLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPISFDVSVWE 1331
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 726 VFGPLSVGGAVVLPDPQRRGDPSHWADLVGTHGVTVWNSVPAQLQMLHDYLVSATATvpdGLRLAMLSGDWIPVALPDQI 805
Cdd:PRK05691 1332 CFWPLITGCRLVLAGPGEHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLAAACT---SLRRLFSGGEALPAELRNRV 1408
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 806 RARVPGLRIVSLGGATEASIWSIWYPIEQVDPEwRSiPYGRPLTNQSFHVLDAALRPRPDLVSGELYIGGVGLAVGYLND 885
Cdd:PRK05691 1409 LQRLPQVQLHNRYGPTETAINVTHWQCQAEDGE-RS-PIGRPLGNVLCRVLDAELNLLPPGVAGELCIGGAGLARGYLGR 1486
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1860141834 886 RERTAERFVVHP--QTGERLYRTGDLGRYLPDGTIEFLGREDLQVKIRGYRIELAEIEAALGGHP 948
Cdd:PRK05691 1487 PALTAERFVPDPlgEDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQP 1551
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
538-973 |
1.41e-87 |
|
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: 293.77 E-value: 1.41e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 538 ALSTPDRPAVVAADRTLDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVDTSQPAARR 617
Cdd:cd05945 1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 618 RTILTNAGircaltqsgvdrngwaeglrlldVDLLGTgqpqpvegsgDPEELAYVIHTSGSTGSPKGVMINHRGAVNTVL 697
Cdd:cd05945 81 REILDAAK-----------------------PALLIA----------DGDDNAYIIFTSGSTGRPKGVQISHDNLVSFTN 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 698 DINDRFGVGPDDRVLGLSNLGFDLSVYDVFGPLSVGGAVVLPDPQRRGDPSHWADLVGTHGVTVWNSVPAQLQMLhdyLV 777
Cdd:cd05945 128 WMLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADPKQLFRFLAEHGITVWVSTPSFAAMC---LL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 778 SATATVP--DGLRLAMLSGDWIPVALPDQIRARVPGLRIVSLGGATEASIWSIWY-----PIEQVDPewrsIPYGRPLTN 850
Cdd:cd05945 205 SPTFTPEslPSLRHFLFCGEVLPHKTARALQQRFPDARIYNTYGPTEATVAVTYIevtpeVLDGYDR----LPIGYAKPG 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 851 QSFHVLDAALRPRPDLVSGELYIGGVGLAVGYLNDRERTAERFvvHPQTGERLYRTGDLGRYLPDGTIEFLGREDLQVKI 930
Cdd:cd05945 281 AKLVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAF--FPDEGQRAYRTGDLVRLEADGLLFYRGRLDFQVKL 358
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1860141834 931 RGYRIELAEIEAALGGHPAVAGAVVVVDGDTPLERRLAAFVEP 973
Cdd:cd05945 359 NGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVP 401
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
110-948 |
4.45e-87 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 318.05 E-value: 4.45e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 110 LDPERMTAAWRALIARHDMLRA-VVEADGAQRVLAEV-PPFEVPVIDLTGRPEAVVDAAVSAVRAEMDHLVHTPDRWPLF 187
Cdd:PRK12316 1590 LDPDRFRAAWQATVDRHEILRSgFLWQDGLEQPLQVIhKQVELPFAELDWRGREDLGQALDALAQAERQKGFDLTRAPLL 1669
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 188 AARITR-ADHRTVLHVSIDFLIADFISVQVVLDELhrLYHRPDEPLPPLEITFRDYqLAERAVRDSPRHERdkqWWLARV 266
Cdd:PRK12316 1670 RLVLVRtGEGRHHLIYTNHHILMDGWSNAQLLGEV--LQRYAGQPVAAPGGRYRDY-IAWLQRQDAAASEA---FWKEQL 1743
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 267 DELPAAPELPTVARPADSEGRFRRWETRLSSQVWEGLRQRAGRHGVSPSGAVLAAFSDTIAAYSRRSRFTLDITLLNRAP 346
Cdd:PRK12316 1744 AALEEPTRLAQAARTEDGQVGYGDHQQLLDPAQTRALAEFARAQKVTLNTLVQAAWLLLLQRYTGQETVAFGATVAGRPA 1823
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 347 VHDQVNALVGDFTSVDLLAVDADPTRRFDERARDLQAQLWEDLDHRSFSGIEVMREIArrQGAEAaLFP--VVFTSaigI 424
Cdd:PRK12316 1824 ELPGIEQQIGLFINTLPVIAAPRPDQSVADWLQEVQALNLALREHEHTPLYDIQRWAG--QGGEA-LFDslLVFEN---Y 1897
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 425 TSAGAAADGAPLG-ELGYGISQTPQVWIDCQNIERDGGLVSNWDVREEVFPPGVVDDMFAAYDAVLHRLAGDDAAWTGTG 503
Cdd:PRK12316 1898 PVAEALKQGAPAGlVFGRVSNHEQTNYPLTLAVTLGETLSLQYSYDRGHFDAAAIERLDRHLLHLLEQMAEDAQAALGEL 1977
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 504 HPDPPEATRDRRAETNRTQAPVPAGML-HDRVVLQALSTPDRPAVVAADRTLDYAELLGRAAGVAEALTAAGCRRQELVA 582
Cdd:PRK12316 1978 ALLDAGERQRILADWDRTPEAYPRGPGvHQRIAEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVA 2057
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 583 VVMDRGWEQVVAVLGALLAGCVYVPVDTSQPAARRRTILTNAGIRCALTQSGV-DRNGWAEGLRLLDVDLLGTGQPQPV- 660
Cdd:PRK12316 2058 IAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQRHLlERLPLPAGVARLPLDRDAEWADYPDt 2137
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 661 --EGSGDPEELAYVIHTSGSTGSPKGVMINHRGAVNTVLDINDRFGVGPDDRVLGLSNLGFDLSVYDVFGPLSVGGAVVL 738
Cdd:PRK12316 2138 apAVQLAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAHEQWFHPLLNGARVLI 2217
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 739 PDPQRRgDPSHWADLVGTHGVTVWNSVPAQLQMLHDylVSATATVPDGLRLAMLSGDWIPVALPDQIRARVPGLRIVSLG 818
Cdd:PRK12316 2218 RDDELW-DPEQLYDEMERHGVTILDFPPVYLQQLAE--HAERDGRPPAVRVYCFGGEAVPAASLRLAWEALRPVYLFNGY 2294
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 819 GATEASIWSIWYPIEQVDPE-WRSIPYGRPLTNQSFHVLDAALRPRPDLVSGELYIGGVGLAVGYLNDRERTAERFVVHP 897
Cdd:PRK12316 2295 GPTEAVVTPLLWKCRPQDPCgAAYVPIGRALGNRRAYILDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDP 2374
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|...
gi 1860141834 898 --QTGERLYRTGDLGRYLPDGTIEFLGREDLQVKIRGYRIELAEIEAALGGHP 948
Cdd:PRK12316 2375 fsASGERLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHP 2427
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
530-1005 |
2.41e-85 |
|
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: 288.67 E-value: 2.41e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 530 LHDRVVLQALSTPDRPAVVAADRTLDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVD 609
Cdd:cd05918 1 VHDLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 610 TSQPAARRRTILTNAGIRCALTqsgvdrngwaeglrlldvdllgtgqpqpvegsGDPEELAYVIHTSGSTGSPKGVMINH 689
Cdd:cd05918 81 PSHPLQRLQEILQDTGAKVVLT--------------------------------SSPSDAAYVIFTSGSTGKPKGVVIEH 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 690 RGAVNTVLDINDRFGVGPDDRVLGLSNLGFDLSVYDVFGPLSVGGAVVLP-DPQRRGDPshwADLVGTHGVTVWNSVPAQ 768
Cdd:cd05918 129 RALSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLCIPsEEDRLNDL---AGFINRLRVTWAFLTPSV 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 769 LQMLHDylvsatATVPDgLRLAMLSGDwiPVAlPDQIRARVPGLRIVSLGGATEASIWSIwypIEQVDPEWRSIPYGRPL 848
Cdd:cd05918 206 ARLLDP------EDVPS-LRTLVLGGE--ALT-QSDVDTWADRVRLINAYGPAECTIAAT---VSPVVPSTDPRNIGRPL 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 849 tNQSFHVLDAA--LRPRPDLVSGELYIGGVGLAVGYLNDRERTAERFVVHP--------QTGERLYRTGDLGRYLPDGTI 918
Cdd:cd05918 273 -GATCWVVDPDnhDRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPawlkqegsGRGRRLYRTGDLVRYNPDGSL 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 919 EFLGREDLQVKIRGYRIELAEIEAALGGHPAVAGAVVV---VDGDTPLERRLAAFVEPAGRPVTAAQAEHDQAALRQLGV 995
Cdd:cd05918 352 EYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKEVVVevvKPKDGSSSPQLVAFVVLDGSSSGSGDGDSLFLEPSDEFR 431
|
490
....*....|
gi 1860141834 996 DACVDADSTL 1005
Cdd:cd05918 432 ALVAELRSKL 441
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
542-985 |
4.80e-85 |
|
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: 286.67 E-value: 4.80e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 542 PDRPAVVAADRTLDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVDTSQPAARRRTIL 621
Cdd:cd17650 1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 622 TNAGIRCALTQsgvdrngwaeglrlldvdllgtgqpqpvegsgdPEELAYVIHTSGSTGSPKGVMINHRGAVNTVLDIND 701
Cdd:cd17650 81 EDSGAKLLLTQ---------------------------------PEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWRR 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 702 RFGVGPDD-RVLGLSNLGFDLSVYDVFGPLSVGGAVVLPDPQRRGDPSHWADLVGTHGVTVWNSVPAQLQMLHDYLVSAT 780
Cdd:cd17650 128 EYELDSFPvRLLQMASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSRITLMESTPALIRPVMAYVYRNG 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 781 ATVPDgLRLAMLSGDWIPVALPDQIRARV-PGLRIVSLGGATEASIWSIWYPIEQVD-PEWRSIPYGRPLTNQSFHVLDA 858
Cdd:cd17650 208 LDLSA-MRLLIVGSDGCKAQDFKTLAARFgQGMRIINSYGVTEATIDSTYYEEGRDPlGDSANVPIGRPLPNTAMYVLDE 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 859 ALRPRPDLVSGELYIGGVGLAVGYLNDRERTAERFVVHP-QTGERLYRTGDLGRYLPDGTIEFLGREDLQVKIRGYRIEL 937
Cdd:cd17650 287 RLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPfAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIEL 366
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1860141834 938 AEIEAALGGHPAVAGAVVVVDGDTPLERRLAAFVEPAGRPVTAAQAEH 985
Cdd:cd17650 367 GEIESQLARHPAIDEAVVAVREDKGGEARLCAYVVAAATLNTAELRAF 414
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
110-948 |
3.36e-84 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 308.63 E-value: 3.36e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 110 LDPERMTAAWRALIARHDMLRA-VVEADGAQRVL------AEVPpfeVPVIDLTGRPeavvdaavsAVRAEMDHLVHTP- 181
Cdd:PRK12467 2680 LDVERFRTAWQAVIDRHEILRSgFLWDGELEEPLqvvykqARLP---FSRLDWRDRA---------DLEQALDALAAADr 2747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 182 ------DRWPLFAARITRAD-HRTVLHVSIDFLIADFISVQVVLDELhrLYHRPDEPLPPLEITFRDYqLAERAVRDSPR 254
Cdd:PRK12467 2748 qqgfdlLSAPLLRLTLVRTGeDRHHLIYTNHHILMDGWSGSQLLGEV--LQRYFGQPPPAREGRYRDY-IAWLQAQDAEA 2824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 255 HERdkqWWLARVDELPAAPELPTVARPADSEG------RFRRWETRLSSQvwegLRQRAGRHGVSPSGAVLAAFSDTIAA 328
Cdd:PRK12467 2825 SEA---FWKEQLAALEEPTRLARALYPAPAEAvaghgaHYLHLDATQTRQ----LIEFARRHRVTLNTLVQGAWLLLLQR 2897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 329 YSRRSRFTLDITLLNRAPVHDQVNALVGDFtsVDLLAVDADPtrRFDERARD-LQAQLWEDLDHRSFSGIEVMrEIAR-- 405
Cdd:PRK12467 2898 FTGQDTVCFGATVAGRPAQLRGAEQQLGLF--INTLPVIASP--RAEQTVSDwLQQVQAQNLALREFEHTPLA-DIQRwa 2972
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 406 RQGAEAaLFP--VVFTSaigITSAGAAADGAPLG-ELGYGISQTPQVWIDCQNIERDGGLVSNWDVREEVFPPGVVDDMF 482
Cdd:PRK12467 2973 GQGGEA-LFDsiLVFEN---YPISEALKQGAPSGlRFGAVSSREQTNYPLTLAVGLGDTLELEFSYDRQHFDAAAIERLA 3048
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 483 AAYDAVLHRLAGDDAAWTGTGHPDPPEATRDRRAETNRTQAPVPAGML-HDRVVLQALSTPDRPAVVAADRTLDYAELLG 561
Cdd:PRK12467 3049 ESFDRLLQAMLNNPAARLGELPTLAAHERRQVLHAWNATAAAYPSERLvHQLIEAQVARTPEAPALVFGDQQLSYAELNR 3128
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 562 RAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVDTSQPAARRRTILTNAGIRCALTQSGV-DRNGW 640
Cdd:PRK12467 3129 RANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLTQAHLlEQLPA 3208
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 641 AEGLRLLDVDLLGTG-----QPQPVEgsgDPEELAYVIHTSGSTGSPKGVMINHRGAVNTVLDINDRFGVGPDDRVLGLS 715
Cdd:PRK12467 3209 PAGDTALTLDRLDLNgysenNPSTRV---MGENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFM 3285
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 716 NLGFDLSVYDVFGPLSVGGAVVLPDPQRRGDPSHWAdLVGTHGVTVWNSVPAQLQMLHDYLVSATATvpdGLRLAMLSGD 795
Cdd:PRK12467 3286 SFSFDGAQERFLWTLICGGCLVVRDNDLWDPEELWQ-AIHAHRISIACFPPAYLQQFAEDAGGADCA---SLDIYVFGGE 3361
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 796 WIPVALPDQIRARVPGLRIVSLGGATEASIWSI-WYPIEQVDPEWRSIPYGRPLTNQSFHVLDAALRPRPDLVSGELYIG 874
Cdd:PRK12467 3362 AVPPAAFEQVKRKLKPRGLTNGYGPTEAVVTVTlWKCGGDAVCEAPYAPIGRPVAGRSIYVLDGQLNPVPVGVAGELYIG 3441
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1860141834 875 GVGLAVGYLNDRERTAERFVVHP--QTGERLYRTGDLGRYLPDGTIEFLGREDLQVKIRGYRIELAEIEAALGGHP 948
Cdd:PRK12467 3442 GVGLARGYHQRPSLTAERFVADPfsGSGGRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHP 3517
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
537-948 |
3.19e-81 |
|
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: 275.20 E-value: 3.19e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 537 QALSTPDRPAVVAADRTLDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVDTSQPAAR 616
Cdd:cd17645 7 QVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGER 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 617 RRTILTNAGIRCALTqsgvdrngwaeglrlldvdllgtgqpqpvegsgDPEELAYVIHTSGSTGSPKGVMINHRGAVNTV 696
Cdd:cd17645 87 IAYMLADSSAKILLT---------------------------------NPDDLAYVIYTSGSTGLPKGVMIEHHNLVNLC 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 697 LDINDRFGVGPDDRVLGLSNLGFDLSVYDVFGPLSVGGAVVLPDPQRRGDPSHWADLVGTHGVTVwNSVPAQLQMlhdyl 776
Cdd:cd17645 134 EWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDLDALNDYFNQEGITI-SFLPTGAAE----- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 777 vSATATVPDGLRLAMLSGDWIPvalpdqiRARVPGLRIVSLGGATEASIWSIWYPIeqvDPEWRSIPYGRPLTNQSFHVL 856
Cdd:cd17645 208 -QFMQLDNQSLRVLLTGGDKLK-------KIERKGYKLVNNYGPTENTVVATSFEI---DKPYANIPIGKPIDNTRVYIL 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 857 DAALRPRPDLVSGELYIGGVGLAVGYLNDRERTAERFVVHPQ-TGERLYRTGDLGRYLPDGTIEFLGREDLQVKIRGYRI 935
Cdd:cd17645 277 DEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFvPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRI 356
|
410
....*....|...
gi 1860141834 936 ELAEIEAALGGHP 948
Cdd:cd17645 357 EPGEIEPFLMNHP 369
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
537-944 |
7.10e-81 |
|
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: 273.80 E-value: 7.10e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 537 QALSTPDRPAVVAADRTLDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVDTSQPAAR 616
Cdd:cd17653 6 IAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 617 RRTILTNAGIRCALTQSGvdrngwaeglrlldvdllgtgqpqpvegsgdPEELAYVIHTSGSTGSPKGVMINHRGAVNTV 696
Cdd:cd17653 86 IQAILRTSGATLLLTTDS-------------------------------PDDLAYIIFTSGSTGIPKGVMVPHRGVLNYV 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 697 LDINDRFGVGPDDRVLGLSNLGFDLSVYDVFGPLSVGGAVVLPDPqrrgdPSHWADLVGThgVTVWNSVPAQLQMLhdyl 776
Cdd:cd17653 135 SQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGTLVLADP-----SDPFAHVART--VDALMSTPSILSTL---- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 777 vsaTATVPDGLRLAMLSGDWIPvalPDQIRARVPGLRIVSLGGATEASIWSIwypIEQVDPEwRSIPYGRPLTNQSFHVL 856
Cdd:cd17653 204 ---SPQDFPNLKTIFLGGEAVP---PSLLDRWSPGRRLYNAYGPTECTISST---MTELLPG-QPVTIGKPIPNSTCYIL 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 857 DAALRPRPDLVSGELYIGGVGLAVGYLNDRERTAERFVVHP-QTGERLYRTGDLGRYLPDGTIEFLGREDLQVKIRGYRI 935
Cdd:cd17653 274 DADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPfWPGSRMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRI 353
|
....*....
gi 1860141834 936 ELAEIEAAL 944
Cdd:cd17653 354 NLEEIEEVV 362
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
542-948 |
6.83e-79 |
|
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: 268.88 E-value: 6.83e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 542 PDRPAVVAADRTLDYAELLGRAAGVAEALTAAGC-RRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVDTSQPAARRRTI 620
Cdd:cd17648 1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAEiRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 621 LTNAGIRCALTqsgvdrngwaeglrlldvdllgtgqpqpvegsgDPEELAYVIHTSGSTGSPKGVMINHRGAVNTVLDIN 700
Cdd:cd17648 81 LEDTGARVVIT---------------------------------NSTDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSLS 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 701 DRFGV-GPDD-RVLGLSNLGFDLSVYDVFGPLSVGGAVVLPDPQRRGDPSHWADLVGTHGVTVWNSVPAQLQMLHdyLVS 778
Cdd:cd17648 128 ERYFGrDNGDeAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPDRFYAYINREKVTYLSGTPSVLQQYD--LAR 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 779 ATAtvpdgLRLAMLSGDWIPVALPDQIRARVPGlRIVSLGGATEASIWSIWYPIEQVDPEWRSIpyGRPLTNQSFHVLDA 858
Cdd:cd17648 206 LPH-----LKRVDAAGEEFTAPVFEKLRSRFAG-LIINAYGPTETTVTNHKRFFPGDQRFDKSL--GRPVRNTKCYVLND 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 859 ALRPRPDLVSGELYIGGVGLAVGYLNDRERTAERFVVHP-QTGE--------RLYRTGDLGRYLPDGTIEFLGREDLQVK 929
Cdd:cd17648 278 AMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFLPNPfQTEQerargrnaRLYKTGDLVRWLPSGELEYLGRNDFQVK 357
|
410
....*....|....*....
gi 1860141834 930 IRGYRIELAEIEAALGGHP 948
Cdd:cd17648 358 IRGQRIEPGEVEAALASYP 376
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
541-973 |
6.96e-77 |
|
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: 263.95 E-value: 6.96e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 541 TPDRPAVVAADRTLDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVDTSQPAARRRTI 620
Cdd:cd17656 1 TPDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 621 LTNAGIRCALTQ----SGVDRNGwaeGLRLLDVDLLGTGQPQPVEGSGDPEELAYVIHTSGSTGSPKGVMINHRGAVNTV 696
Cdd:cd17656 81 MLDSGVRVVLTQrhlkSKLSFNK---STILLEDPSISQEDTSNIDYINNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 697 LDINDRFGVGPDDRVLGLSNLGFDLSVYDVFGPLSVGGAVVLPDPQRRGDPSHWADLVGTHGVTVWNSVPAQLQMLHDyL 776
Cdd:cd17656 158 HFEREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNIEVVFLPVAFLKFIFS-E 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 777 VSATATVPDGLRLAMLSGDWIPVALPDQIRARVPGLRIVSLGGATEASIWSIwYPIEQvDPEWRSIP-YGRPLTNQSFHV 855
Cdd:cd17656 237 REFINRFPTCVKHIITAGEQLVITNEFKEMLHEHNVHLHNHYGPSETHVVTT-YTINP-EAEIPELPpIGKPISNTWIYI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 856 LDAALRPRPDLVSGELYIGGVGLAVGYLNDRERTAERFVVHP-QTGERLYRTGDLGRYLPDGTIEFLGREDLQVKIRGYR 934
Cdd:cd17656 315 LDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPfDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYR 394
|
410 420 430
....*....|....*....|....*....|....*....
gi 1860141834 935 IELAEIEAALGGHPAVAGAVVVVDGDTPLERRLAAFVEP 973
Cdd:cd17656 395 IELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVM 433
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
530-948 |
1.66e-74 |
|
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: 256.28 E-value: 1.66e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 530 LHDRVVLQALSTPDRPAVVAADRTLDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVD 609
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 610 TSQPAARRRTILTNAGIRCALTqsgvdrngwaeglrlldvdllgtgqpqpvegsgdpeelAYVIHTSGSTGSPKGVMINH 689
Cdd:COG0318 81 PRLTAEELAYILEDSGARALVT--------------------------------------ALILYTSGTTGRPKGVMLTH 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 690 RGAVNTVLDINDRFGVGPDDRVLGLSNLGFDLS-VYDVFGPLSVGGAVVLPdpqRRGDPSHWADLVGTHGVTVWNSVPAQ 768
Cdd:COG0318 123 RNLLANAAAIAAALGLTPGDVVLVALPLFHVFGlTVGLLAPLLAGATLVLL---PRFDPERVLELIERERVTVLFGVPTM 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 769 LQMLHDYLVSATATVPdGLRLAMLSGDWIPVALPDQIRARVpGLRIVSLGGATEASIWSIWYPIEQVDPEWRSIpyGRPL 848
Cdd:COG0318 200 LARLLRHPEFARYDLS-SLRLVVSGGAPLPPELLERFEERF-GVRIVEGYGLTETSPVVTVNPEDPGERRPGSV--GRPL 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 849 TNQSFHVLDAALRPRPDLVSGELYIGGVGLAVGYLNDRERTAERFVvhpqtgERLYRTGDLGRYLPDGTIEFLGREDLQV 928
Cdd:COG0318 276 PGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFR------DGWLRTGDLGRLDEDGYLYIVGRKKDMI 349
|
410 420
....*....|....*....|
gi 1860141834 929 KIRGYRIELAEIEAALGGHP 948
Cdd:COG0318 350 ISGGENVYPAEVEEVLAAHP 369
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
530-992 |
1.55e-57 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 221.58 E-value: 1.55e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 530 LHDRVVLQALSTPDRPAVVAADRTLDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVD 609
Cdd:PRK05691 2190 LHGLFAAQAARTPQAPALTFAGQTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLD 2269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 610 TSQPAARRRTILTNAGIRCALTQ-----------SGVDRNGWAEglrllDVDLLGTGQPQPVEGSGDPEELAYVIHTSGS 678
Cdd:PRK05691 2270 PEYPLERLHYMIEDSGIGLLLSDralfealgelpAGVARWCLED-----DAAALAAYSDAPLPFLSLPQHQAYLIYTSGS 2344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 679 TGSPKGVMINHRGAVNTVLDINDRFGVGPDDRVLGLSNLGFDLSVYDVFGPLSVGGAVVLpDPQRRGDPSHWADLVGTHG 758
Cdd:PRK05691 2345 TGKPKGVVVSHGEIAMHCQAVIERFGMRADDCELHFYSINFDAASERLLVPLLCGARVVL-RAQGQWGAEEICQLIREQQ 2423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 759 VTVWNSVPAQLQMLHDYLVSATATVPdgLRLAMLSGDWIPVALPDQIRARVPGLRIVSLGGATEASIWSIWYPI-EQVDP 837
Cdd:PRK05691 2424 VSILGFTPSYGSQLAQWLAGQGEQLP--VRMCITGGEALTGEHLQRIRQAFAPQLFFNAYGPTETVVMPLACLApEQLEE 2501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 838 EWRSIPYGRPLTNQSFHVLDAALRPRPDLVSGELYIGGVGLAVGYLNDRERTAERFVVHP--QTGERLYRTGDLGRYLPD 915
Cdd:PRK05691 2502 GAASVPIGRVVGARVAYILDADLALVPQGATGELYVGGAGLAQGYHDRPGLTAERFVADPfaADGGRLYRTGDLVRLRAD 2581
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1860141834 916 GTIEFLGREDLQVKIRGYRIELAEIEAALGGHPaVAGAVVVVDGDTPLERRLAAFVEPAgrpvTAAQAEHDQAALRQ 992
Cdd:PRK05691 2582 GLVEYVGRIDHQVKIRGFRIELGEIESRLLEHP-AVREAVVLALDTPSGKQLAGYLVSA----VAGQDDEAQAALRE 2653
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
52-992 |
6.49e-55 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 212.72 E-value: 6.49e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 52 VAHLDNLAGNGTLVPdRAHRHDPFPVTDVQAAYLLgrgETFAYGGVACHgYGELVY---PELDPERMTAAWRALIARHDM 128
Cdd:PRK05691 3236 LAQLTQAQLDALPVP-AAEIEDVYPLTPMQEGLLL---HTLLEPGTGLY-YMQDRYrinSALDPERFAQAWQAVVARHEA 3310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 129 LRAVVEADGAQRVLAEV-PPFEVPV--IDLTGRPEAVVDAAVSAVRAEMDHLVHTPDRWPLFAARITRADHRTVL----- 200
Cdd:PRK05691 3311 LRASFSWNAGETMLQVIhKPGRTPIdyLDWRGLPEDGQEQRLQALHKQEREAGFDLLNQPPFHLRLIRVDEARYWfmmsn 3390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 201 -HVSID-----FLIADFISVQVVLDElhrlYHRPDEPLPPleiTFRDY--QLAERAVRDSprherdKQWWLARVDELPAA 272
Cdd:PRK05691 3391 hHILIDawcrsLLMNDFFEIYTALGE----GREAQLPVPP---RYRDYigWLQRQDLAQA------RQWWQDNLRGFERP 3457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 273 PELPTvARP------ADSEG-RFRRWETRLSSQVWEGLRQRAGRHGVSPSGAVLAAFSDTIAAYSRRSRFTLDITLLNRa 345
Cdd:PRK05691 3458 TPIPS-DRPflrehaGDSGGmVVGDCYTRLDAADGARLRELAQAHQLTVNTFAQAAWALVLRRYSGDRDVLFGVTVAGR- 3535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 346 PVH-DQVNALVGDFTSVDLLAV---DADPTRRFDERARDLQAQLWE--DLDHRSFSGIEVMREIARRQGAEAALFpvVFT 419
Cdd:PRK05691 3536 PVSmPQMQRTVGLFINSIALRVqlpAAGQRCSVRQWLQGLLDSNMElrEYEYLPLVAIQECSELPKGQPLFDSLF--VFE 3613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 420 SAIGITSA-------GAAADGA------PLGELGYGisqtpqvwidcqniERDGGLVSNWDVReeVFPPGVVDDMFAAYD 486
Cdd:PRK05691 3614 NAPVEVSVldraqslNASSDSGrthtnfPLTAVCYP--------------GDDLGLHLSYDQR--YFDAPTVERLLGEFK 3677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 487 AVLHRLA----GDDAAWTGTGHpdppEATRDRRAETNRTQAPVPAGMLHDRVV-LQALSTPDRPAVVAADRTLDYAELLG 561
Cdd:PRK05691 3678 RLLLALVqgfhGDLSELPLLGE----QERDFLLDGCNRSERDYPLEQSYVRLFeAQVAAHPQRIAASCLDQQWSYAELNR 3753
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 562 RAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVDTSQPAARRRTILTNAG---IRC-----ALTQS 633
Cdd:PRK05691 3754 AANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGLPAQRLQRIIELSRtpvLVCsaacrEQARA 3833
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 634 GVDRNGWAEGLRLL---DVDLLGTGQPQPVEGSGdPEELAYVIHTSGSTGSPKGVMINHRGAVNTVLDINDRFGVGPDDR 710
Cdd:PRK05691 3834 LLDELGCANRPRLLvweEVQAGEVASHNPGIYSG-PDNLAYVIYTSGSTGLPKGVMVEQRGMLNNQLSKVPYLALSEADV 3912
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 711 VLGLSNLGFDLSVYDVFG-PLSVGGAVVLPDPQRRgDPSHWADLVGTHGVTVWNSVPAQLQMLhdyLVSATATVpDGLRL 789
Cdd:PRK05691 3913 IAQTASQSFDISVWQFLAaPLFGARVEIVPNAIAH-DPQGLLAHVQAQGITVLESVPSLIQGM---LAEDRQAL-DGLRW 3987
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 790 AMLSGDWIPVALPDQIRARVPGLRIVSLGGATEASIWSIWYPIEQVDPEWRSIPYGRPLTNQSFHVLDAALRPRPDLVSG 869
Cdd:PRK05691 3988 MLPTGEAMPPELARQWLQRYPQIGLVNAYGPAECSDDVAFFRVDLASTRGSYLPIGSPTDNNRLYLLDEALELVPLGAVG 4067
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 870 ELYIGGVGLAVGYLNDRERTAERFVVHP--QTGERLYRTGDLGRYLPDGTIEFLGREDLQVKIRGYRIELAEIEAALGGH 947
Cdd:PRK05691 4068 ELCVAGTGVGRGYVGDPLRTALAFVPHPfgAPGERLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQ 4147
|
970 980 990 1000
....*....|....*....|....*....|....*....|....*
gi 1860141834 948 PAVAGAVVVVDGDtPLERRLAAFvepagrpVTAAQAEHDQAALRQ 992
Cdd:PRK05691 4148 AEVREAAVAVQEG-VNGKHLVGY-------LVPHQTVLAQGALLE 4184
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
668-982 |
4.05e-50 |
|
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: 181.33 E-value: 4.05e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 668 ELAYVIHTSGSTGSPKGVMINHRGAVNTVLDINDRFGVGPDDRVLGLSNLGFDLSVYDVFGPLSVGGAVVLPDpqrRGDP 747
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLP---KFDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 748 SHWADLVGTHGVTVWNSVPAQLQMLHDYLVSATATVPDgLRLAMLSGDWIPVALPDQIRARvPGLRIVSLGGATEASIWS 827
Cdd:cd04433 78 EAALELIEREKVTILLGVPTLLARLLKAPESAGYDLSS-LRALVSGGAPLPPELLERFEEA-PGIKLVNGYGLTETGGTV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 828 IWYPIEQVDPEWRSIpyGRPLTNQSFHVLDAALRPRPDLVSGELYIGGVGLAVGYLNDRERTAERFvvhpqtGERLYRTG 907
Cdd:cd04433 156 ATGPPDDDARKPGSV--GRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVD------EDGWYRTG 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1860141834 908 DLGRYLPDGTIEFLGREDLQVKIRGYRIELAEIEAALGGHPAVAGAVVVVDGDTPLERRLAAFVEPA-GRPVTAAQ 982
Cdd:cd04433 228 DLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRpGADLDAEE 303
|
|
| C_NRPS-like |
cd19066 |
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ... |
74-495 |
9.27e-48 |
|
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: 177.60 E-value: 9.27e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 74 PFPVTDVQ----AAYLLGRGETFAYGGVACHGYGELvypelDPERMTAAWRALIARHDMLRAV-VEADGA--QRVLAEVP 146
Cdd:cd19066 1 KIPLSPMQrgmwFLKKLATDPSAFNVAIEMFLTGSL-----DLARLKQALDAVMERHDVLRTRfCEEAGRyeQVVLDKTV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 147 PFEVPVIDLTGRPEAVVDAAVsavraEMDHLVHTP---DRWPL-FAARITRADHRTVLHVSIDFLIADFISVQVVLDELH 222
Cdd:cd19066 76 RFRIEIIDLRNLADPEARLLE-----LIDQIQQTIydlERGPLvRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDIS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 223 RLY--HRPDEP-LPPLEITFRDYQLAERAVRDSPRHERDKQWWLARVDELPAAPELPTVARPADSEG-RFRRWETRLSSQ 298
Cdd:cd19066 151 SVYdaAERQKPtLPPPVGSYADYAAWLEKQLESEAAQADLAYWTSYLHGLPPPLPLPKAKRPSQVASyEVLTLEFFLRSE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 299 VWEGLRQRAGRHGVSPSGAVLAAFSDTIAAYSRRSRFTLDITLLNRAPvhDQVNALVGDFTSVDLLAVDADPTRRFDERA 378
Cdd:cd19066 231 ETKRLREVARESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPD--EAVEDTIGLFLNLLPLRIDTSPDATFPELL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 379 RDLQAQLWEDLDHRSFSGIEVMREIARRQGAE-AALFPVVFTSAIGITSAGAAADGAPLGELgYGISQTPQVWIDCQNIE 457
Cdd:cd19066 309 KRTKEQSREAIEHQRVPFIELVRHLGVVPEAPkHPLFEPVFTFKNNQQQLGKTGGFIFTTPV-YTSSEGTVFDLDLEASE 387
|
410 420 430
....*....|....*....|....*....|....*....
gi 1860141834 458 -RDGGLVSNWDVREEVFPPGVVDDMFAAYDAVLHRLAGD 495
Cdd:cd19066 388 dPDGDLLLRLEYSRGVYDERTIDRFAERYMTALRQLIEN 426
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
542-941 |
4.51e-45 |
|
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: 170.35 E-value: 4.51e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 542 PDRPAVV----AADRTLDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVDTSQPAARR 617
Cdd:cd17654 1 PDRPALIidqtTSDTTVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 618 RTILTNAGIRCALTQsgvdrngwaeglRLLDVDLLGTGQPQPVEGSGDPEELAYVIHTSGSTGSPKGVMINHRGAVNTVL 697
Cdd:cd17654 81 LTVMKKCHVSYLLQN------------KELDNAPLSFTPEHRHFNIRTDECLAYVIHTSGTTGTPKIVAVPHKCILPNIQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 698 DINDRFGVGPDDRVLGLSNLGFDLSVYDVFGPLSVGGAVVLPDPQRRGDPSHWAD-LVGTHGVTVWNSVPAQL-----QM 771
Cdd:cd17654 149 HFRSLFNITSEDILFLTSPLTFDPSVVEIFLSLSSGATLLIVPTSVKVLPSKLADiLFKRHRITVLQATPTLFrrfgsQS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 772 LHDYLVSATATvpdgLRLAMLSGDWIPVALPDQIRARV-PGLRIVSLGGATEASIWSIWYPIEQVDPewrSIPYGRPLTN 850
Cdd:cd17654 229 IKSTVLSATSS----LRVLALGGEPFPSLVILSSWRGKgNRTRIFNIYGITEVSCWALAYKVPEEDS---PVQLGSPLLG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 851 QSFHVLDAAlrprPDLVSGELYIGGVGLaVGYLNDRERTAErfvvhpqtgERLYRTGDLGRyLPDGTIEFLGREDLQVKI 930
Cdd:cd17654 302 TVIEVRDQN----GSEGTGQVFLGGLNR-VCILDDEVTVPK---------GTMRATGDFVT-VKDGELFFLGRKDSQIKR 366
|
410
....*....|.
gi 1860141834 931 RGYRIELAEIE 941
Cdd:cd17654 367 RGKRINLDLIQ 377
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
538-944 |
7.50e-44 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 168.15 E-value: 7.50e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 538 ALSTPDRPAVVAADRTLDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVDTSQPAARR 617
Cdd:PRK04813 12 AQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVDVSSPAERI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 618 RTILTNAGIRCALTQSGVDRNgwAEGLRLLDV----DLLGTGQP----QPVEGsgdpEELAYVIHTSGSTGSPKGVMINH 689
Cdd:PRK04813 92 EMIIEVAKPSLIIATEELPLE--ILGIPVITLdelkDIFATGNPydfdHAVKG----DDNYYIIFTSGTTGKPKGVQISH 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 690 RGAVNTVLDINDRFGVGPDDRVLGLSNLGFDLSVYDVFGPLSVGGAVVLPDPQRRGDPSHWADLVGTHGVTVWNSVP--A 767
Cdd:PRK04813 166 DNLVSFTNWMLEDFALPEGPQFLNQAPYSFDLSVMDLYPTLASGGTLVALPKDMTANFKQLFETLPQLPINVWVSTPsfA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 768 QLQMLHDYLVSATatVPDgLRLAMLSGDWIPVALPDQIRARVPGLRIVSLGGATEAS--IWSIwypieQVDPE----WRS 841
Cdd:PRK04813 246 DMCLLDPSFNEEH--LPN-LTHFLFCGEELPHKTAKKLLERFPSATIYNTYGPTEATvaVTSI-----EITDEmldqYKR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 842 IPYGRPLTNQSFHVLDAALRPRPDLVSGELYIGGVGLAVGYLNDRERTAERFVVHpqTGERLYRTGDLGrYLPDGTIEFL 921
Cdd:PRK04813 318 LPIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFFTF--DGQPAYHTGDAG-YLEDGLLFYQ 394
|
410 420
....*....|....*....|...
gi 1860141834 922 GREDLQVKIRGYRIELAEIEAAL 944
Cdd:PRK04813 395 GRIDFQIKLNGYRIELEEIEQNL 417
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
542-948 |
3.43e-42 |
|
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: 163.46 E-value: 3.43e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 542 PDRPAVV-------AADRTLDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVDTSQPA 614
Cdd:cd17647 2 PERTCVVetpslnsSKTRSFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 615 ARRRTILtnagircaltqsGVDRNGWAEGLRLLDVdllgtgqpqpVEGsgdPEELAYVIHTSGSTGSPKGVMINHRGAVN 694
Cdd:cd17647 82 ARQNIYL------------GVAKPRGLIVIRAAGV----------VVG---PDSNPTLSFTSGSEGIPKGVLGRHFSLAY 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 695 TVLDINDRFGVGPDDRVLGLSNLGFDLSVYDVFGPLSVGGAVVLPDPQRRGDPSHWADLVGTHGVTVWNSVPAQLQMLhd 774
Cdd:cd17647 137 YFPWMAKRFNLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTQDDIGTPGRLAEWMAKYGATVTHLTPAMGQLL-- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 775 yLVSATATVPdGLRLAMLSGDWIPVALPDQIRARVPGLRIVSLGGATEASiWSIWY---PIEQVDPEWRS-----IPYGR 846
Cdd:cd17647 215 -TAQATTPFP-KLHHAFFVGDILTKRDCLRLQTLAENVRIVNMYGTTETQ-RAVSYfevPSRSSDPTFLKnlkdvMPAGR 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 847 PLTNQSFHVLDAALRPRPDLVS--GELYIGGVGLAVGYLNDRERTAERFV----VHP-------QTGE------------ 901
Cdd:cd17647 292 GMLNVQLLVVNRNDRTQICGIGevGEIYVRAGGLAEGYRGLPELNKEKFVnnwfVEPdhwnyldKDNNepwrqfwlgprd 371
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1860141834 902 RLYRTGDLGRYLPDGTIEFLGREDLQVKIRGYRIELAEIEAALGGHP 948
Cdd:cd17647 372 RLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHP 418
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
538-948 |
4.44e-41 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 161.05 E-value: 4.44e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 538 ALSTPDRPAVVAAD-----RTLDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPV--DT 610
Cdd:COG0365 19 AEGRGDKVALIWEGedgeeRTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVfpGF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 611 SQPAARRRtiLTNAGIRCALTQSGVDRNGWAEGLR-LLD--VDLL----------GTGQPQPVEGSGDPEEL-------- 669
Cdd:COG0365 99 GAEALADR--IEDAEAKVLITADGGLRGGKVIDLKeKVDeaLEELpslehvivvgRTGADVPMEGDLDWDELlaaasaef 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 670 ----------AYVIHTSGSTGSPKGVMINHRG-AVNTVLDINDRFGVGPDDRVLGLSNLGF--DLSvYDVFGPLSVGGAV 736
Cdd:COG0365 177 epeptdaddpLFILYTSGTTGKPKGVVHTHGGyLVHAATTAKYVLDLKPGDVFWCTADIGWatGHS-YIVYGPLLNGATV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 737 VL-------PDPQRrgdpshWADLVGTHGVTVWNSVPAQLQMLHDYLVSATATVP-DGLRLAMLSGDWIPVALPDQIRAR 808
Cdd:COG0365 256 VLyegrpdfPDPGR------LWELIEKYGVTVFFTAPTAIRALMKAGDEPLKKYDlSSLRLLGSAGEPLNPEVWEWWYEA 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 809 VpGLRIVSLGGATEA-SIWSIWYPIEQVDPewRSIpyGRPLTNQSFHVLDAALRPRPDLVSGELYIGG--VGLAVGYLND 885
Cdd:COG0365 330 V-GVPIVDGWGQTETgGIFISNLPGLPVKP--GSM--GKPVPGYDVAVVDEDGNPVPPGEEGELVIKGpwPGMFRGYWND 404
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1860141834 886 RERTAERFVvhpQTGERLYRTGDLGRYLPDGTIEFLGREDLQVKIRGYRIELAEIEAALGGHP 948
Cdd:COG0365 405 PERYRETYF---GRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHP 464
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
528-948 |
6.09e-41 |
|
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: 166.01 E-value: 6.09e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 528 GMLHDRVVLQALSTPDRPAVV---------AADRTLDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGA 598
Cdd:TIGR03443 236 GAIHDIFADNAEKHPDRTCVVetpsfldpsSKTRSFTYKQINEASNILAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGV 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 599 LLAGCVYVPVDTSQPAARRRTILTNA------GIRCA--LTQSGVD------------------RNGWAEGLRL--LDVD 650
Cdd:TIGR03443 316 LKAGATFSVIDPAYPPARQTIYLSVAkpraliVIEKAgtLDQLVRDyidkelelrteipalalqDDGSLVGGSLegGETD 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 651 LLgtgqpQPVEGSGD--------PEELAYVIHTSGSTGSPKGVMINHRGAVNTVLDINDRFGVGPDDRVLGLSNLGFDLS 722
Cdd:TIGR03443 396 VL-----APYQALKDtptgvvvgPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFGLSENDKFTMLSGIAHDPI 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 723 VYDVFGPLSVGGAVVLPDPQRRGDPSHWADLVGTHGVTVWNSVPAQLQMLhdylvSATATVP-DGLRLAMLSGDWIPVAL 801
Cdd:TIGR03443 471 QRDMFTPLFLGAQLLVPTADDIGTPGRLAEWMAKYGATVTHLTPAMGQLL-----SAQATTPiPSLHHAFFVGDILTKRD 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 802 PDQIRARVPGLRIVSLGGATEASIWSIWYPIEQV--DPEWRS-----IPYGRPLTNQSFHVLDAALRPRPDLVS--GELY 872
Cdd:TIGR03443 546 CLRLQTLAENVCIVNMYGTTETQRAVSYFEIPSRssDSTFLKnlkdvMPAGKGMKNVQLLVVNRNDRTQTCGVGevGEIY 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 873 IGGVGLAVGYLNDRERTAERFVVH--------PQTGE---------------RLYRTGDLGRYLPDGTIEFLGREDLQVK 929
Cdd:TIGR03443 626 VRAGGLAEGYLGLPELNAEKFVNNwfvdpshwIDLDKennkperefwlgprdRLYRTGDLGRYLPDGNVECCGRADDQVK 705
|
490
....*....|....*....
gi 1860141834 930 IRGYRIELAEIEAALGGHP 948
Cdd:TIGR03443 706 IRGFRIELGEIDTHLSQHP 724
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
561-972 |
5.94e-38 |
|
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: 149.51 E-value: 5.94e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 561 GRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGC----VYVPVDTSQPAARRRTILTNAGIRCALTQSG-V 635
Cdd:cd05922 1 LGVSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGrlglVFVPLNPTLKESVLRYLVADAGGRIVLADAGaA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 636 DRNGWA------EGLRLLDVDLLGTGQPQPVEGSgDPEELAYVIHTSGSTGSPKGVMINHRGAVNTVLDINDRFGVGPDD 709
Cdd:cd05922 81 DRLRDAlpaspdPGTVLDADGIRAARASAPAHEV-SHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 710 RVLGLSNLGFDLSVYDVFGPLSVGGAVVLPDPQRRGDpSHWaDLVGTHGVTVWNSVPAQLQMLhDYLVSATATVPDgLRL 789
Cdd:cd05922 160 RALTVLPLSYDYGLSVLNTHLLRGATLVLTNDGVLDD-AFW-EDLREHGATGLAGVPSTYAML-TRLGFDPAKLPS-LRY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 790 AMLSGDWIPVALPDQIRARVPGLRIVSLGGATEASIWSIWYPIEQVDPEWRSIpyGRPLTNQSFHVLDAALRPRPDLVSG 869
Cdd:cd05922 236 LTQAGGRLPQETIARLRELLPGAQVYVMYGQTEATRRMTYLPPERILEKPGSI--GLAIPGGEFEILDDDGTPTPPGEPG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 870 ELYIGGVGLAVGYLNDrertaERFVVHPQTGERLYRTGDLGRYLPDGTIEFLGREDLQVKIRGYRIELAEIEAALGGHPA 949
Cdd:cd05922 314 EIVHRGPNVMKGYWND-----PPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGL 388
|
410 420
....*....|....*....|...
gi 1860141834 950 VAGAVVVVDGDtPLERRLAAFVE 972
Cdd:cd05922 389 IIEAAAVGLPD-PLGEKLALFVT 410
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
542-948 |
4.72e-36 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 145.05 E-value: 4.72e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 542 PDRPAVVAADRTLDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVDTSQPAARRRTIL 621
Cdd:PRK07656 19 GDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAAYIL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 622 TNAGIRCALTQS---GVDRNGwAEGLRLLDV--------------------DLLGTGQPQPVEGSGDPEELAYVIHTSGS 678
Cdd:PRK07656 99 ARGDAKALFVLGlflGVDYSA-TTRLPALEHvviceteeddphtekmktftDFLAAGDPAERAPEVDPDDVADILFTSGT 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 679 TGSPKGVMINHRGAVNTVLDINDRFGVGPDDRVLGLsnlgfdLSVYDVFGpLSVG-------GAVVLPDPQRrgDPSHWA 751
Cdd:PRK07656 178 TGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAA------NPFFHVFG-YKAGvnaplmrGATILPLPVF--DPDEVF 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 752 DLVGTHGVTVWNSVPAQLQMLHDYlvsatatvPDG-------LRLAMLSGDWIPVALPDQIRARVpGLRIVSLG-GATEA 823
Cdd:PRK07656 249 RLIETERITVLPGPPTMYNSLLQH--------PDRsaedlssLRLAVTGAASMPVALLERFESEL-GVDIVLTGyGLSEA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 824 SIWSIWYPIEQvDPEWRSIPYGRPLTNQSFHVLDAALRPRPDLVSGELYIGGVGLAVGYLNDRERTAERFvvhpqTGERL 903
Cdd:PRK07656 320 SGVTTFNRLDD-DRKTVAGTIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAAI-----DADGW 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1860141834 904 YRTGDLGRYLPDGTIEFLGREDLQVKIRGYRIELAEIEAALGGHP 948
Cdd:PRK07656 394 LHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHP 438
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
538-948 |
2.30e-35 |
|
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: 141.21 E-value: 2.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 538 ALSTPDRPAVVAADRTLDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVDTSQPAARR 617
Cdd:cd17631 5 ARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 618 RTILTNAGIRCALtqsgvdrngwaeglrlldvdllgtgqpqpvegsgdpEELAYVIHTSGSTGSPKGVMINHRGAVNTVL 697
Cdd:cd17631 85 AYILADSGAKVLF------------------------------------DDLALLMYTSGTTGRPKGAMLTHRNLLWNAV 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 698 DINDRFGVGPDDR---VLGLSNLGfDLSVYdVFGPLSVGGAVVLPdpqRRGDPSHWADLVGTHGVTVWNSVPAQLQMLHD 774
Cdd:cd17631 129 NALAALDLGPDDVllvVAPLFHIG-GLGVF-TLPTLLRGGTVVIL---RKFDPETVLDLIERHRVTSFFLVPTMIQALLQ 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 775 YLVSATATVPdGLRLAMLSGDWIPVALPDQIRARvpGLRIVSLGGATEASIWSIWYPIEQVDPEWRSIpyGRPLTNQSFH 854
Cdd:cd17631 204 HPRFATTDLS-SLRAVIYGGAPMPERLLRALQAR--GVKFVQGYGMTETSPGVTFLSPEDHRRKLGSA--GRPVFFVEVR 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 855 VLDAALRPRPDLVSGELYIGGVGLAVGYLNDRERTAERFvvhpqtGERLYRTGDLGRYLPDGTIEFLGREDLQVKIRGYR 934
Cdd:cd17631 279 IVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAF------RDGWFHTGDLGRLDEDGYLYIVDRKKDMIISGGEN 352
|
410
....*....|....
gi 1860141834 935 IELAEIEAALGGHP 948
Cdd:cd17631 353 VYPAEVEDVLYEHP 366
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
542-948 |
3.72e-35 |
|
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.
Pssm-ID: 341269 [Multi-domain] Cd Length: 508 Bit Score: 142.12 E-value: 3.72e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 542 PDRPAVVAADRTLDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVDTSQPAARRRTIL 621
Cdd:cd05959 18 GDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 622 TNAGIRCALTQSG------------------VDRNGWAEGLRLLDV--DLLGTGQPQPVEGSGDPEELAYVIHTSGSTGS 681
Cdd:cd05959 98 EDSRARVVVVSGElapvlaaaltksehtlvvLIVSGGAGPEAGALLlaELVAAEAEQLKPAATHADDPAFWLYSSGSTGR 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 682 PKGVMINHRG-AVNTVLDINDRFGVGPDDRVLGLSNLGFDLSVYD-VFGPLSVGGAVVL-PDpqrRGDPSHWADLVGTHG 758
Cdd:cd05959 178 PKGVVHLHADiYWTAELYARNVLGIREDDVCFSAAKLFFAYGLGNsLTFPLSVGATTVLmPE---RPTPAAVFKRIRRYR 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 759 VTVWNSVPAQL-QMLHDylVSATATVPDGLRLAMLSGDWIPVALPDQIRARVpGLRIVSLGGATEA-SIWSIWYPieqvd 836
Cdd:cd05959 255 PTVFFGVPTLYaAMLAA--PNLPSRDLSSLRLCVSAGEALPAEVGERWKARF-GLDILDGIGSTEMlHIFLSNRP----- 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 837 pewRSIPY---GRPLTNQSFHVLDAALRPRPDLVSGELYIGGVGLAVGYLNDRERTAERFVvhpqtGErLYRTGDLGRYL 913
Cdd:cd05959 327 ---GRVRYgttGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQ-----GE-WTRTGDKYVRD 397
|
410 420 430
....*....|....*....|....*....|....*
gi 1860141834 914 PDGTIEFLGREDLQVKIRGYRIELAEIEAALGGHP 948
Cdd:cd05959 398 DDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHP 432
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
520-982 |
5.33e-34 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 139.42 E-value: 5.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 520 RTQAPVPAGMLHDRVVLQAL-----STPDRPAVVA------ADRTLDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRG 588
Cdd:PRK13295 11 RRAASIAAGHWHDRTINDDLdacvaSCPDKTAVTAvrlgtgAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNW 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 589 WEQVVAVLGALLAGCVYVPVdtsQPAARRRTI---LTNAGIRCALTQS---GVDRNGWAEGLR-----LLDVDLLGTG-- 655
Cdd:PRK13295 91 WEFTVLYLACSRIGAVLNPL---MPIFRERELsfmLKHAESKVLVVPKtfrGFDHAAMARRLRpelpaLRHVVVVGGDga 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 656 -----------------QPQPVEGS-GDPEELAYVIHTSGSTGSPKGVMINHRGAVNTVLDINDRFGVGPDDRVLGLSNL 717
Cdd:PRK13295 168 dsfeallitpaweqepdAPAILARLrPGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASPM 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 718 ----GFdlsVYDVFGPLSVGGAVVLPDPQrrgDPSHWADLVGTHGVTvWNSvpAQLQMLHDYL--VSATATVPDGLRLAM 791
Cdd:PRK13295 248 ahqtGF---MYGLMMPVMLGATAVLQDIW---DPARAAELIRTEGVT-FTM--ASTPFLTDLTraVKESGRPVSSLRTFL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 792 LSGDWIPVALPDQIRARVpGLRIVSLGGATEASIWSIWYPIEqvDPEWRSIPYGRPLTNQSFHVLDAALRPRPDLVSGEL 871
Cdd:PRK13295 319 CAGAPIPGALVERARAAL-GAKIVSAWGMTENGAVTLTKLDD--PDERASTTDGCPLPGVEVRVVDADGAPLPAGQIGRL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 872 YIGGVGLAVGYLNDRERTAERFvvhpqtgERLYRTGDLGRYLPDGTIEFLGREDlQVKIRG-YRIELAEIEAALGGHPAV 950
Cdd:PRK13295 396 QVRGCSNFGGYLKRPQLNGTDA-------DGWFDTGDLARIDADGYIRISGRSK-DVIIRGgENIPVVEIEALLYRHPAI 467
|
490 500 510
....*....|....*....|....*....|...
gi 1860141834 951 AGAVVVVDGDTPLERRLAAFVEP-AGRPVTAAQ 982
Cdd:PRK13295 468 AQVAIVAYPDERLGERACAFVVPrPGQSLDFEE 500
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
542-948 |
1.13e-33 |
|
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: 137.44 E-value: 1.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 542 PDRPAVVAADRTLD--YAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVDTSQPAARRRT 619
Cdd:cd05926 1 PDAPALVVPGSTPAltYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 620 ILTNAGIRCALTQSG----VDRNGWAEGLRLLDVDL-------------LGTGQPQPV----EGSGDPEELAYVIHTSGS 678
Cdd:cd05926 81 YLADLGSKLVLTPKGelgpASRAASKLGLAILELALdvgvlirapsaesLSNLLADKKnaksEGVPLPDDLALILHTSGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 679 TGSPKGVMINHRGAVNTVLDINDRFGVGPDDRVLGLsnlgfdLSVYDVFG-------PLSVGGAVVLPDpqrRGDPSHWA 751
Cdd:cd05926 161 TGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLVV------MPLFHVHGlvasllsTLAAGGSVVLPP---RFSASTFW 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 752 DLVGTHGVTVWNSVPAQLQMLHDYLVSATATVPDGLRLAMLSGDWIPVALPDQIRARVpGLRIVSLGGATEASIWSIWYP 831
Cdd:cd05926 232 PDVRDYNATWYTAVPTIHQILLNRPEPNPESPPPKLRFIRSCSASLPPAVLEALEATF-GAPVLEAYGMTEAAHQMTSNP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 832 IEQVDPEWRSipYGRPlTNQSFHVLDAALRPRPDLVSGELYIGGVGLAVGYLNDRERTAERFvvhpqTGERLYRTGDLGR 911
Cdd:cd05926 311 LPPGPRKPGS--VGKP-VGVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAA-----FKDGWFRTGDLGY 382
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1860141834 912 YLPDGTIEFLGRedlqVK---IR-GYRIELAEIEAALGGHP 948
Cdd:cd05926 383 LDADGYLFLTGR----IKeliNRgGEKISPLEVDGVLLSHP 419
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
543-948 |
3.38e-33 |
|
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: 135.11 E-value: 3.38e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 543 DRPAVVAADRTLDYAELLGRAAGVAEALTAAGC-RRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVDTSQPAARRRTIL 621
Cdd:cd05941 1 DRIAIVDDGDSITYADLVARAARLANRLLALGKdLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 622 TNAGIRCALtqsgvdrngwaeglrlldvdllgtgqpqpvegsgdpeELAYVIHTSGSTGSPKGVMINHRGAVNTVLDIND 701
Cdd:cd05941 81 TDSEPSLVL-------------------------------------DPALILYTSGTTGRPKGVVLTHANLAANVRALVD 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 702 RFGVGPDDRVL---------GLSNLgfdlsvydVFGPLSVGGAVVLpdpQRRGDPSHWADLVGTHGVTVWNSVP------ 766
Cdd:cd05941 124 AWRWTEDDVLLhvlplhhvhGLVNA--------LLCPLFAGASVEF---LPKFDPKEVAISRLMPSITVFMGVPtiytrl 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 767 -AQLQMLHDYLVSATATVPDGLRLaMLSGDwipVALPDQIRAR---VPGLRIVSLGGATEASIwSIWYPIeqvDPEWRSI 842
Cdd:cd05941 193 lQYYEAHFTDPQFARAAAAERLRL-MVSGS---AALPVPTLEEweaITGHTLLERYGMTEIGM-ALSNPL---DGERRPG 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 843 PYGRPLTNQSFHVLDAALRPRPDLVS-GELYIGGVGLAVGYLNDRERTAERFvvhpqTGERLYRTGDLGRYLPDGTIEFL 921
Cdd:cd05941 265 TVGMPLPGVQARIVDEETGEPLPRGEvGEIQVRGPSVFKEYWNKPEATKEEF-----TDDGWFKTGDLGVVDEDGYYWIL 339
|
410 420
....*....|....*....|....*...
gi 1860141834 922 GRE-DLQVKIRGYRIELAEIEAALGGHP 948
Cdd:cd05941 340 GRSsVDIIKSGGYKVSALEIERVLLAHP 367
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
529-980 |
1.05e-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: 134.56 E-value: 1.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 529 MLHDRVVLQALSTPDRPAVVAADRTLD--YAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYV 606
Cdd:cd05923 2 TVFEMLRRAASRAPDACAIADPARGLRltYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 607 PVDTSQPAARRRTILTNAGIRCALTQSGV-----DRNGWAEGLRLLDVDLLGTGQ---PQPVEGSGDPEELAYVIHTSGS 678
Cdd:cd05923 82 LINPRLKAAELAELIERGEMTAAVIAVDAqvmdaIFQSGVRVLALSDLVGLGEPEsagPLIEDPPREPEQPAFVFYTSGT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 679 TGSPKGVMINHRGAVNTVLDINDRFGV--GPDDRVLGLSNLGFDLSVYDVF-GPLSVGGAVVLPdpqRRGDPSHWADLVG 755
Cdd:cd05923 162 TGLPKGAVIPQRAAESRVLFMSTQAGLrhGRHNVVLGLMPLYHVIGFFAVLvAALALDGTYVVV---EEFDPADALKLIE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 756 THGVTVWNSVPAQLqmlhDYLVSATATVP---DGLRLAMLSGDWIPVALPDQIRARVPGlRIVSLGGATEASIWSIwypi 832
Cdd:cd05923 239 QERVTSLFATPTHL----DALAAAAEFAGlklSSLRHVTFAGATMPDAVLERVNQHLPG-EKVNIYGTTEAMNSLY---- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 833 eqvDPEWRSIPYGRPLTNQSFHVLDAALRPR---PDLVSGELYIGGVGLA--VGYLNDRERTAERFVvhpqtgERLYRTG 907
Cdd:cd05923 310 ---MRDARTGTEMRPGFFSEVRIVRIGGSPDealANGEEGELIVAAAADAafTGYLNQPEATAKKLQ------DGWYRTG 380
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1860141834 908 DLGRYLPDGTIEFLGREDLQVKIRGYRIELAEIEAALGGHPAVAGAVVVVDGDTPLERRLAAFVEPAGRPVTA 980
Cdd:cd05923 381 DVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREGTLSA 453
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
553-985 |
2.06e-32 |
|
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: 132.50 E-value: 2.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 553 TLDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVdtsQPAARRRT---ILTNAGIRCA 629
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPI---LPFFREHElafILRRAKAKVF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 630 LTQSGVDRNGWAEglrlldvdllgtgqpqpvegsgDPEELAYVIHTSGSTGSPKGVMINHRGAVNTVLDINDRFGVGPDD 709
Cdd:cd05903 78 VVPERFRQFDPAA----------------------MPDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGD 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 710 RVLGLSNLG-FDLSVYDVFGPLSVGGAVVLpdpQRRGDPSHWADLVGTHGVTVWNSVPAQLQMLHDYLVSATATVPDgLR 788
Cdd:cd05903 136 VFLVASPMAhQTGFVYGFTLPLLLGAPVVL---QDIWDPDKALALMREHGVTFMMGATPFLTDLLNAVEEAGEPLSR-LR 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 789 LAMLSGDWIPVALPDQIRARVpGLRIVSLGGATEASiwSIWYPIEQVDPEWRSIPYGRPLTNQSFHVLDAALRPRPDLVS 868
Cdd:cd05903 212 TFVCGGATVPRSLARRAAELL-GAKVCSAYGSTECP--GAVTSITPAPEDRRLYTDGRPLPGVEIKVVDDTGATLAPGVE 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 869 GELYIGGVGLAVGYLNDRERTAERFvvhpqtGERLYRTGDLGRYLPDGTIEFLGREDlQVKIR-GYRIELAEIEAALGGH 947
Cdd:cd05903 289 GELLSRGPSVFLGYLDRPDLTADAA------PEGWFRTGDLARLDEDGYLRITGRSK-DIIIRgGENIPVLEVEDLLLGH 361
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1860141834 948 PAVAGAVVVVDGDTPLERRLAAFV--EPAGRPVTAAQAEH 985
Cdd:cd05903 362 PGVIEAAVVALPDERLGERACAVVvtKSGALLTFDELVAY 401
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
543-985 |
2.07e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 133.19 E-value: 2.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 543 DRPAVVAADRTLDYAELLGRAAGVAEALtaAGCRRqelVAVVMDRGWEQVVAVLGALLAGCVYVPVDTSQPAARRRTILT 622
Cdd:PRK07787 15 IADAVRIGGRVLSRSDLAGAATAVAERV--AGARR---VAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 623 NAGIRCALTQSGVDrngwAEGLRLLDVDLLGTGQPQPVEGsgDPEELAYVIHTSGSTGSPKGVMINhRGAVNTVLD-IND 701
Cdd:PRK07787 90 DSGAQAWLGPAPDD----PAGLPHVPVRLHARSWHRYPEP--DPDAPALIVYTSGTTGPPKGVVLS-RRAIAADLDaLAE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 702 RFGVGPDDR-VLGLSNLGFDLSVYDVFGPLSVGGAVVlpdPQRRGDPSHWADLVGTHGvTVWNSVPAQLQMLHDYLVSAT 780
Cdd:PRK07787 163 AWQWTADDVlVHGLPLFHVHGLVLGVLGPLRIGNRFV---HTGRPTPEAYAQALSEGG-TLYFGVPTVWSRIAADPEAAR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 781 ATVPDGLrlaMLSGDW-IPVALPDQIRARVpGLRIVSLGGATEASI-WSIwypieQVDPEWRSIPYGRPLTNQSFHVLDA 858
Cdd:PRK07787 239 ALRGARL---LVSGSAaLPVPVFDRLAALT-GHRPVERYGMTETLItLST-----RADGERRPGWVGLPLAGVETRLVDE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 859 ALRPRP--DLVSGELYIGGVGLAVGYLNDRERTAERFvvhpqTGERLYRTGDLGRYLPDGTIEFLGRE--DLqVKIRGYR 934
Cdd:PRK07787 310 DGGPVPhdGETVGELQVRGPTLFDGYLNRPDATAAAF-----TADGWFRTGDVAVVDPDGMHRIVGREstDL-IKSGGYR 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1860141834 935 IELAEIEAALGGHPAVAGAVVVVDGDTPLERRLAAFVEPAGRPVTAAQAEH 985
Cdd:PRK07787 384 IGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGADDVAADELIDF 434
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
556-948 |
2.72e-32 |
|
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: 131.64 E-value: 2.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 556 YAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVDTSQPAARRRTILTNAGIRCALTqsgv 635
Cdd:cd05934 6 YAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 636 drngwaeglrlldvdllgtgqpqpvegsgdpeELAYVIHTSGSTGSPKGVMINHRGAVNTVLDINDRFGVGPDDR---VL 712
Cdd:cd05934 82 --------------------------------DPASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGEDDVyltVL 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 713 GLSNLgfDLSVYDVFGPLSVGGAVVLpdpQRRGDPSHWADLVGTHGVTVWNSVPAQLQMLHdylvsATATVPDG----LR 788
Cdd:cd05934 130 PLFHI--NAQAVSVLAALSVGATLVL---LPRFSASRFWSDVRRYGATVTNYLGAMLSYLL-----AQPPSPDDrahrLR 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 789 LAMLSGdwIPVALPDQIRARVpGLRIVSLGGATEASIwSIWYPIEQVDPeWRSIpyGRPLTNQSFHVLDAALRPRPDLVS 868
Cdd:cd05934 200 AAYGAP--NPPELHEEFEERF-GVRLLEGYGMTETIV-GVIGPRDEPRR-PGSI--GRPAPGYEVRIVDDDGQELPAGEP 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 869 GELYIGGV---GLAVGYLNDRERTAERFvvhpqtGERLYRTGDLGRYLPDGTIEFLGREDLQVKIRGYRIELAEIEAALG 945
Cdd:cd05934 273 GELVIRGLrgwGFFKGYYNMPEATAEAM------RNGWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAIL 346
|
...
gi 1860141834 946 GHP 948
Cdd:cd05934 347 RHP 349
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
556-948 |
4.97e-32 |
|
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: 131.31 E-value: 4.97e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 556 YAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVDTSQPAARRRTILTNAGIRCALTqsgv 635
Cdd:cd05972 3 FRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVT---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 636 drngwaeglrlldvdllgtgqpqpvegsgDPEELAYVIHTSGSTGSPKGVMINHRGAVNTVLDINDRFGVGPDDRVLGLS 715
Cdd:cd05972 79 -----------------------------DAEDPALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRPDDIHWNIA 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 716 NLGFDLSVY-DVFGPLSVGGAVVLpDPQRRGDPSHWADLVGTHGVTVWNSVPAQLQMLHDYLVSATatVPDGLRLAMLSG 794
Cdd:cd05972 130 DPGWAKGAWsSFFGPWLLGATVFV-YEGPRFDAERILELLERYGVTSFCGPPTAYRMLIKQDLSSY--KFSHLRLVVSAG 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 795 DwiPVaLPDQIRA--RVPGLRIVSLGGATEASIWSIWYPIEQVDPEwrSIpyGRPLTNQSFHVLDAALRPRPDLVSGELY 872
Cdd:cd05972 207 E--PL-NPEVIEWwrAATGLPIRDGYGQTETGLTVGNFPDMPVKPG--SM--GRPTPGYDVAIIDDDGRELPPGEEGDIA 279
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1860141834 873 I--GGVGLAVGYLNDRERTAERFVvhpqtgERLYRTGDLGRYLPDGTIEFLGREDLQVKIRGYRIELAEIEAALGGHP 948
Cdd:cd05972 280 IklPPPGLFLGYVGDPEKTEASIR------GDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHP 351
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
542-948 |
8.32e-32 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 132.23 E-value: 8.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 542 PDRPAVVAADRTLDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVDTSQPA------- 614
Cdd:PRK06187 20 PDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIRLKPeeiayil 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 615 --ARRRTILTN-------AGIRCAL-TQSGVDRNGWAEGLRLLD-----VDLLGTGQPQPVEGSGDPEELAYVIHTSGST 679
Cdd:PRK06187 100 ndAEDRVVLVDsefvpllAAILPQLpTVRTVIVEGDGPAAPLAPevgeyEELLAAASDTFDFPDIDENDAAAMLYTSGTT 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 680 GSPKGVMINHRGAVNTVLDINDRFGVGPDDRVLGLsnlgfdLSVYDVFG------PLSVGGAVVLPdpqRRGDPSHWADL 753
Cdd:PRK06187 180 GHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVI------VPMFHVHAwglpylALMAGAKQVIP---RRFDPENLLDL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 754 VGTHGVTVWNSVPAQLQMLHDYLVSATATVPdGLRLAMLSGDWIPVALPDQIRARVpGLRIVSLGGATEAS-IWSIWYPI 832
Cdd:PRK06187 251 IETERVTFFFAVPTIWQMLLKAPRAYFVDFS-SLRLVIYGGAALPPALLREFKEKF-GIDLVQGYGMTETSpVVSVLPPE 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 833 EQVDPEW-RSIPYGRPLTNQSFHVLDAALRPRP-DLVS-GELYIGGVGLAVGYLNDRERTAERFVvhpqtgERLYRTGDL 909
Cdd:PRK06187 329 DQLPGQWtKRRSAGRPLPGVEARIVDDDGDELPpDGGEvGEIIVRGPWLMQGYWNRPEATAETID------GGWLHTGDV 402
|
410 420 430
....*....|....*....|....*....|....*....
gi 1860141834 910 GRYLPDGTIEFLGREDLQVKIRGYRIELAEIEAALGGHP 948
Cdd:PRK06187 403 GYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHP 441
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
537-948 |
1.25e-31 |
|
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: 130.76 E-value: 1.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 537 QALSTPDRPAVVAADRTLDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVDTSQPAAR 616
Cdd:cd05936 8 AARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPRE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 617 RRTILTNAGIRCALTqsgvdrngwAEGLRlldvDLLGTGQPQPVEGSGDPEELAYVIHTSGSTGSPKGVMINHRGAVNTV 696
Cdd:cd05936 88 LEHILNDSGAKALIV---------AVSFT----DLLAAGAPLGERVALTPEDVAVLQYTSGTTGVPKGAMLTHRNLVANA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 697 LDINDRFGVG--PDDRVLGLsnlgfdLSVYDVFG-------PLSVGGAVVL-PDPqrrgDPSHWADLVGTHGVTVWNSVP 766
Cdd:cd05936 155 LQIKAWLEDLleGDDVVLAA------LPLFHVFGltvalllPLALGATIVLiPRF----RPIGVLKEIRKHRVTIFPGVP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 767 AQLQMLHDyLVSATATVPDGLRLAMLSGDWIPVALPDQIRARVpGLRIVSLGGATEASiwsiwyPIEQVDPEWR-----S 841
Cdd:cd05936 225 TMYIALLN-APEFKKRDFSSLRLCISGGAPLPVEVAERFEELT-GVPIVEGYGLTETS------PVVAVNPLDGprkpgS 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 842 IpyGRPLTNQSFHVLDAALRPRPDLVSGELYIGGVGLAVGYLNDRERTAERFVvhpqtgERLYRTGDLGRYLPDGTIEFL 921
Cdd:cd05936 297 I--GIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFV------DGWLRTGDIGYMDEDGYFFIV 368
|
410 420
....*....|....*....|....*...
gi 1860141834 922 GR-EDLqVKIRGYRIELAEIEAALGGHP 948
Cdd:cd05936 369 DRkKDM-IIVGGFNVYPREVEEVLYEHP 395
|
|
| COG4908 |
COG4908 |
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ... |
109-314 |
3.35e-30 |
|
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];
Pssm-ID: 443936 [Multi-domain] Cd Length: 243 Bit Score: 120.91 E-value: 3.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 109 ELDPERMTAAWRALIARHDMLRAV-VEADGA--QRVLAEVPpFEVPVIDLTGRPEAVVDAAVSAvraEMDHLVHTP---D 182
Cdd:COG4908 29 PLDVEALERALRELVRRHPALRTRfVEEDGEpvQRIDPDAD-LPLEVVDLSALPEPEREAELEE---LVAEEASRPfdlA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 183 RWPLFAARITR-ADHRTVLHVSIDFLIADFISVQVVLDELHRLYHRPDE----PLPPLEITFRDYQLAERAVRDSPRHER 257
Cdd:COG4908 105 RGPLLRAALIRlGEDEHVLLLTIHHIISDGWSLGILLRELAALYAALLEgeppPLPELPIQYADYAAWQRAWLQSEALEK 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1860141834 258 DKQWWLARVDELPAAPELPT-VARPADSEGRFRRWETRLSSQVWEGLRQRAGRHGVSP 314
Cdd:COG4908 185 QLEYWRQQLAGAPPVLELPTdRPRPAVQTFRGATLSFTLPAELTEALKALAKAHGATV 242
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
554-948 |
8.22e-29 |
|
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: 121.43 E-value: 8.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 554 LDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVDTSQPAARRRTILTNAGIRCALTQS 633
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 634 GVDrngwaeglrlldvdllgtgqpqpvegsgdpeELAYVIHTSGSTGSPKGVMINHRGAVNTVLDINDRFGVGPDDRVLG 713
Cdd:cd05935 82 ELD-------------------------------DLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSDVILA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 714 LSNL----GFdlsVYDVFGPLSVGGAVVLpdpQRRGDPSHWADLVGTHGVTVWNSVPAqlqMLHDYLVSATATVPDGLRL 789
Cdd:cd05935 131 CLPLfhvtGF---VGSLNTAVYVGGTYVL---MARWDRETALELIEKYKVTFWTNIPT---MLVDLLATPEFKTRDLSSL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 790 AMLS-GDW-IPVALPDQIRARVpGLRIVSLGGATEAsiwsiwYPIEQVDPEWR--SIPYGRPLTNQSFHVLDA-ALRPRP 864
Cdd:cd05935 202 KVLTgGGApMPPAVAEKLLKLT-GLRFVEGYGLTET------MSQTHTNPPLRpkLQCLGIP*FGVDARVIDIeTGRELP 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 865 DLVSGELYIGGVGLAVGYLNDRERTAERFVvhPQTGERLYRTGDLGRYLPDGTIEFLGREDLQVKIRGYRIELAEIEAAL 944
Cdd:cd05935 275 PNEVGEIVVRGPQIFKGYWNRPEETEESFI--EIKGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKL 352
|
....
gi 1860141834 945 GGHP 948
Cdd:cd05935 353 YKHP 356
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
538-948 |
3.31e-28 |
|
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: 121.58 E-value: 3.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 538 ALSTPDRPAVVAAD------RTLDYAELLGRAAGVAEALTAAGcRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPV--D 609
Cdd:cd05931 3 AAARPDRPAYTFLDdeggreETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLppP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 610 TSQPAARR-RTILTNAGIRCALTQSGVD--------RNGWAEGLRLLDVDLLGTGQPQPVEGSG-DPEELAYVIHTSGST 679
Cdd:cd05931 82 TPGRHAERlAAILADAGPRVVLTTAAALaavrafaaSRPAAGTPRLLVVDLLPDTSAADWPPPSpDPDDIAYLQYTSGST 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 680 GSPKGVMINHRGAVNTVLDINDRFGVGPDDRV---------LGLsnlgfdlsVYDVFGPLSVGGAVVLPDPQ---RRgdP 747
Cdd:cd05931 162 GTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVvswlplyhdMGL--------IGGLLTPLYSGGPSVLMSPAaflRR--P 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 748 SHWADLVGTHGVTvWNSVP--AqLQMLHDYLVSATATVPD--GLRLAMLSGDwiPVaLPDQIR------ARVpGLR---- 813
Cdd:cd05931 232 LRWLRLISRYRAT-ISAAPnfA-YDLCVRRVRDEDLEGLDlsSWRVALNGAE--PV-RPATLRrfaeafAPF-GFRpeaf 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 814 -----------IVSLGGATE---------ASIWSIWYPIEQVDPEWRSIP-YGRPLTNQSFHVLDAA-LRPRPDLVSGEL 871
Cdd:cd05931 306 rpsyglaeatlFVSGGPPGTgpvvlrvdrDALAGRAVAVAADDPAARELVsCGRPLPDQEVRIVDPEtGRELPDGEVGEI 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1860141834 872 YIGGVGLAVGYLNDRERTAERFVVHPQTGERLY-RTGDLGrYLPDGTIEFLGR-EDLQVkIRGYRIELAEIEAALGGHP 948
Cdd:cd05931 386 WVRGPSVASGYWGRPEATAETFGALAATDEGGWlRTGDLG-FLHDGELYITGRlKDLII-VRGRNHYPQDIEATAEEAH 462
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
551-948 |
1.66e-27 |
|
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341237 [Multi-domain] Cd Length: 486 Bit Score: 118.47 E-value: 1.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 551 DRTLDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVDTSQPA---------ARRRTIL 621
Cdd:cd05911 8 GKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTAdelahqlkiSKPKVIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 622 TNAG----IRCALTQSGVDRN---------GWAEGLRLLDVDLLGTGQPQPVEGSGDPEELAYVIHTSGSTGSPKGVMIN 688
Cdd:cd05911 88 TDPDglekVKEAAKELGPKDKiivlddkpdGVLSIEDLLSPTLGEEDEDLPPPLKDGKDDTAAILYSSGTTGLPKGVCLS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 689 HRGAVNTVLDINDRFG--VGPDDRVLGLsnlgfdLSVYDVFGPLSVGGAVVLPDPQ---RRGDPSHWADLVGTHGVTVWN 763
Cdd:cd05911 168 HRNLIANLSQVQTFLYgnDGSNDVILGF------LPLYHIYGLFTTLASLLNGATViimPKFDSELFLDLIEKYKITFLY 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 764 SVPAQLQMLhdyLVSATATVPD--GLRLAMLSGDWIPVALPDQIRARVPGLRIVSLGGATEASIWSIWYPIEQVDPEwrS 841
Cdd:cd05911 242 LVPPIAAAL---AKSPLLDKYDlsSLRVILSGGAPLSKELQELLAKRFPNATIKQGYGMTETGGILTVNPDGDDKPG--S 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 842 IpyGRPLTNQSFHVLD----AALRPRpdlVSGELYIGGVGLAVGYLNDRERTAERFvvhpqTGERLYRTGDLGRYLPDGT 917
Cdd:cd05911 317 V--GRLLPNVEAKIVDddgkDSLGPN---EPGEICVRGPQVMKGYYNNPEATKETF-----DEDGWLHTGDIGYFDEDGY 386
|
410 420 430
....*....|....*....|....*....|..
gi 1860141834 918 IEFLGR-EDLqVKIRGYRIELAEIEAALGGHP 948
Cdd:cd05911 387 LYIVDRkKEL-IKYKGFQVAPAELEAVLLEHP 417
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
556-948 |
1.78e-26 |
|
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: 114.91 E-value: 1.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 556 YAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVDTS--QPAARRRtiLTNAGIRCALTQS 633
Cdd:cd05969 3 FAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAfgPEAIRDR--LENSEAKVLITTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 634 gvdrngwaeglRLLDvdllgtgqpqpvegSGDPEELAYVIHTSGSTGSPKGVMINHRGAVNTVLDINDRFGVGPDDRVLG 713
Cdd:cd05969 81 -----------ELYE--------------RTDPEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLHPDDIYWC 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 714 LSNLGFDL-SVYDVFGPLSVGGAVVLPDPqrRGDPSHWADLVGTHGVTVWNSVPAQLQMLHDYLVS-ATATVPDGLRLAM 791
Cdd:cd05969 136 TADPGWVTgTVYGIWAPWLNGVTNVVYEG--RFDAESWYGIIERVKVTVWYTAPTAIRMLMKEGDElARKYDLSSLRFIH 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 792 LSGDwiPVAlPDQIR--ARVPGLRIVSLGGATE-ASIWSIWYPIEQVDPEwrsiPYGRPLTNQSFHVLDAALRPRPDLVS 868
Cdd:cd05969 214 SVGE--PLN-PEAIRwgMEVFGVPIHDTWWQTEtGSIMIANYPCMPIKPG----SMGKPLPGVKAAVVDENGNELPPGTK 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 869 GELYI--GGVGLAVGYLNDRERTAERFVvhpqTGerLYRTGDLGRYLPDGTIEFLGREDLQVKIRGYRIELAEIEAALGG 946
Cdd:cd05969 287 GILALkpGWPSMFRGIWNDEERYKNSFI----DG--WYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALME 360
|
..
gi 1860141834 947 HP 948
Cdd:cd05969 361 HP 362
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
544-948 |
2.83e-26 |
|
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: 114.10 E-value: 2.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 544 RPAVVAADRTLDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVDTSQPAARRRTILTN 623
Cdd:cd05919 1 KTAFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 624 AGIRCALTqsgvdrngwaeglrlldvdllgtgqpqpvegsgDPEELAYVIHTSGSTGSPKGVMINHRGAVNTV-LDINDR 702
Cdd:cd05919 81 CEARLVVT---------------------------------SADDIAYLLYSSGTTGPPKGVMHAHRDPLLFAdAMAREA 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 703 FGVGPDDRVLGLSNLGFDLSV-YDVFGPLSVGGAVVLpDPQRRgDPSHWADLVGTHGVTVWNSVPAqlqMLHDYLVSATA 781
Cdd:cd05919 128 LGLTPGDRVFSSAKMFFGYGLgNSLWFPLAVGASAVL-NPGWP-TAERVLATLARFRPTVLYGVPT---FYANLLDSCAG 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 782 TVPD--GLRLAMLSGDWIPVALPDQIRARVpGLRIVSLGGATEASIWSIwypIEQVDpEWRSIPYGRPLTNQSFHVLDAA 859
Cdd:cd05919 203 SPDAlrSLRLCVSAGEALPRGLGERWMEHF-GGPILDGIGATEVGHIFL---SNRPG-AWRLGSTGRPVPGYEIRLVDEE 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 860 LRPRPDLVSGELYIGGVGLAVGYLNDRERTAERFVvhpqtgERLYRTGDLGRYLPDGTIEFLGREDLQVKIRGYRIELAE 939
Cdd:cd05919 278 GHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFN------GGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVE 351
|
....*....
gi 1860141834 940 IEAALGGHP 948
Cdd:cd05919 352 VESLIIQHP 360
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
1369-1728 |
1.00e-25 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 116.30 E-value: 1.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 1369 VRISRDDLTEHLAGRLPQYMVPSVVQVVDALPLNANGKVDRAVLRRRLPRRGTATAAGSSGaldsdLERRIAAVWAEALR 1448
Cdd:PRK10252 918 LPLDTSALQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKALPLPELKAQVPGRAPKTG-----TETIIAAAFSSLLG 992
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 1449 LPRVGRDENLFELGGDSLVAAQITGRILEEIPQAAGlffdqlLRQVLEQPTVAALAGHVEAESATPVTA--SPSVPATSG 1526
Cdd:PRK10252 993 CDVVDADADFFALGGHSLLAMKLAAQLSRQFARQVT------PGQVMVASTVAKLATLLDAEEDESRRLgfGTILPLREG 1066
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 1527 -GDGLSPLHEGTdGVPWvlvpggegvdAYAGLVPHLAATGPVLGL---APGA----ADDLLRVAAAQ-ARLVTAAVHPAV 1597
Cdd:PRK10252 1067 dGPTLFCFHPAS-GFAW----------QFSVLSRYLDPQWSIYGIqspRPDGpmqtATSLDEVCEAHlATLLEQQPHGPY 1135
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 1598 RLVGYGLGATSTLEVARSLIETGGQVDAVVLISPWrpaagADPAAAYRAETGAagtpGEDFAArLAAVARHEPTL----- 1672
Cdd:PRK10252 1136 HLLGYSLGGTLAQGIAARLRARGEEVAFLGLLDTW-----PPETQNWREKEAN----GLDPEV-LAEIDREREAFlaaqq 1205
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 1673 --------------YAGDLVVLRPTGAVPYDAQSLEFWADLCL--------------GDVRTVDVDADHLTVLGPAAGTA 1724
Cdd:PRK10252 1206 gslstelfttiegnYADAVRLLTTAHSVPFDGKATLFVAERTLqegmspeqawspwiAELDVYRQDCAHVDIISPEAFEK 1285
|
....
gi 1860141834 1725 LAAL 1728
Cdd:PRK10252 1286 IGPI 1289
|
|
| LCL_NRPS-like |
cd19531 |
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ... |
109-322 |
2.07e-25 |
|
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: 111.29 E-value: 2.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 109 ELDPERMTAAWRALIARHDMLRAV-VEADGA--QRVLAEVPpFEVPVIDLTGRPEAVVDAAVSAVraeMDHLVHTP---D 182
Cdd:cd19531 35 PLDVAALERALNELVARHEALRTTfVEVDGEpvQVILPPLP-LPLPVVDLSGLPEAEREAEAQRL---AREEARRPfdlA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 183 RWPLFAAR-ITRADHRTVLHVSIDFLIADFISVQVVLDELHRLY----HRPDEPLPPLEITFRDYQLAERAVRDSPRHER 257
Cdd:cd19531 111 RGPLLRATlLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELAALYaaflAGRPSPLPPLPIQYADYAVWQREWLQGEVLER 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1860141834 258 DKQWWLARVDELPAAPELPT-VARPADSEGRFRRWETRLSSQVWEGLRQRAGRHGVSPSGAVLAAF 322
Cdd:cd19531 191 QLAYWREQLAGAPPVLELPTdRPRPAVQSFRGARVRFTLPAELTAALRALARREGATLFMTLLAAF 256
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
525-948 |
6.97e-25 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 111.21 E-value: 6.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 525 VPAGMLHDRVVLQALSTPDRPAVVAADRTLDYAELLGRAAGVAEAL-TAAGCRRQELVAVVMDRGWEQVVAVLGALLAGC 603
Cdd:PRK08314 7 LPETSLFHNLEVSARRYPDKTAIVFYGRAISYRELLEEAERLAGYLqQECGVRKGDRVLLYMQNSPQFVIAYYAILRANA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 604 VYVPVDTSQPAARRRTILTNAGIRCALTQS-------------------------------------GVDRNGWAEGLRL 646
Cdd:PRK08314 87 VVVPVNPMNREEELAHYVTDSGARVAIVGSelapkvapavgnlrlrhvivaqysdylpaepeiavpaWLRAEPPLQALAP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 647 LDV----DLLGTGQPqPVEGSGDPEELAYVIHTSGSTGSPKGVMINHRGAVNTVLDINDRFGVGPDDRVLGLSNL----G 718
Cdd:PRK08314 167 GGVvawkEALAAGLA-PPPHTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPLfhvtG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 719 FdlsVYDVFGPLSVGGAVVLpdpQRRGDPSHWADLVGTHGVTVWNSVPAqlqMLHDYLVSATATVPDGLRLAMLSGDwiP 798
Cdd:PRK08314 246 M---VHSMNAPIYAGATVVL---MPRWDREAAARLIERYRVTHWTNIPT---MVVDFLASPGLAERDLSSLRYIGGG--G 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 799 VALPDQIRARVP---GLRIVSLGGATEASIWSIWYPIEQVDPEWRSIPygrpltnqSFHVlDA------ALRPRPDLVSG 869
Cdd:PRK08314 315 AAMPEAVAERLKeltGLDYVEGYGLTETMAQTHSNPPDRPKLQCLGIP--------TFGV-DArvidpeTLEELPPGEVG 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1860141834 870 ELYIGGVGLAVGYLNDRERTAERFVVhpQTGERLYRTGDLGRYLPDGTIEFLGREDLQVKIRGYRIELAEIEAALGGHP 948
Cdd:PRK08314 386 EIVVHGPQVFKGYWNRPEATAEAFIE--IDGKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHP 462
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
552-948 |
2.30e-24 |
|
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: 108.45 E-value: 2.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 552 RTLDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVDTSQPAARRRTILTNAGIRCALT 631
Cdd:cd05907 4 QPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 632 qsgvdrngwaeglrlldvdllgtgqpqpvegsGDPEELAYVIHTSGSTGSPKGVMINHRGAVNTVLDINDRFGVGPDDRV 711
Cdd:cd05907 84 --------------------------------EDPDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEGDRH 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 712 LGLSNLGFDL-SVYDVFGPLSVGGAVVLPDPQRRGdpshwADLVGTHGVTVWNSVPAQLQMLHDYLVSATATvpdGLRLA 790
Cdd:cd05907 132 LSFLPLAHVFeRRAGLYVPLLAGARIYFASSAETL-----LDDLSEVRPTVFLAVPRVWEKVYAAIKVKAVP---GLKRK 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 791 ML------SGDWIPV---ALPDQI--RARVPGLRIVSLGGATE-ASIWSIWYPieqVDPEWRSIpyGRPLTnqsfhvlDA 858
Cdd:cd05907 204 LFdlavggRLRFAASggaPLPAELlhFFRALGIPVYEGYGLTEtSAVVTLNPP---GDNRIGTV--GKPLP-------GV 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 859 ALRPRPDlvsGELYIGGVGLAVGYLNDRERTAERFvvhpqTGERLYRTGDLGRYLPDGTIEFLGR-EDLQVKIRGYRIEL 937
Cdd:cd05907 272 EVRIADD---GEILVRGPNVMLGYYKNPEATAEAL-----DADGWLHTGDLGEIDEDGFLHITGRkKDLIITSGGKNISP 343
|
410
....*....|.
gi 1860141834 938 AEIEAALGGHP 948
Cdd:cd05907 344 EPIENALKASP 354
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
542-948 |
2.59e-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: 2.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 542 PDRPAVV------AADRTLDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVDTSQPAA 615
Cdd:cd17634 67 GDRTAIIyegddtSQSRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 616 RRRTILTNAGIRCALTQSG------------------------------VDRNG----WAEGLRLLDVDLLGTGQPQPVE 661
Cdd:cd17634 147 AVAGRIIDSSSRLLITADGgvragrsvplkknvddalnpnvtsvehvivLKRTGsdidWQEGRDLWWRDLIAKASPEHQP 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 662 GSGDPEELAYVIHTSGSTGSPKGVMINHRG-AVNTVLDINDRFGVGPDDRVLGLSNLGFDLS-VYDVFGPLSVGGAVVLP 739
Cdd:cd17634 227 EAMNAEDPLFILYTSGTTGKPKGVLHTTGGyLVYAATTMKYVFDYGPGDIYWCTADVGWVTGhSYLLYGPLACGATTLLY 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 740 DPQRRG-DPSHWADLVGTHGVTVWNSVPAQLQMLHDYLVSATA-TVPDGLRLAMLSGD-WIPVALPDQIRARVPGLR-IV 815
Cdd:cd17634 307 EGVPNWpTPARMWQVVDKHGVNILYTAPTAIRALMAAGDDAIEgTDRSSLRILGSVGEpINPEAYEWYWKKIGKEKCpVV 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 816 SLGGATEASiWSIWYPIEQVDPEWRSIPYgRPLTNQSFHVLDAALRPRPDLVSGELYIGGV--GLAVGYLNDRERtaeRF 893
Cdd:cd17634 387 DTWWQTETG-GFMITPLPGAIELKAGSAT-RPVFGVQPAVVDNEGHPQPGGTEGNLVITDPwpGQTRTLFGDHER---FE 461
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1860141834 894 VVHPQTGERLYRTGDLGRYLPDGTIEFLGREDLQVKIRGYRIELAEIEAALGGHP 948
Cdd:cd17634 462 QTYFSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHP 516
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
1373-1627 |
1.02e-23 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 110.25 E-value: 1.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 1373 RDDLTEHLAGRLPQYMVPSVVQVVDALPLNANGKVDRavlrRRLPRRgTATAAGSSGALDSDLERRIAAVWAEALRLPRV 1452
Cdd:PRK12467 3549 RETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDR----KALPDP-DAKGSREYVAPRSEVEQQLAAIWADVLGVEQV 3623
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 1453 GRDENLFELGGDSLVAAQitgrILEEIPQAAGLffDQLLRQVLEQPTVAALAGHVEAESatpVTASPSVPATSGGDGLSP 1532
Cdd:PRK12467 3624 GVTDNFFELGGDSLLALQ----VLSRIRQSLGL--KLSLRDLMSAPTIAELAGYSPLGD---VPVNLLLDLNRLETGFPA 3694
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 1533 L---HEGT----DGVPWVLVPggEGVDAYAGLVPHLAatgpvlgLAPGAADDLLRVAAAQARLVTAAVHP--AVRLVGYG 1603
Cdd:PRK12467 3695 LfcrHEGLgtvfDYEPLAVIL--EGDRHVLGLTCRHL-------LDDGWQDTSLQAMAVQYADYILWQQAkgPYGLLGWS 3765
|
250 260
....*....|....*....|....
gi 1860141834 1604 LGATSTLEVARsLIETGGQVDAVV 1627
Cdd:PRK12467 3766 LGGTLARLVAE-LLEREGESEAFL 3788
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
542-948 |
2.73e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 106.12 E-value: 2.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 542 PDRPAVVAADRTLDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVDTSQPAARRRTIL 621
Cdd:PRK07798 17 PDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 622 TNAGIRCALTQSG-----VDRNGWAEGLRLLDV-----------------DLLGTGQPQPVEGSGDPEELaYVIHTSGST 679
Cdd:PRK07798 97 DDSDAVALVYEREfaprvAEVLPRLPKLRTLVVvedgsgndllpgavdyeDALAAGSPERDFGERSPDDL-YLLYTGGTT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 680 GSPKGVM-------------INHRG--AVNTVLDINDRFGVGPDDRVLGLSNLGFDLSVYDVFGPLSVGGAVVLPdPQRR 744
Cdd:PRK07798 176 GMPKGVMwrqedifrvllggRDFATgePIEDEEELAKRAAAGPGMRRFPAPPLMHGAGQWAAFAALFSGQTVVLL-PDVR 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 745 GDPSHWADLVGTHGVTVWNSV------P--AQLQMLHDYLVSATATVPDGlrLAMLSGdwipvALPDQIRARVPGLRIVS 816
Cdd:PRK07798 255 FDADEVWRTIEREKVNVITIVgdamarPllDALEARGPYDLSSLFAIASG--GALFSP-----SVKEALLELLPNVVLTD 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 817 LGGATEASIWSIWYPIEqvdpewRSIPYGRPL--TNQSFHVLDAALRPRP--DLVSGELYIGGVgLAVGYLNDRERTAER 892
Cdd:PRK07798 328 SIGSSETGFGGSGTVAK------GAVHTGGPRftIGPRTVVLDEDGNPVEpgSGEIGWIARRGH-IPLGYYKDPEKTAET 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1860141834 893 FVVHpqTGERLYRTGDLGRYLPDGTIEFLGREDLQVKIRGYRIELAEIEAALGGHP 948
Cdd:PRK07798 401 FPTI--DGVRYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHP 454
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
1358-1522 |
5.83e-23 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 107.55 E-value: 5.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 1358 CVLAARFKTDRVRISRDDLTEHLAGRLPQYMVPSVVQVVDALPLNANGKVDRavlrRRLPRRGTATAAGSSGALDSDLER 1437
Cdd:PRK12467 958 LVPAAVADGAEHQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDR----KALPKPDASAVQATFVAPQTELEK 1033
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 1438 RIAAVWAEALRLPRVGRDENLFELGGDSLVAAQITGRileeIPQAAGLffdQL-LRQVLEQPTVAALAGHVEAESATPVT 1516
Cdd:PRK12467 1034 RLAAIWADVLKVERVGLTDNFFELGGHSLLATQVISR----VRQRLGI---QVpLRTLFEHQTLAGFAQAVAAQQQGAQP 1106
|
....*.
gi 1860141834 1517 ASPSVP 1522
Cdd:PRK12467 1107 ALPDVD 1112
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
556-948 |
6.72e-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: 104.05 E-value: 6.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 556 YAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVDT--SQPAARRRtiLTNAGIRCALTqs 633
Cdd:cd05971 9 FKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFAlfGPEALEYR--LSNSGASALVT-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 634 gvdrngwaeglrlldvdllgtgqpqpvEGSGDPeelAYVIHTSGSTGSPKG------VMINHRGAVNTVLDINDRfgvgP 707
Cdd:cd05971 85 ---------------------------DGSDDP---ALIIYTSGTTGPPKGalhahrVLLGHLPGVQFPFNLFPR----D 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 708 DDRVLGLSNLGFDLSVYDVFGPLSVGGAVVLPDPQRRGDPSHWADLVGTHGVTVWNSVPAQLQM-------LHDYLVSAT 780
Cdd:cd05971 131 GDLYWTPADWAWIGGLLDVLLPSLYFGVPVLAHRMTKFDPKAALDLMSRYGVTTAFLPPTALKMmrqqgeqLKHAQVKLR 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 781 ATVPDGLRLAMLSGDWIPVALpdqirarvpGLRIVSLGGATEASIW----SIWYPIeqvdpewRSIPYGRPLTNQSFHVL 856
Cdd:cd05971 211 AIATGGESLGEELLGWAREQF---------GVEVNEFYGQTECNLVigncSALFPI-------KPGSMGKPIPGHRVAIV 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 857 DAALRPRPDLVSGELYI---GGVGLaVGYLNDRERTAERFVvhpqtGERLyRTGDLGRYLPDGTIEFLGREDLQVKIRGY 933
Cdd:cd05971 275 DDNGTPLPPGEVGEIAVelpDPVAF-LGYWNNPSATEKKMA-----GDWL-LTGDLGRKDSDGYFWYVGRDDDVITSSGY 347
|
410
....*....|....*
gi 1860141834 934 RIELAEIEAALGGHP 948
Cdd:cd05971 348 RIGPAEIEECLLKHP 362
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
521-995 |
7.61e-23 |
|
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: 104.33 E-value: 7.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 521 TQAPVPAGMLHDRVVLQ-ALSTPDRPAVVAADRTLDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGAL 599
Cdd:cd05920 7 RAAGYWQDEPLGDLLARsAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 600 LAGCvyVPVdTSQPAARRRTILTNAGIRCALTQSGVDRNGwaeglrllDVDllgtGQPQPVEGSGDPEELAYVIHTSGST 679
Cdd:cd05920 87 RLGA--VPV-LALPSHRRSELSAFCAHAEAVAYIVPDRHA--------GFD----HRALARELAESIPEVALFLLSGGTT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 680 GSPKGVMINHRGAVNTVLDINDRFGVGPDDRVLGLSNLG--FDLSVYDVFGPLSVGGAVVLPDPqrrGDPSHWADLVGTH 757
Cdd:cd05920 152 GTPKLIPRTHNDYAYNVRASAEVCGLDQDTVYLAVLPAAhnFPLACPGVLGTLLAGGRVVLAPD---PSPDAAFPLIERE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 758 GVTVWNSVPAQLQMLHDYLVSATATvPDGLRLAMLSGDWIPVALPDQIRArVPGLRIVSLGGATEASIWSIWYPieqvDP 837
Cdd:cd05920 229 GVTVTALVPALVSLWLDAAASRRAD-LSSLRLLQVGGARLSPALARRVPP-VLGCTLQQVFGMAEGLLNYTRLD----DP 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 838 EWRSI-PYGRPLT-NQSFHVLDAALRPRPDLVSGELYIGGVGLAVGYLNDRERTAERFvvhpqTGERLYRTGDLGRYLPD 915
Cdd:cd05920 303 DEVIIhTQGRPMSpDDEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAF-----TPDGFYRTGDLVRRTPD 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 916 GTIEFLGREDLQVKIRGYRIELAEIEAALGGHPAVAGAVVVVDGDTPLERRLAAFVEPAGRPVTAAQAehdQAALRQLGV 995
Cdd:cd05920 378 GYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLRDPPPSAAQL---RRFLRERGL 454
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
1373-1512 |
1.83e-22 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 106.19 E-value: 1.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 1373 RDDLTEHLAGRLPQYMVPSVVQVVDALPLNANGKVDRavlrRRLPRRGTATAAGSSGALDSDLERRIAAVWAEALRLPRV 1452
Cdd:PRK12316 5015 RDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDR----KALPQPDASLLQQAYVAPRSELEQQVAAIWAEVLQLERV 5090
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 1453 GRDENLFELGGDSLVAAQITGRILEEipqaagLFFDQLLRQVLEQPTVAALAGHVEAESA 1512
Cdd:PRK12316 5091 GLDDNFFELGGHSLLAIQVTSRIQLE------LGLELPLRELFQTPTLAAFVELAAAAGS 5144
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
1373-1524 |
2.92e-22 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 105.42 E-value: 2.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 1373 RDDLTEHLAGRLPQYMVPSVVQVVDALPLNANGKVDRavlrRRLPRRGTATAAGSSGALDSDLERRIAAVWAEALRLPRV 1452
Cdd:PRK12316 3499 REALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDR----KALPRPDAALLQQDYVAPVNELERRLAAIWADVLKLEQV 3574
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1860141834 1453 GRDENLFELGGDSLVAAQITGRIleeipQAAGLFFDqlLRQVLEQPTVAALAGHVEAESATPVTASPSVPAT 1524
Cdd:PRK12316 3575 GLTDNFFELGGDSIISLQVVSRA-----RQAGIRFT--PKDLFQHQTIQGLARVARVGGGVAVDQGPVSGET 3639
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
530-948 |
4.14e-22 |
|
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: 102.31 E-value: 4.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 530 LHDRVVLQALSTPDRPAVV--AADRTLDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVyvp 607
Cdd:cd05904 7 LDSVSFLFASAHPSRPALIdaATGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAV--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 608 VDTSQPAARRRTI---LTNAGIRCALTQSGVdrngwAEGLR-------LLD---VDLLGTGQPQPVEGSGDP-------E 667
Cdd:cd05904 84 VTTANPLSTPAEIakqVKDSGAKLAFTTAEL-----AEKLAslalpvvLLDsaeFDSLSFSDLLFEADEAEPpvvvikqD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 668 ELAYVIHTSGSTGSPKGVMINHRGAVNTVLDINDRFG--VGPDDRVLGLSNL----GFDLSVYdvfGPLSVGGAVVLpdp 741
Cdd:cd05904 159 DVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEGsnSDSEDVFLCVLPMfhiyGLSSFAL---GLLRLGATVVV--- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 742 QRRGDPSHWADLVGTHGVTVWNSVP------AQLQMLHDYLVSAtatvpdgLRLAMLSGDWIPVALPDQIRARVPGLRIV 815
Cdd:cd05904 233 MPRFDLEELLAAIERYKVTHLPVVPpivlalVKSPIVDKYDLSS-------LRQIMSGAAPLGKELIEAFRAKFPNVDLG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 816 SLGGATEAS-IWSIWYPIEQVDPEWRSIpyGRPLTNQSFHVLD----AALRPRPdlvSGELYIGGVGLAVGYLNDRERTA 890
Cdd:cd05904 306 QGYGMTESTgVVAMCFAPEKDRAKYGSV--GRLVPNVEAKIVDpetgESLPPNQ---TGELWIRGPSIMKGYLNNPEATA 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1860141834 891 ERFvvhpqTGERLYRTGDLGRYLPDGTIEFLGREDLQVKIRGYRIELAEIEAALGGHP 948
Cdd:cd05904 381 ATI-----DKEGWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHP 433
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
665-947 |
4.17e-22 |
|
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: 102.02 E-value: 4.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 665 DPEELAYVIHTSGSTGSPKGVMINHRGAVNTVLDINDRFGVGPDDRVLGLsnlgfdLSVYDVFG-------PLSVGGAVV 737
Cdd:cd05909 145 QPDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGA------LPFFHSFGltgclwlPLLSGIKVV 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 738 L-PDPQrrgDPSHWADLVGTHGVTVWNSVPAqlqMLHDYLVSATATVPDGLRLAMLSGDWIPVALPDQIRARVpGLRIVS 816
Cdd:cd05909 219 FhPNPL---DYKKIPELIYDKKATILLGTPT---FLRGYARAAHPEDFSSLRLVVAGAEKLKDTLRQEFQEKF-GIRILE 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 817 LGGATEAS-IWSIWYPieqvDPEWRSIPYGRPLTNQSFHVLD-AALRPRPDLVSGELYIGGVGLAVGYLNDRERTAERFv 894
Cdd:cd05909 292 GYGTTECSpVISVNTP----QSPNKEGTVGRPLPGMEVKIVSvETHEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAF- 366
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1860141834 895 vhpqtGERLYRTGDLGRYLPDGTIEFLGREDLQVKIRGYRIELAEIEAALGGH 947
Cdd:cd05909 367 -----GDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEI 414
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
482-948 |
5.82e-22 |
|
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.
Pssm-ID: 341272 [Multi-domain] Cd Length: 610 Bit Score: 102.57 E-value: 5.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 482 FAAYDAvLHRLAGDDAAW--------TGTGHPDPPEATRDRRAETNRTQAPVPAGMlhdRVVLQALS-----TPDRPAVV 548
Cdd:cd05968 6 IPDLEA-FLERSAEDNAWfwgefvkdVGIEWYEPPYQTLDLSGGKPWAAWFVGGRM---NIVEQLLDkwladTRTRPALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 549 -----AADRTLDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVDTSQPAARRRTILTN 623
Cdd:cd05968 82 wegedGTSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 624 AGIRCALTQSGVDRNGWAEGL--------------------RLLDVDLLGT-----GQPQPVEGSGD------PEELAYV 672
Cdd:cd05968 162 AEAKALITADGFTRRGREVNLkeeadkacaqcptvekvvvvRHLGNDFTPAkgrdlSYDEEKETAGDgaerteSEDPLMI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 673 IHTSGSTGSPKGVMINHRG-AVNTVLDINDRFGVGPDDRVLGLSNLGFDLSVYDVFGPLSVGGAVVLPDpqrrGDPSH-- 749
Cdd:cd05968 242 IYTSGTTGKPKGTVHVHAGfPLKAAQDMYFQFDLKPGDLLTWFTDLGWMMGPWLIFGGLILGATMVLYD----GAPDHpk 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 750 ----WaDLVGTHGVTVWNSVPAqlqmlhdyLVSATATVPDG---------LRLAMLSGD-WIPVA----LPDQIRARVPg 811
Cdd:cd05968 318 adrlW-RMVEDHEITHLGLSPT--------LIRALKPRGDApvnahdlssLRVLGSTGEpWNPEPwnwlFETVGKGRNP- 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 812 lrIVSLGGATEASiWSIW--YPIEQVDPewrsIPYGRPLTNQSFHVLDAALRPRPDLVsGELYIGG--VGLAVGYLNDRE 887
Cdd:cd05968 388 --IINYSGGTEIS-GGILgnVLIKPIKP----SSFNGPVPGMKADVLDESGKPARPEV-GELVLLApwPGMTRGFWRDED 459
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1860141834 888 RTAERFVvhpQTGERLYRTGDLGRYLPDGTIEFLGREDLQVKIRGYRIELAEIEAALGGHP 948
Cdd:cd05968 460 RYLETYW---SRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHP 517
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
537-948 |
2.06e-21 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 100.04 E-value: 2.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 537 QALSTPDRPAVVAADRTLDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVDTSQPAAR 616
Cdd:PRK03640 11 RAFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 617 RRTILTNAGIRCALT-QSGVDRNgwaEGLRLLDVDLLGTGQPQPVE--GSGDPEELAYVIHTSGSTGSPKGVMI---NH- 689
Cdd:PRK03640 91 LLWQLDDAEVKCLITdDDFEAKL---IPGISVKFAELMNGPKEEAEiqEEFDLDEVATIMYTSGTTGKPKGVIQtygNHw 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 690 RGAVNTVLDIndrfGVGPDDRVL---------GLSNLgfdlsvydvFGPLSVGGAVVLpdpQRRGDPSHWADLVGTHGVT 760
Cdd:PRK03640 168 WSAVGSALNL----GLTEDDCWLaavpifhisGLSIL---------MRSVIYGMRVVL---VEKFDAEKINKLLQTGGVT 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 761 VWNSVPAQLQ-MLHDYlvsATATVPDGLRLAMLSGDWIPVALPDQIRARvpGLRIVSLGGATE-ASiwsiwyPIEQVDPE 838
Cdd:PRK03640 232 IISVVSTMLQrLLERL---GEGTYPSSFRCMLLGGGPAPKPLLEQCKEK--GIPVYQSYGMTEtAS------QIVTLSPE 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 839 WR-----SIpyGRPLtnqsFHV---LDAALRPRPDLVSGELYIGGVGLAVGYLNDRERTAERFvvhpQTGerLYRTGDLG 910
Cdd:PRK03640 301 DAltklgSA--GKPL----FPCelkIEKDGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETF----QDG--WFKTGDIG 368
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1860141834 911 rYL-PDGTIEFLGRE-DLQVKiRGYRIELAEIEAALGGHP 948
Cdd:PRK03640 369 -YLdEEGFLYVLDRRsDLIIS-GGENIYPAEIEEVLLSHP 406
|
|
| Condensation |
pfam00668 |
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ... |
108-419 |
2.40e-21 |
|
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: 99.33 E-value: 2.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 108 PELDPERMTAAWRALIARHDMLRAVV--EADG--AQRVLAEVpPFEVPVIDLTGrpeAVVDAAVSAVRAEMDHLVHTP-- 181
Cdd:pfam00668 37 GELDPERLEKALQELINRHDALRTVFirQENGepVQVILEER-PFELEIIDISD---LSESEEEEAIEAFIQRDLQSPfd 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 182 -DRWPLF-AARITRADHRTVLHVSIDFLIADFISVQVVLDELHRLYH--RPDEPLPPLEIT-FRDYQLAERAVRDSPRHE 256
Cdd:pfam00668 113 lEKGPLFrAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQqlLKGEPLPLPPKTpYKDYAEWLQQYLQSEDYQ 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 257 RDKQWWLARVDELPAAPELPTV-ARPADSEGRFRRWETRLSSQVWEGLRQRAGRHGVSPSGAVLAAFSDTIAAYSRRSRF 335
Cdd:pfam00668 193 KDAAYWLEQLEGELPVLQLPKDyARPADRSFKGDRLSFTLDEDTEELLRKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDI 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 336 TLDITLLNRApvHDQVNALVGDFTSVDLLAVDADPTRRFDERARDLQAQLWEDLDHRSFsGIEVMREIARRQGAEA--AL 413
Cdd:pfam00668 273 VVGTPGSGRP--SPDIERMVGMFVNTLPLRIDPKGGKTFSELIKRVQEDLLSAEPHQGY-PFGDLVNDLRLPRDLSrhPL 349
|
....*.
gi 1860141834 414 FPVVFT 419
Cdd:pfam00668 350 FDPMFS 355
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
519-712 |
3.10e-21 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 100.17 E-value: 3.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 519 NRTQAPVPAGMLHDRVVLQALSTPDRPAVVAAD----RTLDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVA 594
Cdd:COG1022 2 SEFSDVPPADTLPDLLRRRAARFPDRVALREKEdgiwQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 595 VLGALLAGCVYVPVDTSQPAARRRTILTNAGIRCALTQSG---------------------VDRNGWAEGLRLLDV-DLL 652
Cdd:COG1022 82 DLAILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDQeqldkllevrdelpslrhivvLDPRGLRDDPRLLSLdELL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1860141834 653 GTG----QPQPVE---GSGDPEELAYVIHTSGSTGSPKGVMINHRGAVNTVLDINDRFGVGPDDRVL 712
Cdd:COG1022 162 ALGrevaDPAELEarrAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTL 228
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
538-948 |
3.35e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 99.62 E-value: 3.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 538 ALSTPDRPAVVAADRTLDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVDTSQPAARR 617
Cdd:PRK08316 21 ARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 618 RTILTNAG-------------IRCALTQSGVDRNGWAEGL-------RLLDVDLLGTGQPQPVEGSG-DPEELAYVIHTS 676
Cdd:PRK08316 101 AYILDHSGaraflvdpalaptAEAALALLPVDTLILSLVLggreapgGWLDFADWAEAGSVAEPDVElADDDLAQILYTS 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 677 GSTGSPKGVMINHRGA----VNTVLDIndrfGVGPDDRVLGlsnlgfDLSVY-----DVF-GP-LSVGGAVVL---PDPQ 742
Cdd:PRK08316 181 GTESLPKGAMLTHRALiaeyVSCIVAG----DMSADDIPLH------ALPLYhcaqlDVFlGPyLYVGATNVIldaPDPE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 743 RrgdpshWADLVGTHGV-------TVWNSVpaqlqmlhdylvsatATVPD-------GLRLAMLSGDWIPVALPDQIRAR 808
Cdd:PRK08316 251 L------ILRTIEAERItsffappTVWISL---------------LRHPDfdtrdlsSLRKGYYGASIMPVEVLKELRER 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 809 VPGLRIVSLGGATE-ASIWSIWYPIEQvdpEWRSIPYGRPLTNQSFHVLDAALRPRPDLVSGELYIGGVGLAVGYLNDRE 887
Cdd:PRK08316 310 LPGLRFYNCYGQTEiAPLATVLGPEEH---LRRPGSAGRPVLNVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPE 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1860141834 888 RTAERFvvhpQTGerLYRTGDLGRYLPDGTIEFLGREDLQVKIRGYRIELAEIEAALGGHP 948
Cdd:PRK08316 387 KTAEAF----RGG--WFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHP 441
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
556-944 |
4.43e-21 |
|
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: 99.28 E-value: 4.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 556 YAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPV----DTSQPAARRR------------T 619
Cdd:cd05906 42 YQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLtvppTYDEPNARLRklrhiwqllgspV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 620 ILTNAGIRCAL-TQSGVDRNgwaEGLRLLDVDLLGTGQPQPVEGSGDPEELAYVIHTSGSTGSPKGVMINHRGAVNTVLD 698
Cdd:cd05906 122 VLTDAELVAEFaGLETLSGL---PGIRVLSIEELLDTAADHDLPQSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAG 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 699 INDRFGVGPDDRvlGLSNLGFD----LSVYDVFGPLSVGGAVVLPDPQRRGDPSHWADLVGTHGVTV-W--NSVPAQLQM 771
Cdd:cd05906 199 KIQHNGLTPQDV--FLNWVPLDhvggLVELHLRAVYLGCQQVHVPTEEILADPLRWLDLIDRYRVTItWapNFAFALLND 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 772 LHDYLVSATATVpDGLRLAMLSGDWIPVALPDQ-IRARVP-GLR---IVSLGGATEAS---IWSIWYPIEQVDPEWRSIP 843
Cdd:cd05906 277 LLEEIEDGTWDL-SSLRYLVNAGEAVVAKTIRRlLRLLEPyGLPpdaIRPAFGMTETCsgvIYSRSFPTYDHSQALEFVS 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 844 YGRPLTNQSFHVLDAALRPRPDLVSGELYIGGVGLAVGYLNDRERTAERFvvhpqTGERLYRTGDLGrYLPDGTIEFLGR 923
Cdd:cd05906 356 LGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAF-----TEDGWFRTGDLG-FLDNGNLTITGR 429
|
410 420
....*....|....*....|.
gi 1860141834 924 EDLQVKIRGYRIELAEIEAAL 944
Cdd:cd05906 430 TKDTIIVNGVNYYSHEIEAAV 450
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
1367-1515 |
6.41e-21 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 101.01 E-value: 6.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 1367 DRVRISRDDLTEHLAGRLPQYMVPSVVQVVDALPLNANGKVDRavlrRRLPRRGTATAAGSSGALDSDLERRIAAVWAEA 1446
Cdd:PRK12467 2034 EAQVALRAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDR----KALPAPDASELQQAYVAPQSELEQRLAAIWQDV 2109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1860141834 1447 LRLPRVGRDENLFELGGDSLVAAQITGRileeiPQAAGLFFDQllRQVLEQPTVAALAGHVEAESATPV 1515
Cdd:PRK12467 2110 LGLEQVGLHDNFFELGGDSIISIQVVSR-----ARQAGIRFTP--KDLFQHQTVQSLAAVAQEGDGTVS 2171
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
1373-1521 |
1.41e-20 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 100.03 E-value: 1.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 1373 RDDLTEHLAGRLPQYMVPSVVQVVDALPLNANGKVDRavlrRRLPRRGTATAAGSSGALDSDLERRIAAVWAEALRLPRV 1452
Cdd:PRK12316 961 REALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDR----KALPAPEASVAQQGYVAPRNALERTLAAIWQDVLGVERV 1036
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1860141834 1453 GRDENLFELGGDSLVAAQITGRileeiPQAAGLFFDQllRQVLEQPTVAALAGHVEAESATPVTASPSV 1521
Cdd:PRK12316 1037 GLDDNFFELGGDSIVSIQVVSR-----ARQAGIQLSP--RDLFQHQTIRSLALVAKAGQATAADQGPAS 1098
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
554-948 |
2.59e-20 |
|
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: 96.05 E-value: 2.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 554 LDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVDTS--QPAARRRtiLTNAGIRCALT 631
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAfgPKAIEHR--LRTSGARLVVT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 632 QsgvdrngwAEGLRLLDVDLLgtgqpqpvegsgdpeelaYVIHTSGSTGSPKGVMINHRGAVNTVLDINDRFGVGPDDRV 711
Cdd:cd05973 79 D--------AANRHKLDSDPF------------------VMMFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPEDSF 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 712 LGLSNLGFDLSVY-DVFGPLSVGGAVVLPDPQRRGdPSHWaDLVGTHGVTVWNSVPAQLQMLHDYLVSATATVPDGLRLA 790
Cdd:cd05973 133 WNAADPGWAYGLYyAITGPLALGHPTILLEGGFSV-ESTW-RVIERLGVTNLAGSPTAYRLLMAAGAEVPARPKGRLRRV 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 791 MLSGDWIPVALPDQIRARVpGLRIVSLGGATE-----ASIWSIWYPIeqvdpewRSIPYGRPLTNQSFHVLDAALRPRPD 865
Cdd:cd05973 211 SSAGEPLTPEVIRWFDAAL-GVPIHDHYGQTElgmvlANHHALEHPV-------HAGSAGRAMPGWRVAVLDDDGDELGP 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 866 LVSGELYIGGVGLAV----GYLNDRERTAErfvvhpqtgERLYRTGDLGRYLPDGTIEFLGREDLQVKIRGYRIELAEIE 941
Cdd:cd05973 283 GEPGRLAIDIANSPLmwfrGYQLPDTPAID---------GGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVE 353
|
....*..
gi 1860141834 942 AALGGHP 948
Cdd:cd05973 354 SALIEHP 360
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
530-948 |
4.86e-20 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 96.11 E-value: 4.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 530 LHDRVVLQALSTPDRPA-VVAADRT-LDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVP 607
Cdd:PRK05852 18 IADLVEVAATRLPEAPAlVVTADRIaISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 608 VDTSQPAARRRTILTNAGIRCALtqsgVDRNG-----------WAEGLRL----------LDVDLLGTGQPQPVEGSgdP 666
Cdd:PRK05852 98 LDPALPIAEQRVRSQAAGARVVL----IDADGphdraepttrwWPLTVNVggdsgpsggtLSVHLDAATEPTPATST--P 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 667 EEL----AYVIHTSGSTGSPKGVMINHRGAVNTVLDINDRFGVGPDDRVLGLSNL--GFDLsVYDVFGPLSVGGAVVLPD 740
Cdd:PRK05852 172 EGLrpddAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLyhGHGL-IAALLATLASGGAVLLPA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 741 PQRRGDPSHWADLVGTHGvTVWNSVPAqlqmLHDYLVSATATVPDGLRLAML------SGDWIP-VALPDQIRARVPGLR 813
Cdd:PRK05852 251 RGRFSAHTFWDDIKAVGA-TWYTAVPT----IHQILLERAATEPSGRKPAALrfirscSAPLTAeTAQALQTEFAAPVVC 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 814 IVSLGGAT-EASIWSIWYPIEQVDPEWRSIPYGRPlTNQSFHVLDAALRPRPDLVSGELYIGGVGLAVGYLNDRERTAER 892
Cdd:PRK05852 326 AFGMTEAThQVTTTQIEGIGQTENPVVSTGLVGRS-TGAQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTITAAN 404
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1860141834 893 FVvhpqtgERLYRTGDLGRYLPDGTIEFLGREDLQVKIRGYRIELAEIEAALGGHP 948
Cdd:PRK05852 405 FT------DGWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHP 454
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
668-990 |
5.27e-20 |
|
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: 93.16 E-value: 5.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 668 ELAYVIHTSGSTGSPKGVMINHRGAVNTVLDINDRFGVGPDDRVLGLSNLGFDLSVYDVFGPLSVGGAVVLPDPQrrgdp 747
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLAILVRSLLAGAELVLLERN----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 748 shWADLVGTH--GVTVWNSVPAQLQMLHDYlvSATATVPDGLRLAMLSGDWIPVALPDQIRARvpGLRIVSLGGATE-AS 824
Cdd:cd17630 76 --QALAEDLAppGVTHVSLVPTQLQRLLDS--GQGPAALKSLRAVLLGGAPIPPELLERAADR--GIPLYTTYGMTEtAS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 825 IWSIWYPIEQVDPEwrsipYGRPLtnqsfhvLDAALRPRPDlvsGELYIGGVGLAVGYLNDRErtaerfvVHPQTGERLY 904
Cdd:cd17630 150 QVATKRPDGFGRGG-----VGVLL-------PGRELRIVED---GEIWVGGASLAMGYLRGQL-------VPEFNEDGWF 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 905 RTGDLGRYLPDGTIEFLGREDLQVKIRGYRIELAEIEAALGGHPAVAGAVVVVDGDTPLERRLAAFVEPAGRPVTAAQAE 984
Cdd:cd17630 208 TTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGPADPAELRA 287
|
....*.
gi 1860141834 985 HDQAAL 990
Cdd:cd17630 288 WLKDKL 293
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
544-948 |
8.31e-20 |
|
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.
Pssm-ID: 341268 [Multi-domain] Cd Length: 439 Bit Score: 94.47 E-value: 8.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 544 RPAVVAADRTLDYAELLGRAAGVAEALTAA-GCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVDTSQPAARRRTILT 622
Cdd:cd05958 1 RTCLRSPEREWTYRDLLALANRIANVLVGElGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 623 NAGIRCALTqsgVDRngwaeglrlldvdllgtgqpqpVEGSGDPEELAYvihTSGSTGSPKGVMINHRgavnTVLDINDR 702
Cdd:cd05958 81 KARITVALC---AHA----------------------LTASDDICILAF---TSGTTGAPKATMHFHR----DPLASADR 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 703 FGVG-----PDDRVLGLSNLGFDLSVYDV-FGPLSVGGAVVLPDpqrRGDPSHWADLVGTHGVTVWNSVPAqlqMLHDYL 776
Cdd:cd05958 129 YAVNvlrlrEDDRFVGSPPLAFTFGLGGVlLFPFGVGASGVLLE---EATPDLLLSAIARYKPTVLFTAPT---AYRAML 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 777 VSATATVPD--GLRLAMLSGDWIPVALPDQIRARVpGLRIVSLGGATEAsiWSIWypIEQVDPEWRSIPYGRPLTNQSFH 854
Cdd:cd05958 203 AHPDAAGPDlsSLRKCVSAGEALPAALHRAWKEAT-GIPIIDGIGSTEM--FHIF--ISARPGDARPGATGKPVPGYEAK 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 855 VLDAALRPRPDLVSGELYIGGvglAVGYLNDRERTAERFVvhpqTGERLYrTGDLGRYLPDGTIEFLGREDLQVKIRGYR 934
Cdd:cd05958 278 VVDDEGNPVPDGTIGRLAVRG---PTGCRYLADKRQRTYV----QGGWNI-TGDTYSRDPDGYFRHQGRSDDMIVSGGYN 349
|
410
....*....|....
gi 1860141834 935 IELAEIEAALGGHP 948
Cdd:cd05958 350 IAPPEVEDVLLQHP 363
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
530-995 |
9.38e-20 |
|
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: 95.21 E-value: 9.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 530 LHDRVVLQALSTPDRPAVVAADRTLDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCvyVPVd 609
Cdd:COG1021 27 LGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGA--IPV- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 610 TSQPAARRRTI-----LTNA-GIRCALTQSGVDRNGWAEGLR-----LLDVDLLGTGQP---------QPVEGSG---DP 666
Cdd:COG1021 104 FALPAHRRAEIshfaeQSEAvAYIIPDRHRGFDYRALARELQaevpsLRHVLVVGDAGEftsldallaAPADLSEprpDP 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 667 EELAYVIHTSGSTGSPKGVMINHRGAVNTVLDINDRFGVGPDDRVLGLSNLG--FDLSVYDVFGPLSVGGAVVL-PDPqr 743
Cdd:COG1021 184 DDVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEICGLDADTVYLAALPAAhnFPLSSPGVLGVLYAGGTVVLaPDP-- 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 744 rgDPSHWADLVGTHGVTVWNSVPAQLQMLHDYLVSATATVPDgLRLAMLSGdwipvA-LPDQIRARV-PGLrivslgGAT 821
Cdd:COG1021 262 --SPDTAFPLIERERVTVTALVPPLALLWLDAAERSRYDLSS-LRVLQVGG-----AkLSPELARRVrPAL------GCT 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 822 easiwsiwypIEQV--------------DPEWRSIPY-GRPLtnqS----FHVLDAALRPRPDLVSGELYIGGVGLAVGY 882
Cdd:COG1021 328 ----------LQQVfgmaeglvnytrldDPEEVILTTqGRPI---SpddeVRIVDEDGNPVPPGEVGELLTRGPYTIRGY 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 883 LNDRERTAERFvvhpqTGERLYRTGDLGRYLPDGTIEFLGREDLQVkIR-GYRIELAEIEAALGGHPAVAGAVVVVDGDT 961
Cdd:COG1021 395 YRAPEHNARAF-----TPDGFYRTGDLVRRTPDGYLVVEGRAKDQI-NRgGEKIAAEEVENLLLAHPAVHDAAVVAMPDE 468
|
490 500 510
....*....|....*....|....*....|....
gi 1860141834 962 PLERRLAAFVEPAGRPVTAAQAehdQAALRQLGV 995
Cdd:COG1021 469 YLGERSCAFVVPRGEPLTLAEL---RRFLRERGL 499
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
1373-1547 |
1.29e-19 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 96.56 E-value: 1.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 1373 RDDLTEHLAGRLPQYMVPSVVQVVDALPLNANGKVDRavlrRRLPRRGTATAAGSSGALDSDLERRIAAVWAEALRLPRV 1452
Cdd:PRK12316 2459 LAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDR----KALPKPDVSQLRQAYVAPQEGLEQRLAAIWQAVLKVEQV 2534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 1453 GRDENLFELGGDSLVAAQITGRileeIPQAAGLFFDqlLRQVLEQPTVAALAGHVEAESATpvTASPSVPATSGGDGLSP 1532
Cdd:PRK12316 2535 GLDDHFFELGGHSLLATQVVSR----VRQDLGLEVP--LRILFERPTLAAFAASLESGQTS--RAPVLQKVTRVQPLPLS 2606
|
170
....*....|....*
gi 1860141834 1533 LHEGTDGVPWVLVPG 1547
Cdd:PRK12316 2607 HAQQRQWFLWQLEPE 2621
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
542-948 |
2.20e-19 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 94.64 E-value: 2.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 542 PDRPAVVA---ADR-----TLDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVyVPV----- 608
Cdd:PRK07529 39 PDAPALSFlldADPldrpeTWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAGIA-NPInplle 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 609 ----------------------------DTSQPAARR----RTILTNAGIRcALTQSGVDRNGWAEG---LRLLDVDLLG 653
Cdd:PRK07529 118 peqiaellraagakvlvtlgpfpgtdiwQKVAEVLAAlpelRTVVEVDLAR-YLPGPKRLAVPLIRRkahARILDFDAEL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 654 TGQPQPVEGSGDP---EELAYVIHTSGSTGSPKGVMINHRGAVNTVLDINDRFGVGPDDRVLglsnlgFDLSVYDVFG-- 728
Cdd:PRK07529 197 ARQPGDRLFSGRPigpDDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDTVF------CGLPLFHVNAll 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 729 -----PLSVGGAVVLPDPQRRGDPSHWAD---LVGTHGVTVWNSVPAqlqmlhdyLVSATATVPDG------LRLAMLSG 794
Cdd:PRK07529 271 vtglaPLARGAHVVLATPQGYRGPGVIANfwkIVERYRINFLSGVPT--------VYAALLQVPVDghdissLRYALCGA 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 795 DWIPVALPDQIRARVpGLRIVSLGGATEASIWSIWYPIEQvdpEWRSIPYGRPLTNQSFHVL---DAALRPRPDLVS--G 869
Cdd:PRK07529 343 APLPVEVFRRFEAAT-GVRIVEGYGLTEATCVSSVNPPDG---ERRIGSVGLRLPYQRVRVVildDAGRYLRDCAVDevG 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 870 ELYIGGVGLAVGYLNDRERTAERFvvhpqtGERLYRTGDLGRYLPDGTIEFLGR-EDLqvKIR-GYRIELAEIEAALGGH 947
Cdd:PRK07529 419 VLCIAGPNVFSGYLEAAHNKGLWL------EDGWLNTGDLGRIDADGYFWLTGRaKDL--IIRgGHNIDPAAIEEALLRH 490
|
.
gi 1860141834 948 P 948
Cdd:PRK07529 491 P 491
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
536-948 |
3.27e-19 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 93.67 E-value: 3.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 536 LQALSTPDRPAVVAADRTLDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVDTSQPAA 615
Cdd:PRK06155 29 RQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGP 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 616 RRRTILTNAGIRCALTQS-----------------------GVDRNGWAEGLRLLDVDLLGTGQPQPVEGSGDPeelAYV 672
Cdd:PRK06155 109 QLEHILRNSGARLLVVEAallaaleaadpgdlplpavwlldAPASVSVPAGWSTAPLPPLDAPAPAAAVQPGDT---AAI 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 673 IHTSGSTGSPKGVMINHRG----AVNTVLDIndrfGVGPDDRVLGLSNLgFDLSVYDVFGPLSVGGAVVLPDPqrRGDPS 748
Cdd:PRK06155 186 LYTSGTTGPSKGVCCPHAQfywwGRNSAEDL----EIGADDVLYTTLPL-FHTNALNAFFQALLAGATYVLEP--RFSAS 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 749 HWADLVGTHGVTVWNSVPAQLQMlhdyLVSATATVPD---GLRLAMLSGdwIPVALPDQIRARVpGLRIVSLGGATEASi 825
Cdd:PRK06155 259 GFWPAVRRHGATVTYLLGAMVSI----LLSQPARESDrahRVRVALGPG--VPAALHAAFRERF-GVDLLDGYGSTETN- 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 826 wsiwYPIEQVDPEWRSIPYGRPLTNQSFHVLDAALRPRPDLVSGELYIGG---VGLAVGYLNDRERTAERFvvhpqtGER 902
Cdd:PRK06155 331 ----FVIAVTHGSQRPGSMGRLAPGFEARVVDEHDQELPDGEPGELLLRAdepFAFATGYFGMPEKTVEAW------RNL 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1860141834 903 LYRTGDLGRYLPDGTIEFLGREDLQVKIRGYRIELAEIEAALGGHP 948
Cdd:PRK06155 401 WFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHP 446
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
530-944 |
7.21e-19 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 93.84 E-value: 7.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 530 LHDRVVLQALSTPDRPAVvaAD---RTLDYAELLGRAAGVAEALtAAGCRRQELVAVVMDRGWEQVVAVLGALLAGcvYV 606
Cdd:PRK08633 617 LAEAWIDTAKRNWSRLAV--ADstgGELSYGKALTGALALARLL-KRELKDEENVGILLPPSVAGALANLALLLAG--KV 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 607 PVD---TSQPAARRRTILtNAGIRCALT---------QSGVDRNG-------WAEGL----------------RLLDVDL 651
Cdd:PRK08633 692 PVNlnyTASEAALKSAIE-QAQIKTVITsrkfleklkNKGFDLELpenvkviYLEDLkakiskvdkltallaaRLLPARL 770
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 652 LGTGQPQPVegsgDPEELAYVIHTSGSTGSPKGVMINHRGAVNTVLDINDRFGVGPDDRVLGlsNL----GFDLSVyDVF 727
Cdd:PRK08633 771 LKRLYGPTF----KPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILS--SLpffhSFGLTV-TLW 843
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 728 GPLSVG-GAVVLPDPQrrgDPSHWADLVGTHGVTVWNSVPAQLQMlhdYLVSATATVPD--GLRLAMLSGDWIPVALPDQ 804
Cdd:PRK08633 844 LPLLEGiKVVYHPDPT---DALGIAKLVAKHRATILLGTPTFLRL---YLRNKKLHPLMfaSLRLVVAGAEKLKPEVADA 917
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 805 IRARVpGLRIVSLGGATEAS-IWSIWYPIEQVDPEWRSI-----PYGRPLTNQSFHVLDA-ALRPRPDLVSGELYIGGVG 877
Cdd:PRK08633 918 FEEKF-GIRILEGYGATETSpVASVNLPDVLAADFKRQTgskegSVGMPLPGVAVRIVDPeTFEELPPGEDGLILIGGPQ 996
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1860141834 878 LAVGYLNDRERTAErfVVHPQTGERLYRTGDLGRYLPDGTIEFLGREDLQVKIRGYRIELAEIEAAL 944
Cdd:PRK08633 997 VMKGYLGDPEKTAE--VIKDIDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEEL 1061
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
675-948 |
2.25e-18 |
|
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: 88.87 E-value: 2.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 675 TSGSTGSPKGVMINHRGAVNTVLDINDRFGVGPDDRV---------LGLsnlgfdlsVYDVFGPLSVGGAVVLPDPQRrg 745
Cdd:cd05917 10 TSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLcipvplfhcFGS--------VLGVLACLTHGATMVFPSPSF-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 746 DPSHWADLVGTHGVTVWNSVP----AQLQmLHDYlvsaTATVPDGLRLAMLSGDWIPVALPDQIRARVPGLRIVSLGGAT 821
Cdd:cd05917 80 DPLAVLEAIEKEKCTALHGVPtmfiAELE-HPDF----DKFDLSSLRTGIMAGAPCPPELMKRVIEVMNMKDVTIAYGMT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 822 EASiwsiwyPI----EQVDP-EWRSIPYGRPLTNQSFHVLDAALRPRPDL-VSGELYIGGVGLAVGYLNDRERTAERFvv 895
Cdd:cd05917 155 ETS------PVstqtRTDDSiEKRVNTVGRIMPHTEAKIVDPEGGIVPPVgVPGELCIRGYSVMKGYWNDPEKTAEAI-- 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1860141834 896 hpqTGERLYRTGDLGRYLPDGTIEFLGR-EDLqvKIRG-YRIELAEIEAALGGHP 948
Cdd:cd05917 227 ---DGDGWLHTGDLAVMDEDGYCRIVGRiKDM--IIRGgENIYPREIEEFLHTHP 276
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
1373-1516 |
2.60e-18 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 92.54 E-value: 2.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 1373 RDDLTEHLAGRLPQYMVPSVVQVVDALPLNANGKVDRavlrRRLPRRGTATAAGSS-GALDSDLERRIAAVWAEALRLPR 1451
Cdd:PRK05691 4183 LERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDR----KALPALDIGQLQSQAyLAPRNELEQTLATIWADVLKVER 4258
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1860141834 1452 VGRDENLFELGGDSLVAAQITGRIleeipQAAgLFFDQLLRQVLEQPTVAALAGHVEAESATPVT 1516
Cdd:PRK05691 4259 VGVHDNFFELGGHSLLATQIASRV-----QKA-LQRNVPLRAMFECSTVEELAEYIEGLAGSAID 4317
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
1373-1512 |
3.70e-18 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 91.77 E-value: 3.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 1373 RDDLTEHLAGRLPQYMVPSVVQVVDALPLNANGKVDRavlrRRLPRRGTATAAGSSGALDSDLERRIAAVWAEALRLPRV 1452
Cdd:PRK05691 2652 REALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDR----RALPAPDPELNRQAYQAPRSELEQQLAQIWREVLNVERV 2727
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1860141834 1453 GRDENLFELGGDSLVAAQITGRileeiPQAAGLFF---DQLLRQVLEqpTVAALAGHVEAESA 1512
Cdd:PRK05691 2728 GLGDNFFELGGDSILSIQVVSR-----ARQLGIHFsprDLFQHQTVQ--TLAAVATHSEAAQA 2783
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
666-948 |
5.08e-18 |
|
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: 87.92 E-value: 5.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 666 PEELAYVIHTSGSTGSPKGVMINHRGAVNT--VLDINDRFGVGpddrvlglSNLGFDLSVYDVFG-------PLSVGGAV 736
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNawMLALNSLFDPD--------DVLLCGLPLFHVNGsvvtlltPLASGAHV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 737 VLPDPQRRGDPSHWAD---LVGTHGVTVWNSVPAQLqmlhdylvSATATVPDG-----LRLAMLSGDWIPVALPDQIRAR 808
Cdd:cd05944 73 VLAGPAGYRNPGLFDNfwkLVERYRITSLSTVPTVY--------AALLQVPVNadissLRFAMSGAAPLPVELRARFEDA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 809 VpGLRIVSLGGATEAS-IWSIWYPIEQVDPEWRSIPYgrPLTNQSFHVLDAA----LRPRPDLVsGELYIGGVGLAVGYL 883
Cdd:cd05944 145 T-GLPVVEGYGLTEATcLVAVNPPDGPKRPGSVGLRL--PYARVRIKVLDGVgrllRDCAPDEV-GEICVAGPGVFGGYL 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1860141834 884 NDrERTAERFVvhpqtGERLYRTGDLGRYLPDGTIEFLGR-EDLQVKiRGYRIELAEIEAALGGHP 948
Cdd:cd05944 221 YT-EGNKNAFV-----ADGWLNTGDLGRLDADGYLFITGRaKDLIIR-GGHNIDPALIEEALLRHP 279
|
|
| DCL_NRPS-like |
cd19536 |
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ... |
75-496 |
5.24e-18 |
|
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: 88.66 E-value: 5.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 75 FPVTDVQAAYLLgRGETFAYGGVACHGYGELVYPELDPERMTAAWRALIARHDMLRAVVEADGAQRVLAEV-PPFEVPVI 153
Cdd:cd19536 2 YPLSSLQEGMLF-HSLLNPGGSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFIEDGLGQPVQVVhRQAQVPVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 154 DLTGRPEAVVDAAVSAVRAEMDHLVHTPDRWPLFAARITRADHRT--VLHVSIDFLIADFISVQVVLDELHRLY-----H 226
Cdd:cd19536 81 ELDLTPLEEQLDPLRAYKEETKIRRFDLGRAPLVRAALVRKDERErfLLVISDHHSILDGWSLYLLVKEILAVYnqlleY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 227 RPDEPLPPLEitFRDYQLAERAVRDSPRHERDKQWWLARVDELPAAPELPTVARPAdsegrFRRWETRLSSQVWEGLRQR 306
Cdd:cd19536 161 KPLSLPPAQP--YRDFVAHERASIQQAASERYWREYLAGATLATLPALSEAVGGGP-----EQDSELLVSVPLPVRSRSL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 307 AGRHGVSPSGAVLAAFSDTIAAYSRRSRFTLDITLLNRAPVHDQVNALVGDFTSVDLLAVDAdPTRRFDERARDLQAQLW 386
Cdd:cd19536 234 AKRSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEETTGAERLLGLFLNTLPLRVTL-SEETVEDLLKRAQEQEL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 387 EDLDHRsfsgiEVMREIARRQGAEAALFPVVFTSAIGITSAGAAADGAPLGELGYGI-SQTPQVWIDCQNIERDGG-LVS 464
Cdd:cd19536 313 ESLSHE-----QVPLADIQRCSEGEPLFDSIVNFRHFDLDFGLPEWGSDEGMRRGLLfSEFKSNYDVNLSVLPKQDrLEL 387
|
410 420 430
....*....|....*....|....*....|..
gi 1860141834 465 NWDVREEVFPPGVVDDMFAAYDAVLHRLAGDD 496
Cdd:cd19536 388 KLAYNSQVLDEEQAQRLAAYYKSAIAELATAP 419
|
|
| SgcC5_NRPS-like |
cd19539 |
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ... |
90-495 |
8.91e-18 |
|
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: 88.21 E-value: 8.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 90 ETFAYGGVACHGYGELVYPE-LDPERMTAAWRALIARHDMLRAVVEADGAQRVLAEVPPFEVPVIDLT--GRPEAVVDAA 166
Cdd:cd19539 15 DQGEDGGPAYNIPGAWRLTGpLDVEALREALRDVVARHEALRTLLVRDDGGVPRQEILPPGPAPLEVRdlSDPDSDRERR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 167 VSAVRAEMDHLVHTPDRWPLFAARITRAD-HRTVLHVSIDFLIADFISVQVVLDELHRLYHR----PDEPLPPLEITFRD 241
Cdd:cd19539 95 LEELLRERESRGFDLDEEPPIRAVLGRFDpDDHVLVLVAHHTAFDAWSLDVFARDLAALYAArrkgPAAPLPELRQQYKE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 242 YQLAERAVRDSPRHERDKQWWLARVDELpAAPELPTvARPADSEGRFRRWETR--LSSQVWEGLRQRAGRHGVSPSGAVL 319
Cdd:cd19539 175 YAAWQREALAAPRAAELLDFWRRRLRGA-EPTALPT-DRPRPAGFPYPGADLRfeLDAELVAALRELAKRARSSLFMVLL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 320 AAFSDTIAAYSRRSRFTLDITLLNRApvHDQVNALVGDFTSVDLLAVDADPTRRFDERARDLQAQLWEDLDHRSFSGIEV 399
Cdd:cd19539 253 AAYCVLLRRYTGQTDIVVGTPVAGRN--HPRFESTVGFFVNLLPLRVDVSDCATFRDLIARVRKALVDAQRHQELPFQQL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 400 MREI-ARRQGAEAALFPVVFTSAIGITSAGAAADGAPLGElGYGISQTPQVWIDCQNIERDGGLVSNWDVREEVFPPGVV 478
Cdd:cd19539 331 VAELpVDRDAGRHPLVQIVFQVTNAPAGELELAGGLSYTE-GSDIPDGAKFDLNLTVTEEGTGLRGSLGYATSLFDEETI 409
|
410
....*....|....*..
gi 1860141834 479 DDMFAAYDAVLHRLAGD 495
Cdd:cd19539 410 QGFLADYLQVLRQLLAN 426
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
671-948 |
1.20e-17 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 86.67 E-value: 1.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 671 YVIHTSGSTGSPKGVMINH--------------RGAVNTVLDINDRFGVGPDDRVLGLSNLGFDLSVYDVFGPLSVGGAV 736
Cdd:cd05924 7 YILYTGGTTGMPKGVMWRQedifrmlmggadfgTGEFTPSEDAHKAAAAAAGTVMFPAPPLMHGTGSWTAFGGLLGGQTV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 737 VLPDPqrRGDPSHWADLVGTHGVTVWNSV-PAQLQMLHDYLVSATATVPDGLRLAMLSGDWIPVALPDQIRARVPGLRIV 815
Cdd:cd05924 87 VLPDD--RFDPEEVWRTIEKHKVTSMTIVgDAMARPLIDALRDAGPYDLSSLFAISSGGALLSPEVKQGLLELVPNITLV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 816 SLGGATEASIWSIWYPIEQvDPEWRSIPYGRPLTNqsfhVLDAALRPRPDLVSGELYIGGVGL-AVGYLNDRERTAERFV 894
Cdd:cd05924 165 DAFGSSETGFTGSGHSAGS-GPETGPFTRANPDTV----VLDDDGRVVPPGSGGVGWIARRGHiPLGYYGDEAKTAETFP 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1860141834 895 VhpQTGERLYRTGDLGRYLPDGTIEFLGREDLQVKIRGYRIELAEIEAALGGHP 948
Cdd:cd05924 240 E--VDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHP 291
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
671-948 |
1.55e-17 |
|
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: 85.53 E-value: 1.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 671 YVIHTSGSTGSPKGVMINHRGAVNTVLDINDRFGVGPDDRVLGLSNLGFDLSVYDVFGPLSVGGAVVLpdpQRRGDPSHW 750
Cdd:cd17633 4 YIGFTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLFLYGAISALYLGGTFIG---QRKFNPKSW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 751 ADLVGTHGVTVWNSVPAQLQML--HDYLVSATATVpdglrlaMLSGDWIPVALPDQIRARVPGLRIVSLGGATEASIWSI 828
Cdd:cd17633 81 IRKINQYNATVIYLVPTMLQALarTLEPESKIKSI-------FSSGQKLFESTKKKLKNIFPKANLIEFYGTSELSFITY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 829 WYPIEQVDPEwrSIpyGRPltnqsFHVLDAALRPRPDLVSGELYIGGVGLAVGYLNDRERTAERFvvhpqtgerlYRTGD 908
Cdd:cd17633 154 NFNQESRPPN--SV--GRP-----FPNVEIEIRNADGGEIGKIFVKSEMVFSGYVRGGFSNPDGW----------MSVGD 214
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1860141834 909 LGRYLPDGTIEFLGREDLQVKIRGYRIELAEIEAALGGHP 948
Cdd:cd17633 215 IGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIP 254
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
537-948 |
1.92e-17 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 87.76 E-value: 1.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 537 QALSTPDRPAVVAAD--RTLDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVDTSQPA 614
Cdd:PRK13390 6 HAQIAPDRPAVIVAEtgEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 615 ARRRTILTNAGIRCALTQSGVDR---------------NGWAEGLRLLDVDLLGTGQPQPVEGSGdpeelAYVIHTSGST 679
Cdd:PRK13390 86 PEADYIVGDSGARVLVASAALDGlaakvgadlplrlsfGGEIDGFGSFEAALAGAGPRLTEQPCG-----AVMLYSSGTT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 680 GSPKGVMInhrgavntvlDINDRFGVGPDDRVLGLSNLGFDLSVYDVFGPLSvggavvlpdPQRRGDPSHWADLVGTHGV 759
Cdd:PRK13390 161 GFPKGIQP----------DLPGRDVDAPGDPIVAIARAFYDISESDIYYSSA---------PIYHAAPLRWCSMVHALGG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 760 TVWNS----VPAQLQMLHDYLVSATATVPDgLRLAMLSgdwipvaLPDQIRAR--VPGLRIVSLGGA------TEASI-- 825
Cdd:PRK13390 222 TVVLAkrfdAQATLGHVERYRITVTQMVPT-MFVRLLK-------LDADVRTRydVSSLRAVIHAAApcpvdvKHAMIdw 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 826 -----WSIWYPIEQ-----VD-PEWRSIP--YGRPLTNqSFHVLDAALRPRPDLVSGELYIGGVGLAVGYLNDRERTAEr 892
Cdd:PRK13390 294 lgpivYEYYSSTEAhgmtfIDsPDWLAHPgsVGRSVLG-DLHICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAA- 371
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1860141834 893 fVVHPqtGERLYRT-GDLGRYLPDGTIEFLGREDLQVKIRGYRIELAEIEAALGGHP 948
Cdd:PRK13390 372 -AQHP--AHPFWTTvGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHP 425
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
537-948 |
1.95e-17 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 87.61 E-value: 1.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 537 QALSTPDRPAVVAADRTLDYAELLGRAAGVAEAL-TAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVDTSQPAA 615
Cdd:PRK06839 11 RAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLiYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTEN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 616 RRRTILTNAGIRCALTQ-------------SGVDRNGWAEGLR-LLDVDLLGTgqpqpVEGSGDPEELayVIHTSGSTGS 681
Cdd:PRK06839 91 ELIFQLKDSGTTVLFVEktfqnmalsmqkvSYVQRVISITSLKeIEDRKIDNF-----VEKNESASFI--ICYTSGTTGK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 682 PKGVMINHRG----AVNTVLDINDRfgvgPDDRVLGLSNLgFDLSVYDVFG--PLSVGGAVVLPDpqrRGDPSHWADLVG 755
Cdd:PRK06839 164 PKGAVLTQENmfwnALNNTFAIDLT----MHDRSIVLLPL-FHIGGIGLFAfpTLFAGGVIIVPR---KFEPTKALSMIE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 756 THGVTVWNSVPAQLQMLHDYLVSATATVpDGLRLAMLSGDWIPVALPDQIRARvpGLRIVSLGGATEASiwSIWYPIEQV 835
Cdd:PRK06839 236 KHKVTVVMGVPTIHQALINCSKFETTNL-QSVRWFYNGGAPCPEELMREFIDR--GFLFGQGFGMTETS--PTVFMLSEE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 836 DPEWRSIPYGRPLTNQSFHVLDAALRPRPDLVSGELYIGGVGLAVGYLNDRERTAERFvvhpQTGerLYRTGDLGRYLPD 915
Cdd:PRK06839 311 DARRKVGSIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETI----QDG--WLCTGDLARVDED 384
|
410 420 430
....*....|....*....|....*....|...
gi 1860141834 916 GTIEFLGREDLQVKIRGYRIELAEIEAALGGHP 948
Cdd:PRK06839 385 GFVYIVGRKKEMIISGGENIYPLEVEQVINKLS 417
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
542-948 |
2.22e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 87.88 E-value: 2.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 542 PDRPAVVAADRTLDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVDTSQPAARRRTIL 621
Cdd:PRK06164 24 PDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHIL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 622 TNAGIRCALTQSG--------------------------VDRNGWA--EGLRLLDVDLLGTGQPQPVEGSG----DPEEL 669
Cdd:PRK06164 104 GRGRARWLVVWPGfkgidfaailaavppdalpplraiavVDDAADAtpAPAPGARVQLFALPDPAPPAAAGeraaDPDAG 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 670 AYVIHTSGSTGSPKGVMINHRGAVNTVLDINDRFGVGPDDRVLGLSNLGFDLSVYDVFGPLSVGGAVVLPDPQrrgDPSH 749
Cdd:PRK06164 184 ALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGFSTLLGALAGGAPLVCEPVF---DAAR 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 750 WADLVGTHGVT-VWNSVPAQLQMLHDYLVSATATVPDGLRLAMLSGDWIPVALpdqiRARVPGLRIVSLGGATEA-SIWS 827
Cdd:PRK06164 261 TARALRRHRVThTFGNDEMLRRILDTAGERADFPSARLFGFASFAPALGELAA----LARARGVPLTGLYGSSEVqALVA 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 828 IWypieQVDPEW--RSIPYGRPLTNQS----FHVLDAALRPrpDLVSGELYIGGVGLAVGYLNDRERTAERFvvhpqTGE 901
Cdd:PRK06164 337 LQ----PATDPVsvRIEGGGRPASPEArvraRDPQDGALLP--DGESGEIEIRAPSLMRGYLDNPDATARAL-----TDD 405
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1860141834 902 RLYRTGDLGRYLPDGTIEFLGREDLQVKIRGYRIELAEIEAALGGHP 948
Cdd:PRK06164 406 GYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALP 452
|
|
| ArgR-Cyc_NRPS-like |
cd20480 |
Cyc (heterocyclization)-like domain of Vibrio anguillarum AngR and similar proteins; belongs ... |
102-496 |
5.95e-17 |
|
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: 85.25 E-value: 5.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 102 YGELVYPELDPERMTAAWRALIARHDMLRAVVEADGAQRVLAEVPPFEVPVIDLTGRPEAVVDAAVSAVRAEmdhLVHTP 181
Cdd:cd20480 29 YQEFDYENISVDTLERCLTVLINHHPMLHALLSDDFYLHINSKNQIDAFAVNDLSSASEQEAAEQLARTRAT---LTKSR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 182 DRWP------LFAARITRadhrtvLHVSIDFLIADFISVQVVLDELHRLYHRPDEPLPPLEITFRDYQLAERAVRDSPrh 255
Cdd:cd20480 106 SKATisvvlsLLPANKIR------LHVRFNSVVVDHPSVNLFFEQLCQLLRGSLLSFLAQEQVILAHNQLVISELQST-- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 256 ERDKQWWLARVDELPAAPELPTVARPAD-SEGRFRRWETRLSSQVWEGLRQRAGRHGVSPSGAVLAAFSDTIAAYSRRSR 334
Cdd:cd20480 178 GLSSAFWNEQILQLPSSANLPTVCEPEKlRETGITRRTLTLSSDKWQQLVTISKQHNVTPELTLASIFSAVLSLWGNQKD 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 335 FTL--DITLLNRapvhdqVNALVGDFTSvDLLAVDADPTRRFDERARDLQAQLWEDLDHRSFSGIEVMREIARRQGAEAA 412
Cdd:cd20480 258 MMLrfDLNKKND------VAGVIGQFTQ-PLLVGLSGFGQSFLSLVKENQKHFEQAYPFRQIPIFDLVRQLAKLSESHRY 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 413 LFPVVFTSAIGITSAgaaadgapLGELGYGISQTPQVWIDCQNIERDGGLVSNWDVREEVFPPGVVDDMFAAYDAVLHRL 492
Cdd:cd20480 331 PANIAFSSQLSGNNT--------LGRSGWGCRQSANTWLSLHAFISQGGLILQWDSQDALFPKDMIQDMLTSYSKLLESL 402
|
....
gi 1860141834 493 AGDD 496
Cdd:cd20480 403 SQSD 406
|
|
| TubC_N |
pfam18563 |
TubC N-terminal docking domain; This is the N-terminal docking domain found in TubC proteins ... |
8-55 |
8.34e-17 |
|
TubC N-terminal docking domain; This is the N-terminal docking domain found in TubC proteins from the tubulysin polyketide synthase and nonribosomal polypeptide synthetase (PKS-NRPS) system, which binds to C-terminal docking domain of TubB.
Pssm-ID: 436580 [Multi-domain] Cd Length: 52 Bit Score: 75.63 E-value: 8.34e-17
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1860141834 8 DLLAELESVGVRVWLEAGQLRFRAPQGAMTPDRREALRARRDEIVAHL 55
Cdd:pfam18563 3 ELLAELYALGIKLWLEGGRLRFRAPKGVLTPELREKLKERKAEIIAFL 50
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
534-948 |
9.37e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 85.24 E-value: 9.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 534 VVLQALSTPDRPAVV--AADRTLDYAEL---LGRAAGVaeaLTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPV 608
Cdd:PRK09088 1 IAFHARLQPQRLAAVdlALGRRWTYAELdalVGRLAAV---LRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 609 DTSQPAARRRTILTNAGIRCALTQSGVdrngwaEGLRLLDVDLLGTGQPQPVEG-----SGDPEELAYVIHTSGSTGSPK 683
Cdd:PRK09088 78 NWRLSASELDALLQDAEPRLLLGDDAV------AAGRTDVEDLAAFIASADALEpadtpSIPPERVSLILFTSGTSGQPK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 684 GVMINHRGAVNTVLDindrFGVgpDDRVLGLSNLGFDLSVYDVFG-------PLSVGGAVVLPD---PQRR----GDPSH 749
Cdd:PRK09088 152 GVMLSERNLQQTAHN----FGV--LGRVDAHSSFLCDAPMFHIIGlitsvrpVLAVGGSILVSNgfePKRTlgrlGDPAL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 750 wadlvgthGVTVWNSVPAQLQMLHDYLVSATATVPdglRLAMLSGDWIPVALPDQIRARVPGLRIVSLGGATEASIwSIW 829
Cdd:PRK09088 226 --------GITHYFCVPQMAQAFRAQPGFDAAALR---HLTALFTGGAPHAAEDILGWLDDGIPMVDGFGMSEAGT-VFG 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 830 YPIEQVDPEWRSIPYGRPLTNQSFHVLDAALRPRPDLVSGELYIGGVGLAVGYLNDRERTAERFvvhpqTGERLYRTGDL 909
Cdd:PRK09088 294 MSVDCDVIRAKAGAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAF-----TGDGWFRTGDI 368
|
410 420 430
....*....|....*....|....*....|....*....
gi 1860141834 910 GRYLPDGTIEFLGREDLQVKIRGYRIELAEIEAALGGHP 948
Cdd:PRK09088 369 ARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHP 407
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
553-948 |
1.00e-16 |
|
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: 84.71 E-value: 1.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 553 TLDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVDTSqpaarrrtiltnagircaLTq 632
Cdd:cd05912 1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTR------------------LT- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 633 sgvdRNGWAEGLRLLDVDLlgtgqpqpvegsgdpEELAYVIHTSGSTGSPKGVMI---NH-RGAVNTVLDIndrfGVGPD 708
Cdd:cd05912 62 ----PNELAFQLKDSDVKL---------------DDIATIMYTSGTTGKPKGVQQtfgNHwWSAIGSALNL----GLTED 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 709 DRVL---------GLSNL------GFDLSVYDVFgplsvggavvlpdpqrrgDPSHWADLVGTHGVTVWNSVPAQLQMLH 773
Cdd:cd05912 119 DNWLcalplfhisGLSILmrsviyGMTVYLVDKF------------------DAEQVLHLINSGKVTIISVVPTMLQRLL 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 774 DYLvsaTATVPDGLRLAMLSGDWIPVALPDQIRARvpGLRIVSLGGATEASIWSIWYPIEqvDPEWRSIPYGRPLTNQSF 853
Cdd:cd05912 181 EIL---GEGYPNNLRCILLGGGPAPKPLLEQCKEK--GIPVYQSYGMTETCSQIVTLSPE--DALNKIGSAGKPLFPVEL 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 854 HVLDAALRPRPDlvsGELYIGGVGLAVGYLNDRERTAERFvvhpQTGerLYRTGDLGrYL-PDGTIEFLGR-EDLQVKiR 931
Cdd:cd05912 254 KIEDDGQPPYEV---GEILLKGPNVTKGYLNRPDATEESF----ENG--WFKTGDIG-YLdEEGFLYVLDRrSDLIIS-G 322
|
410
....*....|....*..
gi 1860141834 932 GYRIELAEIEAALGGHP 948
Cdd:cd05912 323 GENIYPAEIEEVLLSHP 339
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
1368-1508 |
1.61e-16 |
|
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: 86.27 E-value: 1.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 1368 RVRISRDDLTEHLAGRLPQYMVPSVVQVVDALPLNANGKVDRAvlrrRLPRRGTA--TAAGSSGALDSDL------ERRI 1439
Cdd:TIGR03443 778 KYRKLIKDIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKP----ALPFPDTAqlAAVAKNRSASAADeeftetEREI 853
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1860141834 1440 AAVWAEAL--RLPRVGRDENLFELGGDSLVAAQItgrILE-------EIPqaAGLFFDqllrqvleQPTVAALAGHVE 1508
Cdd:TIGR03443 854 RDLWLELLpnRPATISPDDSFFDLGGHSILATRM---IFElrkklnvELP--LGLIFK--------SPTIKGFAKEVD 918
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
536-948 |
1.93e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 84.73 E-value: 1.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 536 LQALSTPDRPAVVAADRTLDYAELLGRAAGVAEALTAAGCR-RQELVAVVMDRGWEQVVAVLGALLAGCVYVPV-DTSQP 613
Cdd:PRK07867 11 LLPLAEDDDRGLYFEDSFTSWREHIRGSAARAAALRARLDPtRPPHVGVLLDNTPEFSLLLGAAALSGIVPVGLnPTRRG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 614 AARRRTILtNAGIRCALTQSG--VDRNGWAEGLRLLDVD-------LLGTGQPQPVEGSGDPEELAYVIHTSGSTGSPKG 684
Cdd:PRK07867 91 AALARDIA-HADCQLVLTESAhaELLDGLDPGVRVINVDspawadeLAAHRDAEPPFRVADPDDLFMLIFTSGTSGDPKA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 685 VMINHRGAVNTVLDINDRFGVGPDDrVLGLSNLGF-------DLSVydvfgPLSVGGAVVLPdpqRRGDPSHWADLVGTH 757
Cdd:PRK07867 170 VRCTHRKVASAGVMLAQRFGLGPDD-VCYVSMPLFhsnavmaGWAV-----ALAAGASIALR---RKFSASGFLPDVRRY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 758 GVTVWNSVPAQLQmlhdYLVsATATVPDG----LRLAMlSGDWIPVALpDQIRARVpGLRIVSLGGATEASIWSIWYP-- 831
Cdd:PRK07867 241 GATYANYVGKPLS----YVL-ATPERPDDadnpLRIVY-GNEGAPGDI-ARFARRF-GCVVVDGFGSTEGGVAITRTPdt 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 832 -----------IEQVDPEWRS-IPYGrpltnqsfhVLDAALRPRPDLVSGELY-IGGVGLAVGYLNDRERTAERFVvhpq 898
Cdd:PRK07867 313 ppgalgplppgVAIVDPDTGTeCPPA---------EDADGRLLNADEAIGELVnTAGPGGFEGYYNDPEADAERMR---- 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1860141834 899 tgERLYRTGDLGRYLPDGTIEFLGREDLQVKIRGYRIELAEIEAALGGHP 948
Cdd:PRK07867 380 --GGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYP 427
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
531-948 |
2.18e-16 |
|
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: 84.47 E-value: 2.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 531 HDRVVLQALSTPDRPAVVAAD-----RTLDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVY 605
Cdd:cd05970 20 YDVVDAMAKEYPDKLALVWCDdageeRIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 606 VPVdTSQPAARR----------RTILTNAG------IRCALTQSGV----------DRNGWaEGLRLLDVDLLGTGQPQP 659
Cdd:cd05970 100 IPA-THQLTAKDivyriesadiKMIVAIAEdnipeeIEKAAPECPSkpklvwvgdpVPEGW-IDFRKLIKNASPDFERPT 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 660 VEGSGDPEELAYVIHTSGSTGSPKGVMINHRGAVNTVLDINDRFGVGPDDRVLGLSNLGFDLSVY-DVFGPLSVGGAVVL 738
Cdd:cd05970 178 ANSYPCGEDILLVYFSSGTTGMPKMVEHDFTYPLGHIVTAKYWQNVREGGLHLTVADTGWGKAVWgKIYGQWIAGAAVFV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 739 PDpQRRGDPSHWADLVGTHGVTVWNSVPAqlqmLHDYLVSATATVPD--GLRLAMLSGDWIPVALPDQIRARVpGLRIVS 816
Cdd:cd05970 258 YD-YDKFDPKALLEKLSKYGVTTFCAPPT----IYRFLIREDLSRYDlsSLRYCTTAGEALNPEVFNTFKEKT-GIKLME 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 817 LGGATEASIWSIWYPIEQVDPEwrSIpyGRPLTNQSFHVLDAALRPRPDLVSGELYIG-----GVGLAVGYLNDRERTAE 891
Cdd:cd05970 332 GFGQTETTLTIATFPWMEPKPG--SM--GKPAPGYEIDLIDREGRSCEAGEEGEIVIRtskgkPVGLFGGYYKDAEKTAE 407
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1860141834 892 rfVVHpqtgERLYRTGDLGRYLPDGTIEFLGREDLQVKIRGYRIELAEIEAALGGHP 948
Cdd:cd05970 408 --VWH----DGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHP 458
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
542-948 |
2.93e-16 |
|
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: 83.89 E-value: 2.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 542 PDRPAVVAADRTLDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVDTSQPAARRRTIL 621
Cdd:cd12118 18 PDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFIL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 622 TNAGIRCALtqsgVDRNGWAEglrlldvDLLGTGQP----QPVEGSGDPEELAYvihTSGSTGSPKGVMINHRGA-VNTV 696
Cdd:cd12118 98 RHSEAKVLF----VDREFEYE-------DLLAEGDPdfewIPPADEWDPIALNY---TSGTTGRPKGVVYHHRGAyLNAL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 697 LDINdRFGVGPDdrvlglsnlgfdlSVY----DVF---------GPLSVGGAVVLpdpQRRGDPSHWADLVGTHGVTVWN 763
Cdd:cd12118 164 ANIL-EWEMKQH-------------PVYlwtlPMFhcngwcfpwTVAAVGGTNVC---LRKVDAKAIYDLIEKHKVTHFC 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 764 SVPAQLQMLHDYLVSATATVPDGLRlAMLSGDWIPVALPDQIRARvpGLRIVSLGGATEAS------IWSiwypieqvdP 837
Cdd:cd12118 227 GAPTVLNMLANAPPSDARPLPHRVH-VMTAGAPPPAAVLAKMEEL--GFDVTHVYGLTETYgpatvcAWK---------P 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 838 EWRSIPYG-----------RPLTNQSFHVLDAALR---PRPDLVSGELYIGGVGLAVGYLNDRERTAERFvvhpQTGerL 903
Cdd:cd12118 295 EWDELPTEerarlkarqgvRYVGLEEVDVLDPETMkpvPRDGKTIGEIVFRGNIVMKGYLKNPEATAEAF----RGG--W 368
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1860141834 904 YRTGDLGRYLPDGTIEFLGREDLQVKIRGYRIELAEIEAALGGHP 948
Cdd:cd12118 369 FHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHP 413
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
532-923 |
3.62e-16 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 83.79 E-value: 3.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 532 DRVVLQALSTPDRPAVVAAD----------RTLDYAELLGRAAGVAEALTAAGCRRQeLVAVVMDRGWEQVVAVLGALL- 600
Cdd:PRK09274 10 RHLPRAAQERPDQLAVAVPGgrgadgklayDELSFAELDARSDAIAHGLNAAGIGRG-MRAVLMVTPSLEFFALTFALFk 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 601 AGCVYVPVD-------------TSQPAA----------RRRTILTNAGIRCALTqsgVDRNGWAEGLRLLDVDLLGTGQP 657
Cdd:PRK09274 89 AGAVPVLVDpgmgiknlkqclaEAQPDAfigipkahlaRRLFGWGKPSVRRLVT---VGGRLLWGGTTLATLLRDGAAAP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 658 QPVEGSgDPEELAYVIHTSGSTGSPKGVMINHRGAVNTVLDINDRFGVGPDDRvlglsnlgfDLSVYDVFG--PLSVGGA 735
Cdd:PRK09274 166 FPMADL-APDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEI---------DLPTFPLFAlfGPALGMT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 736 VVLP--DPQRRG--DPSHWADLVGTHGVTVWNSVPAQLQMLHDYLVSATATVPdGLRLAMLSGDWIPVALPDQIRARVP- 810
Cdd:PRK09274 236 SVIPdmDPTRPAtvDPAKLFAAIERYGVTNLFGSPALLERLGRYGEANGIKLP-SLRRVISAGAPVPIAVIERFRAMLPp 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 811 GLRIVSLGGATEA----SI---------WSIW---------YPIEQVdpEWRSIpygrPLTNQSFHVLDAALRPRPDLVs 868
Cdd:PRK09274 315 DAEILTPYGATEAlpisSIesreilfatRAATdngagicvgRPVDGV--EVRII----AISDAPIPEWDDALRLATGEI- 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1860141834 869 GELYIGGVGLAVGYLNDRERTAERFVVHPQTGERlYRTGDLGRYLPDGTIEFLGR 923
Cdd:PRK09274 388 GEIVVAGPMVTRSYYNRPEATRLAKIPDGQGDVW-HRMGDLGYLDAQGRLWFCGR 441
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
552-948 |
5.11e-16 |
|
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: 82.89 E-value: 5.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 552 RTLDYAELLGRAAGVAEALTAAGCRRQeLVAVVMDRGWEQVVAVLGALL-AGCVYVPVDtsqPAARRRTIltnagIRCal 630
Cdd:cd05910 1 SRLSFRELDERSDRIAQGLTAYGIRRG-MRAVLMVPPGPDFFALTFALFkAGAVPVLID---PGMGRKNL-----KQC-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 631 tqsgvdrngwaeglrlldvdlLGTGQPQPVEGSGDPEELAYVIHTSGSTGSPKGVMINHRGAVNTVLDINDRFGVGPDDR 710
Cdd:cd05910 70 ---------------------LQEAEPDAFIGIPKADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEV 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 711 VLGlsnlGFDLsvYDVFGPLsVGGAVVLP--DPQR--RGDPSHWADLVGTHGVTVWNSVPAQLQMLHDYLVSATATVPDg 786
Cdd:cd05910 129 DLA----TFPL--FALFGPA-LGLTSVIPdmDPTRpaRADPQKLVGAIRQYGVSIVFGSPALLERVARYCAQHGITLPS- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 787 LRLAMLSGDWIPVALPDQIRARV-PGLRIVSLGGATEA----SIWS------------------IWYPIEQVdpEWRSIp 843
Cdd:cd05910 201 LRRVLSAGAPVPIALAARLRKMLsDEAEILTPYGATEAlpvsSIGSrellatttaatsggagtcVGRPIPGV--RVRII- 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 844 ygrPLTNQSFHVLDAALRpRPDLVSGELYIGGVGLAVGYLNDRERTAerFVVHPQTGER-LYRTGDLGRYLPDGTIEFLG 922
Cdd:cd05910 278 ---EIDDEPIAEWDDTLE-LPRGEIGEITVTGPTVTPTYVNRPVATA--LAKIDDNSEGfWHRMGDLGYLDDEGRLWFCG 351
|
410 420
....*....|....*....|....*.
gi 1860141834 923 REDLQVKIRGYRIELAEIEAALGGHP 948
Cdd:cd05910 352 RKAHRVITTGGTLYTEPVERVFNTHP 377
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
534-948 |
5.71e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 83.11 E-value: 5.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 534 VVLQALST-PDRPAVVAADRTLDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVDTSQ 612
Cdd:PRK06188 17 LLVSALKRyPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 613 PAARRRTILTNAGIRCALtqsgVDRNGWAE-GLRLLD-----------------VDLLG---TGQPQPVEGSGDPEELAY 671
Cdd:PRK06188 97 SLDDHAYVLEDAGISTLI----VDPAPFVErALALLArvpslkhvltlgpvpdgVDLLAaaaKFGPAPLVAAALPPDIAG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 672 VIHTSGSTGSPKGVMINHRGAVNTVLDINDRFGVGPDDRVLglsnlgfdlsvydVFGPLS-VGGAVVLPDPQRRG----- 745
Cdd:PRK06188 173 LAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFL-------------MCTPLShAGGAFFLPTLLRGGtvivl 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 746 ---DPSHWADLVGTHGVTVWNSVPAQLQMLHDYLVSATATVPdGLRLAMLSGDWI-PVALPDQIRARVPGLriVSLGGAT 821
Cdd:PRK06188 240 akfDPAEVLRAIEEQRITATFLVPTMIYALLDHPDLRTRDLS-SLETVYYGASPMsPVRLAEAIERFGPIF--AQYYGQT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 822 EASiwsiwYPIEQV--------DPEwRSIPYGRPLTNQSFHVLDAALRPRPDLVSGELYIGGVGLAVGYLNDRERTAERF 893
Cdd:PRK06188 317 EAP-----MVITYLrkrdhdpdDPK-RLTSCGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAF 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1860141834 894 vvhpqTGERLyRTGDLGRYLPDGTIEFLGREDLQVKIRGYRIELAEIEAALGGHP 948
Cdd:PRK06188 391 -----RDGWL-HTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHP 439
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
551-948 |
5.86e-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: 82.88 E-value: 5.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 551 DRTLDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVDTSQPAARRRTILTNAgircal 630
Cdd:cd05914 5 GEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHS------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 631 tqsgvdrngwaeglrllDVDLLGTGqpqpvegsgDPEELAYVIHTSGSTGSPKGVMINHRGAVNTVLDINDRFGVGPDDR 710
Cdd:cd05914 79 -----------------EAKAIFVS---------DEDDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGKGDK 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 711 VLGLSNLGFDLS-VYDVFGPLSVGGAVVLPDPQrrgdPSHWADLVGTHGVTVWNSVPAQLQMLHDYLvsaTATVPdglRL 789
Cdd:cd05914 133 ILSILPLHHIYPlTFTLLLPLLNGAHVVFLDKI----PSAKIIALAFAQVTPTLGVPVPLVIEKIFK---MDIIP---KL 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 790 AMLSGDW---IPVaLPDQIRARV---------PGLRIVSLGGA-----TEASIWSIWYPIEQ------VDPEWRSIPYGR 846
Cdd:cd05914 203 TLKKFKFklaKKI-NNRKIRKLAfkkvheafgGNIKEFVIGGAkinpdVEEFLRTIGFPYTIgygmteTAPIISYSPPNR 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 847 PLTNQSFHVLD----AALRPRPDLVSGELYIGGVGLAVGYLNDRERTAERFvvhpqTGERLYRTGDLGRYLPDGTIEFLG 922
Cdd:cd05914 282 IRLGSAGKVIDgvevRIDSPDPATGEGEIIVRGPNVMKGYYKNPEATAEAF-----DKDGWFHTGDLGKIDAEGYLYIRG 356
|
410 420
....*....|....*....|....*..
gi 1860141834 923 R-EDLQVKIRGYRIELAEIEAALGGHP 948
Cdd:cd05914 357 RkKEMIVLSSGKNIYPEEIEAKINNMP 383
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
530-944 |
9.93e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 82.24 E-value: 9.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 530 LHDRVVLQALSTPDRPAVVAADRTLDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVD 609
Cdd:PRK06145 4 LSASIAFHARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPIN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 610 TSQPAARRRTILTNAGIRCALTQSGVDRNGWAEGLRLL-------DVDLLGTG-QPQPVEGSGDPEELAYVIHTSGSTGS 681
Cdd:PRK06145 84 YRLAADEVAYILGDAGAKLLLVDEEFDAIVALETPKIVidaaaqaDSRRLAQGgLEIPPQAAVAPTDLVRLMYTSGTTDR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 682 PKGVMINHRGAVNTVLDINDRFGVGPDDRVLGLSNL----GFDLSVYDVfgpLSVGGAVVLpdpQRRGDPSHWADLVGTH 757
Cdd:PRK06145 164 PKGVMHSYGNLHWKSIDHVIALGLTASERLLVVGPLyhvgAFDLPGIAV---LWVGGTLRI---HREFDPEAVLAAIERH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 758 GVTVWNSVPAQLqmlhdylvSATATVPDGLRLAMLSGDWIPVA---LPDQ-IRA---RVPGLRIVSLGGATEA----SIW 826
Cdd:PRK06145 238 RLTCAWMAPVML--------SRVLTVPDRDRFDLDSLAWCIGGgekTPESrIRDftrVFTRARYIDAYGLTETcsgdTLM 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 827 SIWYPIEQVDPEwrsipyGRPLTNQSFHVLDAALRPRPDLVSGELYIGGVGLAVGYLNDRERTAERFVvhpqtgERLYRT 906
Cdd:PRK06145 310 EAGREIEKIGST------GRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFY------GDWFRS 377
|
410 420 430
....*....|....*....|....*....|....*...
gi 1860141834 907 GDLGRYLPDGTIEFLGREDLQVKIRGYRIELAEIEAAL 944
Cdd:PRK06145 378 GDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVI 415
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
537-975 |
1.00e-15 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 82.49 E-value: 1.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 537 QALSTPDRPAVV---AADRTldYAELLGRAAGVAEALTAAGCRRQELVAVVMDrGW-EQVVAVLGALLAGCVYVPVDtsq 612
Cdd:PRK06087 32 TARAMPDKIAVVdnhGASYT--YSALDHAASRLANWLLAKGIEPGDRVAFQLP-GWcEFTIIYLACLKVGAVSVPLL--- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 613 PAARRRTI-----LTNAGIRCALTQ-----------------------SGVDRNGWAEGLRLLDvDLLGTGQP--QPVEG 662
Cdd:PRK06087 106 PSWREAELvwvlnKCQAKMFFAPTLfkqtrpvdlilplqnqlpqlqqiVGVDKLAPATSSLSLS-QIIADYEPltTAITT 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 663 SGDpeELAYVIHTSGSTGSPKGVMINHRGAVNTVLDINDRFGVGPDDRVLGLSNL----GFdlsVYDVFGPLSVGGAVVL 738
Cdd:PRK06087 185 HGD--ELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLghatGF---LHGVTAPFLIGARSVL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 739 pdpQRRGDPSHWADLVGTHGVT-VWNSVPAQLQMLhDYLVSATATVPdGLRLAMLSGDWIPVALPDQIRARvpGLRIVSL 817
Cdd:PRK06087 260 ---LDIFTPDACLALLEQQRCTcMLGATPFIYDLL-NLLEKQPADLS-ALRFFLCGGTTIPKKVARECQQR--GIKLLSV 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 818 GGATEASiwsiwyPIEQVDP----EWRSIPYGRPLTNQSFHVLDAALRPRPDLVSGELYIGGVGLAVGYLNDRERTAERF 893
Cdd:PRK06087 333 YGSTESS------PHAVVNLddplSRFMHTDGYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELTARAL 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 894 vvhpqTGERLYRTGDLGRYLPDGTIEFLGREDlQVKIR-GYRIELAEIEAALGGHPAVAGAVVVVDGDTPLERRLAAFVE 972
Cdd:PRK06087 407 -----DEEGWYYSGDLCRMDEAGYIKITGRKK-DIIVRgGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVV 480
|
...
gi 1860141834 973 PAG 975
Cdd:PRK06087 481 LKA 483
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
556-948 |
1.01e-15 |
|
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: 82.02 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 556 YAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVDTSQPAARRRTILTNAGIRCALTQSgv 635
Cdd:cd17640 8 YKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALVVEN-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 636 drngwaeglrlldvdllgtgqpqpvegsgDPEELAYVIHTSGSTGSPKGVMINHRGAVNTVLDINDRFGVGPDDRVLGLS 715
Cdd:cd17640 86 -----------------------------DSDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQPGDRFLSIL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 716 NL--GFDLSV-YDVFgplSVGGA------VVLPDPQRRGDPshwadlvgthgvTVWNSVPAQLQMLH---DYLVSATATV 783
Cdd:cd17640 137 PIwhSYERSAeYFIF---ACGCSqaytsiRTLKDDLKRVKP------------HYIVSVPRLWESLYsgiQKQVSKSSPI 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 784 PDGLRLAMLSGDWIPV------ALPDQIRA--RVPGLRIVSLGGATEASiwsiwyPIEQVDPEWRSI--PYGRPLTNQSF 853
Cdd:cd17640 202 KQFLFLFFLSGGIFKFgisgggALPPHVDTffEAIGIEVLNGYGLTETS------PVVSARRLKCNVrgSVGRPLPGTEI 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 854 HVLDAALR-PRPDLVSGELYIGGVGLAVGYLNDRERTAErfvVHPQTGerLYRTGDLGRYLPDGTIEFLGRE-DLQVKIR 931
Cdd:cd17640 276 KIVDPEGNvVLPPGEKGIVWVRGPQVMKGYYKNPEATSK---VLDSDG--WFNTGDLGWLTCGGELVLTGRAkDTIVLSN 350
|
410
....*....|....*..
gi 1860141834 932 GYRIELAEIEAALGGHP 948
Cdd:cd17640 351 GENVEPQPIEEALMRSP 367
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
552-948 |
1.47e-15 |
|
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: 81.91 E-value: 1.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 552 RTLDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVDTSQPA---------ARRRTILT 622
Cdd:cd12119 24 HRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPeqiayiinhAEDRVVFV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 623 N-------AGIRCALTQ-------SGVDRNGWAEGLRLLDV-DLLGTGQPQPVEGSGDpEELAYVI-HTSGSTGSPKGVM 686
Cdd:cd12119 104 DrdflpllEAIAPRLPTvehvvvmTDDAAMPEPAGVGVLAYeELLAAESPEYDWPDFD-ENTAAAIcYTSGTTGNPKGVV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 687 INHRGAVNTVLDIN--DRFGVGPDDRVLGLSNLgFDLSVYDV-FGPLSVGGAVVLPDPqrRGDPSHWADLVGTHGVTVWN 763
Cdd:cd12119 183 YSHRSLVLHAMAALltDGLGLSESDVVLPVVPM-FHVNAWGLpYAAAMVGAKLVLPGP--YLDPASLAELIEREGVTFAA 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 764 SVPAQLQMLHDYLvSATATVPDGLRLAMLSGDWIPVALPDQIRARvpGLRIVSLGGATEASiwsiwyPI---EQVDPEWR 840
Cdd:cd12119 260 GVPTVWQGLLDHL-EANGRDLSSLRRVVIGGSAVPRSLIEAFEER--GVRVIHAWGMTETS------PLgtvARPPSEHS 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 841 SIPY----------GRPLTNQSFHVLDAALR--PRPDLVSGELYIGGVGLAVGYLNDRERTAERFVvhpqtgERLYRTGD 908
Cdd:cd12119 331 NLSEdeqlalrakqGRPVPGVELRIVDDDGRelPWDGKAVGELQVRGPWVTKSYYKNDEESEALTE------DGWLRTGD 404
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1860141834 909 LGRYLPDGTIEFLGR-EDLqVKIRGYRIELAEIEAALGGHP 948
Cdd:cd12119 405 VATIDEDGYLTITDRsKDV-IKSGGEWISSVELENAIMAHP 444
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
530-948 |
1.74e-15 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 81.57 E-value: 1.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 530 LHDRVVLQALSTPDRPAVV--AADRTLDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYV- 606
Cdd:PLN02246 25 LHDYCFERLSEFSDRPCLIdgATGRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTt 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 607 --PVDTSQPAARRrtiLTNAGIRCALTQSG----VDRNGWAEGLRLLDVDllgtgqpQPVEG--------SGDPEELAYV 672
Cdd:PLN02246 105 anPFYTPAEIAKQ---AKASGAKLIITQSCyvdkLKGLAEDDGVTVVTID-------DPPEGclhfseltQADENELPEV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 673 -IH---------TSGSTGSPKGVMINHRGAVNTVLDI----NDRFGVGPDDRVLGLSNLGFDLSVYDV-FGPLSVGGAVV 737
Cdd:PLN02246 175 eISpddvvalpySSGTTGLPKGVMLTHKGLVTSVAQQvdgeNPNLYFHSDDVILCVLPMFHIYSLNSVlLCGLRVGAAIL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 738 LpdpQRRGDPSHWADLVGTHGVTVWNSVP------AQLQMLHDYLVSATATVPDGlrLAMLSGDwipvaLPDQIRARVPG 811
Cdd:PLN02246 255 I---MPKFEIGALLELIQRHKVTIAPFVPpivlaiAKSPVVEKYDLSSIRMVLSG--AAPLGKE-----LEDAFRAKLPN 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 812 LRIVSLGGATEAS-IWSIW-------YPIEQ--------------VDPEW-RSIPYGRPltnqsfhvldaalrprpdlvs 868
Cdd:PLN02246 325 AVLGQGYGMTEAGpVLAMClafakepFPVKSgscgtvvrnaelkiVDPETgASLPRNQP--------------------- 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 869 GELYIGGVGLAVGYLNDRERTAERFVVhpqtgERLYRTGDLGRYLPDGTIEFLGREDLQVKIRGYRIELAEIEAALGGHP 948
Cdd:PLN02246 384 GEICIRGPQIMKGYLNDPEATANTIDK-----DGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHP 458
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
538-948 |
1.84e-15 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 81.07 E-value: 1.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 538 ALSTPDRPAVVAADRTLDYAELLGRAAGVAEALTAAGCRRQELVAVvmdRGWEQVVAVLgALLA----GCVYVPVDTSQP 613
Cdd:PRK09029 13 AQVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVAL---RGKNSPETLL-AYLAllqcGARVLPLNPQLP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 614 AARRRTILTNAGIRCALTQSGvdrNGWAEGLRLLDVDLlgtgQPQPVEGSGDPEELAYVIHTSGSTGSPKGVMINHRGAV 693
Cdd:PRK09029 89 QPLLEELLPSLTLDFALVLEG---ENTFSALTSLHLQL----VEGAHAVAWQPQRLATMTLTSGSTGLPKAAVHTAQAHL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 694 NTVLDINDRFGVGPDDRVLgLSnlgfdLSVYDVFGP------LSVGGAVVLPDPQRrgdpsHWADLvgtHGVTVWNSVPA 767
Cdd:PRK09029 162 ASAEGVLSLMPFTAQDSWL-LS-----LPLFHVSGQgivwrwLYAGATLVVRDKQP-----LEQAL---AGCTHASLVPT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 768 QLQMLHDYLVSATAtvpdgLRLAMLSGDWIPVALPDQIRARvpGLRIVSLGGATE-ASIWSiwypIEQVDpewrSIP-YG 845
Cdd:PRK09029 228 QLWRLLDNRSEPLS-----LKAVLLGGAAIPVELTEQAEQQ--GIRCWCGYGLTEmASTVC----AKRAD----GLAgVG 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 846 RPLTNQSFHvldaalrprpdLVSGELYIGGVGLAVGYLNDRErtaerfvVHPQTGER-LYRTGDLGRyLPDGTIEFLGRE 924
Cdd:PRK09029 293 SPLPGREVK-----------LVDGEIWLRGASLALGYWRQGQ-------LVPLVNDEgWFATRDRGE-WQNGELTILGRL 353
|
410 420
....*....|....*....|....
gi 1860141834 925 DLQVKIRGYRIELAEIEAALGGHP 948
Cdd:PRK09029 354 DNLFFSGGEGIQPEEIERVINQHP 377
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
542-951 |
2.37e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 80.98 E-value: 2.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 542 PDRPAVVAADRTLDYAELLGRAAGVAEALTAAGcRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVDT--SQPAARRRT 619
Cdd:PRK07638 15 PNKIAIKENDRVLTYKDWFESVCKVANWLNEKE-SKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIkwKQDELKERL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 620 ILTNAGIRCALTQSGVDRNGwAEGlRLLDVD----LLGTGQPQPVEGSGDPEELAYVIHTSGSTGSPKGVMINHRGAVNT 695
Cdd:PRK07638 94 AISNADMIVTERYKLNDLPD-EEG-RVIEIDewkrMIEKYLPTYAPIENVQNAPFYMGFTSGSTGKPKAFLRAQQSWLHS 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 696 VLDINDRFGVGPDDRVLGLSNLGFDLSVYDVFGPLSVGGAVVLpdpQRRGDPSHWADLVGTHGVTVWNSVPAQLqmlhDY 775
Cdd:PRK07638 172 FDCNVHDFHMKREDSVLIAGTLVHSLFLYGAISTLYVGQTVHL---MRKFIPNQVLDKLETENISVMYTVPTML----ES 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 776 LVSATATVPDGLRLAMLSGDWiPVALPDQIRARVPGLRIVSLGGATEASIWSIWYPieqVDPEWRSIPYGRPLTNQSFHV 855
Cdd:PRK07638 245 LYKENRVIENKMKIISSGAKW-EAEAKEKIKNIFPYAKLYEFYGASELSFVTALVD---EESERRPNSVGRPFHNVQVRI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 856 LDAA-LRPRPDLVsGELYIGGVGLAVGYLNDRertaerfVVHPQTGERLYRT-GDLGRYLPDGTIEFLGREDLQVKIRGY 933
Cdd:PRK07638 321 CNEAgEEVQKGEI-GTVYVKSPQFFMGYIIGG-------VLARELNADGWMTvRDVGYEDEEGFIYIVGREKNMILFGGI 392
|
410
....*....|....*...
gi 1860141834 934 RIELAEIEAALGGHPAVA 951
Cdd:PRK07638 393 NIFPEEIESVLHEHPAVD 410
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
1374-1474 |
3.58e-15 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 82.14 E-value: 3.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 1374 DDLTEHLAGRLPQYMVPSVVQVVDALPLNANGKVDRavlrRRLPRRGTATaaGSSGALDSDLERRIAAVWAEALRLPRVG 1453
Cdd:PRK05691 1584 ERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDR----RALPEPVWQQ--REHVEPRTELQQQIAAIWREVLGLPRVG 1657
|
90 100
....*....|....*....|.
gi 1860141834 1454 RDENLFELGGDSLVAAQITGR 1474
Cdd:PRK05691 1658 LRDDFFALGGHSLLATQIVSR 1678
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
655-948 |
6.71e-15 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 80.16 E-value: 6.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 655 GQPQPVEGS-GDPEELAYVIHTSGSTGSPKGVMINHRGAVNTVLDINDRF-GVGPDDRVLGLSNLG--FDLSVYDVFgpL 730
Cdd:PLN02387 237 GKENPVDPDlPSPNDIAVIMYTSGSTGLPKGVMMTHGNIVATVAGVMTVVpKLGKNDVYLAYLPLAhiLELAAESVM--A 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 731 SVGGAVVLPDPQRRGDPSHWADLvGTHG------VTVWNSVPAQLQMLHDYL---VSATATVPDGL-------RLAMLSG 794
Cdd:PLN02387 315 AVGAAIGYGSPLTLTDTSNKIKK-GTKGdasalkPTLMTAVPAILDRVRDGVrkkVDAKGGLAKKLfdiaykrRLAAIEG 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 795 DW-----IPVALPD-----QIRARVPG-LRIVSLGGA-----TEASIwSIWY--PIEQ-----------VDPEWRSIPYG 845
Cdd:PLN02387 394 SWfgawgLEKLLWDalvfkKIRAVLGGrIRFMLSGGAplsgdTQRFI-NICLgaPIGQgygltetcagaTFSEWDDTSVG 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 846 R---PLTNQSFHVLD-------AALRPRPdlvSGELYIGGVGLAVGYLNDRERTAERFVVHpQTGERLYRTGDLGRYLPD 915
Cdd:PLN02387 473 RvgpPLPCCYVKLVSweeggylISDKPMP---RGEIVIGGPSVTLGYFKNQEKTDEVYKVD-ERGMRWFYTGDIGQFHPD 548
|
330 340 350
....*....|....*....|....*....|....
gi 1860141834 916 GTIEFLGREDLQVKIR-GYRIELAEIEAALGGHP 948
Cdd:PLN02387 549 GCLEIIDRKKDIVKLQhGEYVSLGKVEAALSVSP 582
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
672-948 |
9.01e-15 |
|
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: 77.70 E-value: 9.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 672 VIHTSGSTGSPKGVMINHRGAVNTVLDINDRFGVGPDDRVLGLSNL----GFDLSvydvFGPLSVGGAVVLPDpqrRGDP 747
Cdd:cd17637 5 IIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLfhiaGLNLA----LATFHAGGANVVME---KFDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 748 SHWADLVGTHGVTVWNSVPAQLQMLHDylvSATATVPDGLRLAMLSGdwipVALPDQIRA--RVPGLRIVSLGGATEASI 825
Cdd:cd17637 78 AEALELIEEEKVTLMGSFPPILSNLLD---AAEKSGVDLSSLRHVLG----LDAPETIQRfeETTGATFWSLYGQTETSG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 826 WSIWYPIEQvdpewRSIPYGRPLTNQSFHVLDAALRPRPDLVSGELYIGGVGLAVGYLNDRERTAERFvvhpQTGerLYR 905
Cdd:cd17637 151 LVTLSPYRE-----RPGSAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTF----RNG--WHH 219
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1860141834 906 TGDLGRYLPDGTIEFLGR--EDLQVKIRGYRIELAEIEAALGGHP 948
Cdd:cd17637 220 TGDLGRFDEDGYLWYAGRkpEKELIKPGGENVYPAEVEKVILEHP 264
|
|
| starter-C_NRPS |
cd19533 |
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ... |
101-408 |
1.19e-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: 78.18 E-value: 1.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 101 GYGELVYPeLDPERMTAAWRALIARHDMLRA--VVEADGAQRVLAEVPPFEVPVIDLTGRPEAVVDAAVSAvraeMDHLV 178
Cdd:cd19533 28 EYLEITGP-VDLAVLERALRQVIAEAETLRLrfTEEEGEPYQWIDPYTPVPIRHIDLSGDPDPEGAAQQWM----QEDLR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 179 HTPD--RWPLF-AARITRADHRTVLHVSIDFLIADFISVQVVLDELHRLYH---RPDEPLPPLEITFRDYQLAERAVRDS 252
Cdd:cd19533 103 KPLPldNDPLFrHALFTLGDNRHFWYQRVHHIVMDGFSFALFGQRVAEIYTallKGRPAPPAPFGSFLDLVEEEQAYRQS 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 253 PRHERDKQWWLarvDELPAAPELPTVARPADSEGR-FRRWETRLSSQVWEGLRQRAGRHGVSPSGAVLAAFSDTIAAYSR 331
Cdd:cd19533 183 ERFERDRAFWT---EQFEDLPEPVSLARRAPGRSLaFLRRTAELPPELTRTLLEAAEAHGASWPSFFIALVAAYLHRLTG 259
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1860141834 332 RSRFTLDITLLNRAPVHDQvnALVGDFTSVDLLAVDADPTRRFDERARDLQAQLWEDLDHRSFSGIEVMREIARRQG 408
Cdd:cd19533 260 ANDVVLGVPVMGRLGAAAR--QTPGMVANTLPLRLTVDPQQTFAELVAQVSRELRSLLRHQRYRYEDLRRDLGLTGE 334
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
483-948 |
1.83e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 78.54 E-value: 1.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 483 AAYDAVLHRLagDDAAWtgtghpdPPEATRDrraetnrTQAPVPAGMLHDRVVLQALSTPDRPAVVAADRTLDYAELLGR 562
Cdd:PRK06178 4 EAYLAELRAL--QQAAW-------PAGIPRE-------PEYPHGERPLTEYLRAWARERPQRPAIIFYGHVITYAELDEL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 563 AAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVDtsqPAARR---RTILTNAGIRCALTQ------- 632
Cdd:PRK06178 68 SDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVS---PLFREhelSYELNDAGAEVLLALdqlapvv 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 633 -----------------------------------SGVDRNGWAEGLRLLDvdllGTGQPQPVEgSGDPEELAYVIHTSG 677
Cdd:PRK06178 145 eqvraetslrhvivtsladvlpaeptlplpdslraPRLAAAGAIDLLPALR----ACTAPVPLP-PPALDALAALNYTGG 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 678 STGSPKGVMINHRGAVNTVLDINDRFGVGPDDRVLglsnLGFdLSVYDVFG-------PLSVGGAVVLpdpQRRGDPSHW 750
Cdd:PRK06178 220 TTGMPKGCEHTQRDMVYTAAAAYAVAVVGGEDSVF----LSF-LPEFWIAGenfgllfPLFSGATLVL---LARWDAVAF 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 751 ADLVGTHGVTVwnsvpaqLQMLHDYLVSATATvPDGLRLAMLSGDWIPVAlpDQIRARVPGLR--IVSLGGAT--EASiW 826
Cdd:PRK06178 292 MAAVERYRVTR-------TVMLVDNAVELMDH-PRFAEYDLSSLRQVRVV--SFVKKLNPDYRqrWRALTGSVlaEAA-W 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 827 ---------SIWYPIEQVDPEWRSIPY--GRPLTNQSFHVLD-AALRPRPDLVSGELYIGGVGLAVGYLNDRERTAERFV 894
Cdd:PRK06178 361 gmtethtcdTFTAGFQDDDFDLLSQPVfvGLPVPGTEFKICDfETGELLPLGAEGEIVVRTPSLLKGYWNKPEATAEALR 440
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1860141834 895 vhpqtgERLYRTGDLGRYLPDGTIEFLGREDLQVKIRGYRIELAEIEAALGGHP 948
Cdd:PRK06178 441 ------DGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHP 488
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
663-948 |
2.86e-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: 77.64 E-value: 2.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 663 SGDPEELAYVIHTSGSTGSPKGVMINHRGAVNTVLDINDRFG--VGPDDRVLGLSNLG--FDLSVYDVFgpLSVGGAVVL 738
Cdd:cd17639 84 DGKPDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRVPelLGPDDRYLAYLPLAhiFELAAENVC--LYRGGTIGY 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 739 PDPQRRGDPShwadLVGTHG------VTVWNSVPAQLQMLHDYLVSATATVP-------DG---LRLAMLSgdwipvALP 802
Cdd:cd17639 162 GSPRTLTDKS----KRGCKGdltefkPTLMVGVPAIWDTIRKGVLAKLNPMGglkrtlfWTayqSKLKALK------EGP 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 803 D----------QIRARVPG-LRIVSLGGA-----TEASIWSIWYPIEQ-------------VDP-EWRSIPYGRPLTNQS 852
Cdd:cd17639 232 GtplldelvfkKVRAALGGrLRYMLSGGAplsadTQEFLNIVLCPVIQgygltetcaggtvQDPgDLETGRVGPPLPCCE 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 853 FHVLD------AALRPRPdlvSGELYIGGVGLAVGYLNDRERTAERFvvhpqTGERLYRTGDLGRYLPDGTIEFLGR-ED 925
Cdd:cd17639 312 IKLVDweeggySTDKPPP---RGEILIRGPNVFKGYYKNPEKTKEAF-----DGDGWFHTGDIGEFHPDGTLKIIDRkKD 383
|
330 340
....*....|....*....|....
gi 1860141834 926 LqVKIR-GYRIELAEIEAALGGHP 948
Cdd:cd17639 384 L-VKLQnGEYIALEKLESIYRSNP 406
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
554-951 |
3.15e-14 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 77.22 E-value: 3.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 554 LDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVDTS-QPAARRRTILTNAGIRCALTQ 632
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLlTPDDLRDRVDRGGAVYAAVDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 633 sgvdrngwaeglrlldvdllgtgqpqpVEGSGDPEELAYvihTSGSTGSPKGVMINHR----GAVNTVLDIndrfGVGPD 708
Cdd:cd05974 81 ---------------------------NTHADDPMLLYF---TSGTTSKPKLVEHTHRsypvGHLSTMYWI----GLKPG 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 709 DRVLGLSNLGFDLSVYD-VFGPLSVGGAVVLPDpQRRGDPSHWADLVGTHGVTVWNSVPAQLQMLhdyLVSATATVPDGL 787
Cdd:cd05974 127 DVHWNISSPGWAKHAWScFFAPWNAGATVFLFN-YARFDAKRVLAALVRYGVTTLCAPPTVWRML---IQQDLASFDVKL 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 788 RLAMLSGDWIPVALPDQIRaRVPGLRIVSLGGATEASIWSIWYPIEQVDPEwrsiPYGRPLTNQSFHVLDAALRPRPDlv 867
Cdd:cd05974 203 REVVGAGEPLNPEVIEQVR-RAWGLTIRDGYGQTETTALVGNSPGQPVKAG----SMGRPLPGYRVALLDPDGAPATE-- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 868 sGE--LYIGG---VGLAVGYLNDRERTAERFvvhpqtGERLYRTGDLGRYLPDGTIEFLGREDLQVKIRGYRIELAEIEA 942
Cdd:cd05974 276 -GEvaLDLGDtrpVGLMKGYAGDPDKTAHAM------RGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELES 348
|
....*....
gi 1860141834 943 ALGGHPAVA 951
Cdd:cd05974 349 VLIEHPAVA 357
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
524-948 |
3.76e-14 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 77.33 E-value: 3.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 524 PVPAGMLHDRVVLQ-ALSTPDRPAVVAA--DRTLDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALL 600
Cdd:PLN02330 23 PVPDKLTLPDFVLQdAELYADKVAFVEAvtGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 601 AGCVYV---------PVDTSQPAARRRTILTNA-------GIRCALTQSGVDRNGWAEGLRlldvDLLGTGqpqpvEGSG 664
Cdd:PLN02330 103 AGGVFSganptalesEIKKQAEAAGAKLIVTNDtnygkvkGLGLPVIVLGEEKIEGAVNWK----ELLEAA-----DRAG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 665 DPEELAYVIHT--------SGSTGSPKGVMINHRGAVNTVldINDRFGVGPD--DRVLGLSNLGFdLSVYDVFG----PL 730
Cdd:PLN02330 174 DTSDNEEILQTdlcalpfsSGTTGISKGVMLTHRNLVANL--CSSLFSVGPEmiGQVVTLGLIPF-FHIYGITGiccaTL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 731 SVGGAVVLpdpQRRGDPSHWADLVGTHGVTVWNSVPAQ-LQMLHDYLVSATATVPDGLRLAMLSGDWIPVALPDQIRARV 809
Cdd:PLN02330 251 RNKGKVVV---MSRFELRTFLNALITQEVSFAPIVPPIiLNLVKNPIVEEFDLSKLKLQAIMTAAAPLAPELLTAFEAKF 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 810 PGLRIVSLGGATEASIWSIWYPieqvDPE-----WRSIPYGRPLTNQSFHVLDAAL-RPRPDLVSGELYIGGVGLAVGYL 883
Cdd:PLN02330 328 PGVQVQEAYGLTEHSCITLTHG----DPEkghgiAKKNSVGFILPNLEVKFIDPDTgRSLPKNTPGELCVRSQCVMQGYY 403
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1860141834 884 NDRERTAERFvvhpqTGERLYRTGDLGRYLPDGTIEFLGREDLQVKIRGYRIELAEIEAALGGHP 948
Cdd:PLN02330 404 NNKEETDRTI-----DEDGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHP 463
|
|
| CT_NRPS-like |
cd19542 |
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ... |
75-419 |
5.50e-14 |
|
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: 76.19 E-value: 5.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 75 FPVTDVQAAYLLgrgETFAYGGVACHGYGELVYPELDPERMTAAWRALIARHDMLRAV---VEADG--AQRVLAEVPPfe 149
Cdd:cd19542 2 YPCTPMQEGMLL---SQLRSPGLYFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVfveSSAEGtfLQVVLKSLDP-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 150 vPVIDLTGRPEavVDAAVSAVRAEMDHLVHTPdrwPLFAARITRADHRTVLHVSIDFLIADFISVQVVLDELHRLYH-RP 228
Cdd:cd19542 77 -PIEEVETDED--SLDALTRDLLDDPTLFGQP---PHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAYNgQL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 229 DEPLPPleitFRDYQlaeRAVRDSPRhERDKQWWLARVDELPaAPELPTVarpadSEGRFRRWETRLSSQVWEGLRQRAG 308
Cdd:cd19542 151 LPPAPP----FSDYI---SYLQSQSQ-EESLQYWRKYLQGAS-PCAFPSL-----SPKRPAERSLSSTRRSLAKLEAFCA 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 309 RHGVSPSGAVLAAFSDTIAAYSRRSRFTLDITLLNRAPVHDQVNALVGDFTSVdL---LAVDADPTRRfdERARDLQAQL 385
Cdd:cd19542 217 SLGVTLASLFQAAWALVLARYTGSRDVVFGYVVSGRDLPVPGIDDIVGPCINT-LpvrVKLDPDWTVL--DLLRQLQQQY 293
|
330 340 350
....*....|....*....|....*....|....*.
gi 1860141834 386 WEDLDHRSFSgievMREIAR--RQGAEAALFPVVFT 419
Cdd:cd19542 294 LRSLPHQHLS----LREIQRalGLWPSGTLFNTLVS 325
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
538-948 |
5.64e-14 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 76.65 E-value: 5.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 538 ALSTPDRPAVVAA--DRTLDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVDTSQPAA 615
Cdd:PRK13391 7 AQTTPDKPAVIMAstGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 616 RRRTILTNAGIRCALT---QSGVDRNGWAE--GLRL-LDVDLLGTGQ---------------PQPVEGSGDPeelayVIH 674
Cdd:PRK13391 87 EAAYIVDDSGARALITsaaKLDVARALLKQcpGVRHrLVLDGDGELEgfvgyaeavaglpatPIADESLGTD-----MLY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 675 TSGSTGSPKGVMIN-HRGAVNTVLDI----NDRFGVGPDDRVLGLSNLGFDLSVYDVFGPLSVGGAVVLPDpqrRGDPSH 749
Cdd:PRK13391 162 SSGTTGRPKGIKRPlPEQPPDTPLPLtaflQRLWGFRSDMVYLSPAPLYHSAPQRAVMLVIRLGGTVIVME---HFDAEQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 750 WADLVGTHGVTVWNSVPAQL-QMLH-------DYLVS-------ATATVPDGLRLAMLSGdWIPValpdqirarvpglrI 814
Cdd:PRK13391 239 YLALIEEYGVTHTQLVPTMFsRMLKlpeevrdKYDLSslevaihAAAPCPPQVKEQMIDW-WGPI--------------I 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 815 VSLGGATEASIWSIWYPieqvdPEWRSIP--YGRPLTNQsFHVLDAALRPRPDLVSGELYIGGvGLAVGYLNDRERTAEr 892
Cdd:PRK13391 304 HEYYAATEGLGFTACDS-----EEWLAHPgtVGRAMFGD-LHILDDDGAELPPGEPGTIWFEG-GRPFEYLNDPAKTAE- 375
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1860141834 893 fVVHPQTGerLYRTGDLGRYLPDGTIEFLGREDLQVKIRGYRIELAEIEAALGGHP 948
Cdd:PRK13391 376 -ARHPDGT--WSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHP 428
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
542-971 |
8.02e-14 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 76.19 E-value: 8.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 542 PDRPAVVAADRTLDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVDTSQPAARRRTIL 621
Cdd:PRK13383 49 PGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAAL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 622 TNAGIRCALTQSG-VDR-NGWAEGLRLLDVDLLGT----GQPQpVEGSGdpeelAYVIHTSGSTGSPKGV--MINHRGAV 693
Cdd:PRK13383 129 RAHHISTVVADNEfAERiAGADDAVAVIDPATAGAeesgGRPA-VAAPG-----RIVLLTSGTTGKPKGVprAPQLRSAV 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 694 NTVLDINDRFGVGPDDRVL----GLSNLGFDLSVYDVfgplSVGGAVVlpdPQRRGDPSHWADLVGTHGVTVWNSVPAQL 769
Cdd:PRK13383 203 GVWVTILDRTRLRTGSRISvampMFHGLGLGMLMLTI----ALGGTVL---THRHFDAEAALAQASLHRADAFTAVPVVL 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 770 QMLHDYLVSATATVP-DGLRLAMLSGDWIPVALPDQIrARVPGLRIVSLGGATEASIWSIWYPIEQVD-PEwrsiPYGRP 847
Cdd:PRK13383 276 ARILELPPRVRARNPlPQLRVVMSSGDRLDPTLGQRF-MDTYGDILYNGYGSTEVGIGALATPADLRDaPE----TVGKP 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 848 LTNQSFHVLDAALRPRPDLVSGELYIGGVGLAVGYLNDrertAERFVVHPQTGerlyrTGDLGRYLPDGTIEFLGREDLQ 927
Cdd:PRK13383 351 VAGCPVRILDRNNRPVGPRVTGRIFVGGELAGTRYTDG----GGKAVVDGMTS-----TGDMGYLDNAGRLFIVGREDDM 421
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1860141834 928 VKIRGYRIELAEIEAALGGHPAVAGAVVVVDGDTPLERRLAAFV 971
Cdd:PRK13383 422 IISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFV 465
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
1389-1530 |
1.66e-13 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 76.36 E-value: 1.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 1389 VPSVVQVVD--ALPLNANGKVDRAVLRRRLP----------RRGTATAAGSSGALDSDLERRIAAVWAEALRLPRVGRDE 1456
Cdd:PRK05691 529 APSVVLLLNpgALPKTSSGKLQRSACRLRLAdgsldsyalfPALQAVEAAQTAASGDELQARIAAIWCEQLKVEQVAADD 608
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1860141834 1457 NLFELGGDSLVAAQITGRILEEIpqaaGLFFDqlLRQVLEQPTVAALAGHVEAESATPVTASPSVPATSGGDGL 1530
Cdd:PRK05691 609 HFFLLGGNSIAATQVVARLRDEL----GIDLN--LRQLFEAPTLAAFSAAVARQLAGGGAAQAAIARLPRGQAL 676
|
|
| C_PKS-NRPS |
cd20483 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
111-375 |
1.78e-13 |
|
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: 74.60 E-value: 1.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 111 DPERMTAAWRALIARHDMLR-AVVE--ADGAQRVLaEVPPFEVPVIDLTGRPEAVVDAAVSAVRAEMDH----------- 176
Cdd:cd20483 37 DVNLLQKALSELVRRHEVLRtAYFEgdDFGEQQVL-DDPSFHLIVIDLSEAADPEAALDQLVRNLRRQEldieegevirg 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 177 -LVHTPD-RWPLFAAritraDHrtvlHVSIDFliadfISVQVVLDELHRLY-----HRPDEPLPPLEITFRDYQLAERAV 249
Cdd:cd20483 116 wLVKLPDeEFALVLA-----SH----HIAWDR-----GSSKSIFEQFTALYdalraGRDLATVPPPPVQYIDFTLWHNAL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 250 RDSPRHERDKQWWLARVDELPAAPE-LP--TVARPADSEGRFRRWETRLSSQVWEGLRQRAGRHGVSPSGAVLAAFsdti 326
Cdd:cd20483 182 LQSPLVQPLLDFWKEKLEGIPDASKlLPfaKAERPPVKDYERSTVEATLDKELLARMKRICAQHAVTPFMFLLAAF---- 257
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1860141834 327 AAYSRRSRFTLDITLL----NRApvHDQVNALVGDFtsVDLLAV--DADPTRRFD 375
Cdd:cd20483 258 RAFLYRYTEDEDLTIGmvdgDRP--HPDFDDLVGFF--VNMLPIrcRMDCDMSFD 308
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
556-923 |
2.66e-13 |
|
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: 74.56 E-value: 2.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 556 YAELLGRAAGVAEALTAAGCRRQE--LVAVVMDRGWEQVVAVLGALLAGCVYVPV-DTSQPAARRrTILTNAGIRCALTQ 632
Cdd:cd05927 8 YKEVAERADNIGSALRSLGGKPAPasFVGIYSINRPEWIISELACYAYSLVTVPLyDTLGPEAIE-YILNHAEISIVFCD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 633 SGVDRNGWAEglrLLDvdlLGTGQPQPVEgSGDPEELAYVIHTSGSTGSPKGVMINHRGAVNTVLDIN----DRFGVGPD 708
Cdd:cd05927 87 AGVKVYSLEE---FEK---LGKKNKVPPP-PPKPEDLATICYTSGTTGNPKGVMLTHGNIVSNVAGVFkileILNKINPT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 709 DR---VLGLSNLgFDLSVYDVFgpLSVGGAVVLpdpqRRGDPSHWADLVGTHGVTVWNSVPAQLQMLHDYL---VSATAT 782
Cdd:cd05927 160 DVyisYLPLAHI-FERVVEALF--LYHGAKIGF----YSGDIRLLLDDIKALKPTVFPGVPRVLNRIYDKIfnkVQAKGP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 783 VPDGL-------RLAML-------SGDW-------IPVALPDQIRARVPG-----------LRiVSLG-------GATEA 823
Cdd:cd05927 233 LKRKLfnfalnyKLAELrsgvvraSPFWdklvfnkIKQALGGNVRLMLTGsaplspevlefLR-VALGcpvlegyGQTEC 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 824 S-IWSIWYPieqvdPEWRSIPYGRPLTNQSFHVLDA------ALRPRPdlvSGELYIGGVGLAVGYLNDRERTAERFVVh 896
Cdd:cd05927 312 TaGATLTLP-----GDTSVGHVGGPLPCAEVKLVDVpemnydAKDPNP---RGEVCIRGPNVFSGYYKDPEKTAEALDE- 382
|
410 420
....*....|....*....|....*..
gi 1860141834 897 pqtgERLYRTGDLGRYLPDGTIEFLGR 923
Cdd:cd05927 383 ----DGWLHTGDIGEWLPNGTLKIIDR 405
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
538-948 |
5.49e-13 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 73.66 E-value: 5.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 538 ALSTPDRPAVVAADRTLDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVDTSQPAARR 617
Cdd:PRK07786 27 ALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 618 RTILTNAGIRCALTQ-------SGVDR-----------NGWAEGLRLLDVDLLGTGQP--QPVEGSGDPEELayVIHTSG 677
Cdd:PRK07786 107 AFLVSDCGAHVVVTEaalapvaTAVRDivpllstvvvaGGSSDDSVLGYEDLLAEAGPahAPVDIPNDSPAL--IMYTSG 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 678 STGSPKGVMINHRGAVNTVLDINDRFGVGPDDRVLGLSNLGFDLSVYDVFGPLSVGGAVVLPDPQRRGDPSHWADLVGTH 757
Cdd:PRK07786 185 TTGRPKGAVLTHANLTGQAMTCLRTNGADINSDVGFVGVPLFHIAGIGSMLPGLLLGAPTVIYPLGAFDPGQLLDVLEAE 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 758 GVTVWNSVPAQLQMlhdylVSATATV-PDGLRLAMLSGDWIPV--ALPDQIRARVPGLRIVSLGGATEASiwsiwyPIEQ 834
Cdd:PRK07786 265 KVTGIFLVPAQWQA-----VCAEQQArPRDLALRVLSWGAAPAsdTLLRQMAATFPEAQILAAFGQTEMS------PVTC 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 835 V---DPEWRSI-PYGRPLTNQSFHVLDAALRPRPDLVSGELYIGGVGLAVGYLNDRERTAERFvvhpqtGERLYRTGDLG 910
Cdd:PRK07786 334 MllgEDAIRKLgSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAF------AGGWFHSGDLV 407
|
410 420 430
....*....|....*....|....*....|....*...
gi 1860141834 911 RYLPDGTIEFLGREDLQVKIRGYRIELAEIEAALGGHP 948
Cdd:PRK07786 408 RQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHP 445
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
545-948 |
6.85e-13 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 73.40 E-value: 6.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 545 PAVVAA--DRTLDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVDTSQPAARRRTILT 622
Cdd:PRK08276 1 PAVIMApsGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 623 NAGIRCALTQSGVdrngwAEGLRLLdVDLLGTGQPQ------PVEGSGDPEEL---------------AYVIHTSGSTGS 681
Cdd:PRK08276 81 DSGAKVLIVSAAL-----ADTAAEL-AAELPAGVPLllvvagPVPGFRSYEEAlaaqpdtpiadetagADMLYSSGTTGR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 682 PKGVMINHRGavntvLDINDrfGVGPDDRVLGLSNLGFDLSVYDVFGPL-------------SVGGAVVLPDpqrRGDPS 748
Cdd:PRK08276 155 PKGIKRPLPG-----LDPDE--APGMMLALLGFGMYGGPDSVYLSPAPLyhtaplrfgmsalALGGTVVVME---KFDAE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 749 HWADLVGTHGVTVWNSVPAQL-QMLhdylvsatatvpdglrlamlsgdwipvALPDQIRAR--VPGLRIVSLGGA----- 820
Cdd:PRK08276 225 EALALIERYRVTHSQLVPTMFvRML---------------------------KLPEEVRARydVSSLRVAIHAAApcpve 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 821 -TEASI-WsiWYPI--------EQ-----VDPE-WRSIP--YGRPLTNQsFHVLDAALRPRPDLVSGELYIGGVGLAVGY 882
Cdd:PRK08276 278 vKRAMIdW--WGPIiheyyassEGggvtvITSEdWLAHPgsVGKAVLGE-VRILDEDGNELPPGEIGTVYFEMDGYPFEY 354
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1860141834 883 LNDRERTAERFvvHPQTgerLYRTGDLGrYL-PDGTIEFLGREDLQVKIRGYRIELAEIEAALGGHP 948
Cdd:PRK08276 355 HNDPEKTAAAR--NPHG---WVTVGDVG-YLdEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHP 415
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
667-948 |
9.14e-13 |
|
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: 71.52 E-value: 9.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 667 EELAYVIHTSGSTGSPKGVMINHRGAVnTVLD--INDRFGVGPDDRVLGLSNLGFDLSVYDVFGPLSVGGAVVLpdPQRR 744
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFF-AVPDilQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVT--GGEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 745 GDPSHWADLVGTHGVTVWNSVPAQLQMLHDYLVSATATVPDgLRLAMLSGDWiPVALPDQIRARVPGLRIVSLGGATEAS 824
Cdd:cd17635 78 TTYKSLFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPS-LRLIGYGGSR-AIAADVRFIEATGLTNTAQVYGLSETG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 825 IwSIWYPIEQVDPEWRSIpyGRPLTNQSFHVLDAALRPRPDLVSGELYIGGVGLAVGYLNDRERTAERFvvhpqTGERLY 904
Cdd:cd17635 156 T-ALCLPTDDDSIEINAV--GRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVL-----IDGWVN 227
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1860141834 905 rTGDLGRYLPDGTIEFLGREDLQVKIRGYRIELAEIEAALGGHP 948
Cdd:cd17635 228 -TGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVS 270
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
550-948 |
1.06e-12 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 73.01 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 550 ADRTLDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVDTS---QPAARRrtiLTNAGI 626
Cdd:PRK04319 70 RKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAfmeEAVRDR---LEDSEA 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 627 RCALTQSG------------------VDRNGWAEGlRLLDVD-LLGTGQPQPVEGSGDPEELAYVIHTSGSTGSPKGV-- 685
Cdd:PRK04319 147 KVLITTPAllerkpaddlpslkhvllVGEDVEEGP-GTLDFNaLMEQASDEFDIEWTDREDGAILHYTSGSTGKPKGVlh 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 686 ----MINHRGAVNTVLDINdrfgvgPDDR---------VLGLSnlgfdlsvYDVFGPLSVGGAVVLpdpqRRG--DPSHW 750
Cdd:PRK04319 226 vhnaMLQHYQTGKYVLDLH------EDDVywctadpgwVTGTS--------YGIFAPWLNGATNVI----DGGrfSPERW 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 751 ADLVGTHGVTVWNSVPAQLQMlhdyLVSATATVPDGLRLAMLS-----GDwiPVAlPDQIR--ARVPGLRIVSLGGATE- 822
Cdd:PRK04319 288 YRILEDYKVTVWYTAPTAIRM----LMGAGDDLVKKYDLSSLRhilsvGE--PLN-PEVVRwgMKVFGLPIHDNWWMTEt 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 823 ASIWSIWYPIEQVDPEwrSIpyGRPLTNQSFHVLDAALRPRPDLVSGELYI--GGVGLAVGYLNDRERTAERFVvhpqtg 900
Cdd:PRK04319 361 GGIMIANYPAMDIKPG--SM--GKPLPGIEAAIVDDQGNELPPNRMGNLAIkkGWPSMMRGIWNNPEKYESYFA------ 430
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1860141834 901 ERLYRTGDLGRYLPDGTIEFLGREDLQVKIRGYRIELAEIEAALGGHP 948
Cdd:PRK04319 431 GDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHP 478
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
542-948 |
1.23e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 72.38 E-value: 1.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 542 PDRPAVVAADRTLDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVDTSQPAARRRTIL 621
Cdd:PRK07470 21 PDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEVAYLA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 622 TNAGIRCALTQSGVD---RNGWAEGLRLLDVDLLGTGQPQP------VEGSGDPEELAYVIH--------TSGSTGSPKG 684
Cdd:PRK07470 101 EASGARAMICHADFPehaAAVRAASPDLTHVVAIGGARAGLdyealvARHLGARVANAAVDHddpcwfffTSGTTGRPKA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 685 VMINHrGAVNTVldINDRF-----GVGPDDRVLglsnlgfdlsvydVFGPLSVGGAV------------VLPdPQRRGDP 747
Cdd:PRK07470 181 AVLTH-GQMAFV--ITNHLadlmpGTTEQDASL-------------VVAPLSHGAGIhqlcqvargaatVLL-PSERFDP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 748 SHWADLVGTHGVTVWNSVPAQLQML--------HDYlvsatatvpDGLRLAMLSGdwIPVALPDQIRA-RVPGLRIVSLG 818
Cdd:PRK07470 244 AEVWALVERHRVTNLFTVPTILKMLvehpavdrYDH---------SSLRYVIYAG--APMYRADQKRAlAKLGKVLVQYF 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 819 GATEAS--IWSIWYPIEQVD--PEWRSIPYGRPLTNQSFHVLDAALRPRPDLVSGELYIGGVGLAVGYLNDRERTAERFV 894
Cdd:PRK07470 313 GLGEVTgnITVLPPALHDAEdgPDARIGTCGFERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAFR 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1860141834 895 vhpqtgERLYRTGDLGRYLPDGTIEFLGREDLQVKIRGYRIELAEIEAALGGHP 948
Cdd:PRK07470 393 ------DGWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHP 440
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
532-948 |
2.78e-12 |
|
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: 71.58 E-value: 2.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 532 DRVVLQAlsTPDRPAVVA------ADRTLDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVY 605
Cdd:cd05967 57 DRHVEAG--RGDQIALIYdspvtgTERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIH 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 606 VPV-------------DTSQPAarrrTILT-NAGIRC------------ALTQSGVDRN------------GWAEGLRLL 647
Cdd:cd05967 135 SVVfggfaakelasriDDAKPK----LIVTaSCGIEPgkvvpykplldkALELSGHKPHhvlvlnrpqvpaDLTKPGRDL 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 648 D-VDLLGTGQPQ---PVEgSGDPeelAYVIHTSGSTGSPKGVMINHRG-AVNTVLDINDRFGVGPDDRVLGLSNLGFDLS 722
Cdd:cd05967 211 DwSELLAKAEPVdcvPVA-ATDP---LYILYTSGTTGKPKGVVRDNGGhAVALNWSMRNIYGIKPGDVWWAASDVGWVVG 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 723 -VYDVFGPLSVGGAVVLPD--PQRRGDPSHWADLVGTHGVTVWNSVPAQLQMLH----------DY-LVSATATVPDGLR 788
Cdd:cd05967 287 hSYIVYGPLLHGATTVLYEgkPVGTPDPGAFWRVIEKYQVNALFTAPTAIRAIRkedpdgkyikKYdLSSLRTLFLAGER 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 789 LAMLSGDWIPVALPdqirarVPglrIVSLGGATEaSIWSIWYPIEQVDPewRSIPYG---RPLTNQSFHVLDAALRPRPD 865
Cdd:cd05967 367 LDPPTLEWAENTLG------VP---VIDHWWQTE-TGWPITANPVGLEP--LPIKAGspgKPVPGYQVQVLDEDGEPVGP 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 866 LVSGELYIGGvGLAVGYLNDRERTAERFV-VHPQTGERLYRTGDLGRYLPDGTIEFLGREDLQVKIRGYRIELAEIEAAL 944
Cdd:cd05967 435 NELGNIVIKL-PLPPGCLLTLWKNDERFKkLYLSKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESV 513
|
....
gi 1860141834 945 GGHP 948
Cdd:cd05967 514 LSHP 517
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
668-948 |
2.82e-12 |
|
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: 69.84 E-value: 2.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 668 ELAYVIHTSGSTGSPKGVMINHRGAVNTVLDINDRFGVGPDDRVLgLSNLGFDLSVYD--VFGPLSVGGAVVlpdPQRRG 745
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYL-IINPFFHTFGYKagIVACLLTGATVV---PVAVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 746 DPSHWADLVGTHGVTVWNSVPAQLQMLHDYLVSATATVpDGLRLAMLSGDWIPVALPDQIRARVPGLRIVSLGGATEASI 825
Cdd:cd17638 77 DVDAILEAIERERITVLPGPPTLFQSLLDHPGRKKFDL-SSLRAAVTGAATVPVELVRRMRSELGFETVLTAYGLTEAGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 826 WSIWYPIEqvDPEWRSIPYGRPLTNQSFHVLDAalrprpdlvsGELYIGGVGLAVGYLNDRERTAERFvvhpqTGERLYR 905
Cdd:cd17638 156 ATMCRPGD--DAETVATTCGRACPGFEVRIADD----------GEVLVRGYNVMQGYLDDPEATAEAI-----DADGWLH 218
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1860141834 906 TGDLGRYLPDGTIEFLGREDLQVKIRGYRIELAEIEAALGGHP 948
Cdd:cd17638 219 TGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHP 261
|
|
| Methyltransf_12 |
pfam08242 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
1197-1284 |
5.35e-12 |
|
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
Pssm-ID: 400515 [Multi-domain] Cd Length: 98 Bit Score: 63.54 E-value: 5.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 1197 VLAALDGYEvdYLATDLSPFFLGELRTRFGDRPGLRLEAVDIDRDLAGQGLsPNSFDVVVAGDVLHASADVGRALDRLRE 1276
Cdd:pfam08242 14 LLEALPGLE--YTGLDISPAALEAARERLAALGLLNAVRVELFQLDLGELD-PGSFDVVVASNVLHHLADPRAVLRNIRR 90
|
....*...
gi 1860141834 1277 VLAPQGWL 1284
Cdd:pfam08242 91 LLKPGGVL 98
|
|
| DCL_NRPS |
cd19543 |
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ... |
109-391 |
6.81e-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: 69.54 E-value: 6.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 109 ELDPERMTAAWRALIARHDMLRAVVEADGAQR----VLAEVpPFEVPVIDLTGRPEAVVDAAVSAVRAEMDHLVHTPDRW 184
Cdd:cd19543 35 PLDPDRFRAAWQAVVDRHPILRTSFVWEGLGEplqvVLKDR-KLPWRELDLSHLSEAEQEAELEALAEEDRERGFDLARA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 185 PLFAARITR-ADHRTVLHVSIDFLIADFISVQVVLDELHRLYH-------RPDEPLPPleitFRDYQ--LAERavrdspR 254
Cdd:cd19543 114 PLMRLTLIRlGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAalgegqpPSLPPVRP----YRDYIawLQRQ------D 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 255 HERDKQWWLARVDELPAAPELPTVAR-PADSEGRFRRWETRLSSQVWEGLRQRAGRHGVSPSGAVLAAFSDTIAAYSRRS 333
Cdd:cd19543 184 KEAAEAYWREYLAGFEEPTPLPKELPaDADGSYEPGEVSFELSAELTARLQELARQHGVTLNTVVQGAWALLLSRYSGRD 263
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1860141834 334 RFTLDITLLNRAPVHDQVNALVGDFTSVDLLAVDADPTRRFDERARDLQAQLWEDLDH 391
Cdd:cd19543 264 DVVFGTTVSGRPAELPGIETMVGLFINTLPVRVRLDPDQTVLELLKDLQAQQLELREH 321
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
556-948 |
1.84e-11 |
|
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: 68.65 E-value: 1.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 556 YAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVDTSQPAARRRTILTNAGIRC------- 628
Cdd:cd05932 9 WGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKAlfvgkld 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 629 --ALTQSGVDRNGWAEGLRLLDV--------DLLGTGQPQPVEGSGDPEELAYVIHTSGSTGSPKGVMINHRGAVNTVLD 698
Cdd:cd05932 89 dwKAMAPGVPEGLISISLPPPSAancqyqwdDLIAQHPPLEERPTRFPEQLATLIYTSGTTGQPKGVMLTFGSFAWAAQA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 699 INDRFGVGPDDRVLGLSNLGFDLSVYDVFGPLSVGGAVV---------LPDPQRR------GDPSHWADLvgTHGvtVWN 763
Cdd:cd05932 169 GIEHIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVafaesldtfVEDVQRArptlffSVPRLWTKF--QQG--VQD 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 764 SVPAQ-LQMLHDY-LVSATA--TVPDGL-----RLAMLSGDWIPVALPDQIRARvpGLRIVSLGGATEASIWSIwypieq 834
Cdd:cd05932 245 KIPQQkLNLLLKIpVVNSLVkrKVLKGLgldqcRLAGCGSAPVPPALLEWYRSL--GLNILEAYGMTENFAYSH------ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 835 vdpewrsipYGRPLTNQSFHVLDAA----LRPRPDlvsGELYIGGVGLAVGYLNDRERTAERFvvhpqTGERLYRTGDLG 910
Cdd:cd05932 317 ---------LNYPGRDKIGTVGNAGpgveVRISED---GEILVRSPALMMGYYKDPEATAEAF-----TADGFLRTGDKG 379
|
410 420 430
....*....|....*....|....*....|....*....
gi 1860141834 911 RYLPDGTIEFLGR-EDLQVKIRGYRIELAEIEAALGGHP 948
Cdd:cd05932 380 ELDADGNLTITGRvKDIFKTSKGKYVAPAPIENKLAEHD 418
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
538-712 |
2.16e-11 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 68.36 E-value: 2.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 538 ALSTPDRPAVVAAD-RTLDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVDTSQPAAR 616
Cdd:PRK07514 12 AFADRDAPFIETPDgLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 617 RRTILTNAGIRCALTQSGvdRNGW---------AEGLRLLDVDLLGT------GQPQPVEG-SGDPEELAYVIHTSGSTG 680
Cdd:PRK07514 92 LDYFIGDAEPALVVCDPA--NFAWlskiaaaagAPHVETLDADGTGSlleaaaAAPDDFETvPRGADDLAAILYTSGTTG 169
|
170 180 190
....*....|....*....|....*....|..
gi 1860141834 681 SPKGVMINHRGAVNTVLDINDRFGVGPDDRVL 712
Cdd:PRK07514 170 RSKGAMLSHGNLLSNALTLVDYWRFTPDDVLI 201
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
1366-1734 |
2.75e-11 |
|
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: 69.12 E-value: 2.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 1366 TDRVRISRDDLTEHLAGRLPQYMVPSVVQVVDALPLNANGKVDRAvlrrrLPRRGTATAAGSSGALDSDLERRIAAVWAE 1445
Cdd:COG1020 922 EAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRL-----ALPAPAAAAAAAAAAPPAEEEEEEAALALL 996
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 1446 ALRLPRVGRDENLFELGGDSLVAAQITGRILEEIPQAAGLFFDQLLRQVLEQPTVAALAGHVEAESATPVTASPSVPATS 1525
Cdd:COG1020 997 LLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLLFLAAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLPPLL 1076
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 1526 GGDGLSPLHEGTDGVPWVLVPGGEGVDAYAGLVPHLAATGPVLGLAPGAADDLLRVAAAQARLVTAAVHPAVRLVGYGLG 1605
Cdd:COG1020 1077 LSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLALLLALLAALRARRAVRQEGPRLRLLVALAAALALAALLAL 1156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 1606 ATSTLEVARSLIETGGQVDAVVLISPWRPAAGADPAAAYRAETGAAGTPGEDFAARLAAVARHEPTLYAGDLVVLRPTGA 1685
Cdd:COG1020 1157 LLAAAAAAAELLAAAALLLLLALLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALAL 1236
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1860141834 1686 VPYDAQSLEFWADLCLGDVRTVDVDADHLTVLGPAAGTALAALDPEPAR 1734
Cdd:COG1020 1237 LLALLALAALLALAALAALAAALLALALALLALALLLLALALLLPALAR 1285
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
528-758 |
4.75e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 67.66 E-value: 4.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 528 GMLHDRVVLQalstPDRPAVVAAD---------RTLDYAELLGRAAGVAEALT---AAGCRrqelVAVVMDRGWEQVVAV 595
Cdd:PRK05850 5 SLLRERASLQ----PDDAAFTFIDyeqdpagvaETLTWSQLYRRTLNVAEELRrhgSTGDR----AVILAPQGLEYIVAF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 596 LGALLAGCVYVPVDTSQPAAR-RRT-----------ILTNAGIRCALTQSGVDRNGWAEGlRLLDVDLLGTGQPQPVE-G 662
Cdd:PRK05850 77 LGALQAGLIAVPLSVPQGGAHdERVsavlrdtspsvVLTTSAVVDDVTEYVAPQPGQSAP-PVIEVDLLDLDSPRGSDaR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 663 SGDPEELAYVIHTSGSTGSPKGVMINHRGA-VNTVLDINDRF----GVGPDDRVLgLSNLGF--DLS-VYDVFGPLSVGG 734
Cdd:PRK05850 156 PRDLPSTAYLQYTSGSTRTPAGVMVSHRNViANFEQLMSDYFgdtgGVPPPDTTV-VSWLPFyhDMGlVLGVCAPILGGC 234
|
250 260
....*....|....*....|....*...
gi 1860141834 735 AVVLPDP----QRrgdPSHWADLVGTHG 758
Cdd:PRK05850 235 PAVLTSPvaflQR---PARWMQLLASNP 259
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
542-975 |
6.37e-11 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 67.09 E-value: 6.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 542 PDRPAVVAADRTLDYAELLGRAAGVAEALTAAGCRRQELVAVVM--DRGWeqVVAVLGALLAGCVYVPVDTSQPAARRRT 619
Cdd:PRK13382 57 PDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCrnHRGF--VEALLAANRIGADILLLNTSFAGPALAE 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 620 ILTNAGIRCALTQ----SGVDRN-----------GWAEGLRLLDVDLLGTG----QPQPVEGSGDpeelaYVIHTSGSTG 680
Cdd:PRK13382 135 VVTREGVDTVIYDeefsATVDRAladcpqatrivAWTDEDHDLTVEVLIAAhagqRPEPTGRKGR-----VILLTSGTTG 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 681 SPKGVMINHRGAVNTVLDINDR---------FGVGPDDRVLGLSNLGFdlsvydvfgPLSVGGAVVLpdpQRRGDPSHWA 751
Cdd:PRK13382 210 TPKGARRSGPGGIGTLKAILDRtpwraeeptVIVAPMFHAWGFSQLVL---------AASLACTIVT---RRRFDPEATL 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 752 DLVGTHGVTVWNSVPAQLqmlhDYLVSATATVPD-----GLRLAMLSGDWIPvalPDQIRARVP--GLRIVSLGGATEAS 824
Cdd:PRK13382 278 DLIDRHRATGLAVVPVMF----DRIMDLPAEVRNrysgrSLRFAAASGSRMR---PDVVIAFMDqfGDVIYNNYNATEAG 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 825 IWSIWYPieqvdPEWRSIP--YGRPLTNQSFHVLDAALRPRPDLVSGELYIGGVGLAVGYLNDRERtaerfvvhpQTGER 902
Cdd:PRK13382 351 MIATATP-----ADLRAAPdtAGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGYTSGSTK---------DFHDG 416
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1860141834 903 LYRTGDLGRYLPDGTIEFLGREDLQVKIRGYRIELAEIEAALGGHPAVAGAVVVVDGDTPLERRLAAFVEPAG 975
Cdd:PRK13382 417 FMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKP 489
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
1371-1412 |
1.31e-10 |
|
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: 65.63 E-value: 1.31e-10
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1860141834 1371 ISRDDLTEHLAGRLPQYMVPSVVQVVDALPLNANGKVDRAVL 1412
Cdd:cd05930 403 LDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| C_PKS-NRPS |
cd19532 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
110-322 |
1.37e-10 |
|
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: 65.56 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 110 LDPERMTAAWRALIARHDMLRA---VVEADGA--QRVLAEvPPFEVPVIDLTGRPEavvdaavsaVRAEMDHLVHTpdRW 184
Cdd:cd19532 36 LDVARLERAVRAVGQRHEALRTcffTDPEDGEpmQGVLAS-SPLRLEHVQISDEAE---------VEEEFERLKNH--VY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 185 PLFAARITRAdhrTVLHVSID---FLIA------DFISVQVVLDELHRLYHRPdePLPPLEITFRDYQLAERAVRDSPRH 255
Cdd:cd19532 104 DLESGETMRI---VLLSLSPTehyLIFGyhhiamDGVSFQIFLRDLERAYNGQ--PLLPPPLQYLDFAARQRQDYESGAL 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1860141834 256 ERDKQWWLARVDELPAAPEL----PTVARPADSEGRFRRWETRLSSQVWEGLRQRAGRHGVSPSGAVLAAF 322
Cdd:cd19532 179 DEDLAYWKSEFSTLPEPLPLlpfaKVKSRPPLTRYDTHTAERRLDAALAARIKEASRKLRVTPFHFYLAAL 249
|
|
| EntF2 |
COG3319 |
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ... |
938-1728 |
2.81e-10 |
|
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442548 [Multi-domain] Cd Length: 855 Bit Score: 65.49 E-value: 2.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 938 AEIEAALGGHPAVAGAVVVVDGDTPLERRLAAFVEPAGRPVTAAQAEHDQAALRQLGVDACVDADSTLTGVDRERYLAYA 1017
Cdd:COG3319 2 AAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALLLLAAALLVALAALALAALALAALLAVALLAAALALAALAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 1018 HRLDDVALPAMVDAFRAAGLFAAGSRHPLADLLDTAHVASRHHRLVRRWLRALTDAGLLDRDTDGRYGLTPAGAAADTDA 1097
Cdd:COG3319 82 AALALALAAAAAALLLAALALLLALLAALALALLALLLAALLLALAALAAAAAAAALAAAAAAAAALAAAAGLGGGGGGA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 1098 GWREVEQLADAEDRELLDYFRASTAHLPALLRGEDDPLALLFPQGRVDVSQGLYERTLFNRWANEAAAALVRRIAEQRIE 1177
Cdd:COG3319 162 GVLVLVLAALLALLLAALLALALALAALLLLALAAALALALLLLLALLLLLLLLLALLLLLLLALLAAAALLALLLALLL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 1178 PGALRVLEVGAGAGGTTAAVLAALDGYEVDYLATDLSPFFLGELRTRFGDRPGLRLEAVDIDRDLAGQGLSPNSFDVVVA 1257
Cdd:COG3319 242 LLLAALLLLLALALLLLLALLLLLGLLALLLALLLLLALLLLAAAAALAAGGTATTAAVTTTAAAAAPGVAGALGPIGGG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 1258 GDVLHASADVGRALDRLREVLAPQGWLVACEMTRDHHQIMTSLELLVRVDEATADFTDLRRGTEQVFLDRRSWLEVLGAA 1337
Cdd:COG3319 322 PGLLVLLVLLVLLLPLLLGVGGGGGGGGGGGGAGGLAGRGLRAAAALRDPAGAGARGRLRRGGDRGRRLGGGLLLGLGRL 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 1338 GAAQPLCLPEPDGFIAELGMCVLAARFKTDRVRISRDDLTEHLAGRLPQYMVPSVVQVVDALPLNANGKVDRAVLRRRLP 1417
Cdd:COG3319 402 RLQRLRRGLREELEEAEAALAEAAAVAAAVAAAAAAAAAAAALAAAVVAAAALAAAALLLLLLLLLLPPPLPPALLLLLL 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 1418 RRGTATAAGSSGALDSDLERRIAAVWAEALRLPRVGRDENLFELGGDSLVAAQITGRILEEIPQAAGLFFDQLLRQVLEQ 1497
Cdd:COG3319 482 LLLLLLLAALLLAAAAPAAAAAAAAAPAPAAALELALALLLLLLLGLGLVGDDDDFFGGGGGSLLALLLLLLLLALLLRL 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 1498 PTVAALAGHVEAESATPVTASPSvpATSGGDGLSPLHEGTDGVPWVLVPGGEG-VDAYAGLVPHLAATGPVLGLAPGAAD 1576
Cdd:COG3319 562 LLLLALLLAPTLAALAAALAAAA--AAAALSPLVPLRAGGSGPPLFCVHPAGGnVLCYRPLARALGPDRPVYGLQAPGLD 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 1577 D----LLRVAAAQARLVTA--AVHPA--VRLVGYGLGATSTLEVARSLIETGGQVDAVVLI------------------- 1629
Cdd:COG3319 640 GgeppPASVEEMAARYVEAirAVQPEgpYHLLGWSFGGLVAYEMARQLEAQGEEVALLVLLdsyapgalarldeaellaa 719
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 1630 ---------------SPWRPAAGADPAAAYRAETGAAGTPG-----------EDFAARLAAVARHEPTLYAGDLVVLRPT 1683
Cdd:COG3319 720 llrdlargvdlpldaEELRALDPEERLARLLERLREAGLPAgldaerlrrllRVFRANLRALRRYRPRPYDGPVLLFRAE 799
|
810 820 830 840
....*....|....*....|....*....|....*....|....*.
gi 1860141834 1684 GAVPYDAQ-SLEFWADLCLGDVRTVDVDADHLTVLGPAAGTALAAL 1728
Cdd:COG3319 800 EDPPGRADdPALGWRPLVAGGLEVHDVPGDHFSMLREPHVAELAAA 845
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
666-941 |
8.36e-10 |
|
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: 63.28 E-value: 8.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 666 PEELAYVIHTSGSTGSPKGVMINHRGAVNTVLDINDRFGVGPDDRVLGLSNLGFDLSVYDV-FGPLSVG-GAVVLPDPQR 743
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFhLAPLIAGmNQYLMPTRLF 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 744 RGDPSHWADLVGTHGVTVWNSVPAQLQMLHDYLVSATATVPD--GLRLAMLSGDWIPVALPDQI--RARVPGLR---IVS 816
Cdd:cd05908 185 IRRPILWLKKASEHKATIVSSPNFGYKYFLKTLKPEKANDWDlsSIRMILNGAEPIDYELCHEFldHMSKYGLKrnaILP 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 817 LGGATEASI--------------------WSIWYPIEQVDPE----WRSIPYGRPLTNQSFHVLDAALRPRPDLVSGELY 872
Cdd:cd05908 265 VYGLAEASVgaslpkaqspfktitlgrrhVTHGEPEPEVDKKdsecLTFVEVGKPIDETDIRICDEDNKILPDGYIGHIQ 344
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1860141834 873 IGGVGLAVGYLNDRERTAERFvvhpqTGERLYRTGDLGrYLPDGTIEFLGREDLQVKIRGYRIELAEIE 941
Cdd:cd05908 345 IRGKNVTPGYYNNPEATAKVF-----TDDGWLKTGDLG-FIRNGRLVITGREKDIIFVNGQNVYPHDIE 407
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
525-923 |
9.20e-10 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 63.49 E-value: 9.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 525 VPAGMLhDRVVLQALSTPDRPAVVAADRT--LDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAG 602
Cdd:PRK05857 12 LPSTVL-DRVFEQARQQPEAIALRRCDGTsaLRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 603 CVYVPVDTSQPAAR--RRTILTNAGIRCALTQSGVDRNGWAEGLRLLDVDLLGTGQ-------------PQPVEGSGDPE 667
Cdd:PRK05857 91 AIAVMADGNLPIAAieRFCQITDPAAALVAPGSKMASSAVPEALHSIPVIAVDIAAvtresehsldaasLAGNADQGSED 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 668 ELAyVIHTSGSTGSPKGVMINHRgAVNTVLDINDRFGVGPDDRVLGLSnlgfdlsvydVFGPLS---VGGAVVLPDPQRR 744
Cdd:PRK05857 171 PLA-MIFTSGTTGEPKAVLLANR-TFFAVPDILQKEGLNWVTWVVGET----------TYSPLPathIGGLWWILTCLMH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 745 G--------DPSHWADLVGTHGVTVWNSVPAQLQMLHDYLVSATATVPdGLRLAMLSGDWIPVALPDQIRArvPGLRIVS 816
Cdd:PRK05857 239 GglcvtggeNTTSLLEILTTNAVATTCLVPTLLSKLVSELKSANATVP-SLRLVGYGGSRAIAADVRFIEA--TGVRTAQ 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 817 LGGATEASIWSIWYPIEQVD-PEWRSIPYGRPLTNQSFHVLDA------ALRPRPDLVSGELYIGGVGLAVGYLNDRERT 889
Cdd:PRK05857 316 VYGLSETGCTALCLPTDDGSiVKIEAGAVGRPYPGVDVYLAATdgigptAPGAGPSASFGTLWIKSPANMLGYWNNPERT 395
|
410 420 430
....*....|....*....|....*....|....
gi 1860141834 890 AERFVvhpqtgERLYRTGDLGRYLPDGTIEFLGR 923
Cdd:PRK05857 396 AEVLI------DGWVNTGDLLERREDGFFYIKGR 423
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
542-948 |
9.45e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 63.43 E-value: 9.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 542 PDRPAVVAADRTLDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVDTSQPAARRRTIL 621
Cdd:PRK08162 32 PDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFML 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 622 TNAGIRCALTQ---SGVDRNGWAE--GLRLL--DVDLLGTGQPQPVE--------GSGDPE-------------ELAYvi 673
Cdd:PRK08162 112 RHGEAKVLIVDtefAEVAREALALlpGPKPLviDVDDPEYPGGRFIGaldyeaflASGDPDfawtlpadewdaiALNY-- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 674 hTSGSTGSPKGVMINHRGA----VNTVLDindrFGVGPddRVLGLSNL--------GFDLSVydvfgPLSVGGAVVLpdp 741
Cdd:PRK08162 190 -TSGTTGNPKGVVYHHRGAylnaLSNILA----WGMPK--HPVYLWTLpmfhcngwCFPWTV-----AARAGTNVCL--- 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 742 qRRGDPSHWADLVGTHGVTVWNSVPAQLQMlhdyLVSATATVPDGLR---LAMLSGDWIPVALPDQIRARvpGLRIVSLG 818
Cdd:PRK08162 255 -RKVDPKLIFDLIREHGVTHYCGAPIVLSA----LINAPAEWRAGIDhpvHAMVAGAAPPAAVIAKMEEI--GFDLTHVY 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 819 GATEasiwsIWYPIEQV--DPEWRSIPYGRPLTNQS-----FHVLDAA-------LRPRPD--LVSGELYIGGVGLAVGY 882
Cdd:PRK08162 328 GLTE-----TYGPATVCawQPEWDALPLDERAQLKArqgvrYPLQEGVtvldpdtMQPVPAdgETIGEIMFRGNIVMKGY 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1860141834 883 LNDRERTAERFvvhpQTGerLYRTGDLGRYLPDGTIeflgredlQVKIR--------GYRIELAEIEAALGGHP 948
Cdd:PRK08162 403 LKNPKATEEAF----AGG--WFHTGDLAVLHPDGYI--------KIKDRskdiiisgGENISSIEVEDVLYRHP 462
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
526-980 |
1.32e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 63.02 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 526 PAGMLhdrVVLQALSTPDRPAVVAADRTLDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCvy 605
Cdd:PRK07788 50 PFAGL---VAHAARRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGA-- 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 606 vpvdtsqpaarrRTILTNAGIRCALTQSGVDRNG---------WAEGLRLLDVDL------LGTGQPQPVEGSGDP--EE 668
Cdd:PRK07788 125 ------------RIILLNTGFSGPQLAEVAAREGvkalvyddeFTDLLSALPPDLgrlrawGGNPDDDEPSGSTDEtlDD 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 669 LA----------------YVIHTSGSTGSPKGVMINHRGAVNTVLDINDR--FGVG-------PDDRVLGLSNLGfdLSv 723
Cdd:PRK07788 193 LIagsstaplpkppkpggIVILTSGTTGTPKGAPRPEPSPLAPLAGLLSRvpFRAGettllpaPMFHATGWAHLT--LA- 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 724 ydvfgpLSVGGAVVLpdpQRRGDPSHWADLVGTHGVTVWNSVPAQLQMLHDyLVSATATVPD--GLRLAMLSGDwipvAL 801
Cdd:PRK07788 270 ------MALGSTVVL---RRRFDPEATLEDIAKHKATALVVVPVMLSRILD-LGPEVLAKYDtsSLKIIFVSGS----AL 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 802 PDQIRARVP---GLRIVSLGGATEASIWSIWYPieqvdPEWRSIP--YGRPLTNQSFHVLDAALRPRPDLVSGELYIGGV 876
Cdd:PRK07788 336 SPELATRALeafGPVLYNLYGSTEVAFATIATP-----EDLAEAPgtVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNG 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 877 GLAVGYLNDRertaerfvvHPQTGERLYRTGDLGRYLPDGTIEFLGREDLQVKIRGYRIELAEIEAALGGHPAVAGAVVV 956
Cdd:PRK07788 411 FPFEGYTDGR---------DKQIIDGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVI 481
|
490 500
....*....|....*....|....*
gi 1860141834 957 VDGDTPLERRLAAFVEPA-GRPVTA 980
Cdd:PRK07788 482 GVDDEEFGQRLRAFVVKApGAALDE 506
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
507-690 |
1.33e-09 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 62.97 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 507 PPEATRDRRAE-----TNRTQ-APVPAGMLhDRVVLQALSTPDRPAVVAAD-----RTLDYAELLGRAAGVAEALTAAGC 575
Cdd:PRK08180 13 PPAVEVERRADgtiylRSAEPlGDYPRRLT-DRLVHWAQEAPDRVFLAERGadggwRRLTYAEALERVRAIAQALLDRGL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 576 RRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVD-----TSQPAARRRTILT---------------NAGIRcALTQSGV 635
Cdd:PRK08180 92 SAERPLMILSGNSIEHALLALAAMYAGVPYAPVSpayslVSQDFGKLRHVLElltpglvfaddgaafARALA-AVVPADV 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1860141834 636 D---RNGWAEGLRLLDV-DLLGTGQPQPVEGSGD---PEELAYVIHTSGSTGSPKGVMINHR 690
Cdd:PRK08180 171 EvvaVRGAVPGRAATPFaALLATPPTAAVDAAHAavgPDTIAKFLFTSGSTGLPKAVINTHR 232
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
551-948 |
2.13e-09 |
|
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: 62.19 E-value: 2.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 551 DRTLDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVL-----GAL------------LAGCVyvpVDtsqp 613
Cdd:cd05966 82 SRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLacariGAVhsvvfagfsaesLADRI---ND---- 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 614 aARRRTILT-NAGIR------------CALTQSG-------VDRNG----WAEGlRLLDVDLLGTGQPQPVEG-SGDPEE 668
Cdd:cd05966 155 -AQCKLVITaDGGYRggkviplkeivdEALEKCPsvekvlvVKRTGgevpMTEG-RDLWWHDLMAKQSPECEPeWMDSED 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 669 LAYVIHTSGSTGSPKGVMinHR------GAVNT---VLDI--NDRFGVGPD-DRVLGLSnlgfdlsvYDVFGPLSVGGAV 736
Cdd:cd05966 233 PLFILYTSGSTGKPKGVV--HTtggyllYAATTfkyVFDYhpDDIYWCTADiGWITGHS--------YIVYGPLANGATT 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 737 VL----PD-PqrrgDPSHWADLVGTHGVTVWnsvpaqlqmlhdYlvsataTVPDGLRLAMLSGDWIPVALPDQirarvpG 811
Cdd:cd05966 303 VMfegtPTyP----DPGRYWDIVEKHKVTIF------------Y------TAPTAIRALMKFGDEWVKKHDLS------S 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 812 LRIV-SLGGATEASIWsIWY---------PIeqVDPEWRS---------IP---------YGRPLTNQSFHVLDAALRPR 863
Cdd:cd05966 355 LRVLgSVGEPINPEAW-MWYyevigkercPI--VDTWWQTetggimitpLPgatplkpgsATRPFFGIEPAILDEEGNEV 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 864 PDLVSGELYIGGV--GLAVGYLNDRERTAER-FVVHPQtgerLYRTGDLGRYLPDGTIEFLGREDLQVKIRGYRIELAEI 940
Cdd:cd05966 432 EGEVEGYLVIKRPwpGMARTIYGDHERYEDTyFSKFPG----YYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEV 507
|
....*...
gi 1860141834 941 EAALGGHP 948
Cdd:cd05966 508 ESALVAHP 515
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
1359-1423 |
2.91e-09 |
|
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: 61.36 E-value: 2.91e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1860141834 1359 VLAARFKTDRVRISRDDLTEHLAGRLPQYMVPSVVQVVDALPLNANGKVDRAVLRRRLPRRGTAT 1423
Cdd:COG0318 388 VVAFVVLRPGAELDAEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRERYAAGALEA 452
|
|
| C_NRPS-like |
cd19537 |
Condensation family domain with an atypical active site motif; Condensation (C) domains of ... |
108-350 |
4.66e-09 |
|
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: 60.66 E-value: 4.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 108 PELDPERMTAAWRALIARHDMLRA--VVEADGAQRVLAEVPP--FEVPVIDLTG---RPEavvdaavsavRAEMDHLVht 180
Cdd:cd19537 34 GDVDRDRLASAWNTVLARHRILRSryVPRDGGLRRSYSSSPPrvQRVDTLDVWKeinRPF----------DLEREDPI-- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 181 pdrwplfaaRITRAdHRTVLhVSIDFLIADFISVQVVLDELHRLYHRpdEPLPPLEitfRDYQlaeravrDSPRHER--- 257
Cdd:cd19537 102 ---------RVFIS-PDTLL-VVMSHIICDLTTLQLLLREVSAAYNG--KLLPPVR---REYL-------DSTAWSRpas 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 258 --DKQWWLARVDELPAAPeLPTVARPADSEGRFRRWetRLSSQVWEGLRQRAGRHGVSPSGAVLAAFSDTIAAYSRRSrf 335
Cdd:cd19537 159 peDLDFWSEYLSGLPLLN-LPRRTSSKSYRGTSRVF--QLPGSLYRSLLQFSTSSGITLHQLALAAVALALQDLSDRT-- 233
|
250
....*....|....*....
gi 1860141834 336 tlDITL----LNRAPVHDQ 350
Cdd:cd19537 234 --DIVLgapyLNRTSEEDM 250
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
551-948 |
5.16e-09 |
|
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: 60.83 E-value: 5.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 551 DRTLDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVyvpvdtsqpAARRRTILTNAGIRCAL 630
Cdd:cd05940 1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAV---------AALINYNLRGESLAHCL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 631 TQSGVdrngwaeglRLLDVDllgtgqpqpvegsgdpeeLAYVIHTSGSTGSPKGVMINHRGAVNTVLDINDRFGVGPDDR 710
Cdd:cd05940 72 NVSSA---------KHLVVD------------------AALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGGALPSDV 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 711 V-----LGLSNLGfdlsVYDVFGPLSVGGAVVLpdpQRRGDPSHWADLVGTHGVTVWNSVPAQLQmlhdYLVSATATVPD 785
Cdd:cd05940 125 LytclpLYHSTAL----IVGWSACLASGATLVI---RKKFSASNFWDDIRKYQATIFQYIGELCR----YLLNQPPKPTE 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 786 -GLRLAMLSGDWIPVALPDQIRARVPGLRIVSLGGATEASIWSIWYP--------------------IEQVDPEwrsipY 844
Cdd:cd05940 194 rKHKVRMIFGNGLRPDIWEEFKERFGVPRIAEFYAATEGNSGFINFFgkpgaigrnpsllrkvaplaLVKYDLE-----S 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 845 GRPLTNQsfhvlDAALRPRPDLVSGEL--YIGGVGLAVGYLNDRERTAERFVVHPQTGERLYRTGDLGRYLPDGTIEFLG 922
Cdd:cd05940 269 GEPIRDA-----EGRCIKVPRGEPGLLisRINPLEPFDGYTDPAATEKKILRDVFKKGDAWFNTGDLMRLDGEGFWYFVD 343
|
410 420
....*....|....*....|....*.
gi 1860141834 923 REDLQVKIRGYRIELAEIEAALGGHP 948
Cdd:cd05940 344 RLGDTFRWKGENVSTTEVAAVLGAFP 369
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
566-948 |
5.54e-09 |
|
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: 60.94 E-value: 5.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 566 VAEALT-AAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPvDTSQ----------PAARRRTILTN----------- 623
Cdd:cd05928 54 AANVLSgACGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIP-GTIQltakdilyrlQASKAKCIVTSdelapevdsva 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 624 ---AGIRCALTQSGVDRNGWaeglrlLDV-DLLGTGQPQPV---EGSGDPEELAYvihTSGSTGSPKgvMINH-RGAVNT 695
Cdd:cd05928 133 secPSLKTKLLVSEKSRDGW------LNFkELLNEASTEHHcveTGSQEPMAIYF---TSGTTGSPK--MAEHsHSSLGL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 696 VLDINDRFGVG--PDDRVLGLSNLGFDLSVY-DVFGPLsVGGAVVLPDPQRRGDPSHWADLVGTHGVTVWNSVPAQLQML 772
Cdd:cd05928 202 GLKVNGRYWLDltASDIMWNTSDTGWIKSAWsSLFEPW-IQGACVFVHHLPRFDPLVILKTLSSYPITTFCGAPTVYRML 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 773 -HDYLVSATATvpdGLRLAMLSGDWIPVALPDQIRARVpGLRIVSLGGATEASIWSIWYPIEQVDPEWR---SIPYGRPL 848
Cdd:cd05928 281 vQQDLSSYKFP---SLQHCVTGGEPLNPEVLEKWKAQT-GLDIYEGYGQTETGLICANFKGMKIKPGSMgkaSPPYDVQI 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 849 TNQSFHVL------DAALRPRPDLvsgelyigGVGLAVGYLNDRERTAERFvvhpqTGErLYRTGDLGRYLPDGTIEFLG 922
Cdd:cd05928 357 IDDNGNVLppgtegDIGIRVKPIR--------PFGLFSGYVDNPEKTAATI-----RGD-FYLTGDRGIMDEDGYFWFMG 422
|
410 420
....*....|....*....|....*.
gi 1860141834 923 REDLQVKIRGYRIELAEIEAALGGHP 948
Cdd:cd05928 423 RADDVINSSGYRIGPFEVESALIEHP 448
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
657-948 |
5.83e-09 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 60.63 E-value: 5.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 657 PQPVEGSGDpeeLAYVIHTSGSTGSPKGVMINHRGAVNTVlDINDRFGV------GPDDRVLGLSNLG--FDLSVYdVFG 728
Cdd:PLN02574 191 PKPVIKQDD---VAAIMYSSGTTGASKGVVLTHRNLIAMV-ELFVRFEAsqyeypGSDNVYLAALPMFhiYGLSLF-VVG 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 729 PLSVGGAVVLpdpQRRGDPSHWADLVGTHGVTVWNSVPAQLQMLHDYLVSATATVPDGLRL-----AMLSGDWIpvalpD 803
Cdd:PLN02574 266 LLSLGSTIVV---MRRFDASDMVKVIDRFKVTHFPVVPPILMALTKKAKGVCGEVLKSLKQvscgaAPLSGKFI-----Q 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 804 QIRARVPGLRIVSLGGATE-ASIWSIWYPIEQVDpEWRSIPYGRPltNQSFHVLD---AALRPRPDlvSGELYIGGVGLA 879
Cdd:PLN02574 338 DFVQTLPHVDFIQGYGMTEsTAVGTRGFNTEKLS-KYSSVGLLAP--NMQAKVVDwstGCLLPPGN--CGELWIQGPGVM 412
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1860141834 880 VGYLNDRERTAERFVvhpqtGERLYRTGDLGRYLPDGTIEFLGREDLQVKIRGYRIELAEIEAALGGHP 948
Cdd:PLN02574 413 KGYLNNPKATQSTID-----KDGWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHP 476
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
1370-1412 |
6.68e-09 |
|
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: 60.34 E-value: 6.68e-09
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1860141834 1370 RISRDDLTEHLAGRLPQYMVPSVVQVVDALPLNANGKVDRAVL 1412
Cdd:cd17652 393 APTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| AcpP |
COG0236 |
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ... |
1433-1512 |
6.76e-09 |
|
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: 54.09 E-value: 6.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 1433 SDLERRIAAVWAEALRLP--RVGRDENLF-ELGGDSLVAAQITGRILE----EIPqaaglffdqlLRQVLEQPTVAALAG 1505
Cdd:COG0236 4 EELEERLAEIIAEVLGVDpeEITPDDSFFeDLGLDSLDAVELIAALEEefgiELP----------DTELFEYPTVADLAD 73
|
....*..
gi 1860141834 1506 HVEAESA 1512
Cdd:COG0236 74 YLEEKLA 80
|
|
| UbiE |
COG2226 |
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ... |
1156-1300 |
7.23e-09 |
|
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG is part of the Pathway/BioSystem: Biotin biosynthesis
Pssm-ID: 441828 [Multi-domain] Cd Length: 143 Bit Score: 56.16 E-value: 7.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 1156 FNRWAN--EAAAALVRRIAEQriePGAlRVLEVGAGAGGttaaVLAALDGYEVDYLATDLSPFFLGELRTRFGDRpGLRL 1233
Cdd:COG2226 1 FDRVAAryDGREALLAALGLR---PGA-RVLDLGCGTGR----LALALAERGARVTGVDISPEMLELARERAAEA-GLNV 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1860141834 1234 EAVDID-RDLAgqgLSPNSFDVVVAGDVLHASADVGRALDRLREVLAPQGWLVACEMTRDHHQIMTSL 1300
Cdd:COG2226 72 EFVVGDaEDLP---FPDGSFDLVISSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSPPDLAELEEL 136
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
1371-1412 |
8.12e-09 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.
Pssm-ID: 341280 [Multi-domain] Cd Length: 447 Bit Score: 60.02 E-value: 8.12e-09
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1860141834 1371 ISRDDLTEHLAGRLPQYMVPSVVQVVDALPLNANGKVDRAVL 1412
Cdd:cd12115 406 GLVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
1367-1412 |
1.08e-08 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 59.61 E-value: 1.08e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1860141834 1367 DRVRISRDDLTEHLAGRLPQYMVPSVVQVVDALPLNANGKVDRAVL 1412
Cdd:cd12116 425 AGAAPDAAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
540-948 |
1.14e-08 |
|
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: 59.85 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 540 STPDRPAVVAADRTLD--YAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVDT------- 610
Cdd:cd17642 29 SVPGTIAFTDAHTGVNysYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDiynerel 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 611 ------SQPA---ARRRTILTNAGIRCALTqsgvdrngWAEGLRLLD--VDLLGTGQPQPVEGSGDP------------- 666
Cdd:cd17642 109 dhslniSKPTivfCSKKGLQKVLNVQKKLK--------IIKTIIILDskEDYKGYQCLYTFITQNLPpgfneydfkppsf 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 667 ---EELAYVIHTSGSTGSPKGVMINHRGAVNTVLDIND-RFG--VGPDDRVLGLSNLGFDLSVYDVFGPLSVGGAVVLPd 740
Cdd:cd17642 181 drdEQVALIMNSSGSTGLPKGVQLTHKNIVARFSHARDpIFGnqIIPDTAILTVIPFHHGFGMFTTLGYLICGFRVVLM- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 741 pqrrgdPSHWADLVgthgvtvwnsvpaqLQMLHDYLVSATATVP---------------DGLRLAMLSGDWIPVA--LPD 803
Cdd:cd17642 260 ------YKFEEELF--------------LRSLQDYKVQSALLVPtlfaffakstlvdkyDLSNLHEIASGGAPLSkeVGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 804 QIRAR--VPGLRivsLG-GATEASIWSIWYPIEQVDPEwrsiPYGRPLTNQSFHVLD----AALRPRPdlvSGELYIGGV 876
Cdd:cd17642 320 AVAKRfkLPGIR---QGyGLTETTSAILITPEGDDKPG----AVGKVVPFFYAKVVDldtgKTLGPNE---RGELCVKGP 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1860141834 877 GLAVGYLNDRERTAERFVvhpqtGERLYRTGDLGRYLPDGTIEFLGREDLQVKIRGYRIELAEIEAALGGHP 948
Cdd:cd17642 390 MIMKGYVNNPEATKALID-----KDGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHP 456
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
514-690 |
1.27e-08 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 59.89 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 514 RRAETNRTQAPVPAGMLHDRVVLQALSTPDRPAVVAADRTLDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVV 593
Cdd:PRK08279 23 RGLKRTALITPDSKRSLGDVFEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 594 AVLGALLAGCVYVPVDTSQP---------AARRRTILTNAGIRCALTQSGVDRNG----WAEG-------LRLLDVDLLG 653
Cdd:PRK08279 103 AWLGLAKLGAVVALLNTQQRgavlahslnLVDAKHLIVGEELVEAFEEARADLARpprlWVAGgdtlddpEGYEDLAAAA 182
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1860141834 654 TGQPQ--PVEGSGDP-EELAYVIHTSGSTGSPKGVMINHR 690
Cdd:PRK08279 183 AGAPTtnPASRSGVTaKDTAFYIYTSGTTGLPKAAVMSHM 222
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
542-948 |
1.38e-08 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 59.63 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 542 PDRPAVVAADRTLDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYV---PV---------- 608
Cdd:PRK05605 46 GDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVehnPLytahelehpf 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 609 -----------DTSQPAARR-------RTI----LTNA-----------------GIRCALTQSGVDRNGWAeglRLLDV 649
Cdd:PRK05605 126 edhgarvaivwDKVAPTVERlrrttplETIvsvnMIAAmpllqrlalrlpipalrKARAALTGPAPGTVPWE---TLVDA 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 650 DLLGTGQPQPVEgSGDPEELAYVIHTSGSTGSPKGVMINHRGAVNTVL-------DINDRfgvgpDDRVLGLSNL--GFD 720
Cdd:PRK05605 203 AIGGDGSDVSHP-RPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAqgkawvpGLGDG-----PERVLAALPMfhAYG 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 721 LSVYDVFGPlSVGGAVVL-PDPqrrgDPSHWADLVGTHGVTVWNSVPAqlqmLHDYLVSATAT--VP-DGLRLAmLSGdw 796
Cdd:PRK05605 277 LTLCLTLAV-SIGGELVLlPAP----DIDLILDAMKKHPPTWLPGVPP----LYEKIAEAAEErgVDlSGVRNA-FSG-- 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 797 iPVALPDQIRAR---VPGLRIVSLGGATEASiwsiwyPIEQVDP--EWRSIPY-GRPLTNQSFHVLDA--ALRPRPDLVS 868
Cdd:PRK05605 345 -AMALPVSTVELwekLTGGLLVEGYGLTETS------PIIVGNPmsDDRRPGYvGVPFPDTEVRIVDPedPDETMPDGEE 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 869 GELYIGGVGLAVGYLNDRERTAERFvvHPQtgerLYRTGDLGRYLPDGTIEFLGREDLQVKIRGYRIELAEIEAALGGHP 948
Cdd:PRK05605 418 GELLVRGPQVFKGYWNRPEETAKSF--LDG----WFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHP 491
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
672-948 |
1.90e-08 |
|
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: 58.08 E-value: 1.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 672 VIHTSGSTGSPKGVMINHRG--AVNTVL----DINDRFG---VGPddrvlgLSNLGFDLSVYDVFgplSVGGAVVLpdpQ 742
Cdd:cd17636 5 AIYTAAFSGRPNGALLSHQAllAQALVLavlqAIDEGTVflnSGP------LFHIGTLMFTLATF---HAGGTNVF---V 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 743 RRGDPSHWADLVGTHGVT-VWNSVPAQLQMLHdyLVSATATVPDGLRLAMLSGDWIPVALPDqiraRVPGLRIVSLGGAT 821
Cdd:cd17636 73 RRVDAEEVLELIEAERCThAFLLPPTIDQIVE--LNADGLYDLSSLRSSPAAPEWNDMATVD----TSPWGRKPGGYGQT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 822 EAS-IWSI-WYPIEQVDpewrsiPYGRPLTNQSFHVLDAALRPRPDLVSGELYIGGVGLAVGYLNDRERTAERFVvhpqt 899
Cdd:cd17636 147 EVMgLATFaALGGGAIG------GAGRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTR----- 215
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1860141834 900 gERLYRTGDLGRYLPDGTIEFLGREDLQVKIRGYRIELAEIEAALGGHP 948
Cdd:cd17636 216 -GGWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHP 263
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
1368-1412 |
2.16e-08 |
|
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: 58.75 E-value: 2.16e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1860141834 1368 RVRISRDDLTEHLAGRLPQYMVPSVVQVVDALPLNANGKVDRAVL 1412
Cdd:cd12117 439 EGALDAAELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| E_NRPS |
cd19534 |
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
108-371 |
2.17e-08 |
|
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: 58.42 E-value: 2.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 108 PELDPERMTAAWRALIARHDMLRAVV-EADGA--QRVLAEVP-PFEVPVIDLTGRPEAVVDAAVSAVRAE-MDhlvhtPD 182
Cdd:cd19534 32 QGLDPDALRQALRALVEHHDALRMRFrREDGGwqQRIRGDVEeLFRLEVVDLSSLAQAAAIEALAAEAQSsLD-----LE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 183 RWPLFAAR-ITRADHRTVLHVSIDFLIADFISVQVVLDELHRLYHRPDE----PLPPLeITFRDY--QLAERAVRDSPRH 255
Cdd:cd19534 107 EGPLLAAAlFDGTDGGDRLLLVIHHLVVDGVSWRILLEDLEAAYEQALAgepiPLPSK-TSFQTWaeLLAEYAQSPALLE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 256 ERDkqWWLARVDELPAapELPtvARPADSEGRFRRWETRLSSQVWEGLRQRA-GRHGVSPSGAVLAAFSDTIAAYSRRSR 334
Cdd:cd19534 186 ELA--YWRELPAADYW--GLP--KDPEQTYGDARTVSFTLDEEETEALLQEAnAAYRTEINDLLLAALALAFQDWTGRAP 259
|
250 260 270
....*....|....*....|....*....|....*....
gi 1860141834 335 FTLDITLLNRAPVHDQVN--ALVGDFTSVDLLAVDADPT 371
Cdd:cd19534 260 PAIFLEGHGREEIDPGLDlsRTVGWFTSMYPVVLDLEAS 298
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
552-948 |
2.46e-08 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 58.86 E-value: 2.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 552 RTLDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVP-------------VDT-------S 611
Cdd:PRK09192 48 EALPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPlplpmgfggresyIAQlrgmlasA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 612 QPAArrrtILTNAGIRcALTQSGVDRNGWAEGLRLLDVDLL---GTGQPQPvegsgDPEELAYVIHTSGSTGSPKGVMIN 688
Cdd:PRK09192 128 QPAA----IITPDELL-PWVNEATHGNPLLHVLSHAWFKALpeaDVALPRP-----TPDDIAYLQYSSGSTRFPRGVIIT 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 689 HRGAV-NTVLDINDRFGVGPDDRV---------LGLsnLGFDLSvydvfgPLSVGGAV-VLP--DPQRRgdPSHWADLVG 755
Cdd:PRK09192 198 HRALMaNLRAISHDGLKVRPGDRCvswlpfyhdMGL--VGFLLT------PVATQLSVdYLPtrDFARR--PLQWLDLIS 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 756 THGVTVWNSVP---------AQLQMLHDYLVSAtatvpdgLRLAMLSGDWIPvalPDQIRARVPglRIVSLG-------- 818
Cdd:PRK09192 268 RNRGTISYSPPfgyelcarrVNSKDLAELDLSC-------WRVAGIGADMIR---PDVLHQFAE--AFAPAGfddkafmp 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 819 --GATEASIWSIWYPIEQ------------------VDPEWRSIPY------GRPLTNQSFHVLDAALRPRPDLVSGELY 872
Cdd:PRK09192 336 syGLAEATLAVSFSPLGSgivveevdrdrleyqgkaVAPGAETRRVrtfvncGKALPGHEIEIRNEAGMPLPERVVGHIC 415
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1860141834 873 IGGVGLAVGYLNDRERTAERFVvhpqTGerLYRTGDLGrYLPDGTIEFLGREDLQVKIRGYRIELAEIEAALGGHP 948
Cdd:PRK09192 416 VRGPSLMSGYFRDEESQDVLAA----DG--WLDTGDLG-YLLDGYLYITGRAKDLIIINGRNIWPQDIEWIAEQEP 484
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
537-941 |
2.48e-08 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 59.41 E-value: 2.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 537 QALSTPDRPAV-VAAD-----RTLDYAELLGRAAGVAEALTAAGCRRQELVaVVMDRGWEQVVAVLGALLAGCVYVPV-- 608
Cdd:PRK05691 18 RAAQTPDRLALrFLADdpgegVVLSYRDLDLRARTIAAALQARASFGDRAV-LLFPSGPDYVAAFFGCLYAGVIAVPAyp 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 609 -DTSQPA-----------ARRRTILTNAGIRCALTQSGVDRNGWAEGLrlLDVDLLgtgQPQPVEG----SGDPEELAYV 672
Cdd:PRK05691 97 pESARRHhqerllsiiadAEPRLLLTVADLRDSLLQMEELAAANAPEL--LCVDTL---DPALAEAwqepALQPDDIAFL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 673 IHTSGSTGSPKGVMINHRGAVNTVLDINDRFG--VGPDDRVLGLSNLGFDLS-VYDVFGPLSVGGAVVLPDPQR-RGDPS 748
Cdd:PRK05691 172 QYTSGSTALPKGVQVSHGNLVANEQLIRHGFGidLNPDDVIVSWLPLYHDMGlIGGLLQPIFSGVPCVLMSPAYfLERPL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 749 HWADLVGTHGVT---------------VWNSVPAQLQmLHDYLVSATATVP---DGLRLamLSGDWIPVAL-PDQIRARV 809
Cdd:PRK05691 252 RWLEAISEYGGTisggpdfayrlcserVSESALERLD-LSRWRVAYSGSEPirqDSLER--FAEKFAACGFdPDSFFASY 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 810 pGLRIVSL---GGATEASIwsiwyPIEQVDPEW----RSIP-YGRPLTNQSFHVLDAALR---PR-----PDLVSGELYI 873
Cdd:PRK05691 329 -GLAEATLfvsGGRRGQGI-----PALELDAEAlarnRAEPgTGSVLMSCGRSQPGHAVLivdPQslevlGDNRVGEIWA 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1860141834 874 GGVGLAVGYLNDRERTAERFVVHpqTGERLYRTGDLGrYLPDGTIEFLGREDLQVKIRGYRIELAEIE 941
Cdd:PRK05691 403 SGPSIAHGYWRNPEASAKTFVEH--DGRTWLRTGDLG-FLRDGELFVTGRLKDMLIVRGHNLYPQDIE 467
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
666-948 |
3.32e-08 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 58.27 E-value: 3.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 666 PEELAYVIHTSGSTGSPKGVMINHRGAVNTVLDINDRFGVGPDDRVLGLSNLGFDLSVYDVFGPLSVGGA-VVLPdpqrR 744
Cdd:PLN02860 171 PDDAVLICFTSGTTGRPKGVTISHSALIVQSLAKIAIVGYGEDDVYLHTAPLCHIGGLSSALAMLMVGAChVLLP----K 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 745 GDPSHWADLVGTHGVTVWNSVPAqlqMLHDyLVSATAT-----VPDGLRLAMLSGDWIPVALPDQIRARVPGLRIVSLGG 819
Cdd:PLN02860 247 FDAKAALQAIKQHNVTSMITVPA---MMAD-LISLTRKsmtwkVFPSVRKILNGGGSLSSRLLPDAKKLFPNAKLFSAYG 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 820 ATEA----SIWSIWYPIEQvDPEWRSIPYGRPlTNQSFHVLDAA----------LRPRPDLVS--GELYIGGVGLAVGYL 883
Cdd:PLN02860 323 MTEAcsslTFMTLHDPTLE-SPKQTLQTVNQT-KSSSVHQPQGVcvgkpaphveLKIGLDESSrvGRILTRGPHVMLGYW 400
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1860141834 884 NDRERTAERfvvhpQTGERLYRTGDLGRYLPDGTIEFLGREDLQVKIRGYRIELAEIEAALGGHP 948
Cdd:PLN02860 401 GQNSETASV-----LSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHP 460
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
527-948 |
3.71e-08 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 58.11 E-value: 3.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 527 AGMLHDRVvlqalsTPDRPAVVAADRTLDYAELLGRAAGVAEALTA-AGCRRQELVAVVMDRGWEQVVAVLGALLAGCVY 605
Cdd:PRK13388 6 AQLLRDRA------GDDTIAVRYGDRTWTWREVLAEAAARAAALIAlADPDRPLHVGVLLGNTPEMLFWLAAAALGGYVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 606 VPVDTSQPAA------RR---RTILTNAGIRCALtqSGVDRNGwaegLRLLDVD------LLGTGQPQPVEGSGDPEELA 670
Cdd:PRK13388 80 VGLNTTRRGAalaadiRRadcQLLVTDAEHRPLL--DGLDLPG----VRVLDVDtpayaeLVAAAGALTPHREVDAMDPF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 671 YVIHTSGSTGSPKGVMINHRGAVNTVLDINDRFGVGPDDRVLGLSNLGFDLSVYDVFGP-LSVGGAVVLPdpqRRGDPSH 749
Cdd:PRK13388 154 MLIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDDVCYVSMPLFHSNAVMAGWAPaVASGAAVALP---AKFSASG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 750 WADLVGTHGVTVWNSVPAQLQmlhdYLVsATATVPDG----LRLAMLSGdwipvALPDQIR--ARVPGLRIVSLGGATEA 823
Cdd:PRK13388 231 FLDDVRRYGATYFNYVGKPLA----YIL-ATPERPDDadnpLRVAFGNE-----ASPRDIAefSRRFGCQVEDGYGSSEG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 824 SIWSIWYP-------------IEQVDPEwrsipygrPLTNQSFHVLDAALRPR-PDLVSGELY-IGGVGLAVGYLNDRER 888
Cdd:PRK13388 301 AVIVVREPgtppgsigrgapgVAIYNPE--------TLTECAVARFDAHGALLnADEAIGELVnTAGAGFFEGYYNNPEA 372
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 889 TAERFvvhpQTGerLYRTGDLGRYLPDGTIEFLGREDLQVKIRGYRIELAEIEAALGGHP 948
Cdd:PRK13388 373 TAERM----RHG--MYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHP 426
|
|
| E-C_NRPS |
cd19544 |
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ... |
113-323 |
5.11e-08 |
|
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); Dual function Epimerization/Condensation (E/C) domains have both an epimerization and a DCL condensation activity. Dual E/C domains first epimerize the substrate amino acid to produce a D-configuration, then catalyze the condensation between the D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. They are 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. These Dual E/C domains contain an extended His-motif (HHx(N)GD) near the N-terminus of the domain in addition to the standard Condensation (C) domain active site motif (HHxxxD). 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, these include the DCL-type, LCL-type, 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 domains, and the X-domain.
Pssm-ID: 380466 [Multi-domain] Cd Length: 413 Bit Score: 57.45 E-value: 5.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 113 ERMTAAWRALIARHDMLRAVVEADG----AQRVLAEVPpfeVPVIDLTGRPEavvdaavSAVRAEMDHLVHTPDRW---- 184
Cdd:cd19544 39 DAFLAALQQVIDRHDILRTAILWEGlsepVQVVWRQAE---LPVEELTLDPG-------DDALAQLRARFDPRRYRldlr 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 185 --PLFAARITRADH--RTVLHVSIDFLIADFISVQVVLDELHR-LYHRPDEPLPPLeiTFRDYQLAERAVRDSPRHE--- 256
Cdd:cd19544 109 qaPLLRAHVAEDPAngRWLLLLLFHHLISDHTSLELLLEEIQAiLAGRAAALPPPV--PYRNFVAQARLGASQAEHEaff 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1860141834 257 RDKqwwLARVDElPAAP-ELPTVARpadSEGRFRRWETRLSSQVWEGLRQRAGRHGVSPS-------GAVLAAFS 323
Cdd:cd19544 187 REM---LGDVDE-PTAPfGLLDVQG---DGSDITEARLALDAELAQRLRAQARRLGVSPAslfhlawALVLARCS 254
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
1374-1416 |
5.93e-08 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 57.17 E-value: 5.93e-08
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1860141834 1374 DDLTEHLAGRLPQYMVPSVVQVVDALPLNANGKVDRAVLRRRL 1416
Cdd:cd05918 435 AELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRALRELA 477
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
542-948 |
1.49e-07 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 56.32 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 542 PDRPAVVAADRTL--DYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVDtsqPAARRRT 619
Cdd:PRK12583 32 PDREALVVRHQALryTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNIN---PAYRASE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 620 I---LTNAGIR---CA------------------LTQSGVDRNGWAEGLRLLDVDLLGtGQPQP---------------- 659
Cdd:PRK12583 109 LeyaLGQSGVRwviCAdafktsdyhamlqellpgLAEGQPGALACERLPELRGVVSLA-PAPPPgflawhelqargetvs 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 660 ------VEGSGDPEELAYVIHTSGSTGSPKGVMINHRGAVNTVLDINDRFGVGPDDRvlglsnLGFDLSVYDVFGP---- 729
Cdd:PRK12583 188 realaeRQASLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDR------LCVPVPLYHCFGMvlan 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 730 ---LSVGGAVVLPdpQRRGDPSHWADLVGTHGVTVWNSVPAQL--QMLH----DYLVSAtatvpdgLRLAMLSGDWIPVA 800
Cdd:PRK12583 262 lgcMTVGACLVYP--NEAFDPLATLQAVEEERCTALYGVPTMFiaELDHpqrgNFDLSS-------LRTGIMAGAPCPIE 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 801 LPDQIRARVPGLRIVSLGGATEASIWSIWYPIEQvDPEWRSIPYGRPLTNQSFHVLDAALRPRPDLVSGELYIGGVGLAV 880
Cdd:PRK12583 333 VMRRVMDEMHMAEVQIAYGMTETSPVSLQTTAAD-DLERRVETVGRTQPHLEVKVVDPDGATVPRGEIGELCTRGYSVMK 411
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1860141834 881 GYLNDRERTAERFvvhpqTGERLYRTGDLGRYLPDGTIEFLGREDLQVKIRGYRIELAEIEAALGGHP 948
Cdd:PRK12583 412 GYWNNPEATAESI-----DEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHP 474
|
|
| Tam |
COG4106 |
Trans-aconitate methyltransferase [Energy production and conversion]; |
1205-1286 |
1.59e-07 |
|
Trans-aconitate methyltransferase [Energy production and conversion];
Pssm-ID: 443282 [Multi-domain] Cd Length: 100 Bit Score: 50.98 E-value: 1.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 1205 EVDYLATDLSPFFLGELRTRFgdrPGLRLEAVDIdRDLAgqglSPNSFDVVVAGDVLHASADVGRALDRLREVLAPQGWL 1284
Cdd:COG4106 25 GARVTGVDLSPEMLARARARL---PNVRFVVADL-RDLD----PPEPFDLVVSNAALHWLPDHAALLARLAAALAPGGVL 96
|
..
gi 1860141834 1285 VA 1286
Cdd:COG4106 97 AV 98
|
|
| UbiG |
COG2227 |
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ... |
1198-1285 |
2.25e-07 |
|
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and metabolism]; 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase is part of the Pathway/BioSystem: Ubiquinone biosynthesis
Pssm-ID: 441829 [Multi-domain] Cd Length: 126 Bit Score: 51.17 E-value: 2.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 1198 LAALdGYEVdyLATDLSPFFLGELRTRfGDRPGLRLEAVDIdRDLAgqgLSPNSFDVVVAGDVLHASADVGRALDRLREV 1277
Cdd:COG2227 42 LARR-GADV--TGVDISPEALEIARER-AAELNVDFVQGDL-EDLP---LEDGSFDLVICSEVLEHLPDPAALLRELARL 113
|
....*...
gi 1860141834 1278 LAPQGWLV 1285
Cdd:COG2227 114 LKPGGLLL 121
|
|
| LCL_NRPS-like |
cd19540 |
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ... |
109-383 |
2.41e-07 |
|
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: 55.12 E-value: 2.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 109 ELDPERMTAAWRALIARHDMLRAV-VEADG--AQRVL-AEVPPFEVPVIDLTgrPEAVVDAAVSAVRAEMDHLVHTPDRW 184
Cdd:cd19540 35 ALDVDALRAALADVVARHESLRTVfPEDDGgpYQVVLpAAEARPDLTVVDVT--EDELAARLAEAARRGFDLTAELPLRA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 185 PLFaaRITRADHrtVLHVSIDFLIADFISVQVVLDELHRLY------HRPDepLPPLEITFRDYQLAERAVRDSP----- 253
Cdd:cd19540 113 RLF--RLGPDEH--VLVLVVHHIAADGWSMAPLARDLATAYaarragRAPD--WAPLPVQYADYALWQRELLGDEddpds 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 254 RHERDKQWWLARVDELPAAPELPTV-ARPADSEGRFRRWETRLSSQVWEGLRQRAGRHGVSPSGAVLAAFSDTIAAYSRr 332
Cdd:cd19540 187 LAARQLAYWRETLAGLPEELELPTDrPRPAVASYRGGTVEFTIDAELHARLAALAREHGATLFMVLHAALAVLLSRLGA- 265
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1860141834 333 srfTLDITLlnRAPV----HDQVNALVGDF--TSVdlLAVDADPTRRFDE-----RARDLQA 383
Cdd:cd19540 266 ---GDDIPI--GTPVagrgDEALDDLVGMFvnTLV--LRTDVSGDPTFAEllarvRETDLAA 320
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
546-948 |
2.79e-07 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 55.09 E-value: 2.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 546 AVVAADRTLDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVDTSQPAARRRTILTNAG 625
Cdd:PRK12406 4 TIISGDRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 626 IR-----------------------------------------CALTQSGVDRNGWAEGLRLLDvdllGTGQPQPvegsg 664
Cdd:PRK12406 84 ARvliahadllhglasalpagvtvlsvptppeiaaayrispalLTPPAGAIDWEGWLAQQEPYD----GPPVPQP----- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 665 dpeelAYVIHTSGSTGSPKGVMINH---RGAVNTVLDINDRFGVGPDDRVLGLSNLGFdlSVYDVFG--PLSVGGAVVLp 739
Cdd:PRK12406 155 -----QSMIYTSGTTGHPKGVRRAAptpEQAAAAEQMRALIYGLKPGIRALLTGPLYH--SAPNAYGlrAGRLGGVLVL- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 740 dpQRRGDPSHWADLVGTHGVTVWNSVPAQLQMLHD---------------YLVSATATVPDGLRLAMLSGdWIPValpdq 804
Cdd:PRK12406 227 --QPRFDPEELLQLIERHRITHMHMVPTMFIRLLKlpeevrakydvsslrHVIHAAAPCPADVKRAMIEW-WGPV----- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 805 irarvpglrIVSLGGATEASIwSIWYPIEQvdpeWRSIP--YGRPLTNQSFHVLDAALRPRPDLVSGELYIGGVGLA-VG 881
Cdd:PRK12406 299 ---------IYEYYGSTESGA-VTFATSED----ALSHPgtVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPdFT 364
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1860141834 882 YLNDRERTAERfvvhpqtgER--LYRTGDLGRYLPDGTIEFLGREDLQVKIRGYRIELAEIEAALGGHP 948
Cdd:PRK12406 365 YHNKPEKRAEI--------DRggFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVP 425
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
552-750 |
2.86e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 55.51 E-value: 2.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 552 RTLDYAELLGRAAGVAEAL---TAAGCRrqelVAVVMDRGWEQVVAVLGALLAGCVYVPV-DTSQP--AARRRTILTNAG 625
Cdd:PRK07769 54 RDLTWSQFGARNRAVGARLqqvTKPGDR----VAILAPQNLDYLIAFFGALYAGRIAVPLfDPAEPghVGRLHAVLDDCT 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 626 IRCALTQSGVdrngwAEGLRLLDVDLLGTGQP----------------QPVEGsgDPEELAYVIHTSGSTGSPKGVMINH 689
Cdd:PRK07769 130 PSAILTTTDS-----AEGVRKFFRARPAKERPrviavdavpdevgatwVPPEA--NEDTIAYLQYTSGSTRIPAGVQITH 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1860141834 690 RGAVNTVLDINDRFGVGPDDRvlGLSNLGF--DLSVYDVFGPLSVGGAVVLPDPQ---RRgdPSHW 750
Cdd:PRK07769 203 LNLPTNVLQVIDALEGQEGDR--GVSWLPFfhDMGLITVLLPALLGHYITFMSPAafvRR--PGRW 264
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
507-925 |
3.14e-07 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 55.44 E-value: 3.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 507 PPEATRDRRAETN---RTQAPVPAGMLH--DRVVLQALSTPDRPAVVAAD------RTLDYAELLGRAAGVAEALTAAGC 575
Cdd:PRK12582 23 PPDISVERRADGSiviKSRHPLGPYPRSipHLLAKWAAEAPDRPWLAQREpghgqwRKVTYGEAKRAVDALAQALLDLGL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 576 RRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVD-----TSQPAARRRTILTNAGIRCALTQSGVDRNGWAEGLRLLDV- 649
Cdd:PRK12582 103 DPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVSpayslMSHDHAKLKHLFDLVKPRVVFAQSGAPFARALAALDLLDVt 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 650 -----------------DLLGTGQPQPVEGSGD---PEELAYVIHTSGSTGSPKGVMINHRG-AVNTVLDIndrfGVGPD 708
Cdd:PRK12582 183 vvhvtgpgegiasiafaDLAATPPTAAVAAAIAaitPDTVAKYLFTSGSTGMPKAVINTQRMmCANIAMQE----QLRPR 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 709 DRVLGLSNLgFDLSVYD-------VFGPLSVGGAVVLPDPqrrGDPshwadLVGTHGVTVWN----------SVPAQLQM 771
Cdd:PRK12582 259 EPDPPPPVS-LDWMPWNhtmggnaNFNGLLWGGGTLYIDD---GKP-----LPGMFEETIRNlreisptvygNVPAGYAM 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 772 LHDYLVSATA---TVPDGLRLAMLSGDWIPVALPDQIRA---RVPGLRIV--SLGGATEAS--IWSIWYPIEQVDpewrs 841
Cdd:PRK12582 330 LAEAMEKDDAlrrSFFKNLRLMAYGGATLSDDLYERMQAlavRTTGHRIPfyTGYGATETAptTTGTHWDTERVG----- 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 842 iPYGRPLTNqsfhvldAALRPRPDLVSGELYIGGVGLAVGYLNDRERTAERFvvhpqTGERLYRTGDLGRYL----PDGT 917
Cdd:PRK12582 405 -LIGLPLPG-------VELKLAPVGDKYEVRVKGPNVTPGYHKDPELTAAAF-----DEEGFYRLGDAARFVdpddPEKG 471
|
490
....*....|
gi 1860141834 918 IEFLGR--ED 925
Cdd:PRK12582 472 LIFDGRvaED 481
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
1376-1413 |
4.02e-07 |
|
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: 54.68 E-value: 4.02e-07
10 20 30
....*....|....*....|....*....|....*...
gi 1860141834 1376 LTEHLAGRLPQYMVPSVVQVVDALPLNANGKVDRAVLR 1413
Cdd:cd17649 413 LRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
1367-1412 |
4.15e-07 |
|
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: 54.62 E-value: 4.15e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1860141834 1367 DRVRISRDDLTEHLAGRLPQYMVPSVVQVVDALPLNANGKVDRAVL 1412
Cdd:cd17643 405 DGAAADIAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
1374-1414 |
4.24e-07 |
|
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: 54.62 E-value: 4.24e-07
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1860141834 1374 DDLTEHLAGRLPQYMVPSVVQVVDALPLNANGKVDRAVLRR 1414
Cdd:cd17653 393 DGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
1375-1550 |
4.53e-07 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 55.04 E-value: 4.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 1375 DLTEHLAGRLPQYMVPSVVQVVDALPLNANGKVDRAVLRRRLP----------------------RRGTATAAGSSGALD 1432
Cdd:PRK06060 449 DLHRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALRKQSPtkpiwelsltepgsgvraqrddLSASNMTIAGGNDGG 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 1433 SDLERRIAAVWAEALRL-----------------PR-VGRDENLFELGGDSlvaaQITGRILEEIPQAAGLFFDQLLRqv 1494
Cdd:PRK06060 529 ATLRERLVALRQERQRLvvdavcaeaakmlgepdPWsVDQDLAFSELGFDS----QMTVTLCKRLAAVTGLRLPETVG-- 602
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1860141834 1495 LEQPTVAALAGHVEAEsATPVTASPSVP--ATSGGDGLSPLHEGTDGVPWVLVPGGEG 1550
Cdd:PRK06060 603 WDYGSISGLAQYLEAE-LAGGHGRLKSAgpVNSGATGLWAIEEQLNKVEELVAVIADG 659
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
1338-1409 |
4.71e-07 |
|
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: 54.18 E-value: 4.71e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1860141834 1338 GAAQPLCLPEPDG-----FIAELGMCVLAARFKTDRVRisrddltEHLAGRLPQYMVPSVVQVVDALPLNANGKVDR 1409
Cdd:cd05945 377 GVKEAVVVPKYKGekvteLIAFVVPKPGAEAGLTKAIK-------AELAERLPPYMIPRRFVYLDELPLNANGKIDR 446
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
658-974 |
4.71e-07 |
|
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: 54.31 E-value: 4.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 658 QPVEGSGDPEELAYVIHTSGSTGSPKGVMINHRG---AVNTVLDINDRFGVGPDDRVLGLSNLGFDLSVYDVFGPLSVGG 734
Cdd:cd05929 116 SPETPIEDEAAGWKMLYSGGTTGRPKGIKRGLPGgppDNDTLMAAALGFGPGADSVYLSPAPLYHAAPFRWSMTALFMGG 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 735 AVVLpdpQRRGDPSHWADLVGTHGVTVWNSVPAQLQML--------HDYLVSAtatvpdgLRLAMLSGDWIPVALPDQIR 806
Cdd:cd05929 196 TLVL---MEKFDPEEFLRLIERYRVTFAQFVPTMFVRLlklpeavrNAYDLSS-------LKRVIHAAAPCPPWVKEQWI 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 807 ARVPGlRIVSLGGATEAsIWSIWYPIEqvdpEWRSIP--YGRPLTNQsFHVLDAALRPRPDLVSGELYIGGvGLAVGYLN 884
Cdd:cd05929 266 DWGGP-IIWEYYGGTEG-QGLTIINGE----EWLTHPgsVGRAVLGK-VHILDEDGNEVPPGEIGEVYFAN-GPGFEYTN 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 885 DRERTAERFvvhpqtGERLYRT-GDLGRYLPDGTIEFLGREDLQVKIRGYRIELAEIEAALGGHPAVAGAVVVVDGDTPL 963
Cdd:cd05929 338 DPEKTAAAR------NEGGWSTlGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEEL 411
|
330
....*....|.
gi 1860141834 964 ERRLAAFVEPA 974
Cdd:cd05929 412 GQRVHAVVQPA 422
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
660-947 |
5.31e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 54.27 E-value: 5.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 660 VEGSGDPE-ELAYVIHTSGSTGSPKGVMINHRGAV-NTVLDINDRFG-VGPDDRVLGLsnlgfdLSVYDVFGPLSVGG-- 734
Cdd:PRK06710 198 VEVPCDPEnDLALLQYTGGTTGFPKGVMLTHKNLVsNTLMGVQWLYNcKEGEEVVLGV------LPFFHVYGMTAVMNls 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 735 ------AVVLPdpqrRGDPSHWADLVGTHGVTVWNSVPA------QLQMLHDYLVSAtatvpdgLRLAMLSGDWIPVALP 802
Cdd:PRK06710 272 imqgykMVLIP----KFDMKMVFEAIKKHKVTLFPGAPTiyiallNSPLLKEYDISS-------IRACISGSAPLPVEVQ 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 803 DQIRaRVPGLRIVSLGGATEASiwsiwyPIEQVDPEWR-----SIPYGRPLTNQSFHVLDAALRPRPDLVsGELYIGGVG 877
Cdd:PRK06710 341 EKFE-TVTGGKLVEGYGLTESS------PVTHSNFLWEkrvpgSIGVPWPDTEAMIMSLETGEALPPGEI-GEIVVKGPQ 412
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 878 LAVGYLNDRERTAERFvvhpQTGerLYRTGDLGRYLPDGTIEFLGREDLQVKIRGYRIELAEIEAALGGH 947
Cdd:PRK06710 413 IMKGYWNKPEETAAVL----QDG--WLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEH 476
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
1300-1412 |
5.99e-07 |
|
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: 54.01 E-value: 5.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 1300 LELLVRVDEaTADFTDLRRGTEQVFLDRRSWLEVLGAAGAAQplclpEPDGFIAEL-GMCVLAARFKTDRVRisrddltE 1378
Cdd:cd17650 347 VELLGRVDH-QVKIRGFRIELGEIESQLARHPAIDEAVVAVR-----EDKGGEARLcAYVVAAATLNTAELR-------A 413
|
90 100 110
....*....|....*....|....*....|....
gi 1860141834 1379 HLAGRLPQYMVPSVVQVVDALPLNANGKVDRAVL 1412
Cdd:cd17650 414 FLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
552-934 |
6.37e-07 |
|
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341296 [Multi-domain] Cd Length: 569 Bit Score: 54.35 E-value: 6.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 552 RTLDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVDTSQPAARRRTILTNAGIRCALT 631
Cdd:cd17641 10 QEFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 632 --QSGVDR--NGWAE-------------GLR------LLDV-DLLGTGQ------PQPVE---GSGDPEELAYVIHTSGS 678
Cdd:cd17641 90 edEEQVDKllEIADRipsvryviycdprGMRkyddprLISFeDVVALGRaldrrdPGLYErevAAGKGEDVAVLCTTSGT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 679 TGSPKGVMINHRGAVNTVLDINDRFGVGPDDRVLGLSNLGFDLS-VYDVFGPLSVGGAVVLPDPQRrgdpSHWADL--VG 755
Cdd:cd17641 170 TGKPKLAMLSHGNFLGHCAAYLAADPLGPGDEYVSVLPLPWIGEqMYSVGQALVCGFIVNFPEEPE----TMMEDLreIG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 756 THGV----TVWNSVPAQLQ------------MLHDYLVSATATVPDGLR-LAMLSGDWIPVALPDQI-----RARV--PG 811
Cdd:cd17641 246 PTFVllppRVWEGIAADVRarmmdatpfkrfMFELGMKLGLRALDRGKRgRPVSLWLRLASWLADALlfrplRDRLgfSR 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 812 LRIVSLGGA-----------------------TEASIWSIWYPIEQVDPEwrsiPYGRPLTNQSFHVLDAalrprpdlvs 868
Cdd:cd17641 326 LRSAATGGAalgpdtfrffhaigvplkqlygqTELAGAYTVHRDGDVDPD----TVGVPFPGTEVRIDEV---------- 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1860141834 869 GELYIGGVGLAVGYLNDRERTAERFvvhpqTGERLYRTGDLGRYLPDGTIEFLGR-EDLQVKIRGYR 934
Cdd:cd17641 392 GEILVRSPGVFVGYYKNPEATAEDF-----DEDGWLHTGDAGYFKENGHLVVIDRaKDVGTTSDGTR 453
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
1367-1412 |
6.90e-07 |
|
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: 53.82 E-value: 6.90e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1860141834 1367 DRVRISRDDLTEHLAGRLPQYMVPSVVQVVDALPLNANGKVDRAVL 1412
Cdd:cd17646 443 GAAGPDTAALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| PP-binding |
pfam00550 |
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
1437-1502 |
7.67e-07 |
|
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: 47.94 E-value: 7.67e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1860141834 1437 RRIAAVWAEALRLP--RVGRDENLFELGGDSLVAAQITGRILEEIPQAAGlffdqlLRQVLEQPTVAA 1502
Cdd:pfam00550 1 ERLRELLAEVLGVPaeEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIP------PSDLFEHPTLAE 62
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
651-948 |
9.11e-07 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 53.87 E-value: 9.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 651 LLGTGQPQP--------VEGSGDPEELAYvihTSGSTGSPKGVMINHRGAVNTVLDindrfgvgpddrvlglSNLGFDLS 722
Cdd:PLN03102 165 LIQRGEPTPslvarmfrIQDEHDPISLNY---TSGTTADPKGVVISHRGAYLSTLS----------------AIIGWEMG 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 723 VYDVF----------------GPLSVGGAVVLpdpQRRGDPSHWADLVGTHGVTVWNSVPAQLQMLHDYlvSATATVPDG 786
Cdd:PLN03102 226 TCPVYlwtlpmfhcngwtftwGTAARGGTSVC---MRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKG--NSLDLSPRS 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 787 LRLAMLSGDWIPVALPDQIRARVpGLRIVSLGGATEAS---IWSIWypieqvDPEWRSIPYGRPL---TNQSFHVL---D 857
Cdd:PLN03102 301 GPVHVLTGGSPPPAALVKKVQRL-GFQVMHAYGLTEATgpvLFCEW------QDEWNRLPENQQMelkARQGVSILglaD 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 858 AALR--------PRPDLVSGELYIGGVGLAVGYLNDRERTAERFvvhpqtGERLYRTGDLGRYLPDGTIEFLGREDLQVK 929
Cdd:PLN03102 374 VDVKnketqesvPRDGKTMGEIVIKGSSIMKGYLKNPKATSEAF------KHGWLNTGDVGVIHPDGHVEIKDRSKDIII 447
|
330
....*....|....*....
gi 1860141834 930 IRGYRIELAEIEAALGGHP 948
Cdd:PLN03102 448 SGGENISSVEVENVLYKYP 466
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1343-1413 |
9.19e-07 |
|
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: 53.60 E-value: 9.19e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1860141834 1343 LCLPEPDGFIAELGMCVLAArfktdrVRISRDDLTEHLAGRLPQYMVPSVVQVVDALPLNANGKVDRAVLR 1413
Cdd:cd05922 393 AAVGLPDPLGEKLALFVTAP------DKIDPKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| PRK09294 |
PRK09294 |
phthiocerol/phthiodiolone dimycocerosyl transferase; |
90-321 |
1.31e-06 |
|
phthiocerol/phthiodiolone dimycocerosyl transferase;
Pssm-ID: 181765 [Multi-domain] Cd Length: 416 Bit Score: 52.79 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 90 ETFAYGGVACHGYGELvypelDPERMTAAWRALIARHDMLRAVVEAD---GAQRVLAEVPPFEVPVIDLTGrpeavvdaA 166
Cdd:PRK09294 19 RYEAFTGYTAHLRGVL-----DIDALSDAFDALLRAHPVLAAHLEQDsdgGWELVADDLLHPGIVVVDGDA--------A 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 167 VSAVRAEMDhlvhtpDRWPLFAARITRADHRTVLHVSIDFLIADFISVQVVLDELHRLYHR----------PDEPLP-PL 235
Cdd:PRK09294 86 RPLPELQLD------QGVSLLALDVVPDDGGARVTLYIHHSIADAHHSASLLDELWSRYTDvvttgdpgpiRPQPAPqSL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 236 EitfrdYQLAERAVRdspRHERDKQWWLARVDELPAAPELPTVARPADSE--GRFRRWETRLSSQVWEGLRQRAGRHGVS 313
Cdd:PRK09294 160 E-----AVLAQRGIR---RQALSGAERFMPAMYAYELPPTPTAAVLAKPGlpQAVPVTRCRLSKAQTSSLAAFGRRHRLT 231
|
....*...
gi 1860141834 314 PSGAVLAA 321
Cdd:PRK09294 232 VNALVSAA 239
|
|
| AcpA |
COG3433 |
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ... |
1374-1514 |
1.37e-06 |
|
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442659 [Multi-domain] Cd Length: 295 Bit Score: 52.06 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 1374 DDLTEHLAGRLPQYMVPSVVQVVDALPLNANGKVDRAVLRRRLPRRGTATAAGSSGALDSDLERRIAAVWAEALRLP--R 1451
Cdd:COG3433 159 AAALAALDKVPPDVVAASAVVALDALLLLALKVVARAAPALAAAEALLAAASPAPALETALTEEELRADVAELLGVDpeE 238
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1860141834 1452 VGRDENLFELGGDSLVAAQITGRIleeipQAAGLFFDqlLRQVLEQPTVAALAGHVEAESATP 1514
Cdd:COG3433 239 IDPDDNLFDLGLDSIRLMQLVERW-----RKAGLDVS--FADLAEHPTLAAWWALLAAAQAAA 294
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
650-948 |
1.77e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 52.84 E-value: 1.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 650 DLLGTGQPQPV-EGSGDPEELAYVIHTSGSTGSPKGVMINHRGAVNTVLDINDRFGVGPDDrvlGLSNLGFDLSVYDVFG 728
Cdd:PRK05677 189 DALAKGAGQPVtEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCRALMGSNLNE---GCEILIAPLPLYHIYA 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 729 PLSVGGAVVLpdpqrrgdpshwadlVGTHGVTVWN--SVPAQLQMLHDYLVSA-----TATVP------------DGLRL 789
Cdd:PRK05677 266 FTFHCMAMML---------------IGNHNILISNprDLPAMVKELGKWKFSGfvglnTLFVAlcnneafrkldfSALKL 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 790 AMLSGDWIPVALPDQIRaRVPGLRIVSLGGATEASiwsiwyPIEQVDP----EWRSIpyGRPLTNQSFHVLDAALRPRPD 865
Cdd:PRK05677 331 TLSGGMALQLATAERWK-EVTGCAICEGYGMTETS------PVVSVNPsqaiQVGTI--GIPVPSTLCKVIDDDGNELPL 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 866 LVSGELYIGGVGLAVGYLNDRERTAERFvvhpqTGERLYRTGDLGRYLPDGTIEFLGREDLQVKIRGYRIELAEIEAALG 945
Cdd:PRK05677 402 GEVGELCVKGPQVMKGYWQRPEATDEIL-----DSDGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLA 476
|
...
gi 1860141834 946 GHP 948
Cdd:PRK05677 477 ALP 479
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
536-994 |
1.82e-06 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 52.82 E-value: 1.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 536 LQALSTPDRPAVVAADRTL-----DYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVDT 610
Cdd:cd05915 2 ERAAALFGRKEVVSRLHTGevhrtTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 611 SQPAARRRTILTNAGIRCALTQSGVDRNGwAEGLRLLD---------------VDLLGTGQP-----QPVEgSGDPEELA 670
Cdd:cd05915 82 RLSPKEIAYILNHAEDKVLLFDPNLLPLV-EAIRGELKtvqhfvvmdekapegYLAYEEALGeeadpVRVP-ERAACGMA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 671 YvihTSGSTGSPKGVMINHRGAV--NTVLDINDRFGVGPDDRVLGLSNLgFDLSVYDVFGPLSVGGAVVLPDPQRRGDPS 748
Cdd:cd05915 160 Y---TTGTTGLPKGVVYSHRALVlhSLAASLVDGTALSEKDVVLPVVPM-FHVNAWCLPYAATLVGAKQVLPGPRLDPAS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 749 HWADLVgTHGVTVWNSVPAQLQMLHDYLVSATATVPdgLRLAMLSGDWIPVALPDQIRaRVPGLRIVSLGGATE------ 822
Cdd:cd05915 236 LVELFD-GEGVTFTAGVPTVWLALADYLESTGHRLK--TLRRLVVGGSAAPRSLIARF-ERMGVEVRQGYGLTEtspvvv 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 823 ASIWSiwypieqvdPEWRSIPYGRPLT----------NQSFHVLDAALRPRPDlvSGE----LYIGGVGLAVGYLNDRER 888
Cdd:cd05915 312 QNFVK---------SHLESLSEEEKLTlkaktglpipLVRLRVADEEGRPVPK--DGKalgeVQLKGPWITGGYYGNEEA 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 889 T-AERFvvhpQTGerLYRTGDLGRYLPDGTIEFLGREDLQVKIRGYRIELAEIEAALGGHPAVAGAVVVVDGDTPLERRL 967
Cdd:cd05915 381 TrSALT----PDG--FFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERP 454
|
490 500
....*....|....*....|....*..
gi 1860141834 968 AAFVEPagRPVTAAQAEHDQAALRQLG 994
Cdd:cd05915 455 LAVVVP--RGEKPTPEELNEHLLKAGF 479
|
|
| Methyltransf_11 |
pfam08241 |
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
1197-1285 |
2.34e-06 |
|
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
Pssm-ID: 462406 [Multi-domain] Cd Length: 94 Bit Score: 47.27 E-value: 2.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 1197 VLAALDGYEVDYLATDLSPFFLGELRTRFGDRPGLRLEAvdidrDLAGQGLSPNSFDVVVAGDVLHASADVGRALDRLRE 1276
Cdd:pfam08241 10 LTELLARLGARVTGVDISPEMLELAREKAPREGLTFVVG-----DAEDLPFPDNSFDLVLSSEVLHHVEDPERALREIAR 84
|
....*....
gi 1860141834 1277 VLAPQGWLV 1285
Cdd:pfam08241 85 VLKPGGILI 93
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
542-948 |
2.77e-06 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 51.91 E-value: 2.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 542 PDRPAVVAADRTLDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVyvPV------------- 608
Cdd:PRK10946 37 SDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGVA--PVnalfshqrselna 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 609 --DTSQP----AARRRTILTNAG------IRCALTQSGVDRNgwAEGLRLLDvDLLGTGQPQPVEGSGDPEELAYVIHTS 676
Cdd:PRK10946 115 yaSQIEPalliADRQHALFSDDDflntlvAEHSSLRVVLLLN--DDGEHSLD-DAINHPAEDFTATPSPADEVAFFQLSG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 677 GSTGSPKGVMINHRGAVNTVLDINDRFGVGPDDRVL----GLSNlgFDLSVYDVFGPLSVGGAVVL-PDPqrrgDPSHWA 751
Cdd:PRK10946 192 GSTGTPKLIPRTHNDYYYSVRRSVEICGFTPQTRYLcalpAAHN--YPMSSPGALGVFLAGGTVVLaPDP----SATLCF 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 752 DLVGTHGVTVwnsvpaqlqmlhdylvsaTATVPDGLRLamlsgdWIPVALPDQIRARVPGLRIVSLGGATEASIWSIWYP 831
Cdd:PRK10946 266 PLIEKHQVNV------------------TALVPPAVSL------WLQAIAEGGSRAQLASLKLLQVGGARLSETLARRIP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 832 IE------QV--------------DPEWRSI-PYGRPLT-NQSFHVLDAALRPRPDLVSGELYIGGVGLAVGYLNDRERT 889
Cdd:PRK10946 322 AElgcqlqQVfgmaeglvnytrldDSDERIFtTQGRPMSpDDEVWVADADGNPLPQGEVGRLMTRGPYTFRGYYKSPQHN 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1860141834 890 AERFvvhpqTGERLYRTGDLGRYLPDGTIEFLGREDLQVKIRGYRIELAEIEAALGGHP 948
Cdd:PRK10946 402 ASAF-----DANGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHP 455
|
|
| Methyltransf_25 |
pfam13649 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
1198-1282 |
3.67e-06 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 463945 [Multi-domain] Cd Length: 96 Bit Score: 46.79 E-value: 3.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 1198 LAALDGYEVdyLATDLSPFFLGELRTRFGDRpGLRLEAVDID-RDLAgqgLSPNSFDVVVAGDVLH--ASADVGRALDRL 1274
Cdd:pfam13649 15 LARRGGARV--TGVDLSPEMLERARERAAEA-GLNVEFVQGDaEDLP---FPDGSFDLVVSSGVLHhlPDPDLEAALREI 88
|
....*...
gi 1860141834 1275 REVLAPQG 1282
Cdd:pfam13649 89 ARVLKPGG 96
|
|
| COG4976 |
COG4976 |
Predicted methyltransferase, contains TPR repeat [General function prediction only]; |
1151-1285 |
4.31e-06 |
|
Predicted methyltransferase, contains TPR repeat [General function prediction only];
Pssm-ID: 444001 [Multi-domain] Cd Length: 181 Bit Score: 48.84 E-value: 4.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 1151 YERTLFNRWANEAAAALVRRIAEQRIEPGALRVLEV-----GagaggttaaVLAALDGYEVDYLATDLSPFFLGELRTRF 1225
Cdd:COG4976 18 YDAALVEDLGYEAPALLAEELLARLPPGPFGRVLDLgcgtgL---------LGEALRPRGYRLTGVDLSEEMLAKAREKG 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 1226 GDRpglRLEAVDIdRDLAGqglSPNSFDVVVAGDVLHASADVGRALDRLREVLAPQGWLV 1285
Cdd:COG4976 89 VYD---RLLVADL-ADLAE---PDGRFDLIVAADVLTYLGDLAAVFAGVARALKPGGLFI 141
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
1375-1413 |
5.24e-06 |
|
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: 51.19 E-value: 5.24e-06
10 20 30
....*....|....*....|....*....|....*....
gi 1860141834 1375 DLTEHLAGRLPQYMVPSVVQVVDALPLNANGKVDRAVLR 1413
Cdd:cd17651 453 ELRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRRALP 491
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
1368-1412 |
5.98e-06 |
|
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: 50.98 E-value: 5.98e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1860141834 1368 RVRISRDDLTEHLAGRLPQYMVPSVVQVVDALPLNANGKVDRAVL 1412
Cdd:cd17647 473 GYRKLIKDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKL 517
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
674-948 |
6.14e-06 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 50.91 E-value: 6.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 674 HTSGSTGSPKGVMINHRGAVNTVLDIN--DRFGVGPDDRVLGLSNLgFDLSVYDV-FGPLSVGGAVVLPDPQRRGDPSHw 750
Cdd:PRK06018 184 YTSGTTGDPKGVLYSHRSNVLHALMANngDALGTSAADTMLPVVPL-FHANSWGIaFSAPSMGTKLVMPGAKLDGASVY- 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 751 aDLVGTHGVTVWNSVPAQLQMLHDYLVSATATVPDgLRLAMLSGDWIPVALpdqIRARVP-GLRIVSLGGATEASiwsiw 829
Cdd:PRK06018 262 -ELLDTEKVTFTAGVPTVWLMLLQYMEKEGLKLPH-LKMVVCGGSAMPRSM---IKAFEDmGVEVRHAWGMTEMS----- 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 830 yPIEQV---DPEWRSIPY----------GRPLTNQSFHVLDAALR--PRPDLVSGELYIGGVGLAVGYLndrertaeRFV 894
Cdd:PRK06018 332 -PLGTLaalKPPFSKLPGdarldvlqkqGYPPFGVEMKITDDAGKelPWDGKTFGRLKVRGPAVAAAYY--------RVD 402
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1860141834 895 VHPQTGERLYRTGDLGRYLPDGTIEFLGREDLQVKIRGYRIELAEIEAALGGHP 948
Cdd:PRK06018 403 GEILDDDGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHP 456
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
1369-1416 |
7.12e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 50.57 E-value: 7.12e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1860141834 1369 VRISRDDLTEHLAGRLPQYMVPSVVQVVDALPLNANGKVDRAVLRRRL 1416
Cdd:PRK06187 470 ATLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLREQY 517
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
668-948 |
9.94e-06 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 50.33 E-value: 9.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 668 ELAYVIHTSGSTGSPKGVMINHRG-AVNTVLDINDRFGVGPDDRVLGLSNLGFDLS-VYDVFGPLSVGGAVV----LPdp 741
Cdd:PRK10524 234 EPSYILYTSGTTGKPKGVQRDTGGyAVALATSMDTIFGGKAGETFFCASDIGWVVGhSYIVYAPLLAGMATImyegLP-- 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 742 qRRGDPSHWADLVGTHGVTVWNSVPAQLQML--------HDYLVSAtatvpdgLRLAMLSGD--------WIPVALpdqi 805
Cdd:PRK10524 312 -TRPDAGIWWRIVEKYKVNRMFSAPTAIRVLkkqdpallRKHDLSS-------LRALFLAGEpldeptasWISEAL---- 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 806 rarvpGLRIVSLGGATEaSIWSIWYPIEQVDPewRSIPYGRPltnqSFHVLDAALRPRPDLVSGELYIGGVGLAV----- 880
Cdd:PRK10524 380 -----GVPVIDNYWQTE-TGWPILAIARGVED--RPTRLGSP----GVPMYGYNVKLLNEVTGEPCGPNEKGVLViegpl 447
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1860141834 881 --GYLNDRERTAERFVvhpQT-----GERLYRTGDLGRYLPDGTIEFLGREDLQVKIRGYRIELAEIEAALGGHP 948
Cdd:PRK10524 448 ppGCMQTVWGDDDRFV---KTywslfGRQVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHP 519
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
1369-1412 |
1.06e-05 |
|
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: 50.17 E-value: 1.06e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1860141834 1369 VRISRDDLTEHLAGRLPQYMVPSVVQVVDALPLNANGKVDRAVL 1412
Cdd:cd17656 435 QELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
1375-1413 |
1.18e-05 |
|
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: 49.77 E-value: 1.18e-05
10 20 30
....*....|....*....|....*....|....*....
gi 1860141834 1375 DLTEHLAGRLPQYMVPSVVQVVDALPLNANGKVDRAVLR 1413
Cdd:cd05919 398 DIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
130-672 |
1.33e-05 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 50.26 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 130 RAVVEADGAQRVLAEVPPFEvpvidltgRPEAVVDAAVSAVRAEMDHLVHTPDRWPLFAARITRADHRTVLHVSIDFLIA 209
Cdd:COG3321 850 SALYPGRGRRRVPLPTYPFQ--------REDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALAL 921
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 210 DFISVQVVLDELHRLYHRPDEPLPPLEITFRDYQLAERAVRDSPRHERDKQWWLARVDELPAAPELPTVARPADSEGRFR 289
Cdd:COG3321 922 AAAALAALLALVALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAA 1001
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 290 RWETRLSSQVWEGLRQRAGRHGVSPSGAVLAAFSDTIAAYSRRSRFTLDITLLNRAPVHDQVNALVGDFTSVDLLAVDAD 369
Cdd:COG3321 1002 LALLAAAALLLAAAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAA 1081
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 370 PTRRFDERARDLQAQLWEDLDHRSFSGIEVMREIARRQGAEAALFPVVFTSAIGITSAGAAAD-GAPLGELGYGISQTPQ 448
Cdd:COG3321 1082 AALALAAALAAAALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAaAAAALALAAAAAALAA 1161
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 449 VWIDCQNIERDGGLVSNWDVREEVFPPGVVDDMFAAYDAVLHRLAGDDAAWTGTGHPDPPEATRDRRAETNRTQAPVPAG 528
Cdd:COG3321 1162 ALAAALLAAAALLLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAA 1241
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 529 MLHDRVVLQALSTPDRPAVVAADRTLDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPV 608
Cdd:COG3321 1242 AAAVAALAAAAAALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAAL 1321
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1860141834 609 DTSQPAARRRTILTNAGIRCALTQSGVDRNGWAEGLRLLDVDLLGTGQPQPVEGSGDPEELAYV 672
Cdd:COG3321 1322 AAALLAAALAALAAAVAAALALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALALAALAAAV 1385
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
1375-1412 |
1.41e-05 |
|
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: 49.63 E-value: 1.41e-05
10 20 30
....*....|....*....|....*....|....*...
gi 1860141834 1375 DLTEHLAGRLPQYMVPSVVQVVDALPLNANGKVDRAVL 1412
Cdd:cd17655 449 QLREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKAL 486
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
549-690 |
2.45e-05 |
|
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.
Pssm-ID: 341231 [Multi-domain] Cd Length: 571 Bit Score: 48.88 E-value: 2.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 549 AADRTLDYAELLGRAAGVAEAL-TAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVDTSQPAARRRTILTNAGIR 627
Cdd:cd05905 10 KEATTLTWGKLLSRAEKIAAVLqKKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFLLGTCKVR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 628 CALT----------------QSG--VDRNGWAEGLRLLDVDLLGTGQPQPVEGSG--DPEELAYVIHTSGSTGSPKGVMI 687
Cdd:cd05905 90 VALTveaclkglpkkllkskTAAeiAKKKGWPKILDFVKIPKSKRSKLKKWGPHPptRDGDTAYIEYSFSSDGSLSGVAV 169
|
...
gi 1860141834 688 NHR 690
Cdd:cd05905 170 SHS 172
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
110-307 |
2.49e-05 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 49.57 E-value: 2.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 110 LDPERMTAAWRALIARHDMLR-AVVEADG---AQRVLAEVPPFEVPVIDLTGRPEAVVDAAVSAVRAEMDHlvhtpdrWP 185
Cdd:PRK12316 3671 LDAAALEAALQALVEHHDALRlRFVEDAGgwtAEHLPVELGGALLWRAELDDAEELERLGEEAQRSLDLAD-------GP 3743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 186 LFAARITR-ADHRTVLHVSIDFLIADFISVQVVLDELHRLY------HRPDepLPPLEITFRDYQLAERAVRDSPRHERD 258
Cdd:PRK12316 3744 LLRALLATlADGSQRLLLVIHHLVVDGVSWRILLEDLQQAYqqllqgEAPR--LPAKTSSFKAWAERLQEHARGEALKAE 3821
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1860141834 259 KQWWLARVDELPAapELPTVARPADSEGRFRRW-ETRLSSQVWEGLRQRA 307
Cdd:PRK12316 3822 LAYWQEQLQGVSS--ELPCDHPQGALQNRHAASvQTRLDRELTRRLLQQA 3869
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
1348-1409 |
3.31e-05 |
|
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: 48.38 E-value: 3.31e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1860141834 1348 PDGFIAELGMCVLAARfktDRVRISRDDLTEHLAGRLPQYMVPSVVQVVDALPLNANGKVDR 1409
Cdd:cd17631 377 PDEKWGEAVVAVVVPR---PGAELDEDELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
551-948 |
3.35e-05 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 48.74 E-value: 3.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 551 DRTLDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVD---TSQPAARR------RTIL 621
Cdd:PLN02654 118 DASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFagfSAESLAQRivdckpKVVI 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 622 TNAGIR-------------CALTQSgvDRNGWAEGLRLLDVDLLGTGQ-----------------PQ-----PVEGSgDP 666
Cdd:PLN02654 198 TCNAVKrgpktinlkdivdAALDES--AKNGVSVGICLTYENQLAMKRedtkwqegrdvwwqdvvPNyptkcEVEWV-DA 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 667 EELAYVIHTSGSTGSPKGVMINHRG-AVNTVLDINDRFGVGPDDRVLGLSNLGFDLS-VYDVFGPLSVGGAVVL------ 738
Cdd:PLN02654 275 EDPLFLLYTSGSTGKPKGVLHTTGGyMVYTATTFKYAFDYKPTDVYWCTADCGWITGhSYVTYGPMLNGATVLVfegapn 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 739 -PDPQRrgdpsHWaDLVGTHGVTVWnsvpaqlqmlhdylvsatATVPDGLRLAMLSGDWiPVALPDQIRARVPGlrivSL 817
Cdd:PLN02654 355 yPDSGR-----CW-DIVDKYKVTIF------------------YTAPTLVRSLMRDGDE-YVTRHSRKSLRVLG----SV 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 818 GGATEASIWSIWY--------PIEqvDPEWRS---------IPYGRPLTNQS-----FHVLDAALRPRPDLVSGElyigg 875
Cdd:PLN02654 406 GEPINPSAWRWFFnvvgdsrcPIS--DTWWQTetggfmitpLPGAWPQKPGSatfpfFGVQPVIVDEKGKEIEGE----- 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 876 vglAVGYL--------------NDRERTaERFVVHPQTGerLYRTGDLGRYLPDGTIEFLGREDLQVKIRGYRIELAEIE 941
Cdd:PLN02654 479 ---CSGYLcvkkswpgafrtlyGDHERY-ETTYFKPFAG--YYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVE 552
|
....*..
gi 1860141834 942 AALGGHP 948
Cdd:PLN02654 553 SALVSHP 559
|
|
| X-Domain_NRPS |
cd19546 |
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ... |
109-380 |
3.50e-05 |
|
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to the non-ribosomal peptide synthetase (NRPS); The X-domain is a catalytically inactive member of the Condensation (C) domain family of non-ribosomal peptide synthetase (NRPS). It has been shown to recruit oxygenases to the NRPS to perform side-chain crosslinking in the production of glycopeptide antibiotics. 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 this X-domain, 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, and dual E/C (epimerization and condensation) domains. 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 X-domain subfamily lack the second H of this motif.
Pssm-ID: 380468 [Multi-domain] Cd Length: 440 Bit Score: 48.24 E-value: 3.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 109 ELDPERMTAAWRALIARHDMLRAVVEADGA---QRVL-AEVPPFEVPVIDLTgrPEAVVDAAVSAVRAEMDHLVHTPDRW 184
Cdd:cd19546 38 RLDRDALEAALGDVAARHEILRTTFPGDGGdvhQRILdADAARPELPVVPAT--EEELPALLADRAAHLFDLTRETPWRC 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 185 PLFAarITRADHrtVLHVSIDFLIADFISVQVVLDELHRLY-HRPDEPLP---PLEITFRDYQLAERAVRDSPRhERDK- 259
Cdd:cd19546 116 TLFA--LSDTEH--VLLLVVHRIAADDESLDVLVRDLAAAYgARREGRAPeraPLPLQFADYALWERELLAGED-DRDSl 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 260 -----QWWLARVDELPAAPELPT-VARPADSEGRFRRWETRLSSQVWEGLRQRAGRHGVSPSGAVLAAFSDTIAAYSRRS 333
Cdd:cd19546 191 igdqiAYWRDALAGAPDELELPTdRPRPVLPSRRAGAVPLRLDAEVHARLMEAAESAGATMFTVVQAALAMLLTRLGAGT 270
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1860141834 334 RFTLDiTLLNRAPVHDQVNALVGDFTSVDLLAVD--ADPT-RRFDERARD 380
Cdd:cd19546 271 DVTVG-TVLPRDDEEGDLEGMVGPFARPLALRTDlsGDPTfRELLGRVRE 319
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1370-1413 |
4.06e-05 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 48.06 E-value: 4.06e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1860141834 1370 RISRDDLTEHLAGRLPQYMVPSVVQVVDALPLNANGKVDRAVLR 1413
Cdd:cd05934 379 TLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
1348-1420 |
4.24e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 48.11 E-value: 4.24e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1860141834 1348 PDGFIAELGMCVLAARfktDRVRISRDDLTEHLAGRLPQYMVPSVVQVVDALPLNANGKVDRAVLRRRLPRRG 1420
Cdd:PRK07470 451 PDPVWGEVGVAVCVAR---DGAPVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVREELEERG 520
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
552-703 |
4.56e-05 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 48.43 E-value: 4.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 552 RTLDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGA----LLAGCVYVPV--DTSQPAARR---RTILT 622
Cdd:PTZ00216 120 RYITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIwsqsMVAATVYANLgeDALAYALREtecKAIVC 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 623 NA--------GIRCALTQ-----------SGVDrngwAEGLRLL---DVDLLGTGQPQ--PVEGSGDPEELAYVIHTSGS 678
Cdd:PTZ00216 200 NGknvpnllrLMKSGGMPnttiiyldslpASVD----TEGCRLVawtDVVAKGHSAGShhPLNIPENNDDLALIMYTSGT 275
|
170 180
....*....|....*....|....*
gi 1860141834 679 TGSPKGVMINHRGAVNTVLDINDRF 703
Cdd:PTZ00216 276 TGDPKGVMHTHGSLTAGILALEDRL 300
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
666-741 |
5.50e-05 |
|
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: 48.12 E-value: 5.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 666 PEELAYVIHTSGSTGSPKGVMINHRGAVNTVLDINDRFG-VGPDDR------VLGLSNLGfdLSVYDVFGPLSVGGAVVL 738
Cdd:cd05933 149 PNQCCTLIYTSGTTGMPKGVMLSHDNITWTAKAASQHMDlRPATVGqesvvsYLPLSHIA--AQILDIWLPIKVGGQVYF 226
|
...
gi 1860141834 739 PDP 741
Cdd:cd05933 227 AQP 229
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
1370-1413 |
6.29e-05 |
|
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: 47.63 E-value: 6.29e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1860141834 1370 RISRDDLTEHLAGRLPQYMVPSVVQVVDALPLNANGKVDRAVLR 1413
Cdd:cd12119 474 TVTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALR 517
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
535-948 |
6.35e-05 |
|
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: 47.65 E-value: 6.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 535 VLQALSTPDRPAVVAAD----RTLDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVL-----GALLAGC-- 603
Cdd:cd05943 76 LLRHADADDPAAIYAAEdgerTEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLatasiGAIWSSCsp 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 604 -----------------VYVPVDTSQPAARRRTILTN-AGIRCAL-----------TQSGVDRNGWAEGLRLLDVDLLGT 654
Cdd:cd05943 156 dfgvpgvldrfgqiepkVLFAVDAYTYNGKRHDVREKvAELVKGLpsllavvvvpyTVAAGQPDLSKIAKALTLEDFLAT 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 655 GQPQPVEGSGDP-EELAYVIHTSGSTGSPK-------GVMINHRGAVNTVLDIndrfgvGPDDRVLGLSNLGFDLSVYDV 726
Cdd:cd05943 236 GAAGELEFEPLPfDHPLYILYSSGTTGLPKcivhgagGTLLQHLKEHILHCDL------RPGDRLFYYTTCGWMMWNWLV 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 727 FGpLSVGGAVVLPD--PQRRGDPSHWaDLVGTHGVTVWNSVPAQLQML--------HDYLVSATATV-PDGLRLAMLSGD 795
Cdd:cd05943 310 SG-LAVGATIVLYDgsPFYPDTNALW-DLADEEGITVFGTSAKYLDALekaglkpaETHDLSSLRTIlSTGSPLKPESFD 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 796 WIpvalPDQIRARVPglrIVSLGGATE-ASIWSIWYPIeqvDPEWRSIPYGRPLtNQSFHVLDAALRPRPDlVSGELYI- 873
Cdd:cd05943 388 YV----YDHIKPDVL---LASISGGTDiISCFVGGNPL---LPVYRGEIQCRGL-GMAVEAFDEEGKPVWG-EKGELVCt 455
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1860141834 874 -GGVGLAVGYLNDRERTAER---FVVHPQtgerLYRTGDLGRYLPDGTIEFLGREDLQVKIRGYRIELAEIEAALGGHP 948
Cdd:cd05943 456 kPFPSMPVGFWNDPDGSRYRaayFAKYPG----VWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIP 530
|
|
| FUM14_C_NRPS-like |
cd19545 |
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ... |
75-387 |
6.54e-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: 47.29 E-value: 6.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 75 FPVTDVQAAYLlgrGETFAYGGVACHGYGELVYPELDPERMTAAWRALIARHDMLR---AVVEADGA-QRVLAEVPPF-- 148
Cdd:cd19545 2 YPCTPLQEGLM---ALTARQPGAYVGQRVFELPPDIDLARLQAAWEQVVQANPILRtriVQSDSGGLlQVVVKESPISwt 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 149 EVPVIDltgrpeavvdaavsavraemDHLVHTPDR-----WPLFAARITR-ADHRTVLHVSIDFLIADFISVQVVLDELH 222
Cdd:cd19545 79 ESTSLD--------------------EYLEEDRAApmglgGPLVRLALVEdPDTERYFVWTIHHALYDGWSLPLILRQVL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 223 RLYHRPDEPLPPleiTFRDYQlaeRAVRDSpRHERDKQWW---LARVDElPAAPELPtVARPADSEGRFRRWETRLSSQV 299
Cdd:cd19545 139 AAYQGEPVPQPP---PFSRFV---KYLRQL-DDEAAAEFWrsyLAGLDP-AVFPPLP-SSRYQPRPDATLEHSISLPSSA 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 300 weglrqragRHGVSPSGAVLAAFSDTIAAYSRRSRFTLDITLLNR-APVhDQVNALVGD-FTSVDlLAVDADPTRRFDER 377
Cdd:cd19545 210 ---------SSGVTLATVLRAAWALVLSRYTGSDDVVFGVTLSGRnAPV-PGIEQIVGPtIATVP-LRVRIDPEQSVEDF 278
|
330
....*....|
gi 1860141834 378 ARDLQAQLWE 387
Cdd:cd19545 279 LQTVQKDLLD 288
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
1359-1420 |
6.99e-05 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 47.45 E-value: 6.99e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1860141834 1359 VLAARFKTDRVRISRDDLTEHLAGRLPQYMVPSVVQVVDALPLNANGKVDRAVLR---------------RRLPRRG 1420
Cdd:PRK06155 465 VMAAVVLRDGTALEPVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLReqgvtadtwdreaagVQLPRSG 541
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
1354-1430 |
7.45e-05 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 47.46 E-value: 7.45e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1860141834 1354 ELGMCVLAARFKTDRVRIsrDDLTEHLAGRLPQYMVPSVVQVVDALPLNANGKVDRAVLRRRLPRRGTATAAGSSGA 1430
Cdd:PRK07786 462 EVPVAVAAVRNDDAALTL--EDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTELRERYGACVNVERRSASAG 536
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
552-951 |
7.82e-05 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 47.37 E-value: 7.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 552 RTLDYAEL---LGRAAGVAEALtaaGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVDTSQPAARRRTILTNAGIRC 628
Cdd:PRK08008 36 RRYSYLELneeINRTANLFYSL---GIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 629 ALTQSGV----DRNGWAEGLRLLDVDLLGTGQP--------------QPVE-------GSGDPEElayVIHTSGSTGSPK 683
Cdd:PRK08008 113 LVTSAQFypmyRQIQQEDATPLRHICLTRVALPaddgvssftqlkaqQPATlcyapplSTDDTAE---ILFTSGTTSRPK 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 684 GVMINHrgavntvldINDRFG---------VGPDDRVLG-LSNLGFDLSVYDVFGPLSVGGAVVLPD--PQRRgdpshwa 751
Cdd:PRK08008 190 GVVITH---------YNLRFAgyysawqcaLRDDDVYLTvMPAFHIDCQCTAAMAAFSAGATFVLLEkySARA------- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 752 dlvgthgvtVWNSVpaqlqmlHDYLVSATATVPDGLRLAMLSgdwiPVA----------------LPDQ----IRARVpG 811
Cdd:PRK08008 254 ---------FWGQV-------CKYRATITECIPMMIRTLMVQ----PPSandrqhclrevmfylnLSDQekdaFEERF-G 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 812 LRIVSLGGATEASIWSIW-YPIEQvdPEWRSIpyGRPLTNQSFHVLDAALRPRPDLVSGELYIGGV---GLAVGYLNDRE 887
Cdd:PRK08008 313 VRLLTSYGMTETIVGIIGdRPGDK--RRWPSI--GRPGFCYEAEIRDDHNRPLPAGEIGEICIKGVpgkTIFKEYYLDPK 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1860141834 888 RTAERFvvhpqTGERLYRTGDLGRYLPDGTIEFLGREDLQVKIRGYRIELAEIEAALGGHPAVA 951
Cdd:PRK08008 389 ATAKVL-----EADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQ 447
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
656-948 |
8.38e-05 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 47.44 E-value: 8.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 656 QPQPVegsgDPEELAYVIHTSGSTGSPKGVMinHR------GAVNT---VLDINDrfgvgpDDR---------VLGLSnl 717
Cdd:PRK00174 238 EPEPM----DAEDPLFILYTSGSTGKPKGVL--HTtggylvYAAMTmkyVFDYKD------GDVywctadvgwVTGHS-- 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 718 gfdlsvYDVFGPLSVGGAVVL-------PDPQRrgdpshWADLVGTHGVTVWnsvpaqlqmlhdYlvsataTVPDGLRLA 790
Cdd:PRK00174 304 ------YIVYGPLANGATTLMfegvpnyPDPGR------FWEVIDKHKVTIF------------Y------TAPTAIRAL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 791 MLSGDWIPValpdqiRARVPGLRIvsLGgaT-------EAsiWsIWY---------PIeqVDPEWRS---------IPYG 845
Cdd:PRK00174 354 MKEGDEHPK------KYDLSSLRL--LG--SvgepinpEA--W-EWYykvvggercPI--VDTWWQTetggimitpLPGA 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 846 RPLTNQSfhvldaALRP----RPDLV--SGELYIGGVGlavGYLNDRE------RTA----ERFVvhpQT------GErl 903
Cdd:PRK00174 419 TPLKPGS------ATRPlpgiQPAVVdeEGNPLEGGEG---GNLVIKDpwpgmmRTIygdhERFV---KTyfstfkGM-- 484
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1860141834 904 YRTGDLGRYLPDGTIEFLGREDLQVKIRGYRIELAEIEAALGGHP 948
Cdd:PRK00174 485 YFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHP 529
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
650-948 |
9.39e-05 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 47.15 E-value: 9.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 650 DLLGTGQP----QPVEGSGDPEELAYvihTSGSTGSPKGVMINHRGAVntvldindrfgvgpddrVLGLSNlgfdlsvyd 725
Cdd:PLN02479 177 KFLETGDPefawKPPADEWQSIALGY---TSGTTASPKGVVLHHRGAY-----------------LMALSN--------- 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 726 vfgPLSVG---GAV---VLPDPQRRGDPSHW--ADLVGT------------------HGVTVWNSVPAQLQMLHDYLVSA 779
Cdd:PLN02479 228 ---ALIWGmneGAVylwTLPMFHCNGWCFTWtlAALCGTniclrqvtakaiysaianYGVTHFCAAPVVLNTIVNAPKSE 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 780 TATVPDGLRLAMLSGDWIPVALPDQIRARvpGLRIVSLGGATEA---SIWSIWypieqvDPEWRSIPygrPLTNQSFH-- 854
Cdd:PLN02479 305 TILPLPRVVHVMTAGAAPPPSVLFAMSEK--GFRVTHTYGLSETygpSTVCAW------KPEWDSLP---PEEQARLNar 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 855 ------------VLDA-ALRPRP--DLVSGELYIGGVGLAVGYLNDRERTAERFvvhpQTGerLYRTGDLGRYLPDGTIE 919
Cdd:PLN02479 374 qgvryiglegldVVDTkTMKPVPadGKTMGEIVMRGNMVMKGYLKNPKANEEAF----ANG--WFHSGDLGVKHPDGYIE 447
|
330 340
....*....|....*....|....*....
gi 1860141834 920 FLGREDLQVKIRGYRIELAEIEAALGGHP 948
Cdd:PLN02479 448 IKDRSKDIIISGGENISSLEVENVVYTHP 476
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
553-690 |
1.06e-04 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 47.06 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 553 TLDYAELLGRAAGVAEAL-TAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVDTSQPAARRRTILT--------- 622
Cdd:cd17632 67 TITYAELWERVGAVAAAHdPEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAeteprllav 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 623 -----NAGIRCALTQSGVDR--------------------------NGWAEGLRLLDVDLLGTGQPQPVEGSG-DPEELA 670
Cdd:cd17632 147 saehlDLAVEAVLEGGTPPRlvvfdhrpevdahraalesarerlaaVGIPVTTLTLIAVRGRDLPPAPLFRPEpDDDPLA 226
|
170 180
....*....|....*....|
gi 1860141834 671 YVIHTSGSTGSPKGVMINHR 690
Cdd:cd17632 227 LLIYTSGSTGTPKGAMYTER 246
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
1365-1412 |
1.33e-04 |
|
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: 46.50 E-value: 1.33e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1860141834 1365 KTDRVRISRDDLTEHLAGRLPQYMVPSVVQVVDALPLNANGKVDRAVL 1412
Cdd:cd12114 430 DNDGTPIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
651-943 |
1.51e-04 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 46.88 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 651 LLGTGQPQPVEGSGDPEELAYVIHTSGSTGSPKGVMINHRGAVNTVLDINDRFGVGPDDRVLGLsnlgfdLSVYDVFG-- 728
Cdd:PRK06814 777 LLAGRFPLVYFCNRDPDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPEDKVFNA------LPVFHSFGlt 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 729 -----PLSVGGAVVL-PDP-QRRGDPshwaDLVGTHGVTVWNSVPAQL----QMLHDY------LVSATA-TVPDGLRla 790
Cdd:PRK06814 851 gglvlPLLSGVKVFLyPSPlHYRIIP----ELIYDTNATILFGTDTFLngyaRYAHPYdfrslrYVFAGAeKVKEETR-- 924
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 791 mlsgdwipvalpdQIRARVPGLRIVSLGGATEASiwsiwyPIeqvdpewrsIPYGRPLTNQSFHV------LDAALRPRP 864
Cdd:PRK06814 925 -------------QTWMEKFGIRILEGYGVTETA------PV---------IALNTPMHNKAGTVgrllpgIEYRLEPVP 976
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 865 DLVSGE-LYIGGVGLAVGYLNdrertAERFVVHPQTGERLYRTGDLGRYLPDGTIEFLGREDLQVKIRGYRIELAEIEAA 943
Cdd:PRK06814 977 GIDEGGrLFVRGPNVMLGYLR-----AENPGVLEPPADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEEL 1051
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
1371-1414 |
1.56e-04 |
|
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: 46.13 E-value: 1.56e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1860141834 1371 ISRDDLTEHLAGRLPQYMVPSVVQVVDALPLNANGKVDRAVLRR 1414
Cdd:cd05941 399 LSLEELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
1369-1406 |
1.63e-04 |
|
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: 41.76 E-value: 1.63e-04
10 20 30
....*....|....*....|....*....|....*...
gi 1860141834 1369 VRISRDDLTEHLAGRLPQYMVPSVVQVVDALPLNANGK 1406
Cdd:pfam13193 39 VELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| LCL_NRPS |
cd19538 |
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ... |
109-383 |
1.73e-04 |
|
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: 46.10 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 109 ELDPERMTAAWRALIARHDMLRAV-VEADGA--QRVLAEV---PPFEVPVIDltgrpeavvdaavsavRAEMDHLVHTPD 182
Cdd:cd19538 35 KLDVQALQQALYDVVERHESLRTVfPEEDGVpyQLILEEDeatPKLEIKEVD----------------EEELESEINEAV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 183 RWPL-------FAARITRADHRT-VLHVSIDFLIADFISVQVVLDELHRLYHRPDE----PLPPLEITFRDY-----QLA 245
Cdd:cd19538 99 RYPFdlseeppFRATLFELGENEhVLLLLLHHIAADGWSLAPLTRDLSKAYRARCKgeapELAPLPVQYADYalwqqELL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 246 ERAVRDSPRHERDKQWWLARVDELPAAPELPT-VARPADS--EGRFRRWEtrLSSQVWEGLRQRAGRHGVSPSGAVLAAF 322
Cdd:cd19538 179 GDESDPDSLIARQLAYWKKQLAGLPDEIELPTdYPRPAESsyEGGTLTFE--IDSELHQQLLQLAKDNNVTLFMVLQAGF 256
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1860141834 323 SdtiAAYSRRSRFTlDITLlnRAPV----HDQVNALVGDFTSVDLLAVD--ADPTrrFDE-----RARDLQA 383
Cdd:cd19538 257 A---ALLTRLGAGT-DIPI--GSPVagrnDDSLEDLVGFFVNTLVLRTDtsGNPS--FREllervKETNLEA 320
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
110-532 |
2.05e-04 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 46.49 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 110 LDPERMTAAWRALIARHDMLR-AVVEADGAQRVLAEVPPFEVPVIDLTGRPEAVVDAAVSAVRAEMDhLVHTPdrwPLFA 188
Cdd:PRK12316 1133 LDPDRLGRALERLVAHHDALRlRFREEDGGWQQAYAAPQAGEVLWQRQAASEEELLALCEEAQRSLD-LEQGP---LLRA 1208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 189 ARITRADHRTVLHVSIDFLIADFISVQVVLDELHRLYHRPDEPLPPLEITFRdyQLAERAVRDSPRHERDKQWWLARVDE 268
Cdd:PRK12316 1209 LLVDMADGSQRLLLVIHHLVVDGVSWRILLEDLQRAYADLDADLPARTSSYQ--AWARRLHEHAGARAEELDYWQAQLED 1286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 269 lpAAPELPTVARPADSEGRF-RRWETRLSSQVWEGLRQRA-GRHGVSPSGAVLAAFSDTIAAYSRRSRFTLDITLLNRAP 346
Cdd:PRK12316 1287 --APHELPCENPDGALENRHeRKLELRLDAERTRQLLQEApAAYRTQVNDLLLTALARVTCRWSGQASVLVQLEGHGRED 1364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 347 VHDQVN--ALVGDFTSvdLLAVDADPTRRFDERARDLQAQLWEDLDH-------RSFSGIEVMREIAR------------ 405
Cdd:PRK12316 1365 LFEDIDlsRTVGWFTS--LFPVRLTPAADLGESIKAIKEQLRAVPDKgigygllRYLAGEEAAARLAAlpqpritfnylg 1442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 406 ---RQGAEAALFpvvftsAIGITSAGAAAD-GAPLGELgygISQTPQVWidcqnierDGGLVSNWDVREEVFPPGVVDDM 481
Cdd:PRK12316 1443 qfdRQFDEAALF------VPATESAGAAQDpCAPLANW---LSIEGQVY--------GGELSLHWSFSREMFAEATVQRL 1505
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1860141834 482 FAAYDAVLHRLAgDDAAWTGTGHPDPPEATRDRRAETNRTQAPVPAGMLHD 532
Cdd:PRK12316 1506 ADDYARELQALI-EHCCDERNRGVTPSDFPLAGLSQAQLDALPLPAGEIAD 1555
|
|
| PKS_PP |
smart00823 |
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ... |
1424-1510 |
2.20e-04 |
|
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.
Pssm-ID: 214834 [Multi-domain] Cd Length: 86 Bit Score: 41.47 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 1424 AAGSSGALDSDLERRIAAVWAEALRLP---RVGRDENLFELGGDSLVAAQITGRILEE--IPQAAGLFFDqllrqvleQP 1498
Cdd:smart00823 2 AALPPAERRRLLLDLVREQVAAVLGHAaaeAIDPDRPFRDLGLDSLMAVELRNRLEAAtgLRLPATLVFD--------HP 73
|
90
....*....|..
gi 1860141834 1499 TVAALAGHVEAE 1510
Cdd:smart00823 74 TPAALAEHLAAE 85
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
1378-1412 |
2.26e-04 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 45.66 E-value: 2.26e-04
10 20 30
....*....|....*....|....*....|....*
gi 1860141834 1378 EHLAGRLPQYMVPSVVQVVDALPLNANGKVDRAVL 1412
Cdd:PRK04813 463 KELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
543-951 |
2.69e-04 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 45.58 E-value: 2.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 543 DRPAVVAADRTLDYAELLGRAAGVAEALTA-AGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVDTSQPAARRRTIL 621
Cdd:PRK12492 39 DRPAFSNLGVTLSYAELERHSAAFAAYLQQhTDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPLYTAREMRHQF 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 622 TNAGIRC-------------ALTQSGVDR-------------NGW------------------AEGLRLLDVDLLGTGQ- 656
Cdd:PRK12492 119 KDSGARAlvylnmfgklvqeVLPDTGIEYlieakmgdllpaaKGWlvntvvdkvkkmvpayhlPQAVPFKQALRQGRGLs 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 657 PQPVEGSGDpeELAYVIHTSGSTGSPKGVMINHRGAVNTVLDINDRFG-VGPDDRVL---GLSNLGFDLSVYDVFGpLSV 732
Cdd:PRK12492 199 LKPVPVGLD--DIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSqLGPDGQPLmkeGQEVMIAPLPLYHIYA-FTA 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 733 GGAVVLpdpqrrgdpshwadLVGTHGVTVWN--SVPAQLQMLHDYLVSATATVpDGLRLAML-----------------S 793
Cdd:PRK12492 276 NCMCMM--------------VSGNHNVLITNprDIPGFIKELGKWRFSALLGL-NTLFVALMdhpgfkdldfsalkltnS 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 794 GDWIPVALPDQIRARVPGLRIVSLGGATEASiwsiwyPIEQVDP---EWRSIPYGRPLTNQSFHVLDAALRPRPDLVSGE 870
Cdd:PRK12492 341 GGTALVKATAERWEQLTGCTIVEGYGLTETS------PVASTNPygeLARLGTVGIPVPGTALKVIDDDGNELPLGERGE 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 871 LYIGGVGLAVGYLNDRERTAERFvvhpqTGERLYRTGDLGRYLPDGTIEFLGREDLQVKIRGYRIELAEIEAALGGHPAV 950
Cdd:PRK12492 415 LCIKGPQVMKGYWQQPEATAEAL-----DAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKV 489
|
.
gi 1860141834 951 A 951
Cdd:PRK12492 490 A 490
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
552-946 |
2.99e-04 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 45.37 E-value: 2.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 552 RTLDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAG----CVYVP---VDTSQPAARRRTILTNA 624
Cdd:PRK07768 28 VRHTWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGasltMLHQPtprTDLAVWAEDTLRVIGMI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 625 GIRCALTQSGVDRNG---WAEGLRLLDV-DLLGTGQPQPVEGsgDPEELAYVIHTSGSTGSPKGVMINHRGAVNTVLDIN 700
Cdd:PRK07768 108 GAKAVVVGEPFLAAApvlEEKGIRVLTVaDLLAADPIDPVET--GEDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMF 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 701 DRFGVGPDDRV----LGLSN----LGFdLSVydvfgPLSVGGAVVLPDPQR-RGDPSHWADLVGTHGVTVWNSVPAQLQM 771
Cdd:PRK07768 186 VAAEFDVETDVmvswLPLFHdmgmVGF-LTV-----PMYFGAELVKVTPMDfLRDPLLWAELISKYRGTMTAAPNFAYAL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 772 LHDYLVSATatvPDG------LRLAMLSGDWI-PVALPDQIRARVP-GLR---IVSLGGATEASI------WSIWYPIEQ 834
Cdd:PRK07768 260 LARRLRRQA---KPGafdlssLRFALNGAEPIdPADVEDLLDAGARfGLRpeaILPAYGMAEATLavsfspCGAGLVVDE 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 835 VDPEW-----RSIP-----------YGRPLTNQSFHVLDAALRPRPDLVSGELYIGGVGLAVGYLndrerTAERFVvhPQ 898
Cdd:PRK07768 337 VDADLlaalrRAVPatkgntrrlatLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRGESVTPGYL-----TMDGFI--PA 409
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1860141834 899 TGER-LYRTGDLGRYLPDGTIEFLGREDLQVKIRGYRIELAEIEAALGG 946
Cdd:PRK07768 410 QDADgWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAAR 458
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
541-761 |
3.03e-04 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 45.56 E-value: 3.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 541 TPDRPAVVAAD-----RTLDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVL-----GALLAGC------- 603
Cdd:PRK03584 97 RDDRPAIIFRGedgprRELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLataslGAIWSSCspdfgvq 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 604 ------------VYVPVDTSQPAARRRTIL-TNAGIRCALT----------QSGVDRNGWAEGLRLLDvDLLGTGQPQPV 660
Cdd:PRK03584 177 gvldrfgqiepkVLIAVDGYRYGGKAFDRRaKVAELRAALPslehvvvvpyLGPAAAAAALPGALLWE-DFLAPAEAAEL 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 661 EgsgdPEELA-----YVIHTSGSTGSPK-------GVMINHRGAVNTVLDIndrfgvGPDDRVLGLSNLGFDLSVYDVFG 728
Cdd:PRK03584 256 E----FEPVPfdhplWILYSSGTTGLPKcivhghgGILLEHLKELGLHCDL------GPGDRFFWYTTCGWMMWNWLVSG 325
|
250 260 270
....*....|....*....|....*....|....*....
gi 1860141834 729 pLSVGGAVVLPDpqrrGDPSH------WaDLVGTHGVTV 761
Cdd:PRK03584 326 -LLVGATLVLYD----GSPFYpdpnvlW-DLAAEEGVTV 358
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
590-943 |
3.05e-04 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 45.58 E-value: 3.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 590 EQVVAVLGALLAGCVYVPVDTSQPAARRRTILTNAGIRCALTQSGVDRNG--------------------------WAEG 643
Cdd:PLN03051 6 DAVIIYLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFTQDVVLRGGralplyskvveaapakaivlpaagepVAVP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 644 LRLLDV---DLLGTGQPQPVEGSGDP-------EELAYVIHTSGSTGSPKGVMINHRGAVNTVLDINDRFGVGPDDRVLG 713
Cdd:PLN03051 86 LREQDLswcDFLGVAAAQGSVGGNEYspvyapvESVTNILFSSGTTGEPKAIPWTHLSPLRCASDGWAHMDIQPGDVVCW 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 714 LSNLGFDLSVYDVFGPLSVGGAVVL--PDPQRRGdpshWADLVGTHGVTVWNSVP----------AQLQMLHDY------ 775
Cdd:PLN03051 166 PTNLGWMMGPWLLYSAFLNGATLALygGAPLGRG----FGKFVQDAGVTVLGLVPsivkawrhtgAFAMEGLDWsklrvf 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 776 -LVSATATVPDGLRLAMLSGDWIPValpdqirarvpglrIVSLGGATEASIWSIWYPIEQVDPEwrsiPYGRPLTNQSFH 854
Cdd:PLN03051 242 aSTGEASAVDDVLWLSSVRGYYKPV--------------IEYCGGTELASGYISSTLLQPQAPG----AFSTASLGTRFV 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 855 VLDAALRPRPDLVSgelYIGGVGLAVGYL--NDRERTAERFVVH-------PQTGERLYRTGDLGRYLPDGTIEFLGRED 925
Cdd:PLN03051 304 LLNDNGVPYPDDQP---CVGEVALAPPMLgaSDRLLNADHDKVYykgmpmyGSKGMPLRRHGDIMKRTPGGYFCVQGRAD 380
|
410
....*....|....*...
gi 1860141834 926 LQVKIRGYRIELAEIEAA 943
Cdd:PLN03051 381 DTMNLGGIKTSSVEIERA 398
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
1371-1416 |
3.23e-04 |
|
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: 45.52 E-value: 3.23e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1860141834 1371 ISRDDLTEHLAGR-LPQYMVPSVVQVVDALPLNANGKVDRAVLRRRL 1416
Cdd:COG1021 485 LTLAELRRFLRERgLAAFKLPDRLEFVDALPLTAVGKIDKKALRAAL 531
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
1371-1417 |
3.78e-04 |
|
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: 45.12 E-value: 3.78e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1860141834 1371 ISRDDLTEHLAGRLPQYMVPSVVQVVDALPLNANGKVDravlRRRLP 1417
Cdd:cd17644 423 PSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKID----RRALP 465
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
1371-1413 |
4.13e-04 |
|
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: 44.86 E-value: 4.13e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1860141834 1371 ISRDDLTEHLAGRLPQYMVPSVVQVVDALPLNANGKVDRAVLR 1413
Cdd:cd05936 426 LTEEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
665-824 |
4.46e-04 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 45.08 E-value: 4.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 665 DPEELAYVIHTSGSTGSPKGVMINHRgavNTVLdinDRFGVG-PDdrVLGLSNLGFDLSVYDVF----------GPLsVG 733
Cdd:PRK07008 174 DENQASSLCYTSGTTGNPKGALYSHR---STVL---HAYGAAlPD--AMGLSARDAVLPVVPMFhvnawglpysAPL-TG 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 734 GAVVLPDPQRRGDPSHwaDLVGTHGVTVWNSVPAQLQMLHDYLVSAtatvpdGLRLAMLS-----GDWIPvalPDQIRA- 807
Cdd:PRK07008 245 AKLVLPGPDLDGKSLY--ELIEAERVTFSAGVPTVWLGLLNHMREA------GLRFSTLRrtvigGSACP---PAMIRTf 313
|
170
....*....|....*...
gi 1860141834 808 -RVPGLRIVSLGGATEAS 824
Cdd:PRK07008 314 eDEYGVEVIHAWGMTEMS 331
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
1371-1408 |
6.23e-04 |
|
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: 43.81 E-value: 6.23e-04
10 20 30
....*....|....*....|....*....|....*...
gi 1860141834 1371 ISRDDLTEHLAGRLPQYMVPSVVQVVDALPLNANGKVD 1408
Cdd:cd04433 299 LDAEELRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
1348-1416 |
6.95e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 44.41 E-value: 6.95e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1860141834 1348 PDGFIAELGMCVLAARFKTDrvrISRDDLTEHLAGRLPQYMVPSVVQVVDALPLNANGKVDRAVLRRRL 1416
Cdd:PRK09088 418 ADAQWGEVGYLAIVPADGAP---LDLERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLRDAL 483
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
537-741 |
8.65e-04 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 44.03 E-value: 8.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 537 QALSTPDRPAVVAADRTL--DYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVYVPVDtsqPA 614
Cdd:PRK08315 25 TAARYPDREALVYRDQGLrwTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVTIN---PA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 615 ARRrtiltnAGIRCALTQSGVDRNGWAEGLRllDVDL----------LGTGQPQPVEGSGDPEeLAYVIH---------- 674
Cdd:PRK08315 102 YRL------SELEYALNQSGCKALIAADGFK--DSDYvamlyelapeLATCEPGQLQSARLPE-LRRVIFlgdekhpgml 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 675 ----------------------------------TSGSTGSPKGVMINHRGAVNTVLDINDRFGVGPDDR---------- 710
Cdd:PRK08315 173 nfdellalgravddaelaarqatldpddpiniqyTSGTTGFPKGATLTHRNILNNGYFIGEAMKLTEEDRlcipvplyhc 252
|
250 260 270
....*....|....*....|....*....|....*...
gi 1860141834 711 ---VLGlsnlgfdlsvydVFGPLSVGGAVVLP----DP 741
Cdd:PRK08315 253 fgmVLG------------NLACVTHGATMVYPgegfDP 278
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
1366-1425 |
9.12e-04 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 44.19 E-value: 9.12e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1860141834 1366 TDRVRISRDDLTEHLAGR-LPQYMVPSVVQVVDALPLNANGKVDRAVLRRRLPRRGTATAA 1425
Cdd:PRK06814 1079 TTASDATRAAFLAHAKAAgASELMVPAEIITIDEIPLLGTGKIDYVAVTKLAEEAAAKPEA 1139
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
1360-1417 |
9.16e-04 |
|
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: 43.93 E-value: 9.16e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1860141834 1360 LAARFKTDRVRISRDDLTEHLAGRLPQYMVPSVVQVVDALPLNANGKVDravlRRRLP 1417
Cdd:cd17648 400 LVGYYLPEPGHVPESDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKLD----VRALP 453
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
665-948 |
9.95e-04 |
|
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: 43.57 E-value: 9.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 665 DPEELAYVIHTSGSTGSPKGVMINHRGAVNTVLDINDRFGVGPDDRV-----LGLSNLGFDLSVYDvfgpLSVGGAVVLp 739
Cdd:cd05937 85 DPDDPAILIYTSGTTGLPKAAAISWRRTLVTSNLLSHDLNLKNGDRTytcmpLYHGTAAFLGACNC----LMSGGTLAL- 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 740 dpQRRGDPSH-WADLVGThGVTVWNSVPAQLQmlhdYLVSATATVPDGL-RLAMLSGDWIPVALPDQIRAR--VPglRIV 815
Cdd:cd05937 160 --SRKFSASQfWKDVRDS-GATIIQYVGELCR----YLLSTPPSPYDRDhKVRVAWGNGLRPDIWERFRERfnVP--EIG 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 816 SLGGATEA--SIW----------------SIW-------YPIEQVDPEWRSiPYGRPLTnqSFHVldAALRPRPDLVSGE 870
Cdd:cd05937 231 EFYAATEGvfALTnhnvgdfgagaighhgLIRrwkfenqVVLVKMDPETDD-PIRDPKT--GFCV--RAPVGEPGEMLGR 305
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1860141834 871 LYIGGVGLAVGYLNDRERTAERFVVHP-QTGERLYRTGDLGRYLPDGTIEFLGREDLQVKIRGYRIELAEIEAALGGHP 948
Cdd:cd05937 306 VPFKNREAFQGYLHNEDATESKLVRDVfRKGDIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHP 384
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
666-710 |
1.03e-03 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 43.93 E-value: 1.03e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1860141834 666 PEELAYVIHTSGSTGSPKGVMINHRGAVNTVLDINDRFGVGPDDR 710
Cdd:PLN02736 220 PEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKFYPSDV 264
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
665-944 |
1.66e-03 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 43.27 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 665 DPEELAYVIHTSGSTGSPKGVMINHRGAVNTVLDINDRFGVGPDDRVLGLsnlgfdLSVYDVFG-------PLSVGGAVV 737
Cdd:PRK06334 181 DPEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSF------LPPFHAYGfnsctlfPLLSGVPVV 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 738 LP-DPQRrgdPSHWADLVGTHGVTVWNSVPaqlqMLHDYLVSA---TATVPDGLRLAMLSGDWIPVALPDQIRARVPGLR 813
Cdd:PRK06334 255 FAyNPLY---PKKIVEMIDEAKVTFLGSTP----VFFDYILKTakkQESCLPSLRFVVIGGDAFKDSLYQEALKTFPHIQ 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 814 IVSLGGATEASiwsiwyP---IEQVDPEWRSIPYGRPLTNQSFHVLDAALR-PRPDLVSGELYIGGVGLAVGYLNDRErt 889
Cdd:PRK06334 328 LRQGYGTTECS------PvitINTVNSPKHESCVGMPIRGMDVLIVSEETKvPVSSGETGLVLTRGTSLFSGYLGEDF-- 399
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1860141834 890 AERFVvhPQTGERLYRTGDLGRYLPDGTIEFLGREDLQVKIRGYRIELAEIEAAL 944
Cdd:PRK06334 400 GQGFV--ELGGETWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESIL 452
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
1370-1415 |
1.77e-03 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 42.97 E-value: 1.77e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1860141834 1370 RISRDDLTEHLAGRLPQYMVPSVVQVVDALPLNANGKVDRAVLRRR 1415
Cdd:PRK07656 468 ELTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRALREK 513
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
551-711 |
1.80e-03 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 42.80 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 551 DRTLDYAELLGRAAGVAEALTAAGCRRQELVAVVMDRGWEQVVAVLGALLAGCVyvpvdtsqpaarrrTILTNAGIRC-A 629
Cdd:cd05939 1 DRHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVE--------------TALINSNLRLeS 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 630 LTQSGVDRNGWAEGLRLLDVDLLGTGQPQPVEGSGDPEELAYVIHTSGSTGSPKGVMINHRGAVNTVLDINDRFGVGPDD 709
Cdd:cd05939 67 LLHCITVSKAKALIFNLLDPLLTQSSTEPPSQDDVNFRDKLFYIYTSGTTGLPKAAVIVHSRYYRIAAGAYYAFGMRPED 146
|
..
gi 1860141834 710 RV 711
Cdd:cd05939 147 VV 148
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
1373-1416 |
1.99e-03 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 42.79 E-value: 1.99e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1860141834 1373 RDDLTEHLAGRLPQYMVPSVVQVVDALPLNANGKVDRAVLRRRL 1416
Cdd:COG0365 500 AKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKIA 543
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
1331-1416 |
2.02e-03 |
|
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: 42.32 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 1331 LEVLGAAGAAQPL-----CLPEPDgfiAELGMCVLAarFKTDRVRISRDDLTEHLAGRLPQYMVPSVVQVVDALPLNANG 1405
Cdd:cd17630 240 PEEIEAALAAHPAvrdafVVGVPD---EELGQRPVA--VIVGRGPADPAELRAWLKDKLARFKLPKRIYPVPELPRTGGG 314
|
90
....*....|.
gi 1860141834 1406 KVDRAVLRRRL 1416
Cdd:cd17630 315 KVDRRALRAWL 325
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
1355-1416 |
2.19e-03 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 42.34 E-value: 2.19e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1860141834 1355 LGMCVLAARFKTDRVRISRDDLTEHLAGRLPQYMVPSVVQVVDALPLNANGKVDRAVLRRRL 1416
Cdd:PRK07824 294 LGQRVVAAVVGDGGPAPTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVRRF 355
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
1358-1409 |
2.44e-03 |
|
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: 42.26 E-value: 2.44e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1860141834 1358 CVLAARFktdrvRISRDDLTEHLAGRLPQYMVPSVVQVVDALPLNANGKVDR 1409
Cdd:cd17637 287 CVLKPGA-----TLTADELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
1362-1412 |
2.49e-03 |
|
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: 42.54 E-value: 2.49e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1860141834 1362 ARFKTDRVRISRDDLTEHLAGRLPQYMVPSVVQVVDALPLNANGKVDRAVL 1412
Cdd:cd17645 389 VAYVTAPEEIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
550-697 |
2.68e-03 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 42.42 E-value: 2.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 550 ADRTLDYAellGRAAGVAEALT---------AAGCRRQEL------VAVVMDRGWEQVVAVLGALLAGCVYVPV------ 608
Cdd:PRK12476 52 AYRYLDHS---HSAAGCAVELTwtqlgvrlrAVGARLQQVagpgdrVAILAPQGIDYVAGFFAAIKAGTIAVPLfapelp 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 609 ------DTSQPAARRRTILTNAGIRCALTQSgVDRNGWAEGLRLLDVD----LLGTG-QPQPVegsgDPEELAYVIHTSG 677
Cdd:PRK12476 129 ghaerlDTALRDAEPTVVLTTTAAAEAVEGF-LRNLPRLRRPRVIAIDaipdSAGESfVPVEL----DTDDVSHLQYTSG 203
|
170 180
....*....|....*....|
gi 1860141834 678 STGSPKGVMINHRGAVNTVL 697
Cdd:PRK12476 204 STRPPVGVEITHRAVGTNLV 223
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
556-711 |
2.99e-03 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 42.06 E-value: 2.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 556 YAELLGRAAGVAEALTAAGcrRQELVAVVMDRGWEQVVAVLGALLAG-CVYV---PV---DTSQPAARRRTILTNAGIRC 628
Cdd:PRK05851 34 WPEVHGRAENVAARLLDRD--RPGAVGLVGEPTVELVAAIQGAWLAGaAVSIlpgPVrgaDDGRWADATLTRFAGIGVRT 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 629 ALTQSGVDRNGWA--EGLRLLDVDLLG-TGQPQPVEGSgDPEELAYVIHTSGSTGSPKGVMINHRGAVNTVLDINDRFGV 705
Cdd:PRK05851 112 VLSHGSHLERLRAvdSSVTVHDLATAAhTNRSASLTPP-DSGGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVGL 190
|
....*.
gi 1860141834 706 GPDDRV 711
Cdd:PRK05851 191 DAATDV 196
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
1369-1422 |
3.21e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 42.23 E-value: 3.21e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1860141834 1369 VRISRDDLTEHLAGRLPQYMVPSVVQVVDALPLNANGKVDRAVLRRRLPRRGTA 1422
Cdd:PRK08316 470 ATVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKRELRERYAGAFTD 523
|
|
| beta-lac_NRPS |
cd19547 |
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ... |
111-372 |
4.95e-03 |
|
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis NocB which exhibits an unusual cyclization to form beta-lactam rings in pro-nocardicin G synthesis; Nocardia uniformis NRPS NocB acts centrally in the biosynthesis of the nocardicin monocyclic beta-lactam antibiotics. Along with another NRPS NocA, it mediates an unusual cyclization to form beta-lactam rings in the synthesis of the beta-lactam-containing pentapeptide pro-nocardicin G. This small subfamily is related to DCL-type Condensation (C) domains, which catalyze condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. 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; domains belonging to this subfamily have an HHHxxxD motif at the active site.
Pssm-ID: 380469 [Multi-domain] Cd Length: 422 Bit Score: 41.53 E-value: 4.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 111 DPERMTAAWRALIARHDMLRAVV----EADGAQRVLAEV-PPFEVpvIDLTGRPEAVVDAAVSAVRAEMDHLVHTPDRWP 185
Cdd:cd19547 37 DEDVLREAWRRVADRYEILRTGFtwrdRAEPLQYVRDDLaPPWAL--LDWSGEDPDRRAELLERLLADDRAAGLSLADCP 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 186 LFAARITR-ADHRTVLHVSIDFLIADFISVQVVLDELHRLY----HRPDEPLPPLEiTFRDYQLAERAvrDSPRHERDKQ 260
Cdd:cd19547 115 LYRLTLVRlGGGRHYLLWSHHHILLDGWCLSLIWGDVFRVYeelaHGREPQLSPCR-PYRDYVRWIRA--RTAQSEESER 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 261 WWLARVDELPAAPelpTVARPADSEGRFRRWETRLSSQVWEGLRQRAGRHGVSPSGAVLAAFSDTIAAYSRRSRFTLDIT 340
Cdd:cd19547 192 FWREYLRDLTPSP---FSTAPADREGEFDTVVHEFPEQLTRLVNEAARGYGVTTNAISQAAWSMLLALQTGARDVVHGLT 268
|
250 260 270
....*....|....*....|....*....|..
gi 1860141834 341 LLNRAPVHDQVNALVGDFTSVDLLAVDADPTR 372
Cdd:cd19547 269 IAGRPPELEGSEHMVGIFINTIPLRIRLDPDQ 300
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
664-990 |
5.07e-03 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 41.18 E-value: 5.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 664 GDP--EELAYVIHTSGSTGSPKGVMINHRGAVNTVLDINDRFGvGPDDRVLGLSN---LGFDLSVYDVFGplsvGGAVVL 738
Cdd:PRK07824 30 GEPidDDVALVVATSGTTGTPKGAMLTAAALTASADATHDRLG-GPGQWLLALPAhhiAGLQVLVRSVIA----GSEPVE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 739 PDPQRRGDPSHWADLVGT-HGVTVWNS-VPAQLQMLHDYLVSATAtvpdgLRL--AMLSGDwIPVALPDQIRARVPGLRI 814
Cdd:PRK07824 105 LDVSAGFDPTALPRAVAElGGGRRYTSlVPMQLAKALDDPAATAA-----LAEldAVLVGG-GPAPAPVLDAAAAAGINV 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 815 VSLGGATEASIWSIWYpieqvdpewrsipyGRPLTNQSFHVLDaalrprpdlvsGELYIGGVGLAVGYLNdrertaerFV 894
Cdd:PRK07824 179 VRTYGMSETSGGCVYD--------------GVPLDGVRVRVED-----------GRIALGGPTLAKGYRN--------PV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 895 VHPQTGER-LYRTGDLGRyLPDGTIEFLGREDLQVKIRGYRIELAEIEAALGGHPAVAGAVVVVDGDTPLERRLAAFVEP 973
Cdd:PRK07824 226 DPDPFAEPgWFRTDDLGA-LDDGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVVG 304
|
330
....*....|....*....
gi 1860141834 974 AG--RPVTAAQAEHDQAAL 990
Cdd:PRK07824 305 DGgpAPTLEALRAHVARTL 323
|
|
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
1523-1714 |
5.50e-03 |
|
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440361 [Multi-domain] Cd Length: 221 Bit Score: 40.37 E-value: 5.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 1523 ATSGGDGLSPLHEGTDGVPWVLVPG-GEGVDAYAGLVPHLAATGPVLGL---------APGAADDLLRVAAAQARLVTAA 1592
Cdd:COG0596 7 VTVDGVRLHYREAGPDGPPVVLLHGlPGSSYEWRPLIPALAAGYRVIAPdlrghgrsdKPAGGYTLDDLADDLAALLDAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860141834 1593 VHPAVRLVGYGLGATSTLEVARSLietGGQVDAVVLISPWRpaagadpaAAYRAETGAAGTPGEDFAARLAAVARHEPTL 1672
Cdd:COG0596 87 GLERVVLVGHSMGGMVALELAARH---PERVAGLVLVDEVL--------AALAEPLRRPGLAPEALAALLRALARTDLRE 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1860141834 1673 YAGDL----VVLRPTGAVPYDAQSLEFWADLcLGDVRTVDV-DADHL 1714
Cdd:COG0596 156 RLARItvptLVIWGEKDPIVPPALARRLAEL-LPNAELVVLpGAGHF 201
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
1374-1419 |
6.52e-03 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 41.27 E-value: 6.52e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1860141834 1374 DDLTEHLA-GRLPQYMVPSVVQVVDALPLNANGKVDRAVLRRRLPRR 1419
Cdd:PRK06087 491 EEVVAFFSrKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRKDIMRR 537
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
666-741 |
6.79e-03 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 41.23 E-value: 6.79e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1860141834 666 PEELAYVIHTSGSTGSPKGVMINHRGAVNTVLDINDRFGVGPDDRVLGLSNL--GFDLSVyDVFGPLSVGGAVVL-PDP 741
Cdd:PRK08043 364 PEDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRFMSALPLfhSFGLTV-GLFTPLLTGAEVFLyPSP 441
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
1370-1413 |
7.24e-03 |
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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: 40.76 E-value: 7.24e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1860141834 1370 RISRDDLTEHLAGRLPQYMVPSVVQVVDALPLNANGKVDRAVLR 1413
Cdd:cd05926 449 SVTEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVA 492
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