|
Name |
Accession |
Description |
Interval |
E-value |
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
34-546 |
1.38e-158 |
|
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: 470.86 E-value: 1.38e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 34 ADKVALIYQPSTtgqgmapsqSSYRQMNERANRAARLLVAETHGRflqpnsdgDFIVAVCMQPSEGLVTTLLAIWKAGGA 113
Cdd:cd05930 1 PDAVAVVDGDQS---------LTYAELDARANRLARYLRERGVGP--------GDLVAVLLERSLEMVVAILAVLKAGAA 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 114 YLPIDPSFPANRIHHILLEAKPTLVIRDDDidagrfqgtptlsttelyakslqlagsnllseemlrggndHIAIVLYTSG 193
Cdd:cd05930 64 YVPLDPSYPAERLAYILEDSGAKLVLTDPD----------------------------------------DLAYVIYTSG 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 194 STGVPKGVRLPHESILNRLQWQWATFPYTANEAVsVFKTALTFVDSIAELWGPLMCGLAILVVPKAVTKDPQRLVALLER 273
Cdd:cd05930 104 STGKPKGVMVEHRGLVNLLLWMQEAYPLTPGDRV-LQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAE 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 274 YKIRRLVLVPTLLRSLLMYLKMEgggaaqkLLYNLQIWVCSGEPLSVSLASSFFDYFDEgvHRLYNFYGSTEVLGDVTYF 353
Cdd:cd05930 183 EGITVLHLTPSLLRLLLQELELA-------ALPSLRLVLVGGEALPPDLVRRWRELLPG--ARLVNLYGPTEATVDATYY 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 354 ACEskKQLSLYDNVPIGIPLSNTVVYLLDADYRPVKNGEIGEIFASGLNLAAGYVNgrDPE----RFLENPLAvekKYAR 429
Cdd:cd05930 254 RVP--PDDEEDGRVPIGRPIPNTRVYVLDENLRPVPPGVPGELYIGGAGLARGYLN--RPEltaeRFVPNPFG---PGER 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 430 LYRTGDYGS-LKNGSIMYEGRTDSQVKIRGHRVDLSEVEKNVAELPLVDKAIVLCYHAGQVDQAILAFVKLrDDAPMVTE 508
Cdd:cd05930 327 MYRTGDLVRwLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVP-DEGGELDE 405
|
490 500 510
....*....|....*....|....*....|....*....
gi 126789033 509 MQMEARLKDKLADYMTPQVVI-LEHVPLLVNGKVDRQAL 546
Cdd:cd05930 406 EELRAHLAERLPDYMVPSAFVvLDALPLTPNGKVDRKAL 444
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
23-546 |
6.40e-123 |
|
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: 380.47 E-value: 6.40e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 23 HRIFEEQQLRHADKVALIYQPSTTgqgmapsqsSYRQMNERANRAARLLVAETHGRflqpnsdGDfIVAVCMQPSEGLVT 102
Cdd:cd17646 1 HALVAEQAARTPDAPAVVDEGRTL---------TYRELDERANRLAHLLRARGVGP-------ED-RVAVLLPRSADLVV 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 103 TLLAIWKAGGAYLPIDPSFPANRIHHILLEAKPTLVIRDDDI-DAGRFQGTPTLSTTELYAkslqlAGSNLLSEEMLRGg 181
Cdd:cd17646 64 ALLAVLKAGAAYLPLDPGYPADRLAYMLADAGPAVVLTTADLaARLPAGGDVALLGDEALA-----APPATPPLVPPRP- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 182 nDHIAIVLYTSGSTGVPKGVRLPHESILNRLQWQWATFPYTANEAVsVFKTALTFVDSIAELWGPLMCGlAILVVPKAVT 261
Cdd:cd17646 138 -DNLAYVIYTSGSTGRPKGVMVTHAGIVNRLLWMQDEYPLGPGDRV-LQKTPLSFDVSVWELFWPLVAG-ARLVVARPGG 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 262 -KDPQRLVALLERYKIRRLVLVPTLLRSLLMylKMEGGGAAqkllyNLQIWVCSGEPLSVSLASSFFDYFDEgvhRLYNF 340
Cdd:cd17646 215 hRDPAYLAALIREHGVTTCHFVPSMLRVFLA--EPAAGSCA-----SLRRVFCSGEALPPELAARFLALPGA---ELHNL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 341 YGSTEVLGDVTYFACESKKQLSlydNVPIGIPLSNTVVYLLDADYRPVKNGEIGEIFASGLNLAAGYVN--GRDPERFLE 418
Cdd:cd17646 285 YGPTEAAIDVTHWPVRGPAETP---SVPIGRPVPNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGrpALTAERFVP 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 419 NPLAvekKYARLYRTGDYG-SLKNGSIMYEGRTDSQVKIRGHRVDLSEVEKNVAELPLVDKAIVLCYHAGQVDQAILAFV 497
Cdd:cd17646 362 DPFG---PGSRMYRTGDLArWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYV 438
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 126789033 498 KLRDDAPMVTEMQMEARLKDKLADYMTP-QVVILEHVPLLVNGKVDRQAL 546
Cdd:cd17646 439 VPAAGAAGPDTAALRAHLAERLPEYMVPaAFVVLDALPLTANGKLDRAAL 488
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
22-548 |
1.58e-120 |
|
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: 396.53 E-value: 1.58e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 22 LHRIFEEQQLRHADKVALIYQpsttGQGMapsqsSYRQMNERANRAARLLVAetHGrfLQPNSdgdfIVAVCMQPSEGLV 101
Cdd:COG1020 478 LHELFEAQAARTPDAVAVVFG----DQSL-----TYAELNARANRLAHHLRA--LG--VGPGD----LVGVCLERSLEMV 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 102 TTLLAIWKAGGAYLPIDPSFPANRIHHILLEAKPTLVIRDDDIDAG-RFQGTPTLSTTELYAksLQLAGSNLLSEemlrG 180
Cdd:COG1020 541 VALLAVLKAGAAYVPLDPAYPAERLAYMLEDAGARLVLTQSALAARlPELGVPVLALDALAL--AAEPATNPPVP----V 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 181 GNDHIAIVLYTSGSTGVPKGVRLPHESILNRLQWQWATFPYTANEAVSVFkTALTFVDSIAELWGPLMCGLAILVVPKAV 260
Cdd:COG1020 615 TPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQF-ASLSFDASVWEIFGALLSGATLVLAPPEA 693
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 261 TKDPQRLVALLERYKIRRLVLVPTLLRSLLmylkmeggGAAQKLLYNLQIWVCSGEPLSVSLASSFFDYFDEGvhRLYNF 340
Cdd:COG1020 694 RRDPAALAELLARHRVTVLNLTPSLLRALL--------DAAPEALPSLRLVLVGGEALPPELVRRWRARLPGA--RLVNL 763
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 341 YGSTEVLGDVTYFACESKKQLSlyDNVPIGIPLSNTVVYLLDADYRPVKNGEIGEIFASGLNLAAGYVNgrDP----ERF 416
Cdd:COG1020 764 YGPTETTVDSTYYEVTPPDADG--GSVPIGRPIANTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLN--RPeltaERF 839
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 417 LENPLAVEKkyARLYRTGDYGS-LKNGSIMYEGRTDSQVKIRGHRVDLSEVEKNVAELPLVDKAIVLCYHAGQVDQAILA 495
Cdd:COG1020 840 VADPFGFPG--ARLYRTGDLARwLPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVA 917
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 126789033 496 FVKLRDDAPmVTEMQMEARLKDKLADYMTPQVVILEHVPLLVNGKVDRQALLK 548
Cdd:COG1020 918 YVVPEAGAA-AAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALP 969
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
26-546 |
8.22e-108 |
|
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: 340.86 E-value: 8.22e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 26 FEEQQLRHADKVALIYQPSTTgqgmapsqsSYRQMNERANRAARLLVAETHGRflqpnsdGDfIVAVCMQPSEGLVTTLL 105
Cdd:cd17651 1 FERQAARTPDAPALVAEGRRL---------TYAELDRRANRLAHRLRARGVGP-------GD-LVALCARRSAELVVALL 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 106 AIWKAGGAYLPIDPSFPANRIHHILLEAKPTLVIRDDDiDAGRFQGTPTLSTTELYAKSLQLAGSNLlseeMLRGGNDHI 185
Cdd:cd17651 64 AILKAGAAYVPLDPAYPAERLAFMLADAGPVLVLTHPA-LAGELAVELVAVTLLDQPGAAAGADAEP----DPALDADDL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 186 AIVLYTSGSTGVPKGVRLPHESILNRLQWQWATFPYTANEAVSVFKTaLTFVDSIAELWGPLMCGLAILVVPKAVTKDPQ 265
Cdd:cd17651 139 AYVIYTSGSTGRPKGVVMPHRSLANLVAWQARASSLGPGARTLQFAG-LGFDVSVQEIFSTLCAGATLVLPPEEVRTDPP 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 266 RLVALLERYKIRRLVLVPTLLRSLLmylkmEGGGAAQKLLYNLQIWVCSGEPLSVSLAssfFDYF--DEGVHRLYNFYGS 343
Cdd:cd17651 218 ALAAWLDEQRISRVFLPTVALRALA-----EHGRPLGVRLAALRYLLTGGEQLVLTED---LREFcaGLPGLRLHNHYGP 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 344 TEvlgdVTYFACESKKQLSLY--DNVPIGIPLSNTVVYLLDADYRPVKNGEIGEIFASGLNLAAGYVNGRD--PERFLEN 419
Cdd:cd17651 290 TE----THVVTALSLPGDPAAwpAPPPIGRPIDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPEltAERFVPD 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 420 PLAVEkkyARLYRTGDYGS-LKNGSIMYEGRTDSQVKIRGHRVDLSEVEKNVAELPLVDKAIVLCYHAGQVDQAILAFVK 498
Cdd:cd17651 366 PFVPG---ARMYRTGDLARwLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVV 442
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 126789033 499 LRDDAPMVTEmQMEARLKDKLADYMTPQ-VVILEHVPLLVNGKVDRQAL 546
Cdd:cd17651 443 GDPEAPVDAA-ELRAALATHLPEYMVPSaFVLLDALPLTPNGKLDRRAL 490
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
56-481 |
8.81e-104 |
|
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: 327.69 E-value: 8.81e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 56 SYRQMNERANRAARLLVAEthgRFLQPNSdgdfIVAVCMQPSEGLVTTLLAIWKAGGAYLPIDPSFPANRIHHILLEAKP 135
Cdd:TIGR01733 1 TYRELDERANRLARHLRAA---GGVGPGD----RVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 136 TLVIRDDDIdAGRFQGTPTLSTTELYAKSLQLAGSNLLSEEMLRGGNDHIAIVLYTSGSTGVPKGVRLPHESILNRLQWQ 215
Cdd:TIGR01733 74 RLLLTDSAL-ASRLAGLVLPVILLDPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 216 WATFPYTANEAVSVFkTALTFVDSIAELWGPLMCGLAILVVPKAVTKDPQRLVA-LLERYKIRRLVLVPTLLRSLLMylk 294
Cdd:TIGR01733 153 ARRYGLDPDDRVLQF-ASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLAaLIAEHPVTVLNLTPSLLALLAA--- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 295 megggAAQKLLYNLQIWVCSGEPLSVSLASSFFDYFdeGVHRLYNFYGSTEVLGDVTYFACESKKqLSLYDNVPIGIPLS 374
Cdd:TIGR01733 229 -----ALPPALASLRLVILGGEALTPALVDRWRARG--PGARLINLYGPTETTVWSTATLVDPDD-APRESPVPIGRPLA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 375 NTVVYLLDADYRPVKNGEIGEIFASGLNLAAGYVNgrDP----ERFLENPLAVEKKyARLYRTGDYGS-LKNGSIMYEGR 449
Cdd:TIGR01733 301 NTRLYVLDDDLRPVPVGVVGELYIGGPGVARGYLN--RPeltaERFVPDPFAGGDG-ARLYRTGDLVRyLPDGNLEFLGR 377
|
410 420 430
....*....|....*....|....*....|..
gi 126789033 450 TDSQVKIRGHRVDLSEVEKNVAELPLVDKAIV 481
Cdd:TIGR01733 378 IDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
56-546 |
2.58e-101 |
|
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: 323.09 E-value: 2.58e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 56 SYRQMNERANRAARLLVAETHGrflqpnsDGDFiVAVCMQPSEGLVTTLLAIWKAGGAYLPIDPSFPANRIHHILLEAKP 135
Cdd:cd12116 14 SYAELDERANRLAARLRARGVG-------PGDR-VAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 136 TLVIRDDDIDAGRFQGTPtlsTTELYAKSLQLAGSNLLSEEMLrggnDHIAIVLYTSGSTGVPKGVRLPHESILNRLQWQ 215
Cdd:cd12116 86 ALVLTDDALPDRLPAGLP---VLLLALAAAAAAPAAPRTPVSP----DDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 216 WATFPYTANEAVsVFKTALTFVDSIAELWGPLMCGLAILVVPKAVTKDPQRLVALLERYKIRRLVLVPTLLRSLLmylkm 295
Cdd:cd12116 159 RERLGLGPGDRL-LAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHSITVMQATPATWRMLL----- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 296 eggGAAQKLLYNLQIwVCSGEPLSVSLAssffDYFDEGVHRLYNFYGSTEvlgdVTYFACESKKQLSLyDNVPIGIPLSN 375
Cdd:cd12116 233 ---DAGWQGRAGLTA-LCGGEALPPDLA----ARLLSRVGSLWNLYGPTE----TTIWSTAARVTAAA-GPIPIGRPLAN 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 376 TVVYLLDADYRPVKNGEIGEIFASGLNLAAGYVNGRD--PERFLENPLAVEKkyARLYRTGDYGSLK-NGSIMYEGRTDS 452
Cdd:cd12116 300 TQVYVLDAALRPVPPGVPGELYIGGDGVAQGYLGRPAltAERFVPDPFAGPG--SRLYRTGDLVRRRaDGRLEYLGRADG 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 453 QVKIRGHRVDLSEVEKNVAELPLVDKAIVLCYHAGQvDQAILAFVKLRDDAPmVTEMQMEARLKDKLADYMTPQ-VVILE 531
Cdd:cd12116 378 QVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGG-DRRLVAYVVLKAGAA-PDAAALRAHLRATLPAYMVPSaFVRLD 455
|
490
....*....|....*
gi 126789033 532 HVPLLVNGKVDRQAL 546
Cdd:cd12116 456 ALPLTANGKLDRKAL 470
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
35-546 |
5.88e-101 |
|
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: 321.56 E-value: 5.88e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 35 DKVALIYQPSTTgqgmapsqsSYRQMNERANRAARLLVAEthgrFLQPnsdgDFIVAVCMQPSEGLVTTLLAIWKAGGAY 114
Cdd:cd17643 2 EAVAVVDEDRRL---------TYGELDARANRLARTLRAE----GVGP----GDRVALALPRSAELIVALLAILKAGGAY 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 115 LPIDPSFPANRIHHILLEAKPTLVIRDddidagrfqgtptlsttelyakslqlagsnllseemlrggNDHIAIVLYTSGS 194
Cdd:cd17643 65 VPIDPAYPVERIAFILADSGPSLLLTD----------------------------------------PDDLAYVIYTSGS 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 195 TGVPKGVRLPHESILNRLqwqWAT---FPYTANEAVSVFkTALTFVDSIAELWGPLMCGLAILVVPKAVTKDPQRLVALL 271
Cdd:cd17643 105 TGRPKGVVVSHANVLALF---AATqrwFGFNEDDVWTLF-HSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLL 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 272 ERYKIRRLVLVPTLLRSLLMYLKMEGGGAAqkllyNLQIWVCSGEPLSVSLASSFFDYFDEGVHRLYNFYGSTEVLGDVT 351
Cdd:cd17643 181 RDEGVTVLNQTPSAFYQLVEAADRDGRDPL-----ALRYVIFGGEALEAAMLRPWAGRFGLDRPQLVNMYGITETTVHVT 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 352 YFACeSKKQLSLYDNVPIGIPLSNTVVYLLDADYRPVKNGEIGEIFASGLNLAAGYVN--GRDPERFLENPLAVEKkyAR 429
Cdd:cd17643 256 FRPL-DAADLPAAAASPIGRPLPGLRVYVLDADGRPVPPGVVGELYVSGAGVARGYLGrpELTAERFVANPFGGPG--SR 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 430 LYRTGDYGS-LKNGSIMYEGRTDSQVKIRGHRVDLSEVEKNVAELPLVDKAIVLCYHAGQVDQAILAFVKLRDDAPMVTE 508
Cdd:cd17643 333 MYRTGDLARrLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADDGAAADIA 412
|
490 500 510
....*....|....*....|....*....|....*....
gi 126789033 509 mQMEARLKDKLADYMTP-QVVILEHVPLLVNGKVDRQAL 546
Cdd:cd17643 413 -ELRALLKELLPDYMVPaRYVPLDALPLTVNGKLDRAAL 450
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
50-546 |
2.53e-96 |
|
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: 308.80 E-value: 2.53e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 50 MAPSQSSYRQMNERANRAARLLVAETHGRflqpnsdgDFIVAVCMQPSEGLVTTLLAIWKAGGAYLPIDPSFPANRIHHI 129
Cdd:cd17652 8 FGDETLTYAELNARANRLARLLAARGVGP--------ERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 130 LLEAKPTLVIRdddidagrfqgTPtlsttelyakslqlagsnllseemlrggnDHIAIVLYTSGSTGVPKGVRLPHESIL 209
Cdd:cd17652 80 LADARPALLLT-----------TP-----------------------------DNLAYVIYTSGSTGRPKGVVVTHRGLA 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 210 NRLQWQWATFPYTANEAVSVFkTALTFVDSIAELWGPLMCGLAILVVPKAVTKDPQRLVALLERYKIRRLVLVPTLLRSL 289
Cdd:cd17652 120 NLAAAQIAAFDVGPGSRVLQF-ASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLLREHRITHVTLPPAALAAL 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 290 lmylkmEGGGaaqklLYNLQIWVCSGEPLSVSLASSFfdyfdEGVHRLYNFYGSTEVLGDVTYFACeskkqLSLYDNVPI 369
Cdd:cd17652 199 ------PPDD-----LPDLRTLVVAGEACPAELVDRW-----APGRRMINAYGPTETTVCATMAGP-----LPGGGVPPI 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 370 GIPLSNTVVYLLDADYRPVKNGEIGEIFASGLNLAAGYVNGRD--PERFLENPLAVEKkyARLYRTGDYGSLKN-GSIMY 446
Cdd:cd17652 258 GRPVPGTRVYVLDARLRPVPPGVPGELYIAGAGLARGYLNRPGltAERFVADPFGAPG--SRMYRTGDLARWRAdGQLEF 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 447 EGRTDSQVKIRGHRVDLSEVEKNVAELPLVDKAIVLCYHAGQVDQAILAFVKLRDDAPMVTEmQMEARLKDKLADYMTPQ 526
Cdd:cd17652 336 LGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPGAAPTAA-ELRAHLAERLPGYMVPA 414
|
490 500
....*....|....*....|.
gi 126789033 527 -VVILEHVPLLVNGKVDRQAL 546
Cdd:cd17652 415 aFVVLDALPLTPNGKLDRRAL 435
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
24-546 |
3.74e-95 |
|
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: 307.21 E-value: 3.74e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 24 RIFEEQQLRHADKVALIYQpsttGQGMapsqsSYRQMNERANRAARLLVAetHGrfLQPNSdgdfIVAVCMQPSEGLVTT 103
Cdd:cd12117 1 ELFEEQAARTPDAVAVVYG----DRSL-----TYAELNERANRLARRLRA--AG--VGPGD----VVGVLAERSPELVVA 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 104 LLAIWKAGGAYLPIDPSFPANRIHHILLEAKPTLVIrDDDIDAGRFQGTPTLSttELYAKSLQLAGSNLLSeemlRGGND 183
Cdd:cd12117 64 LLAVLKAGAAYVPLDPELPAERLAFMLADAGAKVLL-TDRSLAGRAGGLEVAV--VIDEALDAGPAGNPAV----PVSPD 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 184 HIAIVLYTSGSTGVPKGVRLPHESILnRL---QWqWATFpyTANEaVSVFKTALTFVDSIAELWGPLMCGLAILVVPKAV 260
Cdd:cd12117 137 DLAYVMYTSGSTGRPKGVAVTHRGVV-RLvknTN-YVTL--GPDD-RVLQTSPLAFDASTFEIWGALLNGARLVLAPKGT 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 261 TKDPQRLVALLERYKIRRLVLVPTLLRSLlmylkmegggAAQ--KLLYNL-QIWVcSGEPLSVSLASSFFDYFDEGvhRL 337
Cdd:cd12117 212 LLDPDALGALIAEEGVTVLWLTAALFNQL----------ADEdpECFAGLrELLT-GGEVVSPPHVRRVLAACPGL--RL 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 338 YNFYGSTEVlgdvTYFA-CESKKQLSLY-DNVPIGIPLSNTVVYLLDADYRPVKNGEIGEIFASGLNLAAGYVNGRD--P 413
Cdd:cd12117 279 VNGYGPTEN----TTFTtSHVVTELDEVaGSIPIGRPIANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPAltA 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 414 ERFLENPLAVEkkyARLYRTGDY-GSLKNGSIMYEGRTDSQVKIRGHRVDLSEVEKNVAELPLVDKAIVLCYHAGQVDQA 492
Cdd:cd12117 355 ERFVADPFGPG---ERLYRTGDLaRWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKR 431
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 126789033 493 ILAFVKLRDDapmVTEMQMEARLKDKLADYMTPQVVI-LEHVPLLVNGKVDRQAL 546
Cdd:cd12117 432 LVAYVVAEGA---LDAAELRAFLRERLPAYMVPAAFVvLDELPLTANGKVDRRAL 483
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
56-546 |
8.86e-95 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 324.69 E-value: 8.86e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 56 SYRQMNERANRAARLLVAethgRFLQPnsdGDfIVAVCMQPSEGLVTTLLAIWKAGGAYLPIDPSFPANRIHHILLEAKP 135
Cdd:PRK10252 485 SYREMREQVVALANLLRE----RGVKP---GD-SVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARP 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 136 TLVIRDDDiDAGRFQGTPTLsttELYAKSLQLAGSNllSEEMLRGGNDHIAIVLYTSGSTGVPKGVRLPHESILNRLQWQ 215
Cdd:PRK10252 557 SLLITTAD-QLPRFADVPDL---TSLCYNAPLAPQG--AAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWM 630
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 216 WATFPYTANEAVsVFKTALTFVDSIAELWGPLMCGLAILVVPKAVTKDPQRLVALLERYKIRRLVLVPTLLRSLLMYLKM 295
Cdd:PRK10252 631 QNHYPLTADDVV-LQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTTHFVPSMLAAFVASLTP 709
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 296 EGggaAQKLLYNLQIWVCSGEPLSVSLAssffDYFDEGVH-RLYNFYGSTEVLGDVTYF-ACESKKQLSLYDNVPIGIPL 373
Cdd:PRK10252 710 EG---ARQSCASLRQVFCSGEALPADLC----REWQQLTGaPLHNLYGPTEAAVDVSWYpAFGEELAAVRGSSVPIGYPV 782
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 374 SNTVVYLLDADYRPVKNGEIGEIFASGLNLAAGYVnGRD---PERFLENPLAvekKYARLYRTGDYGS-LKNGSIMYEGR 449
Cdd:PRK10252 783 WNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYL-GRPdltASRFIADPFA---PGERMYRTGDVARwLDDGAVEYLGR 858
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 450 TDSQVKIRGHRVDLSEVEKNVAELPLVDKAIVlcyHAGQVDQA---------ILAFVKLRDDAPMVTEMqMEARLKDKLA 520
Cdd:PRK10252 859 SDDQLKIRGQRIELGEIDRAMQALPDVEQAVT---HACVINQAaatggdarqLVGYLVSQSGLPLDTSA-LQAQLRERLP 934
|
490 500
....*....|....*....|....*..
gi 126789033 521 DYMTPQVVI-LEHVPLLVNGKVDRQAL 546
Cdd:PRK10252 935 PHMVPVVLLqLDQLPLSANGKLDRKAL 961
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
20-625 |
1.04e-94 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 328.07 E-value: 1.04e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 20 RALHRIFEEQQLRHADKVALIYQPSTTGqgmapsqssYRQMNERANRAARLLVAETHGrflqpnsdGDFIVAVCMQPSEG 99
Cdd:PRK12316 511 RGVHRLFEEQVERTPEAPALAFGEETLD---------YAELNRRANRLAHALIERGVG--------PDVLVGVAMERSIE 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 100 LVTTLLAIWKAGGAYLPIDPSFPANRIHHILLEAKPTLVIRDD------DIDAGrfqgtptLSTTELYAKSLQLAGSnll 173
Cdd:PRK12316 574 MVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQShlgrklPLAAG-------VQVLDLDRPAAWLEGY--- 643
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 174 SEEML--RGGNDHIAIVLYTSGSTGVPKGVRLPHESILNRLQWQWATFPYTANEAVsVFKTALTFVDSIAELWGPLMCGL 251
Cdd:PRK12316 644 SEENPgtELNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTV-LQKTPFSFDVSVWEFFWPLMSGA 722
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 252 AILVVPKAVTKDPQRLVALLERYKIRRLVLVPTLLRSLLmylkmEGGGAAQklLYNLQIWVCSGEPLSVSLASSFFDYFD 331
Cdd:PRK12316 723 RLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFL-----QDEDVAS--CTSLRRIVCSGEALPADAQEQVFAKLP 795
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 332 EGvhRLYNFYGSTEVLGDVTYFACESKKQlslyDNVPIGIPLSNTVVYLLDADYRPVKNGEIGEIFASGLNLAAGYVN-- 409
Cdd:PRK12316 796 QA--GLYNLYGPTEAAIDVTHWTCVEEGG----DSVPIGRPIANLACYILDANLEPVPVGVLGELYLAGRGLARGYHGrp 869
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 410 GRDPERFLENPLAvekKYARLYRTGDYGSLK-NGSIMYEGRTDSQVKIRGHRVDLSEVEKNVAELPLVDKAIVLcyhaGQ 488
Cdd:PRK12316 870 GLTAERFVPSPFV---AGERMYRTGDLARYRaDGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVL----AV 942
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 489 VDQAILAFVKLRDDAPMVTEMqMEARLKDKLADYMTP-QVVILEHVPLLVNGKVDRQALLKTyetannnegDSSIVLDfD 567
Cdd:PRK12316 943 DGKQLVGYVVLESEGGDWREA-LKAHLAASLPEYMVPaQWLALERLPLTPNGKLDRKALPAP---------EASVAQQ-G 1011
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 126789033 568 YSQVPEDLKLTARDLFETVGGVigrsTRATLapHSNFYELGGNSLNSIFTVTLLREKG 625
Cdd:PRK12316 1012 YVAPRNALERTLAAIWQDVLGV----ERVGL--DDNFFELGGDSIVSIQVVSRARQAG 1063
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
24-546 |
3.80e-92 |
|
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: 299.63 E-value: 3.80e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 24 RIFEEQQLRHADKVALIYQPSTTgqgmapsqsSYRQMNERANRAARLLVAEThgrfLQPnsdgDFIVAVCMQPSEGLVTT 103
Cdd:cd17655 1 ELFEEQAEKTPDHTAVVFEDQTL---------TYRELNERANQLARTLREKG----VGP----DTIVGIMAERSLEMIVG 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 104 LLAIWKAGGAYLPIDPSFPANRIHHILLEAKPTLVIRDDDIDAG-RFQGTPTLSTTE-LYAKSlqlaGSNLLSEemlrGG 181
Cdd:cd17655 64 ILGILKAGGAYLPIDPDYPEERIQYILEDSGADILLTQSHLQPPiAFIGLIDLLDEDtIYHEE----SENLEPV----SK 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 182 NDHIAIVLYTSGSTGVPKGVRLPHESILNrLQWqWATFPYTANEAVSVFKTA-LTFVDSIAELWGPLMCGLAILVVPKAV 260
Cdd:cd17655 136 SDDLAYVIYTSGSTGKPKGVMIEHRGVVN-LVE-WANKVIYQGEHLRVALFAsISFDASVTEIFASLLSGNTLYIVRKET 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 261 TKDPQRLVALLERYKIRRLVLVPTLLrSLLMYLKMEGGGAAQKLLynlqiwvCSGEPLSVSLASSFFDYFDEGVhRLYNF 340
Cdd:cd17655 214 VLDGQALTQYIRQNRITIIDLTPAHL-KLLDAADDSEGLSLKHLI-------VGGEALSTELAKKIIELFGTNP-TITNA 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 341 YGSTEVLGDVTYFACESKKQLSlyDNVPIGIPLSNTVVYLLDADYRPVKNGEIGEIFASGLNLAAGYVNGRD--PERFLE 418
Cdd:cd17655 285 YGPTETTVDASIYQYEPETDQQ--VSVPIGKPLGNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPEltAEKFVD 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 419 NPLAVEKkyaRLYRTGDYGS-LKNGSIMYEGRTDSQVKIRGHRVDLSEVEKNVAELPLVDKAIVLCYHAGQVDQAILAFV 497
Cdd:cd17655 363 DPFVPGE---RMYRTGDLARwLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYI 439
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 126789033 498 KLRDDAPMvteMQMEARLKDKLADYMTPQVVI-LEHVPLLVNGKVDRQAL 546
Cdd:cd17655 440 VSEKELPV---AQLREFLARELPDYMIPSYFIkLDEIPLTPNGKVDRKAL 486
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
15-627 |
8.99e-92 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 319.03 E-value: 8.99e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 15 QDFVP-RALHRIFEEQQLRHADKVALIYqpsttgqgmAPSQSSYRQMNERANRAARLLVAETHGrflqpnsdGDFIVAVC 93
Cdd:PRK12467 1568 TGYPLaRLVHQLIEDQAAATPEAVALVF---------GEQELTYGELNRRANRLAHRLIALGVG--------PEVLVGIA 1630
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 94 MQPSEGLVTTLLAIWKAGGAYLPIDPSFPANRIHHILLEAKPTLVIRDDDIDAgRFQGTPTLSTTELYAKSLQLAGSNLl 173
Cdd:PRK12467 1631 VERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQSHLQA-RLPLPDGLRSLVLDQEDDWLEGYSD- 1708
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 174 SEEMLRGGNDHIAIVLYTSGSTGVPKGVRLPHESILNRLQWQWATFPYTANEAVSvFKTALTFVDSIAELWGPLMCGLAI 253
Cdd:PRK12467 1709 SNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVL-QFTSFAFDVSVWELFWPLINGARL 1787
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 254 LVVPKAVTKDPQRLVALLERYKIRRLVLVPTLLRSLLMYLKMEGGGAAqkllynLQIWVCSGEPLSVSLASSFFDYFdeG 333
Cdd:PRK12467 1788 VIAPPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQMDEQVEHPLS------LRRVVCGGEALEVEALRPWLERL--P 1859
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 334 VHRLYNFYGSTEVLGDVTYFACeSKKQLSLYDNVPIGIPLSNTVVYLLDADYRPVKNGEIGEIFASGLNLAAGYVN--GR 411
Cdd:PRK12467 1860 DTGLFNLYGPTETAVDVTHWTC-RRKDLEGRDSVPIGQPIANLSTYILDASLNPVPIGVAGELYLGGVGLARGYLNrpAL 1938
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 412 DPERFLENPLAveKKYARLYRTGDYGSLK-NGSIMYEGRTDSQVKIRGHRVDLSEVEKNVAELPLVDKAIVLCyHAGQVD 490
Cdd:PRK12467 1939 TAERFVADPFG--TVGSRLYRTGDLARYRaDGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIA-QDGANG 2015
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 491 QAILAFVkLRDDAPMVTEM--------QMEARLKDKLADYMTP-QVVILEHVPLLVNGKVDRQALLKTyetannnegDSS 561
Cdd:PRK12467 2016 KQLVAYV-VPTDPGLVDDDeaqvalraILKNHLKASLPEYMVPaHLVFLARMPLTPNGKLDRKALPAP---------DAS 2085
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 126789033 562 iVLDFDYSQVPEDLKLTARDLFETVGGV--IGRstratlapHSNFYELGGNSLNSIFTVTLLREKGYN 627
Cdd:PRK12467 2086 -ELQQAYVAPQSELEQRLAAIWQDVLGLeqVGL--------HDNFFELGGDSIISIQVVSRARQAGIR 2144
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
22-546 |
3.96e-91 |
|
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: 295.38 E-value: 3.96e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 22 LHRIFEEQQLRHADKVALIyqpstTGQGmapsQSSYRQMNERANRAARLLVAETHGRflqpnsdgDFIVAVCMQPSEGLV 101
Cdd:cd12115 1 LHDLVEAQAARTPDAIALV-----CGDE----SLTYAELNRRANRLAARLRAAGVGP--------ESRVGVCLERTPDLV 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 102 TTLLAIWKAGGAYLPIDPSFPANRIHHILLEAKPTLVIRDddidagrfqgtptlsttelyakslqlagsnllseemlrgg 181
Cdd:cd12115 64 VALLAVLKAGAAYVPLDPAYPPERLRFILEDAQARLVLTD---------------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 182 NDHIAIVLYTSGSTGVPKGVRLPHESILNRLQWQWATFPytANEAVSVF-KTALTFVDSIAELWGPLMCGLAILVVPKAv 260
Cdd:cd12115 104 PDDLAYVIYTSGSTGRPKGVAIEHRNAAAFLQWAAAAFS--AEELAGVLaSTSICFDLSVFELFGPLATGGKVVLADNV- 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 261 tkdpQRLVALLERYKIRRLVLVPTLLRSLLmylkmegggAAQKLLYNLQIWVCSGEPLSVSLASSFfdYFDEGVHRLYNF 340
Cdd:cd12115 181 ----LALPDLPAAAEVTLINTVPSAAAELL---------RHDALPASVRVVNLAGEPLPRDLVQRL--YARLQVERVVNL 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 341 YGSTEvlgDVTY-FACESKKQLSlyDNVPIGIPLSNTVVYLLDADYRPVKNGEIGEIFASGLNLAAGYVN--GRDPERFL 417
Cdd:cd12115 246 YGPSE---DTTYsTVAPVPPGAS--GEVSIGRPLANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGrpGLTAERFL 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 418 ENPlavEKKYARLYRTGDYGS-LKNGSIMYEGRTDSQVKIRGHRVDLSEVEKNVAELPLVDKAIVLCYHAGQVDQAILAF 496
Cdd:cd12115 321 PDP---FGPGARLYRTGDLVRwRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAY 397
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 126789033 497 VKLRDDAPMVTEmQMEARLKDKLADYMTPQV-VILEHVPLLVNGKVDRQAL 546
Cdd:cd12115 398 IVAEPGAAGLVE-DLRRHLGTRLPAYMVPSRfVRLDALPLTPNGKIDRSAL 447
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
17-654 |
1.52e-90 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 315.56 E-value: 1.52e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 17 FVPRALHRIFEEQQLRHADKVALIYQPSTTgqgmapsqsSYRQMNERANRAARLLVAETHGrflqpnsdGDFIVAVCMQP 96
Cdd:PRK12467 509 YAPDCVHQLIEAQARQHPERPALVFGEQVL---------SYAELNRQANRLAHVLIAAGVG--------PDVLVGIAVER 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 97 SEGLVTTLLAIWKAGGAYLPIDPSFPANRIHHILLEAKPTLVIRDDDIdAGRFQGTPTLSTTELYAKSLQLAGSNLLSEE 176
Cdd:PRK12467 572 SIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQSHL-LAQLPVPAGLRSLCLDEPADLLCGYSGHNPE 650
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 177 mLRGGNDHIAIVLYTSGSTGVPKGVRLPHESILNRLQWQWATFPYTANEAVSVFKTaLTFVDSIAELWGPLMCGLAILVV 256
Cdd:PRK12467 651 -VALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVST-FAFDLGVTELFGALASGATLHLL 728
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 257 PKAVTKDPQRLVALLERYKIRRLVLVPTLLRSLLMylkmeggGAAQKLLYNLQIWVCSGEPLSVSLASSFFDYFDEGvhR 336
Cdd:PRK12467 729 PPDCARDAEAFAALMADQGVTVLKIVPSHLQALLQ-------ASRVALPRPQRALVCGGEALQVDLLARVRALGPGA--R 799
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 337 LYNFYGSTEVLGDVTYFACesKKQLSLYDNVPIGIPLSNTVVYLLDADYRPVKNGEIGEIFASGLNLAAGYVN--GRDPE 414
Cdd:PRK12467 800 LINHYGPTETTVGVSTYEL--SDEERDFGNVPIGQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRrpALTAE 877
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 415 RFLENPLAVEKkyARLYRTGDYGS-LKNGSIMYEGRTDSQVKIRGHRVDLSEVEKNVAELPLVDKAIVLCY---HAGQVD 490
Cdd:PRK12467 878 RFVPDPFGADG--GRLYRTGDLARyRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQpgdAGLQLV 955
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 491 QAILAFVKLRDDAPMVTEMQMEARLKDKLADYMTPQ-VVILEHVPLLVNGKVDRQALLKTYETANNNEgdssivldFDYS 569
Cdd:PRK12467 956 AYLVPAAVADGAEHQATRDELKAQLRQVLPDYMVPAhLLLLDSLPLTPNGKLDRKALPKPDASAVQAT--------FVAP 1027
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 570 QVPEDLKLTArdLFETVGGV--IGRstratlapHSNFYELGGNSLNSIFTVTLLREK-GYNIGISEFIAAKNLGEIIEKM 646
Cdd:PRK12467 1028 QTELEKRLAA--IWADVLKVerVGL--------TDNFFELGGHSLLATQVISRVRQRlGIQVPLRTLFEHQTLAGFAQAV 1097
|
....*...
gi 126789033 647 AANHDAVQ 654
Cdd:PRK12467 1098 AAQQQGAQ 1105
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
35-546 |
9.31e-82 |
|
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: 270.39 E-value: 9.31e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 35 DKVALIYQpsttGQGMapsqsSYRQMNERANRAARLLVAETHGrflqpnsdGDFIVAVCMQPSEGLVTTLLAIWKAGGAY 114
Cdd:cd17649 2 DAVALVFG----DQSL-----SYAELDARANRLAHRLRALGVG--------PEVRVGIALERSLEMVVALLAILKAGGAY 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 115 LPIDPSFPANRIHHILLEAKPTLvirdddidagrfqgtptlsttelyakslqlagsnLLSEEmlrggNDHIAIVLYTSGS 194
Cdd:cd17649 65 VPLDPEYPAERLRYMLEDSGAGL----------------------------------LLTHH-----PRQLAYVIYTSGS 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 195 TGVPKGVRLPHESILNRLQWQWATFPYTANEAVSVFKTaLTFVDSIAELWGPLMCGLAILVVPKAVTKDPQRLVALLERY 274
Cdd:cd17649 106 TGTPKGVAVSHGPLAAHCQATAERYGLTPGDRELQFAS-FNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVREL 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 275 KIRRLVLVPTLLRSLLMYLKMEGGGAAQKLlynlQIWVCSGEPLSVSLASsffDYFDEGVhRLYNFYGSTEVLGDVTYFA 354
Cdd:cd17649 185 GVTVLDLPPAYLQQLAEEADRTGDGRPPSL----RLYIFGGEALSPELLR---RWLKAPV-RLFNAYGPTEATVTPLVWK 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 355 CESKKQlSLYDNVPIGIPLSNTVVYLLDADYRPVKNGEIGEIFASGLNLAAGYVN--GRDPERFLENPLAVEKkyARLYR 432
Cdd:cd17649 257 CEAGAA-RAGASMPIGRPLGGRSAYILDADLNPVPVGVTGELYIGGEGLARGYLGrpELTAERFVPDPFGAPG--SRLYR 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 433 TGDYGSLK-NGSIMYEGRTDSQVKIRGHRVDLSEVEKNVAELPLVDKAIVLCyHAGQVDQAILAFVKLRDDAPM-VTEMQ 510
Cdd:cd17649 334 TGDLARWRdDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVA-LDGAGGKQLVAYVVLRAAAAQpELRAQ 412
|
490 500 510
....*....|....*....|....*....|....*..
gi 126789033 511 MEARLKDKLADYMTP-QVVILEHVPLLVNGKVDRQAL 546
Cdd:cd17649 413 LRTALRASLPDYMVPaHLVFLARLPLTPNGKLDRKAL 449
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
22-553 |
7.21e-81 |
|
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: 268.22 E-value: 7.21e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 22 LHRIFEEQQLRHADKVALIYQPSTTgqgmapsqsSYRQMNERANRAARLLVAetHGrfLQPnsdGDfIVAVCMQPSEGLV 101
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRRL---------TYAELDARARRLAAALRA--LG--VGP---GD-RVALLLPNSPEFV 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 102 TTLLAIWKAGGAYLPIDPSFPANRIHHILLEAKPTLVIrdddidagrfqgtptlsttelyakslqlagsnllseemlrgg 181
Cdd:COG0318 64 VAFLAALRAGAVVVPLNPRLTAEELAYILEDSGARALV------------------------------------------ 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 182 ndhIAIVLYTSGSTGVPKGVRLPHESILNRLQWQWATFPYTANEAVSVFkTALTFVDS-IAELWGPLMCGLAILVVPKAv 260
Cdd:COG0318 102 ---TALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVA-LPLFHVFGlTVGLLAPLLAGATLVLLPRF- 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 261 tkDPQRLVALLERYKIRRLVLVPTLLRSLLMYLkmeggGAAQKLLYNLQIWVCSGEPLSVSLASSFFDYFDegvHRLYNF 340
Cdd:COG0318 177 --DPERVLELIERERVTVLFGVPTMLARLLRHP-----EFARYDLSSLRLVVSGGAPLPPELLERFEERFG---VRIVEG 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 341 YGSTEVLGDVTYfaceSKKQLSLYDNVPIGIPLSNTVVYLLDADYRPVKNGEIGEIFASGLNLAAGYVNgrDPErflenp 420
Cdd:COG0318 247 YGLTETSPVVTV----NPEDPGERRPGSVGRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWN--DPE------ 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 421 lAVEKKYA-RLYRTGDYGSL-KNGSIMYEGRTDSQVKIRGHRVDLSEVEKNVAELPLVDKAIVlcyhAGQVD----QAIL 494
Cdd:COG0318 315 -ATAEAFRdGWLRTGDLGRLdEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAV----VGVPDekwgERVV 389
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 495 AFVKLRDDAPmVTEMQMEARLKDKLADYMTP-QVVILEHVPLLVNGKVDRQALLKTYETA 553
Cdd:COG0318 390 AFVVLRPGAE-LDAEELRAFLRERLARYKVPrRVEFVDELPRTASGKIDRRALRERYAAG 448
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
32-546 |
1.98e-80 |
|
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: 266.81 E-value: 1.98e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 32 RHADKVALIYQPSTTgqgmapsqsSYRQMNERANR-AARLlvaetHGRFLQPNSDgdfiVAVCMQPSEGLVTTLLAIWKA 110
Cdd:cd05945 3 ANPDRPAVVEGGRTL---------TYRELKERADAlAAAL-----ASLGLDAGDP----VVVYGHKSPDAIAAFLAALKA 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 111 GGAYLPIDPSFPANRIHHILLEAKPTLVIRDDDidagrfqgtptlsttELYAkslqlagsnllseemlrggndhiaiVLY 190
Cdd:cd05945 65 GHAYVPLDASSPAERIREILDAAKPALLIADGD---------------DNAY-------------------------IIF 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 191 TSGSTGVPKGVRLPHESILNRLQWQWATFPYTANeavSVF--KTALTFVDSIAELWGPLMCGLAILVVPKAVTKDPQRLV 268
Cdd:cd05945 105 TSGSTGRPKGVQISHDNLVSFTNWMLSDFPLGPG---DVFlnQAPFSFDLSVMDLYPALASGATLVPVPRDATADPKQLF 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 269 ALLERYKIRRLVLVPTLLRSLLMYlkmegGGAAQKLLYNLQIWVCSGEPLSVSLASSFFDYFDEGvhRLYNFYGSTEVLG 348
Cdd:cd05945 182 RFLAEHGITVWVSTPSFAAMCLLS-----PTFTPESLPSLRHFLFCGEVLPHKTARALQQRFPDA--RIYNTYGPTEATV 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 349 DVTYFACeSKKQLSLYDNVPIGIPLSNTVVYLLDADYRPVKNGEIGEIFASGLNLAAGYvngrdperfLENPLAVEKKY- 427
Cdd:cd05945 255 AVTYIEV-TPEVLDGYDRLPIGYAKPGAKLVILDEDGRPVPPGEKGELVISGPSVSKGY---------LNNPEKTAAAFf 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 428 ----ARLYRTGDYGSLKN-GSIMYEGRTDSQVKIRGHRVDLSEVEKNVAELPLVDKAIVLCYHAGQVDQAILAFVKLRDD 502
Cdd:cd05945 325 pdegQRAYRTGDLVRLEAdGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPG 404
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 126789033 503 APMVTEMQMEARLKDKLADYMTPQ-VVILEHVPLLVNGKVDRQAL 546
Cdd:cd05945 405 AEAGLTKAIKAELAERLPPYMIPRrFVYLDELPLNANGKIDRKAL 449
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
20-648 |
7.64e-80 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 283.77 E-value: 7.64e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 20 RALHRIFEEQQLRHADKVALIYQPSTTgqgmapsqsSYRQMNERANRAARLLVAETHGRflqpnsdgDFIVAVCMQPSEG 99
Cdd:PRK12316 4551 RCVHQLVAERARMTPDAVAVVFDEEKL---------TYAELNRRANRLAHALIARGVGP--------EVLVGIAMERSAE 4613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 100 LVTTLLAIWKAGGAYLPIDPSFPANRI--------------HHILLEAKP------TLVIRDDDIDAGRFQGTPtlstte 159
Cdd:PRK12316 4614 MMVGLLAVLKAGGAYVPLDPEYPRERLaymmedsgaallltQSHLLQRLPipdglaSLALDRDEDWEGFPAHDP------ 4687
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 160 lyakSLQLAGSNLlseemlrggndhiAIVLYTSGSTGVPKGVRLPHESILNRLQWQWATFPYTANEAVSVFkTALTFVDS 239
Cdd:PRK12316 4688 ----AVRLHPDNL-------------AYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQF-MSFSFDGS 4749
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 240 IAELWGPLMCGlAILVVPKAVTKDPQRLVALLERYKIRRLVLVPTLLRSLLMylkmegGGAAQKLLYNLQIWVCSGEPLS 319
Cdd:PRK12316 4750 HEGLYHPLING-ASVVIRDDSLWDPERLYAEIHEHRVTVLVFPPVYLQQLAE------HAERDGEPPSLRVYCFGGEAVA 4822
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 320 VSLASSFFDYFDegVHRLYNFYGSTEVLGDVTYFACeSKKQLSLYDNVPIGIPLSNTVVYLLDADYRPVKNGEIGEIFAS 399
Cdd:PRK12316 4823 QASYDLAWRALK--PVYLFNGYGPTETTVTVLLWKA-RDGDACGAAYMPIGTPLGNRSGYVLDGQLNPLPVGVAGELYLG 4899
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 400 GLNLAAGYVN--GRDPERFLENPLavEKKYARLYRTGDYGSLK-NGSIMYEGRTDSQVKIRGHRVDLSEVEKNVAELPLV 476
Cdd:PRK12316 4900 GEGVARGYLErpALTAERFVPDPF--GAPGGRLYRTGDLARYRaDGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAV 4977
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 477 DKAIVLCyHAGQVDQAILAFV-----KLRDDAPMVTEM--QMEARLKDKLADYMTP-QVVILEHVPLLVNGKVDRQALLK 548
Cdd:PRK12316 4978 REAVVIA-QEGAVGKQLVGYVvpqdpALADADEAQAELrdELKAALRERLPEYMVPaHLVFLARMPLTPNGKLDRKALPQ 5056
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 549 tyetannnegdssivldFDYSQVPEDLKLTARDLFETVGGV---IGRSTRATLapHSNFYELGGNSLNSIFTVTLLR-EK 624
Cdd:PRK12316 5057 -----------------PDASLLQQAYVAPRSELEQQVAAIwaeVLQLERVGL--DDNFFELGGHSLLAIQVTSRIQlEL 5117
|
650 660
....*....|....*....|....
gi 126789033 625 GYNIGISEFIAAKNLGEIIEKMAA 648
Cdd:PRK12316 5118 GLELPLRELFQTPTLAAFVELAAA 5141
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
22-552 |
2.86e-77 |
|
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: 259.40 E-value: 2.86e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 22 LHRIFEEQQLRHADKVALIyqpsttgqgmAPSQS-SYRQMNERANRAARLLVaethGRFLQPNSdgdfIVAVCMQPSEGL 100
Cdd:cd05918 1 VHDLIEERARSQPDAPAVC----------AWDGSlTYAELDRLSSRLAHHLR----SLGVGPGV----FVPLCFEKSKWA 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 101 VTTLLAIWKAGGAYLPIDPSFPANRIHHILLEAKPTLVIRDDdidagrfqgtptlsttelyakslqlagsnllseemlrg 180
Cdd:cd05918 63 VVAMLAVLKAGGAFVPLDPSHPLQRLQEILQDTGAKVVLTSS-------------------------------------- 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 181 gNDHIAIVLYTSGSTGVPKGVRLPHESILNRLQWQWATFPYTANEAVSVFkTALTFVDSIAELWGPLMCGLAILVVPKAV 260
Cdd:cd05918 105 -PSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGLTSESRVLQF-ASYTFDVSILEIFTTLAAGGCLCIPSEED 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 261 TKDpqRLVALLERYKIRRLVLVPTLLRSLlmylkmegggaAQKLLYNLQIWVCSGEPLSVSLAssffDYFDEGVhRLYNF 340
Cdd:cd05918 183 RLN--DLAGFINRLRVTWAFLTPSVARLL-----------DPEDVPSLRTLVLGGEALTQSDV----DTWADRV-RLINA 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 341 YGSTEVLGDVTYFACESKKQLSLydnvpIGIPLsNTVVYLLDAD--YRPVKNGEIGEIFASGLNLAAGYVNgrDPER--- 415
Cdd:cd05918 245 YGPAECTIAATVSPVVPSTDPRN-----IGRPL-GATCWVVDPDnhDRLVPIGAVGELLIEGPILARGYLN--DPEKtaa 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 416 -FLENPLAVEK----KYARLYRTGD---YGSlkNGSIMYEGRTDSQVKIRGHRVDLSEVEKNVAELPLVDKAIV--LCYH 485
Cdd:cd05918 317 aFIEDPAWLKQegsgRGRRLYRTGDlvrYNP--DGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKEVVveVVKP 394
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 486 AGQVDQAIL-AFVKLRDDAP---------------MVTEM-QMEARLKDKLADYMTPQVVI-LEHVPLLVNGKVDRQALL 547
Cdd:cd05918 395 KDGSSSPQLvAFVVLDGSSSgsgdgdslflepsdeFRALVaELRSKLRQRLPSYMVPSVFLpLSHLPLTASGKIDRRALR 474
|
....*
gi 126789033 548 KTYET 552
Cdd:cd05918 475 ELAES 479
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
22-546 |
4.37e-77 |
|
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: 258.52 E-value: 4.37e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 22 LHRIFEEQQLRHADKVALIYQPSttgqgmapsQSSYRQMNERANRAARLLvaethgRFLQPNSDGdfIVAVCMQPSEGLV 101
Cdd:cd17644 2 IHQLFEEQVERTPDAVAVVFEDQ---------QLTYEELNTKANQLAHYL------QSLGVKSES--LVGICVERSLEMI 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 102 TTLLAIWKAGGAYLPIDPSFPANRIHHILLEAKPTLVIRDddidagrfqgtptlsttelyakslqlaGSNLlseemlrgg 181
Cdd:cd17644 65 IGLLAILKAGGAYVPLDPNYPQERLTYILEDAQISVLLTQ---------------------------PENL--------- 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 182 ndhiAIVLYTSGSTGVPKGVRLPHESILNRLQWQWATFPYTANEAVSVFkTALTFVDSIAELWGPLMCGLAILVVPKAVT 261
Cdd:cd17644 109 ----AYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGITSSDRVLQF-ASIAFDVAAEEIYVTLLSGATLVLRPEEMR 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 262 KDPQRLVALLERYKIRRLVLVPTLLRSLLMylkmEGGGAAQKLLYNLQIWVCSGEPLSVSLASSFFDYFDEGVhRLYNFY 341
Cdd:cd17644 184 SSLEDFVQYIQQWQLTVLSLPPAYWHLLVL----ELLLSTIDLPSSLRLVIVGGEAVQPELVRQWQKNVGNFI-QLINVY 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 342 GSTEVLGDVTYFACeSKKQLSLYDNVPIGIPLSNTVVYLLDADYRPVKNGEIGEIFASGLNLAAGYVNGRD--PERFLEN 419
Cdd:cd17644 259 GPTEATIAATVCRL-TQLTERNITSVPIGRPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPEltAEKFISH 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 420 PLAvEKKYARLYRTGDYGS-LKNGSIMYEGRTDSQVKIRGHRVDLSEVEKNVAELPLVDKAIVLCYHAGQVDQAILAF-V 497
Cdd:cd17644 338 PFN-SSESERLYKTGDLARyLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYiV 416
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 126789033 498 KLRDDAPMVTEMQmeARLKDKLADYMTPQV-VILEHVPLLVNGKVDRQAL 546
Cdd:cd17644 417 PHYEESPSTVELR--QFLKAKLPDYMIPSAfVVLEELPLTPNGKIDRRAL 464
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
35-546 |
1.44e-76 |
|
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: 257.40 E-value: 1.44e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 35 DKVALIYQPSTTgqgmapsqsSYRQMNERANRAARLLVAETHGRflqpnsdgDFIVAVCMQPSEGLVTTLLAIWKAGGAY 114
Cdd:cd17656 3 DAVAVVFENQKL---------TYRELNERSNQLARFLREKGVKK--------DSIVAIMMERSAEMIVGILGILKAGGAF 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 115 LPIDPSFPANRIHHILLEAKPTLVIRDDDI-DAGRFQGTPTLSTTELYAKSLqlaGSNLLSEEmlrgGNDHIAIVLYTSG 193
Cdd:cd17656 66 VPIDPEYPEERRIYIMLDSGVRVVLTQRHLkSKLSFNKSTILLEDPSISQED---TSNIDYIN----NSDDLLYIIYTSG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 194 STGVPKGVRLPHESILNRLQWQWATFPYTANEAVSVFkTALTFVDSIAELWGPLMCGLAILVVPKAVTKDPQRLVALLER 273
Cdd:cd17656 139 TTGKPKGVQLEHKNMVNLLHFEREKTNINFSDKVLQF-ATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKR 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 274 YKIRRLVLvPTLLRSLLMYLKmeggGAAQKLLYNLQIWVCSGEPLSVSlaSSFFDYFDE-GVHrLYNFYGSTEVlGDVTY 352
Cdd:cd17656 218 HNIEVVFL-PVAFLKFIFSER----EFINRFPTCVKHIITAGEQLVIT--NEFKEMLHEhNVH-LHNHYGPSET-HVVTT 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 353 FACESKKQLSLYDnvPIGIPLSNTVVYLLDADYRPVKNGEIGEIFASGLNLAAGYVNGRD--PERFLENPLaveKKYARL 430
Cdd:cd17656 289 YTINPEAEIPELP--PIGKPISNTWIYILDQEQQLQPQGIVGELYISGASVARGYLNRQEltAEKFFPDPF---DPNERM 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 431 YRTGDYGS-LKNGSIMYEGRTDSQVKIRGHRVDLSEVEKNVAELPLVDKAIVLCYHAGQVDQAILA-FVKLRDdapmVTE 508
Cdd:cd17656 364 YRTGDLARyLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAyFVMEQE----LNI 439
|
490 500 510
....*....|....*....|....*....|....*....
gi 126789033 509 MQMEARLKDKLADYMTPQVVI-LEHVPLLVNGKVDRQAL 546
Cdd:cd17656 440 SQLREYLAKQLPEYMIPSFFVpLDQLPLTPNGKVDRKAL 478
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
26-457 |
2.67e-76 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 254.93 E-value: 2.67e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 26 FEEQQLRHADKVALIYQPSTTgqgmapsqSSYRQMNERANRAARLLVAetHGrfLQPnsdGDFiVAVCMQPSEGLVTTLL 105
Cdd:pfam00501 1 LERQAARTPDKTALEVGEGRR--------LTYRELDERANRLAAGLRA--LG--VGK---GDR-VAILLPNSPEWVVAFL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 106 AIWKAGGAYLPIDPSFPANRIHHILLEAKPTLVIRDDDIDAGR----FQGTPTLSTTELYAKSLQLAGSNLLSEEMLRGG 181
Cdd:pfam00501 65 ACLKAGAVYVPLNPRLPAEELAYILEDSGAKVLITDDALKLEElleaLGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 182 ---------NDHIAIVLYTSGSTGVPKGVRLPHESILNRLQWQWATFPYtaNEAVSVFKTALTFVD------SIAELWGP 246
Cdd:pfam00501 145 ppppppppdPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPR--GFGLGPDDRVLSTLPlfhdfgLSLGLLGP 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 247 LMCGLAILVVPKAVTKDPQRLVALLERYKIRRLVLVPTLLRSLLmylkmEGGGAAQKLLYNLQIWVCSGEPLSVSLASSF 326
Cdd:pfam00501 223 LLAGATVVLPPGFPALDPAALLELIERYKVTVLYGVPTLLNMLL-----EAGAPKRALLSSLRLVLSGGAPLPPELARRF 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 327 FDYFDEGVhrlYNFYGSTEVLGDVTYFACESKKQLSLYdnvPIGIPLSNTVVYLLDADY-RPVKNGEIGEIFASGLNLAA 405
Cdd:pfam00501 298 RELFGGAL---VNGYGLTETTGVVTTPLPLDEDLRSLG---SVGRPLPGTEVKIVDDETgEPVPPGEPGELCVRGPGVMK 371
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 126789033 406 GYVNgrDPERFlenplavEKKY--ARLYRTGDYGS-LKNGSIMYEGRTDSQVKIR 457
Cdd:pfam00501 372 GYLN--DPELT-------AEAFdeDGWYRTGDLGRrDEDGYLEIVGRKKDQIKLG 417
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
20-655 |
3.91e-76 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 272.42 E-value: 3.91e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 20 RALHRIFEEQQLRHADKVALIYqpsttgqgmAPSQSSYRQMNERANRAARLLVAEthgrflqpNSDGDFIVAVCMQPSEG 99
Cdd:PRK12467 3095 RLVHQLIEAQVARTPEAPALVF---------GDQQLSYAELNRRANRLAHRLIAI--------GVGPDVLVGVAVERSVE 3157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 100 LVTTLLAIWKAGGAYLPIDPSFPANRIHHILLEAKPTLVIRDddidAGRFQGTPTLstTELYAKSLQLAGSNLLSEEML- 178
Cdd:PRK12467 3158 MIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLTQ----AHLLEQLPAP--AGDTALTLDRLDLNGYSENNPs 3231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 179 -RGGNDHIAIVLYTSGSTGVPKGVRLPHESILNRLQWQWATFPYTANEAVsVFKTALTFVDSIAELWGPLMCGlAILVVP 257
Cdd:PRK12467 3232 tRVMGENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRV-LLFMSFSFDGAQERFLWTLICG-GCLVVR 3309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 258 KAVTKDPQRLVALLERYKIRRLVLVPTLLRSLLMYlkmeGGGAAqklLYNLQIWVCSGEPLSvslASSFFDYFDEGVHR- 336
Cdd:PRK12467 3310 DNDLWDPEELWQAIHAHRISIACFPPAYLQQFAED----AGGAD---CASLDIYVFGGEAVP---PAAFEQVKRKLKPRg 3379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 337 LYNFYGSTEVLGDVTYFACeSKKQLSLYDNVPIGIPLSNTVVYLLDADYRPVKNGEIGEIFASGLNLAAGYvnGRDP--- 413
Cdd:PRK12467 3380 LTNGYGPTEAVVTVTLWKC-GGDAVCEAPYAPIGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGVGLARGY--HQRPslt 3456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 414 -ERFLENPLAVEKkyARLYRTGDYGSLK-NGSIMYEGRTDSQVKIRGHRVDLSEVEKNVAELPLVDKAIVLCYHaGQVDQ 491
Cdd:PRK12467 3457 aERFVADPFSGSG--GRLYRTGDLARYRaDGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLARD-GAGGK 3533
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 492 AILAFVKLRDDAPMVTEmQMEARLKDKLADYMTP-QVVILEHVPLLVNGKVDRQALLKtyetannnegdssivLDFDYS- 569
Cdd:PRK12467 3534 QLVAYVVPADPQGDWRE-TLRDHLAASLPDYMVPaQLLVLAAMPLGPNGKVDRKALPD---------------PDAKGSr 3597
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 570 --QVPE-DLKLTARDLFETVGGV--IGRStratlaphSNFYELGGNSLNSIFTVTLLREK-GYNIGISEFIAAKNLGEII 643
Cdd:PRK12467 3598 eyVAPRsEVEQQLAAIWADVLGVeqVGVT--------DNFFELGGDSLLALQVLSRIRQSlGLKLSLRDLMSAPTIAELA 3669
|
650
....*....|..
gi 126789033 644 EKMAANHDAVQL 655
Cdd:PRK12467 3670 GYSPLGDVPVNL 3681
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
23-546 |
4.05e-76 |
|
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.
Pssm-ID: 341300 [Multi-domain] Cd Length: 440 Bit Score: 255.17 E-value: 4.05e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 23 HRIFEEQQLRHADKVALIYQpsttGQGMapsqsSYRQMNERANRAARLLvaetHGRFLQPnsdgDFIVAVCMQPSEGLVT 102
Cdd:cd17645 1 HQLFEEQVERTPDHVAVVDR----GQSL-----TYKQLNEKANQLARHL----RGKGVKP----DDQVGIMLDKSLDMIA 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 103 TLLAIWKAGGAYLPIDPSFPANRIHHILLEAKPTLVIRDddidagrfqgtptlsttelyakslqlagsnllseemlrggN 182
Cdd:cd17645 64 AILGVLKAGGAYVPIDPDYPGERIAYMLADSSAKILLTN----------------------------------------P 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 183 DHIAIVLYTSGSTGVPKGVRLPHESILNRLQWQWATFPYTANEAVSVFkTALTFVDSIAELWGPLMCGLAILVVPKAVTK 262
Cdd:cd17645 104 DDLAYVIYTSGSTGLPKGVMIEHHNLVNLCEWHRPYFGVTPADKSLVY-ASFSFDASAWEIFPHLTAGAALHVVPSERRL 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 263 DPQRLVALLERYKIRrLVLVPTLLRSLLMYLKMEgggaaqkllyNLQIWVCSGEPLSVslassffdyFDEGVHRLYNFYG 342
Cdd:cd17645 183 DLDALNDYFNQEGIT-ISFLPTGAAEQFMQLDNQ----------SLRVLLTGGDKLKK---------IERKGYKLVNNYG 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 343 STEVLGDVTYFACESKkqlslYDNVPIGIPLSNTVVYLLDADYRPVKNGEIGEIFASGLNLAAGYVNGRD--PERFLENP 420
Cdd:cd17645 243 PTENTVVATSFEIDKP-----YANIPIGKPIDNTRVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPEltAEKFIVHP 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 421 LAVEKkyaRLYRTGDYGS-LKNGSIMYEGRTDSQVKIRGHRVDLSEVEKNVAELPLVDKAIVLCYHAGQVDQAILAFVKL 499
Cdd:cd17645 318 FVPGE---RMYRTGDLAKfLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTA 394
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 126789033 500 RDDAPMvteMQMEARLKDKLADYMTPQV-VILEHVPLLVNGKVDRQAL 546
Cdd:cd17645 395 PEEIPH---EELREWLKNDLPDYMIPTYfVHLKALPLTANGKVDRKAL 439
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
56-546 |
5.01e-74 |
|
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: 250.65 E-value: 5.01e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 56 SYRQMNERANRAARLLVAETHGRflqpnsdGDfIVAVCMQPSEGLVTTLLAIWKAGGAYLPIDPSFPANRIHHILLEAKP 135
Cdd:cd12114 14 TYGELAERARRVAGALKAAGVRP-------GD-LVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 136 TLVIRDDDIDAGRfQGTPTLSTTELYAKSLQLAGSNLLSEEmlrggnDHIAIVLYTSGSTGVPKGVRLPHESILNRLQWQ 215
Cdd:cd12114 86 RLVLTDGPDAQLD-VAVFDVLILDLDALAAPAPPPPVDVAP------DDLAYVIFTSGSTGTPKGVMISHRAALNTILDI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 216 WATFPYTANE---AVSvfktALTFVDSIAELWGPLMCGLAILVVPKAVTKDPQRLVALLERYKIRRLVLVPTLLRSLLMY 292
Cdd:cd12114 159 NRRFAVGPDDrvlALS----SLSFDLSVYDIFGALSAGATLVLPDEARRRDPAHWAELIERHGVTLWNSVPALLEMLLDV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 293 LkmeggGAAQKLLYNLQIWVCSGEPLSVSLASSFFDYFDEGvhRLYNFYGSTEvlGDVTYFACESKKQLSLYDNVPIGIP 372
Cdd:cd12114 235 L-----EAAQALLPSLRLVLLSGDWIPLDLPARLRALAPDA--RLISLGGATE--ASIWSIYHPIDEVPPDWRSIPYGRP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 373 LSNTVVYLLDADYRPVKNGEIGEIFASGLNLAAGYVNgrDPE----RFLENPLAVekkyaRLYRTGDYGSLK-NGSIMYE 447
Cdd:cd12114 306 LANQRYRVLDPRGRDCPDWVPGELWIGGRGVALGYLG--DPEltaaRFVTHPDGE-----RLYRTGDLGRYRpDGTLEFL 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 448 GRTDSQVKIRGHRVDLSEVEKNVAELPLVDKAIVLCYhAGQVDQAILAFVKLRDDAPMVTEMQMEARLKDKLADYMTP-Q 526
Cdd:cd12114 379 GRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVL-GDPGGKRLAAFVVPDNDGTPIAPDALRAFLAQTLPAYMIPsR 457
|
490 500
....*....|....*....|
gi 126789033 527 VVILEHVPLLVNGKVDRQAL 546
Cdd:cd12114 458 VIALEALPLTANGKVDRAAL 477
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
54-546 |
6.09e-74 |
|
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: 249.31 E-value: 6.09e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 54 QSSYRQMNERANRAARLLvaetHGRFLQPNSdgdfIVAVCMQPSEGLVTTLLAIWKAGGAYLPIDPSFPANRIHHILLEA 133
Cdd:cd17650 12 QLTYRELNERANQLARTL----RGLGVAPGS----VVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLEDS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 134 K-PTLVIRDDDIdagrfqgtptlsttelyakslqlagsnllseemlrggndhiAIVLYTSGSTGVPKGVRLPHESILN-- 210
Cdd:cd17650 84 GaKLLLTQPEDL-----------------------------------------AYVIYTSGTTGKPKGVMVEHRNVAHaa 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 211 ---RLQWQWATFPYTANEAVSvfktaLTFVDSIAELWGPLMCGLAILVVPKAVTKDPQRLVALLERYKIRRLVLVPTLLR 287
Cdd:cd17650 123 hawRREYELDSFPVRLLQMAS-----FSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSRITLMESTPALIR 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 288 SLLMYLKMEGggaaqKLLYNLQIWVCSGEPLSVSLASSFFDYFDEGVhRLYNFYGSTEVLGDVTYFAcESKKQLSLYDNV 367
Cdd:cd17650 198 PVMAYVYRNG-----LDLSAMRLLIVGSDGCKAQDFKTLAARFGQGM-RIINSYGVTEATIDSTYYE-EGRDPLGDSANV 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 368 PIGIPLSNTVVYLLDADYRPVKNGEIGEIFASGLNLAAGYVNgrDPE----RFLENPLAvekKYARLYRTGDYGS-LKNG 442
Cdd:cd17650 271 PIGRPLPNTAMYVLDERLQPQPVGVAGELYIGGAGVARGYLN--RPEltaeRFVENPFA---PGERMYRTGDLARwRADG 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 443 SIMYEGRTDSQVKIRGHRVDLSEVEKNVAELPLVDKAIVLCYHAGQVDQAILAFVkLRDDAPMVTEMQmeARLKDKLADY 522
Cdd:cd17650 346 NVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDKGGEARLCAYV-VAAATLNTAELR--AFLAKELPSY 422
|
490 500
....*....|....*....|....*
gi 126789033 523 MTP-QVVILEHVPLLVNGKVDRQAL 546
Cdd:cd17650 423 MIPsYYVQLDALPLTPNGKVDRRAL 447
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
20-625 |
7.82e-72 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 259.50 E-value: 7.82e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 20 RALHRIFEEQQLRHADKVALIYqpstTGQGMapsqsSYRQMNERANRAARLLVAETHGrflqpnsdGDFIVAVCMQPSEG 99
Cdd:PRK12316 3057 RGVHRLFEEQVERTPDAVALAF----GEQRL-----SYAELNRRANRLAHRLIERGVG--------PDVLVGVAVERSLE 3119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 100 LVTTLLAIWKAGGAYLPIDPSFPANRIHHILLEAKPTLVIRDDDIDAGRFQGTPTLsttELYAKSLQLAGSNLLSEEMlr 179
Cdd:PRK12316 3120 MVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQSHLRLPLAQGVQVL---DLDRGDENYAEANPAIRTM-- 3194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 180 ggNDHIAIVLYTSGSTGVPKGVRLPHESILNRLQWQWATFPYTANEAVSVFkTALTFVDSIAELWGPLMCGLAILVVPKA 259
Cdd:PRK12316 3195 --PENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQF-TTFSFDVFVEELFWPLMSGARVVLAGPE 3271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 260 VTKDPQRLVALLERYKIRRLVLVPTLLRSLLmylkmEGGGAAQklLYNLQIWVCSGEPLSVSLASSFFdyfdeGVHRLYN 339
Cdd:PRK12316 3272 DWRDPALLVELINSEGVDVLHAYPSMLQAFL-----EEEDAHR--CTSLKRIVCGGEALPADLQQQVF-----AGLPLYN 3339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 340 FYGSTEVLGDVTYFACESKKQlslyDNVPIGIPLSNTVVYLLDADYRPVKNGEIGEIFASGLNLAAGYVN--GRDPERFL 417
Cdd:PRK12316 3340 LYGPTEATITVTHWQCVEEGK----DAVPIGRPIANRACYILDGSLEPVPVGALGELYLGGEGLARGYHNrpGLTAERFV 3415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 418 ENPLAvekKYARLYRTGDYGSLK-NGSIMYEGRTDSQVKIRGHRVDLSEVEKNVAELPLVDKAIVLCYHAGQvdqaILAF 496
Cdd:PRK12316 3416 PDPFV---PGERLYRTGDLARYRaDGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAVDGRQ----LVAY 3488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 497 VKLRDDAPMVTEMqMEARLKDKLADYMTP-QVVILEHVPLLVNGKVDRQAL-------LKTYETANNNEGDSSIVLDFdy 568
Cdd:PRK12316 3489 VVPEDEAGDLREA-LKAHLKASLPEYMVPaHLLFLERMPLTPNGKLDRKALprpdaalLQQDYVAPVNELERRLAAIW-- 3565
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 126789033 569 sqvPEDLKLtardlfETVGgvigrstratLAphSNFYELGGNSLNSIFTVTLLREKG 625
Cdd:PRK12316 3566 ---ADVLKL------EQVG----------LT--DNFFELGGDSIISLQVVSRARQAG 3601
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
56-546 |
4.62e-71 |
|
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: 241.92 E-value: 4.62e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 56 SYRQMNERANRAARLLVAETHGRflqpnsdGDFIVAVCMQPSEGLVTTLLAIWKAGGAYLPIDPSFPANRIHHILLEAKP 135
Cdd:cd17648 14 TYRELNERANRLAHYLLSVAEIR-------PDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFILEDTGA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 136 TLVIRDddidagrfqgtptlsTTELyakslqlagsnllseemlrggndhiAIVLYTSGSTGVPKGVRLPHESILNRLQWQ 215
Cdd:cd17648 87 RVVITN---------------STDL-------------------------AYAIYTSGTTGKPKGVLVEHGSVVNLRTSL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 216 WATFPYTAN--EAVSVFkTALTFVDSIAELWGPLMCGLAILVVPKAVTKDPQRLVALLERYKIRRLVLVPTLLrSLLMYL 293
Cdd:cd17648 127 SERYFGRDNgdEAVLFF-SNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPDRFYAYINREKVTYLSGTPSVL-QQYDLA 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 294 KmegggaaqklLYNLQIWVCSGEPLSvslaSSFFDYFDEGVH-RLYNFYGSTE--VLGDVTYFACESKKQLSlydnvpIG 370
Cdd:cd17648 205 R----------LPHLKRVDAAGEEFT----APVFEKLRSRFAgLIINAYGPTEttVTNHKRFFPGDQRFDKS------LG 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 371 IPLSNTVVYLLDADYRPVKNGEIGEIFASGLNLAAGYVNGRD--PERFLENPLAVEK-----KYARLYRTGDYGS-LKNG 442
Cdd:cd17648 265 RPVRNTKCYVLNDAMKRVPVGAVGELYLGGDGVARGYLNRPEltAERFLPNPFQTEQerargRNARLYKTGDLVRwLPSG 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 443 SIMYEGRTDSQVKIRGHRVDLSEVEKNVAELPLVDKAIVLC-YHAGQVDQAILAFV--KLRDDAPMVTEMQMEARLKDKL 519
Cdd:cd17648 345 ELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAkEDASQAQSRIQKYLvgYYLPEPGHVPESDLLSFLRAKL 424
|
490 500
....*....|....*....|....*...
gi 126789033 520 ADYMTP-QVVILEHVPLLVNGKVDRQAL 546
Cdd:cd17648 425 PRYMVPaRLVRLEGIPVTINGKLDVRAL 452
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
21-623 |
1.50e-70 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 255.65 E-value: 1.50e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 21 ALHRIFEEQQLRHADKVALIYQpsttGQGMapsqsSYRQMNERANRAARLLVAETHGrflqpnsdGDFIVAVCMQPSEGL 100
Cdd:PRK12316 2004 GVHQRIAEQAARAPEAIAVVFG----DQHL-----SYAELDSRANRLAHRLRARGVG--------PEVRVAIAAERSFEL 2066
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 101 VTTLLAIWKAGGAYLPIDPSFPANRIHHILLEAKPTLVIRDDDIDAgRF---QGTPTLSTT---EL-----YAKSLQLAG 169
Cdd:PRK12316 2067 VVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQRHLLE-RLplpAGVARLPLDrdaEWadypdTAPAVQLAG 2145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 170 SNLlseemlrggndhiAIVLYTSGSTGVPKGVRLPHESILNRLQWQWATFPYTANEAVSVFkTALTFVDSIAELWGPLMC 249
Cdd:PRK12316 2146 ENL-------------AYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCELQF-MSFSFDGAHEQWFHPLLN 2211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 250 GLAILVVPKAVtKDPQRLVALLERYKIRRLVLVPTLLRSLLMYLKMEGGGAaqkllyNLQIWVCSGEPLSVSLASSFFDY 329
Cdd:PRK12316 2212 GARVLIRDDEL-WDPEQLYDEMERHGVTILDFPPVYLQQLAEHAERDGRPP------AVRVYCFGGEAVPAASLRLAWEA 2284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 330 FDEGvhRLYNFYGSTEVLGDVTYFACESKKQLSLYdNVPIGIPLSNTVVYLLDADYRPVKNGEIGEIFASGLNLAAGYVN 409
Cdd:PRK12316 2285 LRPV--YLFNGYGPTEAVVTPLLWKCRPQDPCGAA-YVPIGRALGNRRAYILDADLNLLAPGMAGELYLGGEGLARGYLN 2361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 410 --GRDPERFLENPLAVEKkyARLYRTGDYGSLK-NGSIMYEGRTDSQVKIRGHRVDLSEVEKNVAELPLVDKAIVLCyHA 486
Cdd:PRK12316 2362 rpGLTAERFVPDPFSASG--ERLYRTGDLARYRaDGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVA-QD 2438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 487 GQVDQAILAFVkLRDDAPMVTEMQMEARLKDKLADYMTP-QVVILEHVPLLVNGKVDRQALLKTYETAnnnegdssivLD 565
Cdd:PRK12316 2439 GASGKQLVAYV-VPDDAAEDLLAELRAWLAARLPAYMVPaHWVVLERLPLNPNGKLDRKALPKPDVSQ----------LR 2507
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 126789033 566 FDYSQVPEDLKLTARDLFETVGGVIGrstratLAPHSNFYELGGNSLNSIFTVTLLRE 623
Cdd:PRK12316 2508 QAYVAPQEGLEQRLAAIWQAVLKVEQ------VGLDDHFFELGGHSLLATQVVSRVRQ 2559
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
19-546 |
2.23e-68 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 249.31 E-value: 2.23e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 19 PRALHRIFEEQQLRHADKVALIYQPSTTGqgmapsqssYRQMNERANRAARllvaethgrFLQPNSDG-DFIVAVCMQPS 97
Cdd:PRK05691 1130 QAWLPELLNEQARQTPERIALVWDGGSLD---------YAELHAQANRLAH---------YLRDKGVGpDVCVAIAAERS 1191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 98 EGLVTTLLAIWKAGGAYLPIDPSFPANRIHHILLEAKPTLVIRDDDIdAGRFQGTPTLSTTELyaKSLQLAgSNLLSEEM 177
Cdd:PRK05691 1192 PQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQSHL-LERLPQAEGVSAIAL--DSLHLD-SWPSQAPG 1267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 178 LRGGNDHIAIVLYTSGSTGVPKGVRLPHESILNRLQWQWATFPYTANEaVSVFKTALTFVDSIAELWGPLMCGLAILVVP 257
Cdd:PRK05691 1268 LHLHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSD-VLMQKAPISFDVSVWECFWPLITGCRLVLAG 1346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 258 KAVTKDPQRLVALLERYKIRRLVLVPTLLRsllmyLKMEGGGAAQklLYNLQIWVCSGEPLSVSLASSFFDYFdEGVhRL 337
Cdd:PRK05691 1347 PGEHRDPQRIAELVQQYGVTTLHFVPPLLQ-----LFIDEPLAAA--CTSLRRLFSGGEALPAELRNRVLQRL-PQV-QL 1417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 338 YNFYGSTEVLGDVTYFACeskkQLSLYDNVPIGIPLSNTVVYLLDADYRPVKNGEIGEIFASGLNLAAGYVN--GRDPER 415
Cdd:PRK05691 1418 HNRYGPTETAINVTHWQC----QAEDGERSPIGRPLGNVLCRVLDAELNLLPPGVAGELCIGGAGLARGYLGrpALTAER 1493
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 416 FLENPLAVEKkyARLYRTGDYGSLK-NGSIMYEGRTDSQVKIRGHRVDLSEVEKNVAELPLVDKAIVLCyHAGQVDQAIL 494
Cdd:PRK05691 1494 FVPDPLGEDG--ARLYRTGDRARWNaDGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLV-REGAAGAQLV 1570
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 126789033 495 AFVKLrDDAPMVTEMQMEARLKDKLADYMTP-QVVILEHVPLLVNGKVDRQAL 546
Cdd:PRK05691 1571 GYYTG-EAGQEAEAERLKAALAAELPEYMVPaQLIRLDQMPLGPSGKLDRRAL 1622
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
24-546 |
1.41e-67 |
|
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: 231.43 E-value: 1.41e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 24 RIFEEQQLRHADKVALiyqpsttgqgMAPSQS-SYRQMNERANRAARLLVAEthgrFLQPnsdGDfIVAVCMQPSEGLVT 102
Cdd:cd17653 1 DAFERIAAAHPDAVAV----------ESLGGSlTYGELDAASNALANRLLQL----GVVP---GD-VVPLLSDRSLEMLV 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 103 TLLAIWKAGGAYLPIDPSFPANRIHHILLEAKPTLVIRDDdidagrfqgtptlsttelyakslqlagsnllseemlrGGN 182
Cdd:cd17653 63 AILAILKAGAAYVPLDAKLPSARIQAILRTSGATLLLTTD-------------------------------------SPD 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 183 DhIAIVLYTSGSTGVPKGVRLPHESILNRLQWQWATFPYTANEAVSVFkTALTFVDSIAELWGPLMCGlAILVVpkavtK 262
Cdd:cd17653 106 D-LAYIIFTSGSTGIPKGVMVPHRGVLNYVSQPPARLDVGPGSRVAQV-LSIAFDACIGEIFSTLCNG-GTLVL-----A 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 263 DPQRLVALLERyKIRRLVLVPTLLRSLlmylkmegggaAQKLLYNLQIWVCSGEPLSVSLASSFfdyfdEGVHRLYNFYG 342
Cdd:cd17653 178 DPSDPFAHVAR-TVDALMSTPSILSTL-----------SPQDFPNLKTIFLGGEAVPPSLLDRW-----SPGRRLYNAYG 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 343 STEVLGDVTYfaceskKQLSLYDNVPIGIPLSNTVVYLLDADYRPVKNGEIGEIFASGLNLAAGYVNgrDPE----RFLE 418
Cdd:cd17653 241 PTECTISSTM------TELLPGQPVTIGKPIPNSTCYILDADLQPVPEGVVGEICISGVQVARGYLG--NPAltasKFVP 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 419 NPLaveKKYARLYRTGDYGSL-KNGSIMYEGRTDSQVKIRGHRVDLSEVEKNV-AELPLVDKAIVLcyhagQVDQAILAF 496
Cdd:cd17653 313 DPF---WPGSRMYRTGDYGRWtEDGGLEFLGREDNQVKVRGFRINLEEIEEVVlQSQPEVTQAAAI-----VVNGRLVAF 384
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 126789033 497 VklrddAPM-VTEMQMEARLKDKLADYMTPQVVI-LEHVPLLVNGKVDRQAL 546
Cdd:cd17653 385 V-----TPEtVDVDGLRSELAKHLPSYAVPDRIIaLDSFPLTANGKVDRKAL 431
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
22-548 |
9.83e-62 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 217.46 E-value: 9.83e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 22 LHRIFEEQQlRHADKVALIYQPSTtgqgmapsqSSYRQMNERANRAARLLVAethgrfLQPNSDGDFIVAVCMQPsEGLV 101
Cdd:PRK04813 5 IETIEEFAQ-TQPDFPAYDYLGEK---------LTYGQLKEDSDALAAFIDS------LKLPDKSPIIVFGHMSP-EMLA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 102 TtLLAIWKAGGAYLPIDPSFPANRIHHILLEAKPTLVIRDDDIDAGRfQGTPTLSTTELYAkslQLAGSNLLSEEMLRGG 181
Cdd:PRK04813 68 T-FLGAVKAGHAYIPVDVSSPAERIEMIIEVAKPSLIIATEELPLEI-LGIPVITLDELKD---IFATGNPYDFDHAVKG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 182 NDHIAIVlYTSGSTGVPKGVRLPHESILNRLQWQWATF-----PYTANEA-----VSVFKtaltfvdsiaelWGP-LMCG 250
Cdd:PRK04813 143 DDNYYII-FTSGTTGKPKGVQISHDNLVSFTNWMLEDFalpegPQFLNQApysfdLSVMD------------LYPtLASG 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 251 LAILVVPKAVTKDPQRLVALLERYKIRRLVLVPT------LLRSLlmylkmegggaAQKLLYNLQIWVCSGEPLSVSLAS 324
Cdd:PRK04813 210 GTLVALPKDMTANFKQLFETLPQLPINVWVSTPSfadmclLDPSF-----------NEEHLPNLTHFLFCGEELPHKTAK 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 325 SFFDYFDEGvhRLYNFYGSTEVLGDVTyfACE-SKKQLSLYDNVPIGIPLSNTVVYLLDADYRPVKNGEIGEIFASGLNL 403
Cdd:PRK04813 279 KLLERFPSA--TIYNTYGPTEATVAVT--SIEiTDEMLDQYKRLPIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSV 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 404 AAGYVNgrDPER----FLEnplavEKKYaRLYRTGDYGSLKNGSIMYEGRTDSQVKIRGHRVDLSEVEKNVAELPLVDKA 479
Cdd:PRK04813 355 SKGYLN--NPEKtaeaFFT-----FDGQ-PAYHTGDAGYLEDGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESA 426
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 126789033 480 IVLCYH-AGQVDQAILAFV----KLRDDAPMVTEMQMEarLKDKLADYMTPQ-VVILEHVPLLVNGKVDRQALLK 548
Cdd:PRK04813 427 VVVPYNkDHKVQYLIAYVVpkeeDFEREFELTKAIKKE--LKERLMEYMIPRkFIYRDSLPLTPNGKIDRKALIE 499
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
22-625 |
1.56e-58 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 219.27 E-value: 1.56e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 22 LHRIFEEQQLRHADKVALIYqpstTGQGMapsqsSYRQMNERANRAARLLvaetHGRFLQPNSDgdfiVAVCMQPSEGLV 101
Cdd:PRK05691 2190 LHGLFAAQAARTPQAPALTF----AGQTL-----SYAELDARANRLARAL----RERGVGPQVR----VGLALERSLEMV 2252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 102 TTLLAIWKAGGAYLPIDPSFPANRIHHILLEAKPTLVIRDDDIDAGRFQGTPTLSTTELYAKSLQLAGSNLLSEEMLrGG 181
Cdd:PRK05691 2253 VGLLAILKAGGAYVPLDPEYPLERLHYMIEDSGIGLLLSDRALFEALGELPAGVARWCLEDDAAALAAYSDAPLPFL-SL 2331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 182 NDHIAIVLYTSGSTGVPKGVRLPHESILNRLQWQWATFPYTANEAVSVFKTaLTFVDSIAELWGPLMCGlAILVVPKAVT 261
Cdd:PRK05691 2332 PQHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDCELHFYS-INFDAASERLLVPLLCG-ARVVLRAQGQ 2409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 262 KDPQRLVALLERYKIRRLVLVPTLLRSLLMYLKMEGggaaQKLLYNLQIwvCSGEPLSVSLASSFFDYFDEGVhrLYNFY 341
Cdd:PRK05691 2410 WGAEEICQLIREQQVSILGFTPSYGSQLAQWLAGQG----EQLPVRMCI--TGGEALTGEHLQRIRQAFAPQL--FFNAY 2481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 342 GSTEVLgdVTYFACESKKQLSL-YDNVPIGIPLSNTVVYLLDADYRPVKNGEIGEIFASGLNLAAGYVN--GRDPERFLE 418
Cdd:PRK05691 2482 GPTETV--VMPLACLAPEQLEEgAASVPIGRVVGARVAYILDADLALVPQGATGELYVGGAGLAQGYHDrpGLTAERFVA 2559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 419 NPLAVEKkyARLYRTGDYGSLK-NGSIMYEGRTDSQVKIRGHRVDLSEVEKNVAELPLVDKAIVLCYHAGQVDQAILAFV 497
Cdd:PRK05691 2560 DPFAADG--GRLYRTGDLVRLRaDGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLALDTPSGKQLAGYLV 2637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 498 ----KLRDDAPMVTEMQMEARLKDKLADYMTP-QVVILEHVPLLVNGKVDRQALLKTYETANNNegdssivldfDYSQVP 572
Cdd:PRK05691 2638 savaGQDDEAQAALREALKAHLKQQLPDYMVPaHLILLDSLPLTANGKLDRRALPAPDPELNRQ----------AYQAPR 2707
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 126789033 573 EDLKLTARDLFETVGGVigrstrATLAPHSNFYELGGNSLNSIFTVTLLREKG 625
Cdd:PRK05691 2708 SELEQQLAQIWREVLNV------ERVGLGDNFFELGGDSILSIQVVSRARQLG 2754
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
184-542 |
2.70e-58 |
|
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: 202.90 E-value: 2.70e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 184 HIAIVLYTSGSTGVPKGVRLPHESILNRLQWQWATFPYTANEAVSVFkTALTFVDSIAELWGPLMCGLAILVVPKavtKD 263
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLST-LPLFHIGGLFGLLGALLAGGTVVLLPK---FD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 264 PQRLVALLERYKIRRLVLVPTLLRSLLMYLKMEGGGaaqklLYNLQIWVCSGEPLSVSLASSFFDYFDEgvhRLYNFYGS 343
Cdd:cd04433 77 PEAALELIEREKVTILLGVPTLLARLLKAPESAGYD-----LSSLRALVSGGAPLPPELLERFEEAPGI---KLVNGYGL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 344 TEVLGDVTYFACESKKQLSlydnVPIGIPLSNTVVYLLDADYRPVKNGEIGEIFASGLNLAAGYVNgrDPERflenplAV 423
Cdd:cd04433 149 TETGGTVATGPPDDDARKP----GSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWN--NPEA------TA 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 424 EKKYARLYRTGDYGSL-KNGSIMYEGRTDSQVKIRGHRVDLSEVEKNVAELPLVDKAIVLCYHAGQVDQAILAFVKLRDD 502
Cdd:cd04433 217 AVDEDGWYRTGDLGRLdEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPG 296
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 126789033 503 APMVTEmQMEARLKDKLADYMTPQ-VVILEHVPLLVNGKVD 542
Cdd:cd04433 297 ADLDAE-ELRAHVRERLAPYKVPRrVVFVDALPRTASGKID 336
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
13-612 |
2.96e-57 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 215.03 E-value: 2.96e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 13 LQQDFVpralhRIFEEQQLRHADKVALiyqpSTTGQgmapsQSSYRQMNERANRAARLLVAETHGrFLQPnsdgdfiVAV 92
Cdd:PRK05691 3718 LEQSYV-----RLFEAQVAAHPQRIAA----SCLDQ-----QWSYAELNRAANRLGHALRAAGVG-VDQP-------VAL 3775
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 93 CMQPSEGLVTTLLAIWKAGGAYLPIDPSFPANRIHHIL-LEAKPTLVIRDddidAGRFQGTPTLSTTELYAKSLQLAGSN 171
Cdd:PRK05691 3776 LAERGLDLLGMIVGSFKAGAGYLPLDPGLPAQRLQRIIeLSRTPVLVCSA----ACREQARALLDELGCANRPRLLVWEE 3851
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 172 LLSEEM------LRGGNDHIAIVLYTSGSTGVPKGVRLPHESILNRlqwQWATFPYTA-NEAVSVFKTALTFVD-SIAE- 242
Cdd:PRK05691 3852 VQAGEVashnpgIYSGPDNLAYVIYTSGSTGLPKGVMVEQRGMLNN---QLSKVPYLAlSEADVIAQTASQSFDiSVWQf 3928
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 243 LWGPLMcGLAILVVPKAVTKDPQRLVALLERYKIRRLVLVPTLLRSLLmylkmeggGAAQKLLYNLQIWVCSGEPLSVSL 322
Cdd:PRK05691 3929 LAAPLF-GARVEIVPNAIAHDPQGLLAHVQAQGITVLESVPSLIQGML--------AEDRQALDGLRWMLPTGEAMPPEL 3999
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 323 ASSFFD-YFDEGvhrLYNFYGSTEVLGDVTYFACESKKQLSLYdnVPIGIPLSNTVVYLLDADYRPVKNGEIGEIFASGL 401
Cdd:PRK05691 4000 ARQWLQrYPQIG---LVNAYGPAECSDDVAFFRVDLASTRGSY--LPIGSPTDNNRLYLLDEALELVPLGAVGELCVAGT 4074
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 402 NLAAGYVNgrDPER----FLENPLAVEKKyaRLYRTGDYG-SLKNGSIMYEGRTDSQVKIRGHRVDLSEVEKNVAELPLV 476
Cdd:PRK05691 4075 GVGRGYVG--DPLRtalaFVPHPFGAPGE--RLYRTGDLArRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEV 4150
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 477 DKAIVLCyHAGQVDQAILAFVKLRDDAPMVTEM--QMEARLKDKLADYMTP-QVVILEHVPLLVNGKVDRQALLKtyeta 553
Cdd:PRK05691 4151 REAAVAV-QEGVNGKHLVGYLVPHQTVLAQGALleRIKQRLRAELPDYMVPlHWLWLDRLPLNANGKLDRKALPA----- 4224
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 126789033 554 nnnegdssivldFDYSQVPEDLKLTARD-LFETVGGVIGRSTRAT-LAPHSNFYELGGNSL 612
Cdd:PRK05691 4225 ------------LDIGQLQSQAYLAPRNeLEQTLATIWADVLKVErVGVHDNFFELGGHSL 4273
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
95-546 |
1.30e-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: 1.30e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 95 QPSEGLVTTLLAIWKAGGAYLPIDPSFPANRIHHILleaKPTLVirdDDIDAGRFQGT-PTLSTTELYAKSLQLAGSnll 173
Cdd:cd17654 49 DRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVM---KKCHV---SYLLQNKELDNaPLSFTPEHRHFNIRTDEC--- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 174 seemlrggndhIAIVLYTSGSTGVPKGVRLPHESILNRLQWQWATFPYTAnEAVSVFKTALTFVDSIAELWGPLMCGLAI 253
Cdd:cd17654 120 -----------LAYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFNITS-EDILFLTSPLTFDPSVVEIFLSLSSGATL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 254 LVVPKAVTKDPQRLV-ALLERYKIRRLVLVPTLLRSLLMYLKMEGGGAAQKllyNLQIWVCSGEPL-SVSLASSFFDYFD 331
Cdd:cd17654 188 LIVPTSVKVLPSKLAdILFKRHRITVLQATPTLFRRFGSQSIKSTVLSATS---SLRVLALGGEPFpSLVILSSWRGKGN 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 332 EgvHRLYNFYGSTEVLGDVTYFACESKKQlslydNVPIGIPLSNTVVYLLDADYRPVKngeiGEIFASGLNLAAgyvngr 411
Cdd:cd17654 265 R--TRIFNIYGITEVSCWALAYKVPEEDS-----PVQLGSPLLGTVIEVRDQNGSEGT----GQVFLGGLNRVC------ 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 412 dperFLENPLAVEKkyARLYRTGDYGSLKNGSIMYEGRTDSQVKIRGHRVDLSEVEKnVAELPLVDKAIVLCYHAgqvDQ 491
Cdd:cd17654 328 ----ILDDEVTVPK--GTMRATGDFVTVKDGELFFLGRKDSQIKRRGKRINLDLIQQ-VIESCLGVESCAVTLSD---QQ 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 126789033 492 AILAF-VKLRDDAPMVTEMQMEARLKDKLADYMtpqvVILEHVPLLVNGKVDRQAL 546
Cdd:cd17654 398 RLIAFiVGESSSSRIHKELQLTLLSSHAIPDTF----VQIDKLPLTSHGKVDKSEL 449
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
32-546 |
5.21e-45 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 171.06 E-value: 5.21e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 32 RHA----DKVALIYQpSTTGQgmapSQS-SYRQMNERANRAARLLVAetHGrfLQPnsdGDfIVAVCMQPSEGLVTTLLA 106
Cdd:COG0365 17 RHAegrgDKVALIWE-GEDGE----ERTlTYAELRREVNRFANALRA--LG--VKK---GD-RVAIYLPNIPEAVIAMLA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 107 IWKAGGAYLPIDPSFPANRIHHILLEAKPTLVIRDDD-------------IDA--------------GRFQGTPTLSTTE 159
Cdd:COG0365 84 CARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGglrggkvidlkekVDEaleelpslehvivvGRTGADVPMEGDL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 160 LYAKSLQLAGSNLLSEEMlrgGNDHIAIVLYTSGSTGVPKGVRLPHESILNRLQW-QWATFPYTANEavsVFktaLTFVD 238
Cdd:COG0365 164 DWDELLAAASAEFEPEPT---DADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATtAKYVLDLKPGD---VF---WCTAD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 239 S--IAELW----GPLMCGLAILVVP-KAVTKDPQRLVALLERYKIRRLVLVPTLLRSLLmylKMEGGGAAQKLLYNLQIW 311
Cdd:COG0365 235 IgwATGHSyivyGPLLNGATVVLYEgRPDFPDPGRLWELIEKYGVTVFFTAPTAIRALM---KAGDEPLKKYDLSSLRLL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 312 VCSGEPLSVSLASSFFDYFdeGVHrLYNFYGSTEVLGDVtyfaceskkqLSLYDNVP-----IGIPLSNTVVYLLDADYR 386
Cdd:COG0365 312 GSAGEPLNPEVWEWWYEAV--GVP-IVDGWGQTETGGIF----------ISNLPGLPvkpgsMGKPVPGYDVAVVDEDGN 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 387 PVKNGEIGEI-----FASglnLAAGYVNgrDPERFLEnplAVEKKYARLYRTGDYGSL-KNGSIMYEGRTDSQVKIRGHR 460
Cdd:COG0365 379 PVPPGEEGELvikgpWPG---MFRGYWN--DPERYRE---TYFGRFPGWYRTGDGARRdEDGYFWILGRSDDVINVSGHR 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 461 VDLSEVEKNVAELPLVDKAIVLcyhaGQVD----QAILAFVKLRDDAP----MVTEMQmeARLKDKLADYMTP-QVVILE 531
Cdd:COG0365 451 IGTAEIESALVSHPAVAEAAVV----GVPDeirgQVVKAFVVLKPGVEpsdeLAKELQ--AHVREELGPYAYPrEIEFVD 524
|
570
....*....|....*
gi 126789033 532 HVPLLVNGKVDRQAL 546
Cdd:COG0365 525 ELPKTRSGKIMRRLL 539
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
32-543 |
8.04e-43 |
|
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: 162.01 E-value: 8.04e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 32 RHADKVALIYQPSTTgqgmapsqsSYRQMNERANRAARLLVAETHGRflqpnsdGDfIVAVCMQPSEGLVTTLLAIWKAG 111
Cdd:cd17631 7 RHPDRTALVFGGRSL---------TYAELDERVNRLAHALRALGVAK-------GD-RVAVLSKNSPEFLELLFAAARLG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 112 GAYLPIDPSFPANRIHHILLEAKPTLVIRDddidagrfqgtptlsttelyakslqlagsnllseemlrggndhIAIVLYT 191
Cdd:cd17631 70 AVFVPLNFRLTPPEVAYILADSGAKVLFDD-------------------------------------------LALLMYT 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 192 SGSTGVPKGVRLPHESILNRLQWQWATFPYTAnEAVSVFKTALTFVDSIAELWGP-LMCGLAILVVPKAvtkDPQRLVAL 270
Cdd:cd17631 107 SGTTGRPKGAMLTHRNLLWNAVNALAALDLGP-DDVLLVVAPLFHIGGLGVFTLPtLLRGGTVVILRKF---DPETVLDL 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 271 LERYKIRRLVLVPTLLRSLLmylkmEGGGAAQKLLYNLQIWVCSGEPLSVSLASSFFDYfdeGVhRLYNFYGSTEVLGDV 350
Cdd:cd17631 183 IERHRVTSFFLVPTMIQALL-----QHPRFATTDLSSLRAVIYGGAPMPERLLRALQAR---GV-KFVQGYGMTETSPGV 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 351 TyfACESKKQLSLYDNVpiGIPLSNTVVYLLDADYRPVKNGEIGEIFASGLNLAAGYVNgrDPErflENPLAVEKKYarl 430
Cdd:cd17631 254 T--FLSPEDHRRKLGSA--GRPVFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWN--RPE---ATAAAFRDGW--- 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 431 YRTGDYGSLKNGSIMY-EGRTDSQVKIRGHRVDLSEVEKNVAELPLVDKAIVLcyhaGQVD----QAILAFVKLRDDAPm 505
Cdd:cd17631 322 FHTGDLGRLDEDGYLYiVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVI----GVPDekwgEAVVAVVVPRPGAE- 396
|
490 500 510
....*....|....*....|....*....|....*....
gi 126789033 506 VTEMQMEARLKDKLADYMTP-QVVILEHVPLLVNGKVDR 543
Cdd:cd17631 397 LDEDELIAHCRERLARYKIPkSVEFVDALPRNATGKILK 435
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
21-624 |
1.77e-38 |
|
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: 155.61 E-value: 1.77e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 21 ALHRIFEEQQLRHADKVALIYQPSTTGqGMAPSQS-SYRQMNERANRAARLLVAETHGRflqpnsdGDfIVAVCMQPSEG 99
Cdd:TIGR03443 237 AIHDIFADNAEKHPDRTCVVETPSFLD-PSSKTRSfTYKQINEASNILAHYLLKTGIKR-------GD-VVMIYAYRGVD 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 100 LVTTLLAIWKAGGAYLPIDPSFPANRIHHILLEAKPT--LVIRDddidagrfQGTPTLSTTELYAKSLQL---------- 167
Cdd:TIGR03443 308 LVVAVMGVLKAGATFSVIDPAYPPARQTIYLSVAKPRalIVIEK--------AGTLDQLVRDYIDKELELrteipalalq 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 168 -----------AGSN--LLSEEMLRG-------GNDHIAIVLYTSGSTGVPKGVRLPHESILNRLQWQWATFPYTANEAv 227
Cdd:TIGR03443 380 ddgslvggsleGGETdvLAPYQALKDtptgvvvGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFGLSENDK- 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 228 svfktaLTFVDSIA------ELWGPLMCGlAILVVPkavTKD----PQRLVALLERYKIRRLVLVPTLLRSLlmylkmeg 297
Cdd:TIGR03443 459 ------FTMLSGIAhdpiqrDMFTPLFLG-AQLLVP---TADdigtPGRLAEWMAKYGATVTHLTPAMGQLL-------- 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 298 ggAAQKllyNLQIwvcsgePlsvSLASSFF-------------DYFDEGVhRLYNFYGSTEVLGDVTYFACESKKQLSLY 364
Cdd:TIGR03443 521 --SAQA---TTPI------P---SLHHAFFvgdiltkrdclrlQTLAENV-CIVNMYGTTETQRAVSYFEIPSRSSDSTF 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 365 -----DNVPIGIPLSNtvVYLLdadyrpVKN----------GEIGEIFASGLNLAAGYVNGRD--PERFLENPLAVEKKY 427
Cdd:TIGR03443 586 lknlkDVMPAGKGMKN--VQLL------VVNrndrtqtcgvGEVGEIYVRAGGLAEGYLGLPElnAEKFVNNWFVDPSHW 657
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 428 A-------------------RLYRTGDYGS-LKNGSIMYEGRTDSQVKIRGHRVDLSEVEKNVAELPLVDKAIVLC---- 483
Cdd:TIGR03443 658 IdldkennkperefwlgprdRLYRTGDLGRyLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVrrdk 737
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 484 --------YHAGQVDQA-ILAFVKLRDDA----PMV------TEMQMEAR--LKDKLADYMTPQVVI-LEHVPLLVNGKV 541
Cdd:TIGR03443 738 deeptlvsYIVPQDKSDeLEEFKSEVDDEessdPVVkglikyRKLIKDIReyLKKKLPSYAIPTVIVpLKKLPLNPNGKV 817
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 542 DRQALL--KTYETANNNEGDSSIVLDFDYSQVPEDLkltaRDLFEtvgGVIGRSTrATLAPHSNFYELGGNSL---NSIF 616
Cdd:TIGR03443 818 DKPALPfpDTAQLAAVAKNRSASAADEEFTETEREI----RDLWL---ELLPNRP-ATISPDDSFFDLGGHSIlatRMIF 889
|
....*...
gi 126789033 617 TvtlLREK 624
Cdd:TIGR03443 890 E---LRKK 894
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
22-546 |
4.06e-37 |
|
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: 145.78 E-value: 4.06e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 22 LHRIFEEQQLRHADKVALIYQpsttGQGMapsqsSYRQMNERANRAARLLvaetHGRFLQPnsdGDFiVAVCMQPSEGLV 101
Cdd:cd05936 1 LADLLEEAARRFPDKTALIFM----GRKL-----TYRELDALAEAFAAGL----QNLGVQP---GDR-VALMLPNCPQFP 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 102 TTLLAIWKAGGAYLPIDPSFPANRIHHILLEAKPTLVIRDDDIDAGRFQGTPTLSTTELYAkslqlagsnllseemlrgg 181
Cdd:cd05936 64 IAYFGALKAGAVVVPLNPLYTPRELEHILNDSGAKALIVAVSFTDLLAAGAPLGERVALTP------------------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 182 nDHIAIVLYTSGSTGVPKGVRLPHESIL-NRLQ-WQWATFPYTANEavsVFKTAL----TFVDSIAeLWGPLMCGLAILV 255
Cdd:cd05936 125 -EDVAVLQYTSGTTGVPKGAMLTHRNLVaNALQiKAWLEDLLEGDD---VVLAALplfhVFGLTVA-LLLPLALGATIVL 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 256 VPKAvtkDPQRLVALLERYKIRRLVLVPTllrsllMYLKMEGGGAAQKL-LYNLQIWVCSGEPLSVSLASSFFDYFdeGV 334
Cdd:cd05936 200 IPRF---RPIGVLKEIRKHRVTIFPGVPT------MYIALLNAPEFKKRdFSSLRLCISGGAPLPVEVAERFEELT--GV 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 335 hRLYNFYGSTEVLGDVTYFACE-SKKQLSlydnvpIGIPLSNTVVYLLDADYRPVKNGEIGEIFASGLNLAAGYVNgrDP 413
Cdd:cd05936 269 -PIVEGYGLTETSPVVAVNPLDgPRKPGS------IGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWN--RP 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 414 ErflENPLAVEKKYarlYRTGDYGSL-KNGSIMYEGRTDSQVKIRGHRVDLSEVEKNVAELPLVDKAIVLcyhaGQVDQ- 491
Cdd:cd05936 340 E---ETAEAFVDGW---LRTGDIGYMdEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVV----GVPDPy 409
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 126789033 492 ---AILAFVKLRDDAPmVTEMQMEARLKDKLADYMTP-QVVILEHVPLLVNGKVDRQAL 546
Cdd:cd05936 410 sgeAVKAFVVLKEGAS-LTEEEIIAFCREQLAGYKVPrQVEFRDELPKSAVGKILRREL 467
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
56-549 |
1.32e-36 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 145.84 E-value: 1.32e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 56 SYRQMNERANRAARLLVAethgRFLQPnsdGDfIVAVCMQPSEGLVTTLLAIWKAGGAYLPIDPSFPANRIHHILLEAKP 135
Cdd:PRK07788 76 TYAELDEQSNALARGLLA----LGVRA---GD-GVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQLAEVAAREGV 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 136 TLVIRDDDIdAGRFQGTPT----LSTTELYAKSLQLAGSNLLSEEMLRGGND---------HIAIVLYTSGSTGVPKGVR 202
Cdd:PRK07788 148 KALVYDDEF-TDLLSALPPdlgrLRAWGGNPDDDEPSGSTDETLDDLIAGSStaplpkppkPGGIVILTSGTTGTPKGAP 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 203 LPHESILNRLQWQWATFPYTANEAVSVfkTAltfvdSIAELWGPLMCGLAILVVPKAVTK---DPQRLVALLERYKIRRL 279
Cdd:PRK07788 227 RPEPSPLAPLAGLLSRVPFRAGETTLL--PA-----PMFHATGWAHLTLAMALGSTVVLRrrfDPEATLEDIAKHKATAL 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 280 VLVPTLLRSLLmylKMEGGGAAQKLLYNLQIWVCSGEPLSVSLASSFFDYFDEgvhRLYNFYGSTEVlgdvTYFACESKK 359
Cdd:PRK07788 300 VVVPVMLSRIL---DLGPEVLAKYDTSSLKIIFVSGSALSPELATRALEAFGP---VLYNLYGSTEV----AFATIATPE 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 360 QLSLyDNVPIGIPLSNTVVYLLDADYRPVKNGEIGEIFASGLNLAAGYVNGRDPERFLEnplavekkyarLYRTGDYGSL 439
Cdd:PRK07788 370 DLAE-APGTVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGYTDGRDKQIIDG-----------LLSSGDVGYF 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 440 -KNGSIMYEGRTDSQVKIRGHRVDLSEVEKNVAELPLVDKAivlcyHAGQVD-----QAILAFVKLRDDAPmVTEMQMEA 513
Cdd:PRK07788 438 dEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEA-----AVIGVDdeefgQRLRAFVVKAPGAA-LDEDAIKD 511
|
490 500 510
....*....|....*....|....*....|....*..
gi 126789033 514 RLKDKLADYMTPQ-VVILEHVPLLVNGKVDRQALLKT 549
Cdd:PRK07788 512 YVRDNLARYKVPRdVVFLDELPRNPTGKVLKRELREM 548
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
33-546 |
1.96e-35 |
|
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: 141.89 E-value: 1.96e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 33 HADKVALIYQPSTTGqgmAPSQS-SYRQMNERANRAARLLVAETHGRflqpnsdGDfIVAVCMQPSEGLVTTLLAIWKAG 111
Cdd:cd17647 1 FPERTCVVETPSLNS---SKTRSfTYRDINEASNIVAHYLIKTGIKR-------GD-VVMIYSYRGVDLMVAVMGVLKAG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 112 GAYLPIDPSFPANRIHHILLEAKPT--LVIRDDDIDAGRfQGTPTLSttelyakslqlagsnllseemlrggndhiaivl 189
Cdd:cd17647 70 ATFSVIDPAYPPARQNIYLGVAKPRglIVIRAAGVVVGP-DSNPTLS--------------------------------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 190 YTSGSTGVPKGVRLPHESILNRLQWQWATFPYTANEAvsvfktaLTFVDSIA------ELWGPLMCGlAILVVPkavTKD 263
Cdd:cd17647 116 FTSGSEGIPKGVLGRHFSLAYYFPWMAKRFNLSENDK-------FTMLSGIAhdpiqrDMFTPLFLG-AQLLVP---TQD 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 264 ----PQRLVALLERYKIRRLVLVPTLLRSLLmylkmeGGGAAQ--KLLYNLQIwvcsGEPLS-------VSLASSFfdyf 330
Cdd:cd17647 185 digtPGRLAEWMAKYGATVTHLTPAMGQLLT------AQATTPfpKLHHAFFV----GDILTkrdclrlQTLAENV---- 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 331 degvhRLYNFYGSTEVLGDVTYFACESKKQ-----LSLYDNVPIGIPLSNtVVYLLDADYRPVKN---GEIGEIFASGLN 402
Cdd:cd17647 251 -----RIVNMYGTTETQRAVSYFEVPSRSSdptflKNLKDVMPAGRGMLN-VQLLVVNRNDRTQIcgiGEVGEIYVRAGG 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 403 LAAGYVNGRD--PERFLENPLAVEKKYA-------------------RLYRTGDYGS-LKNGSIMYEGRTDSQVKIRGHR 460
Cdd:cd17647 325 LAEGYRGLPElnKEKFVNNWFVEPDHWNyldkdnnepwrqfwlgprdRLYRTGDLGRyLPNGDCECCGRADDQVKIRGFR 404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 461 VDLSEVEKNVAELPLVDKAIVLCYHAGQVDQAILAFVKLRDDAPMVTEMQME--------------------------AR 514
Cdd:cd17647 405 IELGEIDTHISQHPLVRENITLVRRDKDEEPTLVSYIVPRFDKPDDESFAQEdvpkevstdpivkgligyrklikdirEF 484
|
570 580 590
....*....|....*....|....*....|...
gi 126789033 515 LKDKLADYMTPQVVI-LEHVPLLVNGKVDRQAL 546
Cdd:cd17647 485 LKKRLASYAIPSLIVvLDKLPLNPNGKVDKPKL 517
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
22-549 |
2.05e-34 |
|
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.
Pssm-ID: 211788 [Multi-domain] Cd Length: 517 Bit Score: 138.76 E-value: 2.05e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 22 LHRIFEEQQLRHADKVALIYQPSTTgqgmapsqsSYRQMNERANRAARLLvaetHGRFLQPNSDgdfiVAVCMQPSEGLV 101
Cdd:TIGR03098 2 LHHLLEDAAARLPDATALVHHDRTL---------TYAALSERVLALASGL----RGLGLARGER----VAIYLDKRLETV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 102 TTLLAIWKAGGAYLPIDPSFPANRIHHIL-------LEAKPTLVIRDDDIDAGRFQGTPTLSTTELYAKSLQLAGSNLLS 174
Cdd:TIGR03098 65 TAMFGAALAGGVFVPINPLLKAEQVAHILadcnvrlLVTSSERLDLLHPALPGCHDLRTLIIVGDPAHASEGHPGEEPAS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 175 -EEML---------RGGNDHIAIVLYTSGSTGVPKGVRLPH-------ESILNRLQWQWA---------TFPYTANEAVS 228
Cdd:TIGR03098 145 wPKLLalgdadpphPVIDSDMAAILYTSGSTGRPKGVVLSHrnlvagaQSVATYLENRPDdrllavlplSFDYGFNQLTT 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 229 VFKTALTFVdsiaeLWGPLMcglailvvpkavtkdPQRLVALLERYKIRRLVLVPTLLRSLLMYLKMEGGGAAQKLLYNl 308
Cdd:TIGR03098 225 AFYVGATVV-----LHDYLL---------------PRDVLKALEKHGITGLAAVPPLWAQLAQLDWPESAAPSLRYLTN- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 309 qiwvcSGEPLSVSLASSFFDYFDEGvhRLYNFYGSTEVLGDvTYFACEskkqlsLYDNVP--IGIPLSNTVVYLLDADYR 386
Cdd:TIGR03098 284 -----SGGAMPRATLSRLRSFLPNA--RLFLMYGLTEAFRS-TYLPPE------EVDRRPdsIGKAIPNAEVLVLREDGS 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 387 PVKNGEIGEIFASGLNLAAGYVNgrDPE----RFLENP----------LAVekkyarlyRTGDYGSL-KNGSIMYEGRTD 451
Cdd:TIGR03098 350 ECAPGEEGELVHRGALVAMGYWN--DPEktaeRFRPLPpfpgelhlpeLAV--------WSGDTVRRdEEGFLYFVGRRD 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 452 SQVKIRGHRVDLSEVEKNVAELPLVDKAIVLCYHAGQVDQAILAFVKLRDDAPMVTEmQMEARLKDKLADYMTPQVVILE 531
Cdd:TIGR03098 420 EMIKTSGYRVSPTEVEEVAYATGLVAEAVAFGVPDPTLGQAIVLVVTPPGGEELDRA-ALLAECRARLPNYMVPALIHVR 498
|
570
....*....|....*....
gi 126789033 532 HV-PLLVNGKVDRQALLKT 549
Cdd:TIGR03098 499 QAlPRNANGKIDRKALAKE 517
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
56-546 |
9.98e-34 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 136.81 E-value: 9.98e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 56 SYRQMNERANRAARLLVAETHGrflQPNsdgdfIVAVCMQPSEGLVTTLLAIWKAGGAYLPIDPSFPANRIHHILLEAKP 135
Cdd:PRK13382 70 TWRELDERSDALAAALQALPIG---EPR-----VVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPALAEVVTREGV 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 136 TLVIRDDDID-------AGRFQGTPTLSTTELYAKSLQLAGSNLLSEEMLRGGNDHIAIVLYTSGSTGVPKGVR------ 202
Cdd:PRK13382 142 DTVIYDEEFSatvdralADCPQATRIVAWTDEDHDLTVEVLIAAHAGQRPEPTGRKGRVILLTSGTTGTPKGARrsgpgg 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 203 -LPHESILNRLQWQwatfpytANEAVsvFKTALTFvdsiaELWGPLMCGLAILVVPKAVTK---DPQRLVALLERYKIRR 278
Cdd:PRK13382 222 iGTLKAILDRTPWR-------AEEPT--VIVAPMF-----HAWGFSQLVLAASLACTIVTRrrfDPEATLDLIDRHRATG 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 279 LVLVPTLLRSLlMYLKMEGggAAQKLLYNLQIWVCSGEPLSVSLASSFFDYFDEGvhrLYNFYGSTEVlgdvTYFACESK 358
Cdd:PRK13382 288 LAVVPVMFDRI-MDLPAEV--RNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGDV---IYNNYNATEA----GMIATATP 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 359 KQLSLYDNVPiGIPLSNTVVYLLDADYRPVKNGEIGEIFASGLNLAAGYVNGRDPErFLENPLAvekkyarlyrTGDYGS 438
Cdd:PRK13382 358 ADLRAAPDTA-GRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGYTSGSTKD-FHDGFMA----------SGDVGY 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 439 L-KNGSIMYEGRTDSQVKIRGHRVDLSEVEKNVAELPLVDKAIVLCYHAGQVDQAILAFVKLRDDAPmVTEMQMEARLKD 517
Cdd:PRK13382 426 LdENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPGAS-ATPETLKQHVRD 504
|
490 500 510
....*....|....*....|....*....|
gi 126789033 518 KLADYMTPQ-VVILEHVPLLVNGKVDRQAL 546
Cdd:PRK13382 505 NLANYKVPRdIVVLDELPRGATGKILRREL 534
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
56-541 |
1.16e-33 |
|
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: 135.80 E-value: 1.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 56 SYRQMNERANRAARLLVAEthgrFLQPnsdGDfIVAVCMQPSEGLVTTLLAIWKAGGAYLPIDPSFPANRIHHILLEAKP 135
Cdd:cd05911 12 TYAQLRTLSRRLAAGLRKL----GLKK---GD-VVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 136 TLVIRDDD-----IDAGRFQGTP----TLSTTELYAKSLQLAGSNLLSEEM------LRGGNDHIAIVLYTSGSTGVPKG 200
Cdd:cd05911 84 KVIFTDPDglekvKEAAKELGPKdkiiVLDDKPDGVLSIEDLLSPTLGEEDedlpppLKDGKDDTAAILYSSGTTGLPKG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 201 VRLPHESILNRLQWQWATFPYTANEAVSVFkTALTFvDSIAELWGPLMC---GLAILVVPKAvtkDPQRLVALLERYKIR 277
Cdd:cd05911 164 VCLSHRNLIANLSQVQTFLYGNDGSNDVIL-GFLPL-YHIYGLFTTLASllnGATVIIMPKF---DSELFLDLIEKYKIT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 278 RLVLVPTLLRSLLMYlkmeggGAAQKL-LYNLQIWVCSGEPLSVSLASSFFDYFDEGvhRLYNFYGSTEVLGDVTYface 356
Cdd:cd05911 239 FLYLVPPIAAALAKS------PLLDKYdLSSLRVILSGGAPLSKELQELLAKRFPNA--TIKQGYGMTETGGILTV---- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 357 skkqLSLYDNVP--IGIPLSNTVVYLLDADYRPVKN-GEIGEIFASGLNLAAGYVNG-------RDPERFLenplavekk 426
Cdd:cd05911 307 ----NPDGDDKPgsVGRLLPNVEAKIVDDDGKDSLGpNEPGEICVRGPQVMKGYYNNpeatketFDEDGWL--------- 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 427 yarlyRTGDYGSL-KNGSIMYEGRTDSQVKIRGHRVDLSEVEKNVAELPLVDKAIVlcyhAGQVD----QAILAFVKLRD 501
Cdd:cd05911 374 -----HTGDIGYFdEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAV----IGIPDevsgELPRAYVVRKP 444
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 126789033 502 DaPMVTEMQMEARLKDKLADY--MTPQVVILEHVPLLVNGKV 541
Cdd:cd05911 445 G-EKLTEKEVKDYVAKKVASYkqLRGGVVFVDEIPKSASGKI 485
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
22-546 |
2.19e-31 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 129.54 E-value: 2.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 22 LHRIFEEQQLRHADKVALIYqpstTGQGMapsqsSYRQMNERANRAARLLVAEthGrfLQPnsdGDfIVAVCMQPSEGLV 101
Cdd:PRK06187 8 IGRILRHGARKHPDKEAVYF----DGRRT-----TYAELDERVNRLANALRAL--G--VKK---GD-RVAVFDWNSHEYL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 102 TTLLAIWKAGGAYLPIDPSFPANRIHHILLEAKPTLVIRDDDID------AGRFQGTPTLSTTELYAKSlQLAGSNLLSE 175
Cdd:PRK06187 71 EAYFAVPKIGAVLHPINIRLKPEEIAYILNDAEDRVVLVDSEFVpllaaiLPQLPTVRTVIVEGDGPAA-PLAPEVGEYE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 176 EMLRGGNDH----------IAIVLYTSGSTGVPKGVRLPHESI-LNRLQWQwATFPYTANE----AVSVFKTALtfvdsi 240
Cdd:PRK06187 150 ELLAAASDTfdfpdidendAAAMLYTSGTTGHPKGVVLSHRNLfLHSLAVC-AWLKLSRDDvylvIVPMFHVHA------ 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 241 aelWG----PLMCGLAIlVVPKAVtkDPQRLVALLERYKIRRLVLVPTLLRSLLMYLKmegggAAQKLLYNLQIWVCSGE 316
Cdd:PRK06187 223 ---WGlpylALMAGAKQ-VIPRRF--DPENLLDLIETERVTFFFAVPTIWQMLLKAPR-----AYFVDFSSLRLVIYGGA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 317 PLSVSLASSFFDYFDEGVHRLYnfyGSTEVLGDVTY------FACESKKQLSlydnvpIGIPLSNTVVYLLDADYR--PV 388
Cdd:PRK06187 292 ALPPALLREFKEKFGIDLVQGY---GMTETSPVVSVlppedqLPGQWTKRRS------AGRPLPGVEARIVDDDGDelPP 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 389 KNGEIGEIFASGLNLAAGYVNgrDPErflenplAVEKK-YARLYRTGDYGSL-KNGSIMYEGRTDSQVKIRGHRVDLSEV 466
Cdd:PRK06187 363 DGGEVGEIIVRGPWLMQGYWN--RPE-------ATAETiDGGWLHTGDVGYIdEDGYLYITDRIKDVIISGGENIYPREL 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 467 EKNVAELPLVDKAIVLcyhaGQVD----QAILAFVKLRDDAPmVTEMQMEARLKDKLADYMTP-QVVILEHVPLLVNGKV 541
Cdd:PRK06187 434 EDALYGHPAVAEVAVI----GVPDekwgERPVAVVVLKPGAT-LDAKELRAFLRGRLAKFKLPkRIAFVDELPRTSVGKI 508
|
....*
gi 126789033 542 DRQAL 546
Cdd:PRK06187 509 LKRVL 513
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
62-547 |
2.47e-31 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 128.33 E-value: 2.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 62 ERANRAARLLVAetHGrflqpNSDGDFIVAVCMQPSEgLVTTLLAIWKAGGA----YLPIDPSFPANRIHHILLEAKPTL 137
Cdd:cd05922 1 LGVSAAASALLE--AG-----GVRGERVVLILPNRFT-YIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 138 VIrdddIDAG-----RFQGTPTLSTTELY-AKSLQLAGSNLlseEMLRGGNDHIAIVLYTSGSTGVPKGVRLPHESILNR 211
Cdd:cd05922 73 VL----ADAGaadrlRDALPASPDPGTVLdADGIRAARASA---PAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLAN 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 212 LQWQWATFPYTANEAVSVfKTALTFVDSIAELWGPLMCGLAILVVPKAVTkdPQRLVALLERYKIRRLVLVPTLLrSLLM 291
Cdd:cd05922 146 ARSIAEYLGITADDRALT-VLPLSYDYGLSVLNTHLLRGATLVLTNDGVL--DDAFWEDLREHGATGLAGVPSTY-AMLT 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 292 YLKMEGGGAAQkLLYNLQiwvcSGEPLSVSLASSFFDYFDEGvhRLYNFYGSTEVLGDVTYFACEskkqlsLYDNVP--I 369
Cdd:cd05922 222 RLGFDPAKLPS-LRYLTQ----AGGRLPQETIARLRELLPGA--QVYVMYGQTEATRRMTYLPPE------RILEKPgsI 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 370 GIPLSNTVVYLLDADYRPVKNGEIGEIFASGLNLAAGYVNgrDPerflENPLAVEKKYARLYrTGDYGSL-KNGSIMYEG 448
Cdd:cd05922 289 GLAIPGGEFEILDDDGTPTPPGEPGEIVHRGPNVMKGYWN--DP----PYRRKEGRGGGVLH-TGDLARRdEDGFLFIVG 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 449 RTDSQVKIRGHRVDLSEVEKNVAELPLVDKAivLCYHAGQVDQAILAFVKLRDDAPMVTEMQMEARlkDKLADYMTP-QV 527
Cdd:cd05922 362 RRDRMIKLFGNRISPTEIEAAARSIGLIIEA--AAVGLPDPLGEKLALFVTAPDKIDPKDVLRSLA--ERLPPYKVPaTV 437
|
490 500
....*....|....*....|
gi 126789033 528 VILEHVPLLVNGKVDRQALL 547
Cdd:cd05922 438 RVVDELPLTASGKVDYAALR 457
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
34-547 |
6.51e-31 |
|
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: 127.87 E-value: 6.51e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 34 ADKVALIYQPSTTgqgmapsqsSYRQMNERANRAARLLVaethGRFLQPNSDgdfiVAVCMQPSEGLVTTLLAIWKAGGA 113
Cdd:cd05959 18 GDKTAFIDDAGSL---------TYAELEAEARRVAGALR----ALGVKREER----VLLIMLDTVDFPTAFLGAIRAGIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 114 YLPIDPSFPANRIHHILLEAKPTLVIRDDDIdAGRFQGTPTLSTTELY-----------AKSLQLAgsNLLSEEMLRGGN 182
Cdd:cd05959 81 PVPVNTLLTPDDYAYYLEDSRARVVVVSGEL-APVLAAALTKSEHTLVvlivsggagpeAGALLLA--ELVAAEAEQLKP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 183 -----DHIAIVLYTSGSTGVPKGVRLPHESIlnrlqwQWATFPYTAN-----EAVSVFKTA-----------LTFvdsia 241
Cdd:cd05959 158 aathaDDPAFWLYSSGSTGRPKGVVHLHADI------YWTAELYARNvlgirEDDVCFSAAklffayglgnsLTF----- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 242 elwgPLMCGLAILVVPKAVTkdPQRLVALLERYKIRRLVLVPTLLRSLLmylkmEGGGAAQKLLYNLQIWVCSGEPLSVS 321
Cdd:cd05959 227 ----PLSVGATTVLMPERPT--PAAVFKRIRRYRPTVFFGVPTLYAAML-----AAPNLPSRDLSSLRLCVSAGEALPAE 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 322 LASSFFDYFdegVHRLYNFYGSTEVL--------GDVTYFACeskkqlslydnvpiGIPLSNTVVYLLDADYRPVKNGEI 393
Cdd:cd05959 296 VGERWKARF---GLDILDGIGSTEMLhiflsnrpGRVRYGTT--------------GKPVPGYEVELRDEDGGDVADGEP 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 394 GEIFASGLNLAAGYVNGRDPERflenplAVEKKYarLYRTGD-YGSLKNGSIMYEGRTDSQVKIRGHRVDLSEVEKNVAE 472
Cdd:cd05959 359 GELYVRGPSSATMYWNNRDKTR------DTFQGE--WTRTGDkYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQ 430
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 126789033 473 LPLVDKAIVLCYHAGQVDQAILAFVKLRD--DAPMVTEMQMEARLKDKLADYMTP-QVVILEHVPLLVNGKVDRQALL 547
Cdd:cd05959 431 HPAVLEAAVVGVEDEDGLTKPKAFVVLRPgyEDSEALEEELKEFVKDRLAPYKYPrWIVFVDELPKTATGKIQRFKLR 508
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
56-546 |
3.78e-30 |
|
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: 124.50 E-value: 3.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 56 SYRQMNERANRAARLLvaETHGRflqpnSDGDfIVAVCMQPSEGLVTTLLAIWKAGGAYLPIDPSFPANRIHHILLEAKP 135
Cdd:cd05919 12 TYGQLHDGANRLGSAL--RNLGV-----SSGD-RVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 136 TLVIRDDDidagrfqgtptlsttelyakslqlagsnllseemlrggndHIAIVLYTSGSTGVPKGVRLPHESILNRLQwQ 215
Cdd:cd05919 84 RLVVTSAD----------------------------------------DIAYLLYSSGTTGPPKGVMHAHRDPLLFAD-A 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 216 WATFPYTANEAVSVFKTA-LTFVDSIA-ELWGPLMCGLAILVVPKAVTkdPQRLVALLERYKIRRLVLVPTLLRSLLmyl 293
Cdd:cd05919 123 MAREALGLTPGDRVFSSAkMFFGYGLGnSLWFPLAVGASAVLNPGWPT--AERVLATLARFRPTVLYGVPTFYANLL--- 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 294 kmEGGGAAQKLLYNLQIWVCSGEPLSVSLASSFFDYFD----EGVhrlynfyGSTEVL--------GDVTYFACeskkql 361
Cdd:cd05919 198 --DSCAGSPDALRSLRLCVSAGEALPRGLGERWMEHFGgpilDGI-------GATEVGhiflsnrpGAWRLGST------ 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 362 slydnvpiGIPLSNTVVYLLDADYRPVKNGEIGEIFASGLNLAAGYVNGRdperflenplavEKKYARL----YRTGD-Y 436
Cdd:cd05919 263 --------GRPVPGYEIRLVDEEGHTIPPGEEGDLLVRGPSAAVGYWNNP------------EKSRATFnggwYRTGDkF 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 437 GSLKNGSIMYEGRTDSQVKIRGHRVDLSEVEKNVAELPLVDKAIVLCYHAGQVDQAILAFVKLRDD-APMVTEMQ-MEAR 514
Cdd:cd05919 323 CRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPaAPQESLARdIHRH 402
|
490 500 510
....*....|....*....|....*....|...
gi 126789033 515 LKDKLADYMTP-QVVILEHVPLLVNGKVDRQAL 546
Cdd:cd05919 403 LLERLSAHKVPrRIAFVDELPRTATGKLQRFKL 435
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
56-548 |
1.10e-29 |
|
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: 123.17 E-value: 1.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 56 SYRQMNERANRAARLLVAETHGRflqpnsDGDFIVAVCmQPSEGLVTTLLAIWKAGGAYLPIDPSFPANRIHHILLEAKP 135
Cdd:cd05941 13 TYADLVARAARLANRLLALGKDL------RGDRVAFLA-PPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDSEP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 136 TLVIRDddidagrfqgtptlsttelyakslqlagsnllseemlrggndhiAIVLYTSGSTGVPKGVRLPHESILNRLQ-- 213
Cdd:cd05941 86 SLVLDP--------------------------------------------ALILYTSGTTGRPKGVVLTHANLAANVRal 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 214 ---WQWatfpyTAN----EAVSVFKTALTFVdsiaELWGPLMCGLAILVVPKAvtkDPQRLVALLERYKIRRLVLVPTLL 286
Cdd:cd05941 122 vdaWRW-----TEDdvllHVLPLHHVHGLVN----ALLCPLFAGASVEFLPKF---DPKEVAISRLMPSITVFMGVPTIY 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 287 RSLLMYLK---MEGGGAAQKLLYNLQIWVCSGEPLSVSLassfFDYFDE-GVHRLYNFYGSTEVLgdvtyfaceskkqLS 362
Cdd:cd05941 190 TRLLQYYEahfTDPQFARAAAAERLRLMVSGSAALPVPT----LEEWEAiTGHTLLERYGMTEIG-------------MA 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 363 L---YDNVPI----GIPLSNTVVYLLDAD-YRPVKNGEIGEIFASGLNLAAGYVNgrdperfleNPLAVEKKYA--RLYR 432
Cdd:cd05941 253 LsnpLDGERRpgtvGMPLPGVQARIVDEEtGEPLPRGEVGEIQVRGPSVFKEYWN---------KPEATKEEFTddGWFK 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 433 TGDYGSLK-NGSIMYEGRT-DSQVKIRGHRVDLSEVEKNVAELPLVDKAIVLcyhaGQVD----QAILAFVKLRDDAPMV 506
Cdd:cd05941 324 TGDLGVVDeDGYYWILGRSsVDIIKSGGYKVSALEIERVLLAHPGVSECAVI----GVPDpdwgERVVAVVVLRAGAAAL 399
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 126789033 507 TEMQMEARLKDKLADYMTPQVVIL-EHVPLLVNGKVDRQALLK 548
Cdd:cd05941 400 SLEELKEWAKQRLAPYKRPRRLILvDELPRNAMGKVNKKELRK 442
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
56-548 |
1.04e-28 |
|
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: 120.13 E-value: 1.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 56 SYRQMNERANRAARLLVAETHGRflqpnsdGDfIVAVCMQPSEGLVTTLLAIWKAGGAYLPIDPSFPANRIHHILLEAKP 135
Cdd:cd05972 2 SFRELKRESAKAANVLAKLGLRK-------GD-RVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 136 TLVIRDDDidagrfqgtptlsttelyakslqlagsnllseemlrggndHIAIVLYTSGSTGVPKGVRLPHESILNRL--- 212
Cdd:cd05972 74 KAIVTDAE----------------------------------------DPALIYFTSGTTGLPKGVLHTHSYPLGHIpta 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 213 ----------------QWQWATFPYTAneavsvfktaltfvdsiaeLWGPLMCGLAIlVVPKAVTKDPQRLVALLERYKI 276
Cdd:cd05972 114 aywlglrpddihwniaDPGWAKGAWSS-------------------FFGPWLLGATV-FVYEGPRFDAERILELLERYGV 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 277 RRLVLVPTLLRSLlmylkMEGGGAAQKLLyNLQIWVCSGEPLSVSLASSFFDYFDEGVHrlyNFYGSTEVLGDVTYFACE 356
Cdd:cd05972 174 TSFCGPPTAYRML-----IKQDLSSYKFS-HLRLVVSAGEPLNPEVIEWWRAATGLPIR---DGYGQTETGLTVGNFPDM 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 357 SKKQLSlydnvpIGIPLSNTVVYLLDADYRPVKNGEIGEIfASGLN---LAAGYVNgrdperfleNPLAVEKKYAR-LYR 432
Cdd:cd05972 245 PVKPGS------MGRPTPGYDVAIIDDDGRELPPGEEGDI-AIKLPppgLFLGYVG---------DPEKTEASIRGdYYL 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 433 TGDYGSL-KNGSIMYEGRTDSQVKIRGHRVDLSEVEKNVAELPLVDKAIVLcyhaGQVD----QAILAFVKLRDDAPMVT 507
Cdd:cd05972 309 TGDRAYRdEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVV----GSPDpvrgEVVKAFVVLTSGYEPSE 384
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 126789033 508 EMQMEARL--KDKLADYMTPQVV-ILEHVPLLVNGKVDRQALLK 548
Cdd:cd05972 385 ELAEELQGhvKKVLAPYKYPREIeFVEELPKTISGKIRRVELRD 428
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
18-546 |
5.09e-28 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 119.24 E-value: 5.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 18 VPRALHRIFEeqqlRHADKVALIYQPSTTgqgmapsqsSYRQMNERANRAARLLVAE-----THGRFLQPNSdGDFIVAv 92
Cdd:PRK07656 7 LPELLARAAR----RFGDKEAYVFGDQRL---------TYAELNARVRRAAAALAALgigkgDRVAIWAPNS-PHWVIA- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 93 cmqpseglvttLLAIWKAGGAYLPIDPSFPANRIHHILLEAKPTLVIRDDD---IDAGRFQGTPTLSTTEL--YAKSLQL 167
Cdd:PRK07656 72 -----------ALGALKAGAVVVPLNTRYTADEAAYILARGDAKALFVLGLflgVDYSATTRLPALEHVVIceTEEDDPH 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 168 AGSNLLSEEMLRGGN----------DHIAIVLYTSGSTGVPKGVRLPHESILnRLQWQWA-------------------T 218
Cdd:PRK07656 141 TEKMKTFTDFLAAGDpaerapevdpDDVADILFTSGTTGRPKGAMLTHRQLL-SNAADWAeylgltegdrylaanpffhV 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 219 FPYTANeavsvfktaltfvdsiaeLWGPLMCGLAILVVPKAvtkDPQRLVALLERYKIRRLVLVPTLLRSLLMYlkmEGG 298
Cdd:PRK07656 220 FGYKAG------------------VNAPLMRGATILPLPVF---DPDEVFRLIETERITVLPGPPTMYNSLLQH---PDR 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 299 GAAQklLYNLQIWVCSGEPLSVSLASSFFDYFdeGVHRLYNFYGSTEVLGdvtyFACESKKQLSlYDNVP--IGIPLSNT 376
Cdd:PRK07656 276 SAED--LSSLRLAVTGAASMPVALLERFESEL--GVDIVLTGYGLSEASG----VTTFNRLDDD-RKTVAgtIGTAIAGV 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 377 VVYLLDADYRPVKNGEIGEIFASGLNLAAGYVNgrDPErflENPLAVeKKYARLYrTGDYGSL-KNGSIMYEGRTDSQVK 455
Cdd:PRK07656 347 ENKIVNELGEEVPVGEVGELLVRGPNVMKGYYD--DPE---ATAAAI-DADGWLH-TGDLGRLdEEGYLYIVDRKKDMFI 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 456 IRGHRVDLSEVEKNVAELPLVDKAIVLcyhaGQVD----QAILAFVKLRDDAPmVTEMQMEARLKDKLADYMTPQ-VVIL 530
Cdd:PRK07656 420 VGGFNVYPAEVEEVLYEHPAVAEAAVI----GVPDerlgEVGKAYVVLKPGAE-LTEEELIAYCREHLAKYKVPRsIEFL 494
|
570
....*....|....*.
gi 126789033 531 EHVPLLVNGKVDRQAL 546
Cdd:PRK07656 495 DELPKNATGKVLKRAL 510
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
51-546 |
3.59e-25 |
|
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: 109.44 E-value: 3.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 51 APSQSSYRQMNERANRAARLLvaetHGRFLQPnsdGDfIVAVCMQPSEGLVTTLLAIWKAGGAYLPIDPSFPANRIHHIL 130
Cdd:cd05971 3 TPEKVTFKELKTASNRFANVL----KEIGLEK---GD-RVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 131 LEAKPTLVIRDddidagrfqgtptlsttelyakslqlagsnllseemlrgGNDHIAIVLYTSGSTGVPKGVRLPHESILN 210
Cdd:cd05971 75 SNSGASALVTD---------------------------------------GSDDPALIIYTSGTTGPPKGALHAHRVLLG 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 211 RL---QWQWATFPYTANeavsVFktaltfvdsiaelWGPL----MCGLAILVVP-----------KAVTKDPQRLVALLE 272
Cdd:cd05971 116 HLpgvQFPFNLFPRDGD----LY-------------WTPAdwawIGGLLDVLLPslyfgvpvlahRMTKFDPKAALDLMS 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 273 RYKIRRLVLVPTLLRslLMylKMEGGGAAQKLLyNLQIWVCSGEPLSVSLASSFFDYFDEGVHRlynFYGSTE---VLGD 349
Cdd:cd05971 179 RYGVTTAFLPPTALK--MM--RQQGEQLKHAQV-KLRAIATGGESLGEELLGWAREQFGVEVNE---FYGQTEcnlVIGN 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 350 vtyfaCESkkqLSLYDNVPIGIPLSNTVVYLLDADYRPVKNGEIGEIfasGLNLAagyvngrDPERFLE---NPLAVEKK 426
Cdd:cd05971 251 -----CSA---LFPIKPGSMGKPIPGHRVAIVDDNGTPLPPGEVGEI---AVELP-------DPVAFLGywnNPSATEKK 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 427 YARLY-RTGDYGSL-KNGSIMYEGRTDSQVKIRGHRVDLSEVEKNVAELPLVDKAIVLcyhaGQVD----QAILAFVKLR 500
Cdd:cd05971 313 MAGDWlLTGDLGRKdSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVV----GIPDpirgEIVKAFVVLN 388
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 126789033 501 ----DDAPMVTEMQmeARLKDKLADYMTPQVVI-LEHVPLLVNGKVDRQAL 546
Cdd:cd05971 389 pgetPSDALAREIQ--ELVKTRLAAHEYPREIEfVNELPRTATGKIRRREL 437
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
34-548 |
2.64e-24 |
|
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: 107.78 E-value: 2.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 34 ADKVALIyqpsTTGQGMapsQSSYRQMNERANRAARLLVAETHGRflqpnsdGDfIVAVCMQPSEGLVTTLLAIWKAGGA 113
Cdd:cd05926 1 PDAPALV----VPGSTP---ALTYADLAELVDDLARQLAALGIKK-------GD-RVAIALPNGLEFVVAFLAAARAGAV 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 114 YLPIDPSFPANRIHHILLEAKPTLVIRDDDID--AGRFQGTPTLSTTELY--AKSLQLAGSN----------LLSEEMLR 179
Cdd:cd05926 66 VAPLNPAYKKAEFEFYLADLGSKLVLTPKGELgpASRAASKLGLAILELAldVGVLIRAPSAeslsnlladkKNAKSEGV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 180 GGNDHIAIVLYTSGSTGVPKGVRLPHESILNrlqwqwatfpyTANEAVSVFKtaLTFVDS-------------IAELWGP 246
Cdd:cd05926 146 PLPDDLALILHTSGTTGRPKGVPLTHRNLAA-----------SATNITNTYK--LTPDDRtlvvmplfhvhglVASLLST 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 247 LMCGLAILVVPKAvtkDPQRLVALLERYKIRRLVLVPTLLRSLLMYLKMEGGGAAQKLLYnlqIWVCSGePLSVSLASSF 326
Cdd:cd05926 213 LAAGGSVVLPPRF---SASTFWPDVRDYNATWYTAVPTIHQILLNRPEPNPESPPPKLRF---IRSCSA-SLPPAVLEAL 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 327 FDYFDEGVhrlYNFYGSTEVLGDVTY--FACESKKQLSlydnvpIGIPlSNTVVYLLDADYRPVKNGEIGEIFASGLNLA 404
Cdd:cd05926 286 EATFGAPV---LEAYGMTEAAHQMTSnpLPPGPRKPGS------VGKP-VGVEVRILDEDGEILPPGVVGEICLRGPNVT 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 405 AGYVNgrDPERFLENPLAVekkyaRLYRTGDYGSLK-NGSIMYEGRTDSQVKIRGHRVDLSEVEKNVAELPLVDKAIVL- 482
Cdd:cd05926 356 RGYLN--NPEANAEAAFKD-----GWFRTGDLGYLDaDGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFg 428
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 126789033 483 CYHAgQVDQAILAFVKLRDDAPMvTEMQMEARLKDKLADYMTP-QVVILEHVPLLVNGKVDRQALLK 548
Cdd:cd05926 429 VPDE-KYGEEVAAAVVLREGASV-TEEELRAFCRKHLAAFKVPkKVYFVDELPKTATGKIQRRKVAE 493
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
53-546 |
4.25e-24 |
|
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: 106.22 E-value: 4.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 53 SQSSYRQMNERANRAARLLVAethgRFLQPnsdGDFiVAVCMQPSEGLVTTLLAIWKAGGAYLPIDPSFPANRIHHILLE 132
Cdd:cd05934 2 RRWTYAELLRESARIAAALAA----LGIRP---GDR-VALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 133 AKPTLVIRDddidagrfqgtptlsttelyakslqlagsnllseemlrggndhIAIVLYTSGSTGVPKGVRLPHESILNRL 212
Cdd:cd05934 74 SGAQLVVVD-------------------------------------------PASILYTSGTTGPPKGVVITHANLTFAG 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 213 QWQWATFPYTANEavsVFKTALTFVDSIAELWG---PLMCGLAILVVPKAvtkDPQRLVALLERYKIRRLVLVPTLLRSL 289
Cdd:cd05934 111 YYSARRFGLGEDD---VYLTVLPLFHINAQAVSvlaALSVGATLVLLPRF---SASRFWSDVRRYGATVTNYLGAMLSYL 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 290 LMYLKMEGGGAAQkllynlqIWVCSGEPLSVSLASSFFDYFdeGVhRLYNFYGSTE----VLGDVTYfaceskkqlslyD 365
Cdd:cd05934 185 LAQPPSPDDRAHR-------LRAAYGAPNPPELHEEFEERF--GV-RLLEGYGMTEtivgVIGPRDE------------P 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 366 NVP--IGIPLSNTVVYLLDADYRPVKNGEIGEIF---ASGLNLAAGYVNgrdperfleNPLAVEKKYARL-YRTGDYGSL 439
Cdd:cd05934 243 RRPgsIGRPAPGYEVRIVDDDGQELPAGEPGELVirgLRGWGFFKGYYN---------MPEATAEAMRNGwFHTGDLGYR 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 440 -KNGSIMYEGRTDSQVKIRGHRVDLSEVEKNVAELPLVDKAIVLCYHAGQVDQAILAFVKLRDDAPmVTEMQMEARLKDK 518
Cdd:cd05934 314 dADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGET-LDPEELFAFCEGQ 392
|
490 500
....*....|....*....|....*....
gi 126789033 519 LADYMTPQVV-ILEHVPLLVNGKVDRQAL 546
Cdd:cd05934 393 LAYFKVPRYIrFVDDLPKTPTEKVAKAQL 421
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
35-541 |
4.26e-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: 108.05 E-value: 4.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 35 DKVALIYQpstTGQGMAPSQSSYRQMNERANRAARLLVAethgrflQPNSDGDfIVAVCMQPSEGLVTTLLAIWKAGGAY 114
Cdd:cd17634 68 DRTAIIYE---GDDTSQSRTISYRELHREVCRFAGTLLD-------LGVKKGD-RVAIYMPMIPEAAVAMLACARIGAVH 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 115 LPIDPSFPANRIHHILLEAKPTLVIRDDD-IDAGRfqgtpTLSTTELYAKSLQLAGSNLLSEEMLR---------GGND- 183
Cdd:cd17634 137 SVIFGGFAPEAVAGRIIDSSSRLLITADGgVRAGR-----SVPLKKNVDDALNPNVTSVEHVIVLKrtgsdidwqEGRDl 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 184 ----HIA-----------------IVLYTSGSTGVPKGVRLPHESILNRLQWQWA-TFPYTANEAVSVFKTALTFVDSIA 241
Cdd:cd17634 212 wwrdLIAkaspehqpeamnaedplFILYTSGTTGKPKGVLHTTGGYLVYAATTMKyVFDYGPGDIYWCTADVGWVTGHSY 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 242 ELWGPLMCGLAILVVP-KAVTKDPQRLVALLERYKIRRLVLVPTLLRSllmyLKMEGGGAAQKL-LYNLQIWVCSGEPLS 319
Cdd:cd17634 292 LLYGPLACGATTLLYEgVPNWPTPARMWQVVDKHGVNILYTAPTAIRA----LMAAGDDAIEGTdRSSLRILGSVGEPIN 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 320 VSLASSFFDYFDEGVHRLYNFYGSTEVLGdvtyfACESkkqlslydNVPIGIPL---SNTV------VYLLDADYRPVKN 390
Cdd:cd17634 368 PEAYEWYWKKIGKEKCPVVDTWWQTETGG-----FMIT--------PLPGAIELkagSATRpvfgvqPAVVDNEGHPQPG 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 391 GEIGEIfASGLNLAAGYVNG-RDPERFLENPLAVEKKYarlYRTGDYGSL-KNGSIMYEGRTDSQVKIRGHRVDLSEVEK 468
Cdd:cd17634 435 GTEGNL-VITDPWPGQTRTLfGDHERFEQTYFSTFKGM---YFSGDGARRdEDGYYWITGRSDDVINVAGHRLGTAEIES 510
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 126789033 469 NVAELPLVDKAIVLCYHAGQVDQAILAFVKLR---DDAPMVTEmQMEARLKDKLADYMTPQVV-ILEHVPLLVNGKV 541
Cdd:cd17634 511 VLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNhgvEPSPELYA-ELRNWVRKEIGPLATPDVVhWVDSLPKTRSGKI 586
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
185-546 |
4.44e-24 |
|
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: 103.95 E-value: 4.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 185 IAIVLYTSGSTGVPKGVRLPHESILNRLQWQWATFPYTANEaVSVFKTALTFVDSIAELWGPLMCGlAILVVPkavtkDP 264
Cdd:cd17630 2 LATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGD-SWLLSLPLYHVGGLAILVRSLLAG-AELVLL-----ER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 265 QRLVAL-LERYKIRRLVLVPTLLRSLLMYLkmeGGGAAQKLLYNLQIwvcSGEPLSVSLASSFFDYfdeGVhRLYNFYGS 343
Cdd:cd17630 75 NQALAEdLAPPGVTHVSLVPTQLQRLLDSG---QGPAALKSLRAVLL---GGAPIPPELLERAADR---GI-PLYTTYGM 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 344 TEVLGDVTyfacesKKQLSLYDNVPIGIPLsntvvylldaDYRPVKNGEIGEIFASGLNLAAGYVNGRDPERFLENPlav 423
Cdd:cd17630 145 TETASQVA------TKRPDGFGRGGVGVLL----------PGRELRIVEDGEIWVGGASLAMGYLRGQLVPEFNEDG--- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 424 ekkyarLYRTGDYGSL-KNGSIMYEGRTDSQVKIRGHRVDLSEVEKNVAELPLVDKAIVLcyhaGQVD----QAILAFVK 498
Cdd:cd17630 206 ------WFTTKDLGELhADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVV----GVPDeelgQRPVAVIV 275
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 126789033 499 LRDDAPmvtEMQMEARLKDKLADYMTP-QVVILEHVPLLVNGKVDRQAL 546
Cdd:cd17630 276 GRGPAD---PAELRAWLKDKLARFKLPkRIYPVPELPRTGGGKVDRRAL 321
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
90-546 |
1.29e-23 |
|
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.
Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 104.87 E-value: 1.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 90 VAVCMQPSEGLVTTLLAIWKAGGAYLPIDPSFPANRIHHILLEAKPTLVIrdddidagrfqgtptlsttelyakslqlAG 169
Cdd:cd05935 29 VGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAV----------------------------VG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 170 SNLlseemlrggnDHIAIVLYTSGSTGVPKGVRLPHESILnrlqwqwatfpytANEAVSVFKTALTFVDSI--------- 240
Cdd:cd05935 81 SEL----------DDLALIPYTSGTTGLPKGCMHTHFSAA-------------ANALQSAVWTGLTPSDVIlaclplfhv 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 241 AELWGPLMcgLAILVVPKAVTK---DPQRLVALLERYKIRRLVLVPTLLRSLL----------MYLKMEGGGAAqkllyn 307
Cdd:cd05935 138 TGFVGSLN--TAVYVGGTYVLMarwDRETALELIEKYKVTFWTNIPTMLVDLLatpefktrdlSSLKVLTGGGA------ 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 308 lqiwvcsgePLSVSLASSFFD----YFDEGvhrlynfYGSTEVLGDVTYFACESKKQLSLydnvpiGIPLSNTVVYLLDA 383
Cdd:cd05935 210 ---------PMPPAVAEKLLKltglRFVEG-------YGLTETMSQTHTNPPLRPKLQCL------GIP*FGVDARVIDI 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 384 -DYRPVKNGEIGEIFASGLNLAAGYVNgrdpeRFLENPLA-VEKKYARLYRTGDYGSL-KNGSIMYEGRTDSQVKIRGHR 460
Cdd:cd05935 268 eTGRELPPNEVGEIVVRGPQIFKGYWN-----RPEETEESfIEIKGRRFFRTGDLGYMdEEGYFFFVDRVKRMINVSGFK 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 461 VDLSEVEKNVAELPLVDKAIVLCYHAGQVDQAILAFVKLRDDAPM-VTEMQMEARLKDKLADYMTPQVVIL-EHVPLLVN 538
Cdd:cd05935 343 VWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYRGkVTEEDIIEWAREQMAAYKYPREVEFvDELPRSAS 422
|
....*...
gi 126789033 539 GKVDRQAL 546
Cdd:cd05935 423 GKILWRLL 430
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
56-548 |
1.57e-23 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 104.52 E-value: 1.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 56 SYRQMNERANRAARLLVAetHGrfLQPnsdGDfIVAVCMQPSEGLVTTLLAIWKAGGAYLPIDPSFPANRIHHILLEAKP 135
Cdd:cd05973 2 TFGELRALSARFANALQE--LG--VGP---GD-VVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 136 TLVIRDDD----IDAGRFqgtptlsttelyakslqlagsnllseemlrggndhiaIVLYTSGSTGVPKGVRLPHESIlnr 211
Cdd:cd05973 74 RLVVTDAAnrhkLDSDPF-------------------------------------VMMFTSGTTGLPKGVPVPLRAL--- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 212 lqwqwATFPYTANEAVSVfKTALTFVDSIAELW---------GPLMCGLAILVVPKAVTkdPQRLVALLERYKIRRLVLV 282
Cdd:cd05973 114 -----AAFGAYLRDAVDL-RPEDSFWNAADPGWayglyyaitGPLALGHPTILLEGGFS--VESTWRVIERLGVTNLAGS 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 283 PTLLRSLLMylkmEGGGAAQKLLYNLQIWVCSGEPLSVSLASSFFDYFDEGVHrlyNFYGSTEvLGDVTyfacesKKQLS 362
Cdd:cd05973 186 PTAYRLLMA----AGAEVPARPKGRLRRVSSAGEPLTPEVIRWFDAALGVPIH---DHYGQTE-LGMVL------ANHHA 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 363 LYDNV---PIGIPLSNTVVYLLDADYRPVKNGEIG----EIFASGLNLAAGYVNGRDPerflenplAVEKKYarlYRTGD 435
Cdd:cd05973 252 LEHPVhagSAGRAMPGWRVAVLDDDGDELGPGEPGrlaiDIANSPLMWFRGYQLPDTP--------AIDGGY---YLTGD 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 436 YGSLK-NGSIMYEGRTDSQVKIRGHRVDLSEVEKNVAELPLVDKAIVLCYHAGQVDQAILAFVKLRDDAPMVTEMQMEAR 514
Cdd:cd05973 321 TVEFDpDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGTPALADELQ 400
|
490 500 510
....*....|....*....|....*....|....*..
gi 126789033 515 L--KDKLADYMTP-QVVILEHVPLLVNGKVDRQALLK 548
Cdd:cd05973 401 LhvKKRLSAHAYPrTIHFVDELPKTPSGKIQRFLLRR 437
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
32-552 |
5.34e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 103.81 E-value: 5.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 32 RHADKVALIYQpsttGQGMapsqsSYRQMNERANRAARLLVAETHGRflqpnsdGDfIVAVCMQPSEGLVTTLLAIWKAG 111
Cdd:PRK06145 14 RTPDRAALVYR----DQEI-----SYAEFHQRILQAAGMLHARGIGQ-------GD-VVALLMKNSAAFLELAFAASYLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 112 GAYLPIDPSFPANRIHHILLEAKPTLVIRDDDIDAGRFQGTPTLSTTEL-YAKSLQLAGSNLLSEEMLRGGNDHIAIVLY 190
Cdd:PRK06145 77 AVFLPINYRLAADEVAYILGDAGAKLLLVDEEFDAIVALETPKIVIDAAaQADSRRLAQGGLEIPPQAAVAPTDLVRLMY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 191 TSGSTGVPKGVRLPHESIlnrlqwQWATFPYTANEAVSVfKTALTFVDSIAELWGPLMCGLAILVVPKAVTK----DPQR 266
Cdd:PRK06145 157 TSGTTDRPKGVMHSYGNL------HWKSIDHVIALGLTA-SERLLVVGPLYHVGAFDLPGIAVLWVGGTLRIhrefDPEA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 267 LVALLERYKIRRLVLVPTLLRSLLMylkmegggAAQKLLYNLQ--IWVCS-GEPLSVSLASSFFDYFDEGvhRLYNFYGS 343
Cdd:PRK06145 230 VLAAIERHRLTCAWMAPVMLSRVLT--------VPDRDRFDLDslAWCIGgGEKTPESRIRDFTRVFTRA--RYIDAYGL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 344 TEVLGDVTYFacESKKQLSLYDNVpiGIPLSNTVVYLLDADYRPVKNGEIGEIFASGLNLAAGYVNgrDPERflenplAV 423
Cdd:PRK06145 300 TETCSGDTLM--EAGREIEKIGST--GRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWK--DPEK------TA 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 424 EKKYARLYRTGDYGSLKNGSIMY-EGRTDSQVKIRGHRVDLSEVEKNVAELPLVDKAIVLCYHAGQVDQAILAFVKLRDD 502
Cdd:PRK06145 368 EAFYGDWFRSGDVGYLDEEGFLYlTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPG 447
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 126789033 503 APMVTEmQMEARLKDKLADYMTP-QVVILEHVPLLVNGKVDRQALLKTYET 552
Cdd:PRK06145 448 ATLTLE-ALDRHCRQRLASFKVPrQLKVRDELPRNPSGKVLKRVLRDELNG 497
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
56-546 |
9.37e-23 |
|
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: 102.17 E-value: 9.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 56 SYRQMNERANRAARLLVAE----THGRFLQPNSDGDFivavcmqpsegLVTTLLAIWKAGGAYLPIDPSFPANRIHHILL 131
Cdd:cd05958 12 TYRDLLALANRIANVLVGElgivPGNRVLLRGSNSPE-----------LVACWFGIQKAGAIAVATMPLLRPKELAYILD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 132 EAKPTLVIRDDDIDAgrfqgtptlsttelyakslqlagsnllseemlrggNDHIAIVLYTSGSTGVPKGVRLPHESILNR 211
Cdd:cd05958 81 KARITVALCAHALTA-----------------------------------SDDICILAFTSGTTGAPKATMHFHRDPLAS 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 212 LQwQWATF---PYTANEAVSVFKTALTFVDSIAELWgPLMCGLAILVVPKAVtkdPQRLVALLERYKIRRLVLVPTLLRS 288
Cdd:cd05958 126 AD-RYAVNvlrLREDDRFVGSPPLAFTFGLGGVLLF-PFGVGASGVLLEEAT---PDLLLSAIARYKPTVLFTAPTAYRA 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 289 LLmylkmEGGGAAQKLLYNLQIWVCSGEPLSVSLASSFFDYFdeGVhRLYNFYGSTEVLGDVTYFACESKKQLSLydnvp 368
Cdd:cd05958 201 ML-----AHPDAAGPDLSSLRKCVSAGEALPAALHRAWKEAT--GI-PIIDGIGSTEMFHIFISARPGDARPGAT----- 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 369 iGIPLSNTVVYLLDADYRPVKNGEIGEIFASGLNLAAGYVNGRDPERFLENPLAVEKKYarlYRTGDygslknGSIMYEG 448
Cdd:cd05958 268 -GKPVPGYEAKVVDDEGNPVPDGTIGRLAVRGPTGCRYLADKRQRTYVQGGWNITGDTY---SRDPD------GYFRHQG 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 449 RTDSQVKIRGHRVDLSEVEKNVAELPLVDKAIVLcyhaGQVDQAIL----AFVKLR----DDAPMVTEMQMEArlKDKLA 520
Cdd:cd05958 338 RSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVV----GHPDESRGvvvkAFVVLRpgviPGPVLARELQDHA--KAHIA 411
|
490 500
....*....|....*....|....*..
gi 126789033 521 DYMTPQ-VVILEHVPLLVNGKVDRQAL 546
Cdd:cd05958 412 PYKYPRaIEFVTELPRTATGKLQRFAL 438
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
32-546 |
1.52e-22 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 102.67 E-value: 1.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 32 RHADKVALIYQPSTTGQGMAPSQS-SYRQMNERANRAARLLVAetHGrfLQPnsdGDfiVAVCM-QPSEGLVTTLLAIWK 109
Cdd:PRK09274 18 ERPDQLAVAVPGGRGADGKLAYDElSFAELDARSDAIAHGLNA--AG--IGR---GM--RAVLMvTPSLEFFALTFALFK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 110 AGGAYLPIDPSFPANRIHHILLEAKPTLVI--------------------RDDDIDAGRFQGTPTLSTTELYAKSLQLAG 169
Cdd:PRK09274 89 AGAVPVLVDPGMGIKNLKQCLAEAQPDAFIgipkahlarrlfgwgkpsvrRLVTVGGRLLWGGTTLATLLRDGAAAPFPM 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 170 SNLLSEEMlrggndhiAIVLYTSGSTGVPKGVRLPHESILNRLQ-----WQW-------ATFPytaneAVSVFKTAltfv 237
Cdd:PRK09274 169 ADLAPDDM--------AAILFTSGSTGTPKGVVYTHGMFEAQIEalredYGIepgeidlPTFP-----LFALFGPA---- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 238 dsiaelwgplmCGLAIlVVP-----KAVTKDPQRLVALLERYKIRRLVLVPTLLRSLLMYLKmegggAAQKLLYNLQIWV 312
Cdd:PRK09274 232 -----------LGMTS-VIPdmdptRPATVDPAKLFAAIERYGVTNLFGSPALLERLGRYGE-----ANGIKLPSLRRVI 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 313 CSGEPLSVSLASSFFDYFDEGVhRLYNFYGSTEVLgDVTyfACESKKQLSLYDNVP-------IGIPLSNTVVYLLD--- 382
Cdd:PRK09274 295 SAGAPVPIAVIERFRAMLPPDA-EILTPYGATEAL-PIS--SIESREILFATRAATdngagicVGRPVDGVEVRIIAisd 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 383 ------ADYRPVKNGEIGEIFASGLNLAAGYVNgrDPErflENPLAvekKYAR-----LYRTGDYGSLKN-GSIMYEGRt 450
Cdd:PRK09274 371 apipewDDALRLATGEIGEIVVAGPMVTRSYYN--RPE---ATRLA---KIPDgqgdvWHRMGDLGYLDAqGRLWFCGR- 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 451 dsqvkiRGHRVDLSE-------VEKNVAELPLVDK-AIVLCYHAGQVDQAILafVKLRDDApMVTEMQMEARLKDKLADY 522
Cdd:PRK09274 442 ------KAHRVETAGgtlytipCERIFNTHPGVKRsALVGVGVPGAQRPVLC--VELEPGV-ACSKSALYQELRALAAAH 512
|
570 580 590
....*....|....*....|....*....|
gi 126789033 523 MTPQVV--ILEHVPLLV----NGKVDRQAL 546
Cdd:PRK09274 513 PHTAGIerFLIHPSFPVdirhNAKIFREKL 542
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
190-543 |
4.04e-22 |
|
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: 98.25 E-value: 4.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 190 YTSGSTGVPKGVRLPHESilnrlqwqWATFpYTANEAVSVFKTAltfvDSIAELwGPLMCGLAI------LVVPKAV--- 260
Cdd:cd17633 7 FTSGTTGLPKAYYRSERS--------WIES-FVCNEDLFNISGE----DAILAP-GPLSHSLFLygaisaLYLGGTFigq 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 261 -TKDPQRLVALLERYKIRRLVLVPTLLRSLLMYLKMEgggaaqkllYNLQIWVCSGEPLSVSLASSFFDYFDEGVhrLYN 339
Cdd:cd17633 73 rKFNPKSWIRKINQYNATVIYLVPTMLQALARTLEPE---------SKIKSIFSSGQKLFESTKKKLKNIFPKAN--LIE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 340 FYGSTEvLGDVTY-FACESKKQLSlydnvpIGIPLSNTVVYLLDADyrpvkNGEIGEIFASGLNLAAGYVNGRDperflE 418
Cdd:cd17633 142 FYGTSE-LSFITYnFNQESRPPNS------VGRPFPNVEIEIRNAD-----GGEIGKIFVKSEMVFSGYVRGGF-----S 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 419 NPlavekkyARLYRTGDYGSLK-NGSIMYEGRTDSQVKIRGHRVDLSEVEKNVAELPLVDKAIVLCYHAGQVDQAILAFV 497
Cdd:cd17633 205 NP-------DGWMSVGDIGYVDeEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALY 277
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 126789033 498 KLRDdapmVTEMQMEARLKDKLADYMTPQVVI-LEHVPLLVNGKVDR 543
Cdd:cd17633 278 SGDK----LTYKQLKRFLKQKLSRYEIPKKIIfVDSLPYTSSGKIAR 320
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
183-542 |
1.88e-21 |
|
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: 98.94 E-value: 1.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 183 DHIAIVLYTSGSTGVPKGVRLPHESILNRLQWQWATFPYTANEavsVFKTALTFVDSI---AELWGPLMCGLAILVVPKA 259
Cdd:cd05909 147 DDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPED---VVFGALPFFHSFgltGCLWLPLLSGIKVVFHPNP 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 260 VtkDPQRLVALLERYKIRRLVLVPTLLRSllmYLKmegggAAQKL-LYNLQIWVCSGEPLSVSLASSFFDYFdeGVhRLY 338
Cdd:cd05909 224 L--DYKKIPELIYDKKATILLGTPTFLRG---YAR-----AAHPEdFSSLRLVVAGAEKLKDTLRQEFQEKF--GI-RIL 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 339 NFYGSTE---VLgdvtyfACESKKqlslYDNVP--IGIPLSNTVVYLLD-ADYRPVKNGEIGEIFASGLNLAAGYVNGRD 412
Cdd:cd05909 291 EGYGTTEcspVI------SVNTPQ----SPNKEgtVGRPLPGMEVKIVSvETHEEVPIGEGGLLLVRGPNVMLGYLNEPE 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 413 PERFlenplAVEKKYarlYRTGDYGSL-KNGSIMYEGRTDSQVKIRGHRVDLSEVEKNVAELPLVDK--AIVLCYHAGQV 489
Cdd:cd05909 361 LTSF-----AFGDGW---YDTGDIGKIdGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEILPEDNevAVVSVPDGRKG 432
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 126789033 490 DQAILAFVKLRDDAPMVTEMQMEARLKD--KLADYMTpqvviLEHVPLLVNGKVD 542
Cdd:cd05909 433 EKIVLLTTTTDTDPSSLNDILKNAGISNlaKPSYIHQ-----VEEIPLLGTGKPD 482
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
19-546 |
7.13e-21 |
|
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: 97.01 E-value: 7.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 19 PRALHRIFEEQQLRHADKVALIyqpsttgqgMAPSQSSYRQMNERANRAARLLVaethGRFLQPnsdGDFIVaVCMQPSE 98
Cdd:cd05920 14 DEPLGDLLARSAARHPDRIAVV---------DGDRRLTYRELDRRADRLAAGLR----GLGIRP---GDRVV-VQLPNVA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 99 GLVTTLLAIWKAGGAYLPIDPSFPANRIHHILLEAKPTLVIRDDDIdaGRFQGTPtlsttelyakslqlagsnlLSEEML 178
Cdd:cd05920 77 EFVVLFFALLRLGAVPVLALPSHRRSELSAFCAHAEAVAYIVPDRH--AGFDHRA-------------------LARELA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 179 RGGNDhIAIVLYTSGSTGVPKGVRLPHESilnrlqwqwatFPYTANEAV--------SVFKTAL----TFVDSIAELWGP 246
Cdd:cd05920 136 ESIPE-VALFLLSGGTTGTPKLIPRTHND-----------YAYNVRASAevcgldqdTVYLAVLpaahNFPLACPGVLGT 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 247 LMCGLAILVVPKAvtkDPQRLVALLERYKIRRLVLVPTLLRSLLMYLkmEGGGAAQKLLYNLQIwvcSGEPLSVSLASSF 326
Cdd:cd05920 204 LLAGGRVVLAPDP---SPDAAFPLIEREGVTVTALVPALVSLWLDAA--ASRRADLSSLRLLQV---GGARLSPALARRV 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 327 FDYFDEGVHRLYnfyGSTEvlGDVTYFACESKKQLSLYDNvpiGIPLS-NTVVYLLDADYRPVKNGEIGEIFASGLNLAA 405
Cdd:cd05920 276 PPVLGCTLQQVF---GMAE--GLLNYTRLDDPDEVIIHTQ---GRPMSpDDEIRVVDEEGNPVPPGEEGELLTRGPYTIR 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 406 GYV-----NGR--DPERFlenplavekkyarlYRTGDYGSL-KNGSIMYEGRTDSQVKIRGHRVDLSEVEKNVAELPLVD 477
Cdd:cd05920 348 GYYrapehNARafTPDGF--------------YRTGDLVRRtPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVH 413
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 126789033 478 KAIVLCYHAGQVDQAILAFVKLRDDAPMVTEM--QMEARlkdKLADYMTP-QVVILEHVPLLVNGKVDRQAL 546
Cdd:cd05920 414 DAAVVAMPDELLGERSCAFVVLRDPPPSAAQLrrFLRER---GLAAYKLPdRIEFVDSLPLTAVGKIDKKAL 482
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
32-546 |
1.77e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 96.21 E-value: 1.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 32 RHADKVALiYQPSTTgqgmapsqSSYRQMNERANRAARLLvaetHGRFLQPNSDGDFIVAVCMQpsegLVTTLLAIWKAG 111
Cdd:PRK06188 24 RYPDRPAL-VLGDTR--------LTYGQLADRISRYIQAF----EALGLGTGDAVALLSLNRPE----VLMAIGAAQLAG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 112 GAYLPIDPSFPANRIHHILLEAKPTLVIrdddIDAGRFQGtptlSTTELYAKSLQLA----------GSNLLSE------ 175
Cdd:PRK06188 87 LRRTALHPLGSLDDHAYVLEDAGISTLI----VDPAPFVE----RALALLARVPSLKhvltlgpvpdGVDLLAAaakfgp 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 176 EMLRGGNDH--IAIVLYTSGSTGVPKGVRLPHESILNRLQWQWATFPYTANEAVSV-----FKTALTFVDSiaelwgpLM 248
Cdd:PRK06188 159 APLVAAALPpdIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMctplsHAGGAFFLPT-------LL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 249 CGLAILVVPKAvtkDPQRLVALLERYKIRRLVLVPTLLrsllmYLKMEGGGAAQKLLYNLQIWVCSGEPLS-VSLAssff 327
Cdd:PRK06188 232 RGGTVIVLAKF---DPAEVLRAIEEQRITATFLVPTMI-----YALLDHPDLRTRDLSSLETVYYGASPMSpVRLA---- 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 328 dyfdEGVHR----LYNFYGSTEVLGDVTYfaceskkqLSLYDNVPI--------GIPLSNTVVYLLDADYRPVKNGEIGE 395
Cdd:PRK06188 300 ----EAIERfgpiFAQYYGQTEAPMVITY--------LRKRDHDPDdpkrltscGRPTPGLRVALLDEDGREVAQGEVGE 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 396 IFASGLNLAAGYVNgrDPErflenplavekKYARLYR-----TGDYGSLKNGSIMY-EGRTDSQVKIRGHRVDLSEVEKN 469
Cdd:PRK06188 368 ICVRGPLVMDGYWN--RPE-----------ETAEAFRdgwlhTGDVAREDEDGFYYiVDRKKDMIVTGGFNVFPREVEDV 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 470 VAELPLVDKAIVLcyhaGQVD----QAILAFVKLRDDAPmVTEMQMEARLKDKLADYMTP-QVVILEHVPLLVNGKVDRQ 544
Cdd:PRK06188 435 LAEHPAVAQVAVI----GVPDekwgEAVTAVVVLRPGAA-VDAAELQAHVKERKGSVHAPkQVDFVDSLPLTALGKPDKK 509
|
..
gi 126789033 545 AL 546
Cdd:PRK06188 510 AL 511
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
56-541 |
3.41e-20 |
|
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.
Pssm-ID: 341229 [Multi-domain] Cd Length: 437 Bit Score: 94.37 E-value: 3.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 56 SYRQMNERANRAARLLVAETHGRflqpnsdGDfIVAVCMQPSEGLVTTLLAIWKAGGAYLPIDPSFPANRIHHILLEAKP 135
Cdd:cd05903 3 TYSELDTRADRLAAGLAALGVGP-------GD-VVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 136 TLVIRDDDIDAGRFQGTPtlsttelyakslqlagsnllseemlrggnDHIAIVLYTSGSTGVPKGVRLPHESILNRLQWQ 215
Cdd:cd05903 75 KVFVVPERFRQFDPAAMP-----------------------------DAVALLLFTSGTTGEPKGVMHSHNTLSASIRQY 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 216 WATFPYTANEAVSVFKTALTFVDSIAELWGPLMCGLAILVVPkavTKDPQRLVALLERYKIRRLVLVPTLLRSLLMYLKM 295
Cdd:cd05903 126 AERLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQD---IWDPDKALALMREHGVTFMMGATPFLTDLLNAVEE 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 296 EGGGAAQkllynLQIWVCSGEPLSVSLASSFFDYFDEGVHRLynfYGSTEVLGDVTyfACES-KKQLSLYDNvpiGIPLS 374
Cdd:cd05903 203 AGEPLSR-----LRTFVCGGATVPRSLARRAAELLGAKVCSA---YGSTECPGAVT--SITPaPEDRRLYTD---GRPLP 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 375 NTVVYLLDADYRPVKNGEIGEIFASGLNLAAGYvngrdperfLENPLAVEKKYARL-YRTGDYGSL-KNGSIMYEGRTdS 452
Cdd:cd05903 270 GVEIKVVDDTGATLAPGVEGELLSRGPSVFLGY---------LDRPDLTADAAPEGwFRTGDLARLdEDGYLRITGRS-K 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 453 QVKIR-GHRVDLSEVEKNVAELPLVDKAIVLCYHAGQVDQAILAFVKLRDDAPMVTEMQMEARLKDKLADYMTP-QVVIL 530
Cdd:cd05903 340 DIIIRgGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGALLTFDELVAYLDRQGVAKQYWPeRLVHV 419
|
490
....*....|.
gi 126789033 531 EHVPLLVNGKV 541
Cdd:cd05903 420 DDLPRTPSGKV 430
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
35-542 |
7.99e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 94.18 E-value: 7.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 35 DKVALIYqpsttgqgmAPSQSSYRQMNERANRAARLLVAetHGrfLQPnsdGDFiVAVCMQPSEGLVTTLLAIWKAGGAY 114
Cdd:PRK07798 18 DRVALVC---------GDRRLTYAELEERANRLAHYLIA--QG--LGP---GDH-VGIYARNRIEYVEAMLGAFKARAVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 115 LPIDPSFPANRIHHILLEAKPTLVIRDDDIdAGRFQG----TPTLSTT---------------ELYAKSLQLAGSNLLSE 175
Cdd:PRK07798 81 VNVNYRYVEDELRYLLDDSDAVALVYEREF-APRVAEvlprLPKLRTLvvvedgsgndllpgaVDYEDALAAGSPERDFG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 176 EmlRGGNDHIaiVLYTSGSTGVPKGVRLPHESILnRLQWQWATFpYTANEAVSVFKTALTFVDSIAELW---GPLMCGLA 252
Cdd:PRK07798 160 E--RSPDDLY--LLYTGGTTGMPKGVMWRQEDIF-RVLLGGRDF-ATGEPIEDEEELAKRAAAGPGMRRfpaPPLMHGAG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 253 I------------LVVPKAVTKDPQRLVALLERYKIRRLVLV-PTLLRSLLMYLKMEGGGaaqkLLYNLQIWVCSGEPLS 319
Cdd:PRK07798 234 QwaafaalfsgqtVVLLPDVRFDADEVWRTIEREKVNVITIVgDAMARPLLDALEARGPY----DLSSLFAIASGGALFS 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 320 VSLASSFFDYFDEGVhrLYNFYGSTEvlGDVTYFACESKKQL-SLYDNVPIGiplSNTVVylLDADYRPVK--NGEIGEI 396
Cdd:PRK07798 310 PSVKEALLELLPNVV--LTDSIGSSE--TGFGGSGTVAKGAVhTGGPRFTIG---PRTVV--LDEDGNPVEpgSGEIGWI 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 397 fASGLNLAAGYVNgrDPErflenplavekKYARLYRT---------GDYGSL-KNGSIMYEGRtDSQVkIR--GHRVDLS 464
Cdd:PRK07798 381 -ARRGHIPLGYYK--DPE-----------KTAETFPTidgvryaipGDRARVeADGTITLLGR-GSVC-INtgGEKVFPE 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 465 EVEKNVAELPLVDKAIVlcyhAGQVD----QAILAFVKLRDDApMVTEMQMEARLKDKLADYMTP-QVVILEHVPLLVNG 539
Cdd:PRK07798 445 EVEEALKAHPDVADALV----VGVPDerwgQEVVAVVQLREGA-RPDLAELRAHCRSSLAGYKVPrAIWFVDEVQRSPAG 519
|
...
gi 126789033 540 KVD 542
Cdd:PRK07798 520 KAD 522
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
32-551 |
1.02e-19 |
|
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: 94.30 E-value: 1.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 32 RHA-----DKVALIYQPSTTGQgmapSQS-SYRQMNERANRAARLLVAetHGRflqpnSDGD-FIVAVCMQPSEglVTTL 104
Cdd:cd05967 58 RHVeagrgDQIALIYDSPVTGT----ERTyTYAELLDEVSRLAGVLRK--LGV-----VKGDrVIIYMPMIPEA--AIAM 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 105 LAIWKAGGAYLPIDPSFPAN----RIHHilleAKPTLVIrddDIDAGrFQGTPTLSTTELYAKSLQLAGSN--------- 171
Cdd:cd05967 125 LACARIGAIHSVVFGGFAAKelasRIDD----AKPKLIV---TASCG-IEPGKVVPYKPLLDKALELSGHKphhvlvlnr 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 172 -LLSEEMLRGGND---------------------HIAIVLYTSGSTGVPKGVRLPHESILNRLQWQWATFpYTANeAVSV 229
Cdd:cd05967 197 pQVPADLTKPGRDldwsellakaepvdcvpvaatDPLYILYTSGTTGKPKGVVRDNGGHAVALNWSMRNI-YGIK-PGDV 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 230 FKTALTF---VDSIAELWGPLMCGLA-ILVVPKAV-TKDPQRLVALLERYKIRRLVLVPTLLRSLlmylKMEGGGAAQKL 304
Cdd:cd05967 275 WWAASDVgwvVGHSYIVYGPLLHGATtVLYEGKPVgTPDPGAFWRVIEKYQVNALFTAPTAIRAI----RKEDPDGKYIK 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 305 LYNLQ----IWVcSGEPLSVSLASSFFDYFDEGVHrlyNFYGSTEVLGDVTYfACESKKQLSLYDNVPiGIPLSNTVVYL 380
Cdd:cd05967 351 KYDLSslrtLFL-AGERLDPPTLEWAENTLGVPVI---DHWWQTETGWPITA-NPVGLEPLPIKAGSP-GKPVPGYQVQV 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 381 LDADYRPVKNGEIGEIfASGLNLAAGYVNG--RDPERFLENPLAvekKYARLYRTGDYGSL-KNGSIMYEGRTDSQVKIR 457
Cdd:cd05967 425 LDEDGEPVGPNELGNI-VIKLPLPPGCLLTlwKNDERFKKLYLS---KFPGYYDTGDAGYKdEDGYLFIMGRTDDVINVA 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 458 GHRVDLSEVEKNVAELPLVDKAIVLCYH---AGQVdqaILAFVKLRDDAPMVTEMQME---ARLKDKLADYMTPQVVIL- 530
Cdd:cd05967 501 GHRLSTGEMEESVLSHPAVAECAVVGVRdelKGQV---PLGLVVLKEGVKITAEELEKelvALVREQIGPVAAFRLVIFv 577
|
570 580
....*....|....*....|.
gi 126789033 531 EHVPLLVNGKVDRQALLKTYE 551
Cdd:cd05967 578 KRLPKTRSGKILRRTLRKIAD 598
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
181-546 |
1.13e-19 |
|
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: 93.71 E-value: 1.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 181 GNDHIAIVLYTSGSTGVPKGVRLPHESILNRLqwqwATFPYTANeaVSVFKTALTFVDS------IAELWGPLMCGLAIL 254
Cdd:cd05970 183 CGEDILLVYFSSGTTGMPKMVEHDFTYPLGHI----VTAKYWQN--VREGGLHLTVADTgwgkavWGKIYGQWIAGAAVF 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 255 VVPKAVTkDPQRLVALLERYKIRRLVLVPTLLRSLLmylkmegggaAQKL----LYNLQIWVCSGEPLSVSLassfFDYF 330
Cdd:cd05970 257 VYDYDKF-DPKALLEKLSKYGVTTFCAPPTIYRFLI----------REDLsrydLSSLRYCTTAGEALNPEV----FNTF 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 331 DE--GVhRLYNFYGSTEVLGDVTYFACESKKQLSlydnvpIGIPLSNTVVYLLDADYRPVKNGEIGEI---FASG--LNL 403
Cdd:cd05970 322 KEktGI-KLMEGFGQTETTLTIATFPWMEPKPGS------MGKPAPGYEIDLIDREGRSCEAGEEGEIvirTSKGkpVGL 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 404 AAGYvnGRDPERflenplAVEKKYARLYRTGDYGSL-KNGSIMYEGRTDSQVKIRGHRVDLSEVEKNVAELPlvdkAIVL 482
Cdd:cd05970 395 FGGY--YKDAEK------TAEVWHDGYYHTGDAAWMdEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHP----AVLE 462
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 126789033 483 CYHAGQVD----QAILAFVKLRDD--APMVTEMQMEARLKDKLADYMTPQVV-ILEHVPLLVNGKVDRQAL 546
Cdd:cd05970 463 CAVTGVPDpirgQVVKATIVLAKGyePSEELKKELQDHVKKVTAPYKYPRIVeFVDELPKTISGKIRRVEI 533
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
56-546 |
3.22e-19 |
|
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: 91.41 E-value: 3.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 56 SYRQMNERANRAARLLVAETHGRflqpnsdGDFiVAVCMQPSEGLVTTLLAIWKAGGAYLPIDPSFPANRIHHILLEAKP 135
Cdd:cd05969 2 TFAQLKVLSARFANVLKSLGVGK-------GDR-VFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 136 TLVIrdddidagrfqgtptlSTTELYAKslqlagsnllseemlRGGNDhIAIVLYTSGSTGVPKGVRLPHESILNrlQWQ 215
Cdd:cd05969 74 KVLI----------------TTEELYER---------------TDPED-PTLLHYTSGTTGTPKGVLHVHDAMIF--YYF 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 216 WATFPYTANEAVSVFKTA----LTfvDSIAELWGPLMCGLAILVVPKAVtkDPQRLVALLERYKIRRLVLVPTLLRsLLM 291
Cdd:cd05969 120 TGKYVLDLHPDDIYWCTAdpgwVT--GTVYGIWAPWLNGVTNVVYEGRF--DAESWYGIIERVKVTVWYTAPTAIR-MLM 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 292 YLKMEggGAAQKLLYNLQIWVCSGEPLSVSLASSFFDYFDEGVHrlyNFYGSTEVLGDV-TYFACESKKQLSLydnvpiG 370
Cdd:cd05969 195 KEGDE--LARKYDLSSLRFIHSVGEPLNPEAIRWGMEVFGVPIH---DTWWQTETGSIMiANYPCMPIKPGSM------G 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 371 IPLSNTVVYLLDADYRPVKNGEIGEI-FASGL-NLAAGYVNgrDPERFlenplaveKKYAR--LYRTGDYGSL-KNGSIM 445
Cdd:cd05969 264 KPLPGVKAAVVDENGNELPPGTKGILaLKPGWpSMFRGIWN--DEERY--------KNSFIdgWYLTGDLAYRdEDGYFW 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 446 YEGRTDSQVKIRGHRVDLSEVEKNVAELPLVDKAIVLcyhaGQVD----QAILAFVKLRDDAPMVTEMQMEARL--KDKL 519
Cdd:cd05969 334 FVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVI----GKPDplrgEIIKAFISLKEGFEPSDELKEEIINfvRQKL 409
|
490 500
....*....|....*....|....*...
gi 126789033 520 ADYMTP-QVVILEHVPLLVNGKVDRQAL 546
Cdd:cd05969 410 GAHVAPrEIEFVDNLPKTRSGKIMRRVL 437
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
56-546 |
3.57e-19 |
|
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.
Pssm-ID: 341247 [Multi-domain] Cd Length: 493 Bit Score: 91.80 E-value: 3.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 56 SYRQMNERANRaarlLVAETHGRFLQPNSdgdfIVAVCMQPSEGLVTTLLAIWKAGGAYLPIDPSFPANRIHHILLEAKP 135
Cdd:cd05923 30 TYSELRARIEA----VAARLHARGLRPGQ----RVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 136 TLVIRDDDidAGRFQGTPTLSTTELYAKSLQLAGSN-----LLSEEMLRGGNDhiAIVLYTSGSTGVPKGVRLPHESILN 210
Cdd:cd05923 102 TAAVIAVD--AQVMDAIFQSGVRVLALSDLVGLGEPesagpLIEDPPREPEQP--AFVFYTSGTTGLPKGAVIPQRAAES 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 211 RLQW--QWATFPYTANEAV-------------SVFKTALTFVDSIaelwgplmcglailVVPKAVtkDPQRLVALLERYK 275
Cdd:cd05923 178 RVLFmsTQAGLRHGRHNVVlglmplyhvigffAVLVAALALDGTY--------------VVVEEF--DPADALKLIEQER 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 276 IRRLVLVPTLLRSLLmylkmegGGAAQkllynlqiwvcSGEPLSvSLASSFF------DYFDEGVHR-----LYNFYGST 344
Cdd:cd05923 242 VTSLFATPTHLDALA-------AAAEF-----------AGLKLS-SLRHVTFagatmpDAVLERVNQhlpgeKVNIYGTT 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 345 EVLGdvtyfaceskkqlSLYDNVP----IGIPLSNTVVYLLDADYRPVK---NGEIGEIFASGLNLAAGyvngrdpERFL 417
Cdd:cd05923 303 EAMN-------------SLYMRDArtgtEMRPGFFSEVRIVRIGGSPDEalaNGEEGELIVAAAADAAF-------TGYL 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 418 ENPLA-VEKKYARLYRTGDYGSLK-NGSIMYEGRTDSQVKIRGHRVDLSEVEKNVAELPLVDKAIVLCYHAGQVDQAILA 495
Cdd:cd05923 363 NQPEAtAKKLQDGWYRTGDVGYVDpSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTA 442
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 126789033 496 FVKLRDDAPMVTEMQMEARlKDKLADYMTPQ-VVILEHVPLLVNGKVDRQAL 546
Cdd:cd05923 443 CVVPREGTLSADELDQFCR-ASELADFKRPRrYFFLDELPKNAMNKVLRRQL 493
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
27-546 |
6.87e-19 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 91.07 E-value: 6.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 27 EEQQLRHADKVALIyqpsTTGQGMapsqsSYRQMNERANRAARLLVAETHgrfLQPnsdGDFIvAVCMQPSEGLVTTLLA 106
Cdd:PRK06839 9 EKRAYLHPDRIAII----TEEEEM-----TYKQLHEYVSKVAAYLIYELN---VKK---GERI-AILSQNSLEYIVLLFA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 107 IWKAGGAYLPIDPSFPANRIHHILLEAKPTLVIRDDDIDA------GRFQGTPTLSTTELyAKSLQLAGSNLLSeemlrG 180
Cdd:PRK06839 73 IAKVECIAVPLNIRLTENELIFQLKDSGTTVLFVEKTFQNmalsmqKVSYVQRVISITSL-KEIEDRKIDNFVE-----K 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 181 GNDHIAIVLYTSGSTGVPKGVRLPHESILNRLQWQWATFPYTANEaVSVFKTALTFVDSIAELWGPLMCGLAILVVPKAV 260
Cdd:PRK06839 147 NESASFIICYTSGTTGKPKGAVLTQENMFWNALNNTFAIDLTMHD-RSIVLLPLFHIGGIGLFAFPTLFAGGVIIVPRKF 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 261 tkDPQRLVALLERYKIRRLVLVPTLLRSLLMYLKMEGGGAAQ-KLLYNlqiwvcSGEPLSVSLASSFFDyfdegvhRLYN 339
Cdd:PRK06839 226 --EPTKALSMIEKHKVTVVMGVPTIHQALINCSKFETTNLQSvRWFYN------GGAPCPEELMREFID-------RGFL 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 340 F---YGSTEVLGDVTYFACE--SKKQLSlydnvpIGIPLSNTVVYLLDADYRPVKNGEIGEIFASGLNLAAGYVNgrdpe 414
Cdd:PRK06839 291 FgqgFGMTETSPTVFMLSEEdaRRKVGS------IGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWN----- 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 415 rfleNPLAVEK--KYARLYrTGDYGSL-KNGSIMYEGRTDSQVKIRGHRVDLSEVEKNVAELPLVDKAIVLCYHAGQVDQ 491
Cdd:PRK06839 360 ----RPDATEEtiQDGWLC-TGDLARVdEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGE 434
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 126789033 492 AILAFVKLRDDApMVTEMQMEARLKDKLADYMTPQ-VVILEHVPLLVNGKVDRQAL 546
Cdd:PRK06839 435 IPIAFIVKKSSS-VLIEKDVIEHCRLFLAKYKIPKeIVFLKELPKNATGKIQKAQL 489
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
56-503 |
1.40e-18 |
|
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: 89.58 E-value: 1.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 56 SYRQMNERANRAARLLVAetHGrfLQPnsdGDfIVAVCMQPSEGLVTTLLAIWKAGGAYLPIDPSFPANRIHHILLEAKP 135
Cdd:cd05907 7 TWAEFAEEVRALAKGLIA--LG--VEP---GD-RVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 136 TLVIRDDdidagrfqgtPtlsttelyakslqlagsnllseemlrggnDHIAIVLYTSGSTGVPKGVRLPHESILnrlqwq 215
Cdd:cd05907 79 KALFVED----------P-----------------------------DDLATIIYTSGTTGRPKGVMLSHRNIL------ 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 216 WATfpYTANEAVSVFKTA--LTF------VDSIAELWGPLMCGLAILVVPkavtkDPQRLVALLERYKIRRLVLVPTLLR 287
Cdd:cd05907 114 SNA--LALAERLPATEGDrhLSFlplahvFERRAGLYVPLLAGARIYFAS-----SAETLLDDLSEVRPTVFLAVPRVWE 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 288 SLLMYLKMEGGGAAQKLLY------NLQIWVCSGEPLSVSLAsSFFDYFdeGVHrLYNFYGSTEVLGDVTyfaceskkqL 361
Cdd:cd05907 187 KVYAAIKVKAVPGLKRKLFdlavggRLRFAASGGAPLPAELL-HFFRAL--GIP-VYEGYGLTETSAVVT---------L 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 362 SLYDNVPI---GIPLSNTVvylldadyrpVKNGEIGEIFASGLNLAAGYVNgrDPErflenPLAVEKKYARLYRTGDYGS 438
Cdd:cd05907 254 NPPGDNRIgtvGKPLPGVE----------VRIADDGEILVRGPNVMLGYYK--NPE-----ATAEALDADGWLHTGDLGE 316
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 126789033 439 LK-NGSIMYEGRT-DSQVKIRGHRVDLSEVEKNVAELPLVDKAIVLcyhaGQVDQAILAFVKLRDDA 503
Cdd:cd05907 317 IDeDGFLHITGRKkDLIITSGGKNISPEPIENALKASPLISQAVVI----GDGRPFLVALIVPDPEA 379
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
7-551 |
2.04e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 89.72 E-value: 2.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 7 LSIVKGLQQDF----VPRALHRIFEEQQ----LRH-----ADKVALIYQPSTTgqgmapsqsSYRQMNERANRAARLLVA 73
Cdd:PRK06178 7 LAELRALQQAAwpagIPREPEYPHGERPlteyLRAwarerPQRPAIIFYGHVI---------TYAELDELSDRFAALLRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 74 etHGrfLQPnsdGDFiVAVCMQPSEGLVTTLLAIWKAGGAYLPIDPSFPANRIHHILLEAKPTLVIRDDDIDAGRFQGTP 153
Cdd:PRK06178 78 --RG--VGA---GDR-VAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLALDQLAPVVEQVRA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 154 TLSTTELYAKSL--------------QLAGSNLLSEEML----------------RGGNDHIAIVLYTSGSTGVPKGVRL 203
Cdd:PRK06178 150 ETSLRHVIVTSLadvlpaeptlplpdSLRAPRLAAAGAIdllpalractapvplpPPALDALAALNYTGGTTGMPKGCEH 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 204 PHESILnrlqwqwatfpYTA--NEAVSVFKTA-LTFVDSIAELW--G-------PLMCGlAILVVpkaVTK-DPQRLVAL 270
Cdd:PRK06178 230 TQRDMV-----------YTAaaAYAVAVVGGEdSVFLSFLPEFWiaGenfgllfPLFSG-ATLVL---LARwDAVAFMAA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 271 LERYKIRRLVLVPTLLRSLlmylkMEGGGAAQkllYNLQiwvcsgePLSVSLASSFFDYFDEGVHRLYN----------F 340
Cdd:PRK06178 295 VERYRVTRTVMLVDNAVEL-----MDHPRFAE---YDLS-------SLRQVRVVSFVKKLNPDYRQRWRaltgsvlaeaA 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 341 YGSTEVLGDVTYFACESKKQLSL-YDNVPIGIPLSNTVVYLLDADY-RPVKNGEIGEIFASGLNLAAGYVNGRDPERfle 418
Cdd:PRK06178 360 WGMTETHTCDTFTAGFQDDDFDLlSQPVFVGLPVPGTEFKICDFETgELLPLGAEGEIVVRTPSLLKGYWNKPEATA--- 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 419 nplavEKKYARLYRTGDYGSL-KNGSIMYEGRTDSQVKIRGHRVDLSEVEKNVAELPLVDKAIVLcyhaGQVD----QAI 493
Cdd:PRK06178 437 -----EALRDGWLHTGDIGKIdEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVV----GRPDpdkgQVP 507
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 126789033 494 LAFVKLRDDAPmVTEMQMEARLKDKLADYMTPQVVILEHVPLLVNGKVDRQALLKTYE 551
Cdd:PRK06178 508 VAFVQLKPGAD-LTAAALQAWCRENMAVYKVPEIRIVDALPMTATGKVRKQDLQALAE 564
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
32-553 |
1.76e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 86.53 E-value: 1.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 32 RHADKVALIYQPSTTgqgmapsqsSYRQMNERANRAARLLVAEThgrfLQPnsdGDFiVAVCMQPSEGLVTTLLAIWKAG 111
Cdd:PRK08316 23 RYPDKTALVFGDRSW---------TYAELDAAVNRVAAALLDLG----LKK---GDR-VAALGHNSDAYALLWLACARAG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 112 GAYLPIDPSFPANRIHHILLEAKPTLVIRDDDIdAGRFQGTPTLSTTELYAKSLQL-----AGSNLLSEEMLRGGNDH-- 184
Cdd:PRK08316 86 AVHVPVNFMLTGEELAYILDHSGARAFLVDPAL-APTAEAALALLPVDTLILSLVLggreaPGGWLDFADWAEAGSVAep 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 185 --------IAIVLYTSGSTGVPKGVRLPHESILnrlqWQW----ATFPYTANE----AVSVFKTALTFVdsiaeLWGP-L 247
Cdd:PRK08316 165 dveladddLAQILYTSGTESLPKGAMLTHRALI----AEYvsciVAGDMSADDiplhALPLYHCAQLDV-----FLGPyL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 248 MCGLAILVVPKAvtkDPQRLVALLERYKIRRLVLVPTLLRSLLMYLKMEGG--GAAQKLLYNLQIWvcsgePLSV--SLA 323
Cdd:PRK08316 236 YVGATNVILDAP---DPELILRTIEAERITSFFAPPTVWISLLRHPDFDTRdlSSLRKGYYGASIM-----PVEVlkELR 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 324 SSFFDYfdegvhRLYNFYGSTE------VLGdvtyfaceSKKQLSLYDNVpiGIPLSNTVVYLLDADYRPVKNGEIGEIF 397
Cdd:PRK08316 308 ERLPGL------RFYNCYGQTEiaplatVLG--------PEEHLRRPGSA--GRPVLNVETRVVDDDGNDVAPGEVGEIV 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 398 ASGLNLAAGYVNgrDPERFLEnplAVEKKYarlYRTGDYGSL-KNGSIMYEGRTDSQVKIRGHRVDLSEVEKNVAELPLV 476
Cdd:PRK08316 372 HRSPQLMLGYWD--DPEKTAE---AFRGGW---FHSGDLGVMdEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAV 443
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 126789033 477 DKAIVL-CYHAGQVdQAILAFVKLRDDApMVTEMQMEARLKDKLADYMTP-QVVILEHVPLLVNGKVDRQALLKTYETA 553
Cdd:PRK08316 444 AEVAVIgLPDPKWI-EAVTAVVVPKAGA-TVTEDELIAHCRARLAGFKVPkRVIFVDELPRNPSGKILKRELRERYAGA 520
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
32-565 |
4.83e-17 |
|
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: 85.69 E-value: 4.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 32 RHADKVALIYQPSTTGQGmapSQSSYRQMNERANRAARLLVAETHGRflqpnsdGDfIVAVCMQPSEGLVTTLLAIWKAG 111
Cdd:cd05966 65 ERGDKVAIIWEGDEPDQS---RTITYRELLREVCRFANVLKSLGVKK-------GD-RVAIYMPMIPELVIAMLACARIG 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 112 GAYLPIDPSFPA----NRIHHilleAKPTLVIRDDdidaGRFQGTPTLSTTELYAKSLQLAGS--------NLLSEEMLR 179
Cdd:cd05966 134 AVHSVVFAGFSAeslaDRIND----AQCKLVITAD----GGYRGGKVIPLKEIVDEALEKCPSvekvlvvkRTGGEVPMT 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 180 GGND----------------------HIAIVLYTSGSTGVPKGVRlpHeSILNRLQWQWATFPYtaneavsVFK------ 231
Cdd:cd05966 206 EGRDlwwhdlmakqspecepewmdseDPLFILYTSGSTGKPKGVV--H-TTGGYLLYAATTFKY-------VFDyhpddi 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 232 ----------TALTFVdsiaeLWGPLMCGLAILV---VPkaVTKDPQRLVALLERYKIRRLVLVPTLLRSLLMYlkmeGG 298
Cdd:cd05966 276 ywctadigwiTGHSYI-----VYGPLANGATTVMfegTP--TYPDPGRYWDIVEKHKVTIFYTAPTAIRALMKF----GD 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 299 GAAQKL-LYNLQIWVCSGEPLSVslassffdyfdEGVHRLYNFYGSTEV-LGDvTYFACESKKQLslYDNVPIGIPL--- 373
Cdd:cd05966 345 EWVKKHdLSSLRVLGSVGEPINP-----------EAWMWYYEVIGKERCpIVD-TWWQTETGGIM--ITPLPGATPLkpg 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 374 SNT------VVYLLDADYRPVKNGEIGeifasglNLAA-----GYVNG--RDPERFLENPLaveKKYARLYRTGDYGSL- 439
Cdd:cd05966 411 SATrpffgiEPAILDEEGNEVEGEVEG-------YLVIkrpwpGMARTiyGDHERYEDTYF---SKFPGYYFTGDGARRd 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 440 KNGSIMYEGRTDSQVKIRGHRVDLSEVEKNVAELPLVDKAIVLCYHAGQVDQAILAFVKLRDDAPMVTEMQMEAR--LKD 517
Cdd:cd05966 481 EDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSDELRKELRkhVRK 560
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 126789033 518 KLADYMTPQVVILehVPLLV---NGKVDRQaLLKTYETANNNEGDSSIVLD 565
Cdd:cd05966 561 EIGPIATPDKIQF--VPGLPktrSGKIMRR-ILRKIAAGEEELGDTSTLAD 608
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
22-414 |
8.95e-17 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 84.77 E-value: 8.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 22 LHRIFEEQQLRHADKVALIYQPSTTGQGMapsqsSYRQMNERANRAARLLVAetHGrfLQPnsdGDfIVAVCMQPSEGLV 101
Cdd:COG1022 13 LPDLLRRRAARFPDRVALREKEDGIWQSL-----TWAEFAERVRALAAGLLA--LG--VKP---GD-RVAILSDNRPEWV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 102 TTLLAIWKAGGAYLPIDPSFPANRIHHIL-------------------LEAK---PTL--VIRDDDIDAGRFQGTPTLSt 157
Cdd:COG1022 80 IADLAILAAGAVTVPIYPTSSAEEVAYILndsgakvlfvedqeqldklLEVRdelPSLrhIVVLDPRGLRDDPRLLSLD- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 158 tELYAKSLQLAGSNLLSEEMLRGGNDHIAIVLYTSGSTGVPKGVRLPHESILnrlqwqwatfpYTANEAVSVFK-----T 232
Cdd:COG1022 159 -ELLALGREVADPAELEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLL-----------SNARALLERLPlgpgdR 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 233 ALTF--VDSIAE-LWG--PLMCGLAIlvvpkAVTKDPQRLVALLERYKIRRLVLVPTLLRSLL--MYLKMEGGGA----- 300
Cdd:COG1022 227 TLSFlpLAHVFErTVSyyALAAGATV-----AFAESPDTLAEDLREVKPTFMLAVPRVWEKVYagIQAKAEEAGGlkrkl 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 301 -------------------------------AQKLLY---------NLQIWVCSGEPLSVSLAsSFFDYFdeGVHrLYNF 340
Cdd:COG1022 302 frwalavgrryararlagkspslllrlkhalADKLVFsklrealggRLRFAVSGGAALGPELA-RFFRAL--GIP-VLEG 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 341 YGSTEVLGDVTYfaceskkqlslydNVP-------IGIPLSNTVvylldadyrpVKNGEIGEIFASGLNLAAGYVNgrDP 413
Cdd:COG1022 378 YGLTETSPVITV-------------NRPgdnrigtVGPPLPGVE----------VKIAEDGEILVRGPNVMKGYYK--NP 432
|
.
gi 126789033 414 E 414
Cdd:COG1022 433 E 433
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
28-551 |
9.50e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 84.06 E-value: 9.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 28 EQQLRHA----DKVALIYQPSttgqgmapsQSSYRQMNERANRAARLLVAETHgrflQPNSdgdfiVAVCMQPSEGLVTT 103
Cdd:PRK07638 5 KEYKKHAslqpNKIAIKENDR---------VLTYKDWFESVCKVANWLNEKES----KNKT-----IAILLENRIEFLQL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 104 LLAIWKAGGAYLPIDPSFPANRIHHILLEAKPTLVIRDD----DIDAGRfqgTPTLS------TTELYAKSLqLAGSNLL 173
Cdd:PRK07638 67 FAGAAMAGWTCVPLDIKWKQDELKERLAISNADMIVTERyklnDLPDEE---GRVIEidewkrMIEKYLPTY-APIENVQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 174 SEEMLRGgndhiaivlYTSGSTGVPKGVRLPHESILNRLQWQWATFPYTANEAVSVfktALTFVDSIAeLWGP---LMCG 250
Cdd:PRK07638 143 NAPFYMG---------FTSGSTGKPKAFLRAQQSWLHSFDCNVHDFHMKREDSVLI---AGTLVHSLF-LYGAistLYVG 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 251 LAILVVPKAVtkdPQRLVALLERYKIRRLVLVPTLLRSLLmylkmegggAAQKLLYNLQIWVCSG---EPLSVSLASSFF 327
Cdd:PRK07638 210 QTVHLMRKFI---PNQVLDKLETENISVMYTVPTMLESLY---------KENRVIENKMKIISSGakwEAEAKEKIKNIF 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 328 DYFdegvhRLYNFYGSTEvLGDVTYFACESKKQlslydnVP--IGIPLSNTVVYLLDADYRPVKNGEIGEIFASGLNLAA 405
Cdd:PRK07638 278 PYA-----KLYEFYGASE-LSFVTALVDEESER------RPnsVGRPFHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFM 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 406 GYVNGRDPERFLEnplavekkyARLYRT-GDYGSL-KNGSIMYEGRTDSQVKIRGHRVDLSEVEKNVAELPLVDKAIVLc 483
Cdd:PRK07638 346 GYIIGGVLARELN---------ADGWMTvRDVGYEdEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVI- 415
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 126789033 484 yhaGQVD----QAILAFVKLRDDApmvteMQMEARLKDKLADYMTP-QVVILEHVPLLVNGKVDRQALLKTYE 551
Cdd:PRK07638 416 ---GVPDsywgEKPVAIIKGSATK-----QQLKSFCLQRLSSFKIPkEWHFVDEIPYTNSGKIARMEAKSWIE 480
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
182-542 |
2.18e-16 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 84.21 E-value: 2.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 182 NDHIAIVLYTSGSTGVPKGVRLPHESILNRLQWQWATFPYTANEAVSvfkTALTFVDSI---AELWGPLMCGLAILVVPk 258
Cdd:PRK08633 781 PDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVIL---SSLPFFHSFgltVTLWLPLLEGIKVVYHP- 856
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 259 avtkDP---QRLVALLERYKIRRLVLVPTLLRsllMYLKMEgggAAQKLLY-NLQIWVCSGEPLSVSLASSFFDYFDegv 334
Cdd:PRK08633 857 ----DPtdaLGIAKLVAKHRATILLGTPTFLR---LYLRNK---KLHPLMFaSLRLVVAGAEKLKPEVADAFEEKFG--- 923
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 335 HRLYNFYGSTEV-------LGDVtyfacESKKQLSLYDNVP--IGIPLSNTVVYLLDAD-YRPVKNGEIGEIFASGLNLA 404
Cdd:PRK08633 924 IRILEGYGATETspvasvnLPDV-----LAADFKRQTGSKEgsVGMPLPGVAVRIVDPEtFEELPPGEDGLILIGGPQVM 998
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 405 AGYVNgrDPERFLEnpLAVEKKYARLYRTGDYGSL-KNGSIMYEGRTDSQVKIRGHRVDLSEVEKNVAELpLVDKAIVLC 483
Cdd:PRK08633 999 KGYLG--DPEKTAE--VIKDIDGIGWYVTGDKGHLdEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKA-LGGEEVVFA 1073
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 126789033 484 yhAGQVD------QAILAFVKLRDDAPMVTEMQMEArlkdKLADYMTP-QVVILEHVPLLVNGKVD 542
Cdd:PRK08633 1074 --VTAVPdekkgeKLVVLHTCGAEDVEELKRAIKES----GLPNLWKPsRYFKVEALPLLGSGKLD 1133
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
56-551 |
2.66e-16 |
|
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: 83.10 E-value: 2.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 56 SYRQMNERANRAARLLVAEThgrfLQPnsdGDFIVAVCMQPSEglvtTLLAIWKA--GGaYLP-IDPSFPA--------N 124
Cdd:cd05906 41 SYQDLLEDARRLAAGLRQLG----LRP---GDSVILQFDDNED----FIPAFWACvlAG-FVPaPLTVPPTydepnarlR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 125 RIHHI--LLEaKPTLVIRDDDIDAGRFQGTPTlsttelyakslQLAGSNLLS-EEMLRGGNDH---------IAIVLYTS 192
Cdd:cd05906 109 KLRHIwqLLG-SPVVLTDAELVAEFAGLETLS-----------GLPGIRVLSiEELLDTAADHdlpqsrpddLALLMLTS 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 193 GSTGVPKGVRLPHESILNRLQWQWATFPYTANEavsVFKTALTFvDSIAELwgpLMCGLA--------ILVVPKAVTKDP 264
Cdd:cd05906 177 GSTGFPKAVPLTHRNILARSAGKIQHNGLTPQD---VFLNWVPL-DHVGGL---VELHLRavylgcqqVHVPTEEILADP 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 265 QRLVALLERYKIRRlVLVP----TLLRSLLMYLKmegggAAQKLLYNLQIWVCSGEPLSVSLASSFFDYFDEgvHRLYNF 340
Cdd:cd05906 250 LRWLDLIDRYRVTI-TWAPnfafALLNDLLEEIE-----DGTWDLSSLRYLVNAGEAVVAKTIRRLLRLLEP--YGLPPD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 341 -----YGSTEVLGDVTYFAceskkQLSLYDN------VPIGIPLSNTVVYLLDADYRPVKNGEIGEIFASGLNLAAGYVN 409
Cdd:cd05906 322 airpaFGMTETCSGVIYSR-----SFPTYDHsqalefVSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 410 grdperfleNPLAVEKKYAR--LYRTGDYGSLKNGSIMYEGRTDSQVKIRGHRVDLSEVEKNVAELPLVDKAIVLCY--- 484
Cdd:cd05906 397 ---------NPEANAEAFTEdgWFRTGDLGFLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPSFTAAFavr 467
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 126789033 485 HAGQV-DQAILAFVKLRD-DAPMVTEMQmeaRLKDKLADYMT--PQVVI-LEH--VPLLVNGKVDRQALLKTYE 551
Cdd:cd05906 468 DPGAEtEELAIFFVPEYDlQDALSETLR---AIRSVVSREVGvsPAYLIpLPKeeIPKTSLGKIQRSKLKAAFE 538
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
32-458 |
3.00e-16 |
|
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: 83.06 E-value: 3.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 32 RHADKVALIYqpsTTGQGMAPSQSSYRQMNERANRAARLLVAEThgrflqpnSDGDFIVAVCMQPSEgLVTTLLAIWKAG 111
Cdd:cd05931 5 ARPDRPAYTF---LDDEGGREETLTYAELDRRARAIAARLQAVG--------KPGDRVLLLAPPGLD-FVAAFLGCLYAG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 112 G----AYLPiDPSFPANRIHHILLEAKPTLVIRDDDIDAG---RFQGTPTLSTTELYAKSLQLAGSNLLSEEMLRGGNDh 184
Cdd:cd05931 73 AiavpLPPP-TPGRHAERLAAILADAGPRVVLTTAAALAAvraFAASRPAAGTPRLLVVDLLPDTSAADWPPPSPDPDD- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 185 IAIVLYTSGSTGVPKGVRLPHESILNRLQWQWATFPYTANeavSVFKTAL-TFVDS--IAELWGPLMCGL-AILVVPKAV 260
Cdd:cd05931 151 IAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPG---DVVVSWLpLYHDMglIGGLLTPLYSGGpSVLMSPAAF 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 261 TKDPQRLVALLERYK--------------IRRlvlvptllrsllmylkmegGGAAQKLLYNLQIW---VCSGEPLSVSLA 323
Cdd:cd05931 228 LRRPLRWLRLISRYRatisaapnfaydlcVRR-------------------VRDEDLEGLDLSSWrvaLNGAEPVRPATL 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 324 SSFFDYFdegvhRLYNF--------YG--------STEVLGD---VTYFACESKKQLSL---------YDNVPIGIPLSN 375
Cdd:cd05931 289 RRFAEAF-----APFGFrpeafrpsYGlaeatlfvSGGPPGTgpvVLRVDRDALAGRAVavaaddpaaRELVSCGRPLPD 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 376 TVVYLLDAD-YRPVKNGEIGEIFASGLNLAAGYVNGRDPERFLENPLAVEKKYARLyRTGDYGSLKNGSIMYEGRTDSQV 454
Cdd:cd05931 364 QEVRIVDPEtGRELPDGEVGEIWVRGPSVASGYWGRPEATAETFGALAATDEGGWL-RTGDLGFLHDGELYITGRLKDLI 442
|
....
gi 126789033 455 KIRG 458
Cdd:cd05931 443 IVRG 446
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
12-546 |
3.26e-16 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 83.08 E-value: 3.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 12 GLQQDFVPRALHRIFEEQQLRHADKVALIYQPSTTGQGmAPSQSSYRQMNERANRAARLLvaetHGRFLQPNSDGDFIVA 91
Cdd:PRK07529 17 PLAARDLPASTYELLSRAAARHPDAPALSFLLDADPLD-RPETWTYAELLADVTRTANLL----HSLGVGPGDVVAFLLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 92 VCMQpseglvtTLLAIW--KAGGAYLPIDPSFPANRIHHILLEAKPTLVIR-----DDDI-------------------- 144
Cdd:PRK07529 92 NLPE-------THFALWggEAAGIANPINPLLEPEQIAELLRAAGAKVLVTlgpfpGTDIwqkvaevlaalpelrtvvev 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 145 DAGRFQGTPTLSTTELYAKSLQlAGSNLLSEEMLRGGNDH-----------IAIVLYTSGSTGVPKGVRLPHES-ILNrl 212
Cdd:PRK07529 165 DLARYLPGPKRLAVPLIRRKAH-ARILDFDAELARQPGDRlfsgrpigpddVAAYFHTGGTTGMPKLAQHTHGNeVAN-- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 213 QWQWATFPYTANEAVSVFKTALTFVD-SIAELWGPLMCGLAILVVPKAVTKDP---QRLVALLERYKIRRLVLVPTLLRS 288
Cdd:PRK07529 242 AWLGALLLGLGPGDTVFCGLPLFHVNaLLVTGLAPLARGAHVVLATPQGYRGPgviANFWKIVERYRINFLSGVPTVYAA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 289 LLmylKMEGGGAAqklLYNLQIWVCSGEPLSVSLASSFFDYfdEGVhRLYNFYGSTEVlgdvtyfACES--------KKQ 360
Cdd:PRK07529 322 LL---QVPVDGHD---ISSLRYALCGAAPLPVEVFRRFEAA--TGV-RIVEGYGLTEA-------TCVSsvnppdgeRRI 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 361 LSlydnvpIGIPLSNT---VVYLLDA--DYRPVKNGEIGEIFASGLNLAAGYVNGRDPER-FLENplavekkyaRLYRTG 434
Cdd:PRK07529 386 GS------VGLRLPYQrvrVVILDDAgrYLRDCAVDEVGVLCIAGPNVFSGYLEAAHNKGlWLED---------GWLNTG 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 435 DYGSL-KNGSIMYEGRTDSQVkIR-GHRVDLSEVEKNVAELPLVDKAIVLCY---HAGQVDqaiLAFVKLRDDAPmVTEM 509
Cdd:PRK07529 451 DLGRIdADGYFWLTGRAKDLI-IRgGHNIDPAAIEEALLRHPAVALAAAVGRpdaHAGELP---VAYVQLKPGAS-ATEA 525
|
570 580 590
....*....|....*....|....*....|....*....
gi 126789033 510 QMEARLKDKLADYMT-P-QVVILEHVPLLVNGKVDRQAL 546
Cdd:PRK07529 526 ELLAFARDHIAERAAvPkHVRILDALPKTAVGKIFKPAL 564
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
56-546 |
3.68e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 82.35 E-value: 3.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 56 SYRQMNERANRAARLLVAETHGrflqPNSdgdfIVAVCMQPSEGLVTTLLAIWKAGGAYLPIDPSFPANRIHHILLEAKP 135
Cdd:PRK13383 62 SYRELQRATESLARRLTRDGVA----PGR----AVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAALRAHHI 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 136 TLVIRDDDIdAGRFQGTPTlsttelyaKSLQLAGSNLLSEEMlrGGNDHIA----IVLYTSGSTGVPKGVrlPHESILNR 211
Cdd:PRK13383 134 STVVADNEF-AERIAGADD--------AVAVIDPATAGAEES--GGRPAVAapgrIVLLTSGTTGKPKGV--PRAPQLRS 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 212 LQWQWATFpytaneavsVFKTALTfVDSIAELWGPLM--CGLAILVVPKAVTK--------DPQRLVALLERYKIRRLVL 281
Cdd:PRK13383 201 AVGVWVTI---------LDRTRLR-TGSRISVAMPMFhgLGLGMLMLTIALGGtvlthrhfDAEAALAQASLHRADAFTA 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 282 VPTLLRSLLmylKMEGGGAAQKLLYNLQIWVCSGEPLSVSLASSFFDYFDEgvhRLYNFYGSTEV-LGdvtyfACESKKQ 360
Cdd:PRK13383 271 VPVVLARIL---ELPPRVRARNPLPQLRVVMSSGDRLDPTLGQRFMDTYGD---ILYNGYGSTEVgIG-----ALATPAD 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 361 LSLYDNVpIGIPLSNTVVYLLDADYRPVKNGEIGEIFASGLNLAAGYVNGRDPerflenplAVEKKYArlyRTGDYGSLK 440
Cdd:PRK13383 340 LRDAPET-VGKPVAGCPVRILDRNNRPVGPRVTGRIFVGGELAGTRYTDGGGK--------AVVDGMT---STGDMGYLD 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 441 N-GSIMYEGRTDSQVKIRGHRVDLSEVEKNVAELPLVDKAIVLCYHAGQVDQAILAFVKLRDDAPmVTEMQMEARLKDKL 519
Cdd:PRK13383 408 NaGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSG-VDAAQLRDYLKDRV 486
|
490 500
....*....|....*....|....*...
gi 126789033 520 ADYMTPQ-VVILEHVPLLVNGKVDRQAL 546
Cdd:PRK13383 487 SRFEQPRdINIVSSIPRNPTGKVLRKEL 514
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
56-476 |
3.97e-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: 82.10 E-value: 3.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 56 SYRQMNERANRAARLLVAETHGRflqpnsdGDFiVAVCMQPSEGLVTTLLAIWKAGGAYLPIDPSFPANRIHHILLEAKP 135
Cdd:cd05914 9 TYKDLADNIAKFALLLKINGVGT-------GDR-VALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 136 TLVIRDDdidagrfqgtptlsttelyakslqlagsnllseemlrggNDHIAIVLYTSGSTGVPKGVRLPHESILNRLQWQ 215
Cdd:cd05914 81 KAIFVSD---------------------------------------EDDVALINYTSGTTGNSKGVMLTYRNIVSNVDGV 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 216 WATFPYTANEAV-------SVFKTALTFVDsiaelwgPLMCGLAILVvpkaVTKDPQRLVALLERYKIRRLVLVPTLLRS 288
Cdd:cd05914 122 KEVVLLGKGDKIlsilplhHIYPLTFTLLL-------PLLNGAHVVF----LDKIPSAKIIALAFAQVTPTLGVPVPLVI 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 289 LLMYL-----KMEGGGAAQKL---LYNLQIWVCSGEPLSVSLASSfFDYFDEG-------VHRLY---NF-----YGSTE 345
Cdd:cd05914 191 EKIFKmdiipKLTLKKFKFKLakkINNRKIRKLAFKKVHEAFGGN-IKEFVIGgakinpdVEEFLrtiGFpytigYGMTE 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 346 VLGDVTYFACESKKQLSlydnvpIGIPLSNTVVYLldadYRPVKNGEIGEIFASGLNLAAGYVNgrdperfleNPLAVEK 425
Cdd:cd05914 270 TAPIISYSPPNRIRLGS------AGKVIDGVEVRI----DSPDPATGEGEIIVRGPNVMKGYYK---------NPEATAE 330
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 126789033 426 KYAR--LYRTGDYGSL-KNGSIMYEGRTDSQ-VKIRGHRVDLSEVEKNVAELPLV 476
Cdd:cd05914 331 AFDKdgWFHTGDLGKIdAEGYLYIRGRKKEMiVLSSGKNIYPEEIEAKINNMPFV 385
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
13-561 |
2.35e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 80.21 E-value: 2.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 13 LQQDFVPRALHriFEEQQLRHA----DKVALIYQPSTTgqgmapsqsSYRQMNERANRAARLLVAETHGRflqpnsdGDF 88
Cdd:PRK07786 8 QEQPYLARRQN--WVNQLARHAlmqpDAPALRFLGNTT---------TWRELDDRVAALAGALSRRGVGF-------GDR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 89 IVAVCMQPSEgLVTTLLAIWKAGGAYLPIDPSFPANRIHHILLEAKPTLVIRDD---DIDAGRFQGTPTLSTTELYAKSL 165
Cdd:PRK07786 70 VLILMLNRTE-FVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVVTEAalaPVATAVRDIVPLLSTVVVAGGSS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 166 Q---LAGSNLLSEE-----MLRGGNDHIAIVLYTSGSTGVPKGVRLPHesilNRLQWQWATFPYT----ANEAVSVFKTA 233
Cdd:PRK07786 149 DdsvLGYEDLLAEAgpahaPVDIPNDSPALIMYTSGTTGRPKGAVLTH----ANLTGQAMTCLRTngadINSDVGFVGVP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 234 LTFVDSIAELWGPLMCGLAILVVP-KAVtkDPQRLVALLERYKIRRLVLVPTLLRSLL---------MYLKMEGGGAAqk 303
Cdd:PRK07786 225 LFHIAGIGSMLPGLLLGAPTVIYPlGAF--DPGQLLDVLEAEKVTGIFLVPAQWQAVCaeqqarprdLALRVLSWGAA-- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 304 llynlqiwvcsgePLSVSLASSFFDYFDEGvhRLYNFYGSTEvLGDVTyfaCESKKQLSLYDNVPIGIPLSNTVVYLLDA 383
Cdd:PRK07786 301 -------------PASDTLLRQMAATFPEA--QILAAFGQTE-MSPVT---CMLLGEDAIRKLGSVGKVIPTVAARVVDE 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 384 DYRPVKNGEIGEIFASGLNLAAGYVNgrdperfleNPLAVEKKYA-RLYRTGDYGSL-KNGSIMYEGRTDSQVKIRGHRV 461
Cdd:PRK07786 362 NMNDVPVGEVGEIVYRAPTLMSGYWN---------NPEATAEAFAgGWFHSGDLVRQdEEGYVWVVDRKKDMIISGGENI 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 462 DLSEVEKNVAELP-LVDKAIVLCYHA--GQVDQAILAfvkLRDDAPMVTEMQMEARLKDKLADYMTPQ-VVILEHVPLLV 537
Cdd:PRK07786 433 YCAEVENVLASHPdIVEVAVIGRADEkwGEVPVAVAA---VRNDDAALTLEDLAEFLTDRLARYKHPKaLEIVDALPRNP 509
|
570 580
....*....|....*....|....
gi 126789033 538 NGKVDRQALLKTYETANNNEGDSS 561
Cdd:PRK07786 510 AGKVLKTELRERYGACVNVERRSA 533
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
187-542 |
2.36e-15 |
|
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: 78.11 E-value: 2.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 187 IVLYTSGSTGVPKGVRLPHESILnrlqWQ-WATFPYTANEAVSVFktaltfVDSiaelwGPL------MCGLAILV---- 255
Cdd:cd17636 4 LAIYTAAFSGRPNGALLSHQALL----AQaLVLAVLQAIDEGTVF------LNS-----GPLfhigtlMFTLATFHaggt 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 256 ---VPKAvtkDPQRLVALLERYKIRRLVLVPTllrsllMYLKMEGGGAAQKllYNLQ-IWVCSGEPLSVSLASSffdyfD 331
Cdd:cd17636 69 nvfVRRV---DAEEVLELIEAERCTHAFLLPP------TIDQIVELNADGL--YDLSsLRSSPAAPEWNDMATV-----D 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 332 E--GVHRLYNfYGSTEVLGDVTYFAceskkqlslYDNVPIGI---PLSNTVVYLLDADYRPVKNGEIGEIFASGLNLAAG 406
Cdd:cd17636 133 TspWGRKPGG-YGQTEVMGLATFAA---------LGGGAIGGagrPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAG 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 407 YVNgrDPErflENplaVEKKYARLYRTGDYGS-LKNGSIMYEGRTDSQVKIRGHRVDLSEVEKNVAELPLVDKAIVLCYH 485
Cdd:cd17636 203 YWN--RPE---VN---ARRTRGGWHHTNDLGRrEPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVP 274
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 126789033 486 AGQVDQAILAFVKLRDDApMVTEMQMEARLKDKLADYMTPQ-VVILEHVPLLVNGKVD 542
Cdd:cd17636 275 DPRWAQSVKAIVVLKPGA-SVTEAELIEHCRARIASYKKPKsVEFADALPRTAGGADD 331
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
58-547 |
4.49e-15 |
|
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: 78.96 E-value: 4.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 58 RQMNERANRAARLLVAETHGRFLqpnsdgdfivavCMQPSEGLVTTLLAIWKAGGAYLPIDPSFPaNRIHHILLEAKPT- 136
Cdd:cd05929 25 IALNRNARAAAAEGVWIADGVYI------------YLINSILTVFAAAAAWKCGACPAYKSSRAP-RAEACAIIEIKAAa 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 137 -LVIRDDDIDAgrfqgtptLSTTELYAKSLQLAGSNLLSEEmlRGGNDhiaiVLYTSGSTGVPKGVR--LPHESILNRLQ 213
Cdd:cd05929 92 lVCGLFTGGGA--------LDGLEDYEAAEGGSPETPIEDE--AAGWK----MLYSGGTTGRPKGIKrgLPGGPPDNDTL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 214 WQWAT--FPYTANEAVSV---FKTAltfvDSIAELWGPLMCGLAILVVpkavTKDPQRLVALLERYKIRRLVLVPTLLRS 288
Cdd:cd05929 158 MAAALgfGPGADSVYLSPaplYHAA----PFRWSMTALFMGGTLVLME----KFDPEEFLRLIERYRVTFAQFVPTMFVR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 289 LlmyLKMEGGGAAQKLLYNLQIWVCSGEPLSVSLASSFFDYFDEgvhRLYNFYGSTEVLGdVTyfACESKKQLSLYDNVp 368
Cdd:cd05929 230 L---LKLPEAVRNAYDLSSLKRVIHAAAPCPPWVKEQWIDWGGP---IIWEYYGGTEGQG-LT--IINGEEWLTHPGSV- 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 369 iGIPLSNtVVYLLDADYRPVKNGEIGEIFASGlnlAAGYVNGRDPERflenplAVEKKYARLYRT-GDYGSLKNGSIMYE 447
Cdd:cd05929 300 -GRAVLG-KVHILDEDGNEVPPGEIGEVYFAN---GPGFEYTNDPEK------TAAARNEGGWSTlGDVGYLDEDGYLYL 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 448 GRTDSQVKIRGHR-VDLSEVEKNVAELPLV-DKAIVLCYHA--GQVDQAILAFVKLRDDAPMVTEmQMEARLKDKLADYM 523
Cdd:cd05929 369 TDRRSDMIISGGVnIYPQEIENALIAHPKVlDAAVVGVPDEelGQRVHAVVQPAPGADAGTALAE-ELIAFLRDRLSRYK 447
|
490 500
....*....|....*....|....*
gi 126789033 524 TPQVV-ILEHVPLLVNGKVDRQALL 547
Cdd:cd05929 448 CPRSIeFVAELPRDDTGKLYRRLLR 472
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
172-551 |
7.96e-15 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 78.30 E-value: 7.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 172 LLSEEMLRGGNDHIAIVLYTSGSTGVPKGVRLPHE-------SILNRLQWQ-------WatFPYTANEAVSVFKTAltfv 237
Cdd:cd05908 95 ITEEEVLCELADELAFIQFSSGSTGDPKGVMLTHEnlvhnmfAILNSTEWKtkdrilsW--MPLTHDMGLIAFHLA---- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 238 dsiaelwgPLMCGLAILVVPKAV-TKDPQRLVALLERYKIRRLVLVPTLLRSLLMYLKMEGggAAQKLLYNLQIWVCSGE 316
Cdd:cd05908 169 --------PLIAGMNQYLMPTRLfIRRPILWLKKASEHKATIVSSPNFGYKYFLKTLKPEK--ANDWDLSSIRMILNGAE 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 317 PLSVSLASSFFDYFDE-GVHR--LYNFYGstevLGDVTYFACESKKQLSL--------------------------YDNV 367
Cdd:cd05908 239 PIDYELCHEFLDHMSKyGLKRnaILPVYG----LAEASVGASLPKAQSPFktitlgrrhvthgepepevdkkdsecLTFV 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 368 PIGIPLSNTVVYLLDADYRPVKNGEIGEIFASGLNLAAGYVNgrdperfleNPLAVEKKYAR--LYRTGDYGSLKNGSIM 445
Cdd:cd05908 315 EVGKPIDETDIRICDEDNKILPDGYIGHIQIRGKNVTPGYYN---------NPEATAKVFTDdgWLKTGDLGFIRNGRLV 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 446 YEGRTDSQVKIRGHRVDLSEVEKNVAELPLVDKA-IVLC--YHAGQVDQAILAFVKLR----DDAPMVTEMQmeaRLKDK 518
Cdd:cd05908 386 ITGREKDIIFVNGQNVYPHDIERIAEELEGVELGrVVACgvNNSNTRNEEIFCFIEHRksedDFYPLGKKIK---KHLNK 462
|
410 420 430
....*....|....*....|....*....|...
gi 126789033 519 LADYMTPQVVILEHVPLLVNGKVDRQALLKTYE 551
Cdd:cd05908 463 RGGWQINEVLPIRRIPKTTSGKVKRYELAQRYQ 495
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
18-541 |
9.51e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 78.08 E-value: 9.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 18 VPRA-LHRIFEEQQLRHADKVALIYQPSTTgqgmapsqsSYRQMNERANRAARLLVAETHgrfLQPnsdGDFiVAVCMQP 96
Cdd:PRK08314 7 LPETsLFHNLEVSARRYPDKTAIVFYGRAI---------SYRELLEEAERLAGYLQQECG---VRK---GDR-VLLYMQN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 97 SEGLVTTLLAIWKAGGAYLPIDPSFPANRIHHILLEAKPTLVIRDDD----------------IDAGRFQGT-------- 152
Cdd:PRK08314 71 SPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSGARVAIVGSElapkvapavgnlrlrhVIVAQYSDYlpaepeia 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 153 -PTLSTTELYAKSLQLAGSNLLSEEM--------LRGGNDHIAIVLYTSGSTGVPKGVRLPHESILNRL--QWQWATFPy 221
Cdd:PRK08314 151 vPAWLRAEPPLQALAPGGVVAWKEALaaglapppHTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAvgSVLWSNST- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 222 taneAVSVFKTALTF------VDSiaeLWGPLMCGLAILVVPKAvtkdpQRLVA--LLERYKIRRLVLVPTLLRSLLMYL 293
Cdd:PRK08314 230 ----PESVVLAVLPLfhvtgmVHS---MNAPIYAGATVVLMPRW-----DREAAarLIERYRVTHWTNIPTMVVDFLASP 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 294 KME-----------GGGA------AQKL--LYNLQiwvcsgeplsvslassffdyFDEGvhrlynfYGSTEVLGDVTYFA 354
Cdd:PRK08314 298 GLAerdlsslryigGGGAampeavAERLkeLTGLD--------------------YVEG-------YGLTETMAQTHSNP 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 355 CESKKQLSLydnvpiGIPLSNTVVYLLDAD-YRPVKNGEIGEIFASGLNLAAGYVNGRDP--ERFLEnplaVEKKyaRLY 431
Cdd:PRK08314 351 PDRPKLQCL------GIPTFGVDARVIDPEtLEELPPGEVGEIVVHGPQVFKGYWNRPEAtaEAFIE----IDGK--RFF 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 432 RTGDYGSL-KNGSIMYEGRTDSQVKIRGHRVDLSEVEKNVAELPLVDKAIVLCYHAGQVDQAILAFVKLRDDAP-MVTEM 509
Cdd:PRK08314 419 RTGDLGRMdEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGETVKAVVVLRPEARgKTTEE 498
|
570 580 590
....*....|....*....|....*....|...
gi 126789033 510 QMEARLKDKLADYMTPQVVIL-EHVPLLVNGKV 541
Cdd:PRK08314 499 EIIAWAREHMAAYKYPRIVEFvDSLPKSGSGKI 531
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
56-550 |
1.08e-14 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 77.61 E-value: 1.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 56 SYRQMNERANRAARLLVAethgRFLQPnsdGDFiVAVCMQPS-EGLVTtLLAIWKAGGAYLPIDPSFPANRIHHILLEAK 134
Cdd:PRK07514 30 TYGDLDAASARLANLLVA----LGVKP---GDR-VAVQVEKSpEALAL-YLATLRAGAVFLPLNTAYTLAELDYFIGDAE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 135 PTLVIRDDDIDAG-----RFQGTPTLSTtelyaksLQLAGSNLLSEEML----------RGGNDHIAIvLYTSGSTGVPK 199
Cdd:PRK07514 101 PALVVCDPANFAWlskiaAAAGAPHVET-------LDADGTGSLLEAAAaapddfetvpRGADDLAAI-LYTSGTTGRSK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 200 GVRLPHESILNRLQ-----WQWatfpyTANE----AVSVFKTALTFVDSiaelWGPLMCGLAILVVPKAvtkDPQRLVAL 270
Cdd:PRK07514 173 GAMLSHGNLLSNALtlvdyWRF-----TPDDvlihALPIFHTHGLFVAT----NVALLAGASMIFLPKF---DPDAVLAL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 271 LERYKIrrLVLVPTLLRSLLmylkmEGGGAAQKLLYNLQIWVCSGEPLsvsLASSFFDYFDEGVHRLYNFYGSTEVlGDV 350
Cdd:PRK07514 241 MPRATV--MMGVPTFYTRLL-----QEPRLTREAAAHMRLFISGSAPL---LAETHREFQERTGHAILERYGMTET-NMN 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 351 TYFACESkkqlslyDNVP--IGIPLSNTVVYLLDADY-RPVKNGEIGEIFASGLNLAAGYvnGRDPERflenpLAVEKKY 427
Cdd:PRK07514 310 TSNPYDG-------ERRAgtVGFPLPGVSLRVTDPETgAELPPGEIGMIEVKGPNVFKGY--WRMPEK-----TAEEFRA 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 428 ARLYRTGDYGSL-KNGSIMYEGRTDSQVKIRGHRVDLSEVEKNVAELP-LVDKAIVLCYHAgqvD--QAILAFVKLRDDA 503
Cdd:PRK07514 376 DGFFITGDLGKIdERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPgVVESAVIGVPHP---DfgEGVTAVVVPKPGA 452
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 126789033 504 PmVTEMQMEARLKDKLADYMTP-QVVILEHVPLLVNGKVDRQALLKTY 550
Cdd:PRK07514 453 A-LDEAAILAALKGRLARFKQPkRVFFVDELPRNTMGKVQKNLLREQY 499
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
23-550 |
2.25e-14 |
|
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: 77.15 E-value: 2.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 23 HRIFEEQQLRHADKVALIYQpsttGQGMAPSQSSYRQMNERANRAARLLVAETHGRflqpnsdGDFI-VAVCMQPSegLV 101
Cdd:cd05968 64 EQLLDKWLADTRTRPALRWE----GEDGTSRTLTYGELLYEVKRLANGLRALGVGK-------GDRVgIYLPMIPE--IV 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 102 TTLLAIWKAGGAYLPIDPSFPANRIHHILLEAKPTLVI-------RDDDIDAG-------------------RFQGTPTL 155
Cdd:cd05968 131 PAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALItadgftrRGREVNLKeeadkacaqcptvekvvvvRHLGNDFT 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 156 STTELYAKS-LQLAGSNLLSEEMlrgGNDHIAIVLYTSGSTGVPKGVRLPHesilnrlqwqwATFPY-TANEAVSVFKTA 233
Cdd:cd05968 211 PAKGRDLSYdEEKETAGDGAERT---ESEDPLMIIYTSGTTGKPKGTVHVH-----------AGFPLkAAQDMYFQFDLK 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 234 ----LTFVDSIAELWGPLMCGLAILVVPKAVTKD-------PQRLVALLERYKIRRLVLVPTLLRSLLMylKMEGGGAAQ 302
Cdd:cd05968 277 pgdlLTWFTDLGWMMGPWLIFGGLILGATMVLYDgapdhpkADRLWRMVEDHEITHLGLSPTLIRALKP--RGDAPVNAH 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 303 KLLyNLQIWVCSGEPLSVSLASSFFDYFDEGVHRLYNFYGSTEVLGDVtyFACESKKQLSlydnvPIGI--PLSNTVVYL 380
Cdd:cd05968 355 DLS-SLRVLGSTGEPWNPEPWNWLFETVGKGRNPIINYSGGTEISGGI--LGNVLIKPIK-----PSSFngPVPGMKADV 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 381 LDADYRPVKnGEIGEifasgLNLAA---GYVNG--RDPERFLEnplAVEKKYARLYRTGDYGSLKNGSIMY-EGRTDSQV 454
Cdd:cd05968 427 LDESGKPAR-PEVGE-----LVLLApwpGMTRGfwRDEDRYLE---TYWSRFDNVWVHGDFAYYDEEGYFYiLGRSDDTI 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 455 KIRGHRVDLSEVEKNVAELPLVDKAIVLCYHAGQVDQAILAFVKLRDDAPMVTEMQME--ARLKDKLADYMTPQ-VVILE 531
Cdd:cd05968 498 NVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGVTPTEALAEElmERVADELGKPLSPErILFVK 577
|
570
....*....|....*....
gi 126789033 532 HVPLLVNGKVDRQALLKTY 550
Cdd:cd05968 578 DLPKTRNAKVMRRVIRAAY 596
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
53-546 |
3.80e-14 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 75.96 E-value: 3.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 53 SQSSYRQMNERANRAARLLVAETHGRFLQpnsdgdfivAVCM-QPSEGLVTTLLAIWKAGGAYLPIDPSFPANRIHHILL 131
Cdd:cd05910 1 SRLSFRELDERSDRIAQGLTAYGIRRGMR---------AVLMvPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 132 EAKPtlvirdddiDAgrFQGTPtlsttelyakslqLAgsnllseemlrggnDHIAIVLYTSGSTGVPKGVRLPH---ESI 208
Cdd:cd05910 72 EAEP---------DA--FIGIP-------------KA--------------DEPAAILFTSGSTGTPKGVVYRHgtfAAQ 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 209 LNRLQWQW---------ATFPYTAneavsvfktaltfvdsiaeLWGPLMcGLAIlVVP-----KAVTKDPQRLVALLERY 274
Cdd:cd05910 114 IDALRQLYgirpgevdlATFPLFA-------------------LFGPAL-GLTS-VIPdmdptRPARADPQKLVGAIRQY 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 275 KIRRLVLVPTLLRSLLMYlkmegGGAAQKLLYNLQIWVCSGEPLSVSLASSFFDYFDEGVhRLYNFYGSTEVLgDVTyfA 354
Cdd:cd05910 173 GVSIVFGSPALLERVARY-----CAQHGITLPSLRRVLSAGAPVPIALAARLRKMLSDEA-EILTPYGATEAL-PVS--S 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 355 CESKKQLSLYDNVP-------IGIPLSNTVVYLLDADYRPVKN---------GEIGEIFASGLNLAAGYVNGRDPERFLE 418
Cdd:cd05910 244 IGSRELLATTTAATsggagtcVGRPIPGVRVRIIEIDDEPIAEwddtlelprGEIGEITVTGPTVTPTYVNRPVATALAK 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 419 NPlavEKKYARLYRTGDYGSLKN-GSIMYEGRtdsqvkiRGHRVDLS-------EVEKNVAELPLVDK-AIVLCYHAGQv 489
Cdd:cd05910 324 ID---DNSEGFWHRMGDLGYLDDeGRLWFCGR-------KAHRVITTggtlytePVERVFNTHPGVRRsALVGVGKPGC- 392
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 126789033 490 DQAILAFVKLRDDAPMVTemQMEARLKDKLADYMTPQVV--ILEHVPLLV----NGKVDRQAL 546
Cdd:cd05910 393 QLPVLCVEPLPGTITPRA--RLEQELRALAKDYPHTQRIgrFLIHPSFPVdirhNAKIFREKL 453
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
183-546 |
4.57e-14 |
|
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: 75.08 E-value: 4.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 183 DHIAIVLYTSGSTGVPKGVRLPHESILNRLQWQWATFPYTANE----AVSVFKtaltfVDSIAELWGPLMCGLAILVVPK 258
Cdd:cd05912 77 DDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLTEDDnwlcALPLFH-----ISGLSILMRSVIYGMTVYLVDK 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 259 AvtkDPQRLVALLERYKIRRLVLVPTLLRSLLmylKMEGGGAAqkllYNLQIWVCSGEPLSVSLassffdyFDEGVHR-- 336
Cdd:cd05912 152 F---DAEQVLHLINSGKVTIISVVPTMLQRLL---EILGEGYP----NNLRCILLGGGPAPKPL-------LEQCKEKgi 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 337 -LYNFYGSTEVLGDVTYFACE-SKKQLSlydnvPIGIPLSNTVVYLLDADYRPvknGEIGEIFASGLNLAAGYVNGRDPe 414
Cdd:cd05912 215 pVYQSYGMTETCSQIVTLSPEdALNKIG-----SAGKPLFPVELKIEDDGQPP---YEVGEILLKGPNVTKGYLNRPDA- 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 415 rfleNPLAVEKKYarlYRTGDYGSLKNGSIMYegrtdsqvkIRGHRVDL----------SEVEKNVAELPLVDKAIVlcy 484
Cdd:cd05912 286 ----TEESFENGW---FKTGDIGYLDEEGFLY---------VLDRRSDLiisggeniypAEIEEVLLSHPAIKEAGV--- 346
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 126789033 485 hAGQVD----QAILAFVKLRDDapmVTEMQMEARLKDKLADYMTP-QVVILEHVPLLVNGKVDRQAL 546
Cdd:cd05912 347 -VGIPDdkwgQVPVAFVVSERP---ISEEELIAYCSEKLAKYKVPkKIYFVDELPRTASGKLLRHEL 409
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
183-546 |
5.89e-14 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 74.44 E-value: 5.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 183 DHIAIVLYTSGSTGVPKGVRLPHESILNRlQWQWATFPYTANEAVSVFKTALTFVD-SIAELWGPLMCGLAILVVPKAVT 261
Cdd:cd05944 2 DDVAAYFHTGGTTGTPKLAQHTHSNEVYN-AWMLALNSLFDPDDVLLCGLPLFHVNgSVVTLLTPLASGAHVVLAGPAGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 262 KDP---QRLVALLERYKIRRLVLVPTLLRSLlmylkMEGGGAAQklLYNLQIWVCSGEPLSVSLASSFFDYfdEGVhRLY 338
Cdd:cd05944 81 RNPglfDNFWKLVERYRITSLSTVPTVYAAL-----LQVPVNAD--ISSLRFAMSGAAPLPVELRARFEDA--TGL-PVV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 339 NFYGSTEVLGDVTYFACESKKQLSlydNVPIGIPLSNTVVYLLDAD---YRPVKNGEIGEIFASGLNLAAGYVNG-RDPE 414
Cdd:cd05944 151 EGYGLTEATCLVAVNPPDGPKRPG---SVGLRLPYARVRIKVLDGVgrlLRDCAPDEVGEICVAGPGVFGGYLYTeGNKN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 415 RFLENplavekkyaRLYRTGDYGSL-KNGSIMYEGRTDSQVkIR-GHRVDLSEVEKNVAELPLVDKAIVLCY---HAGQV 489
Cdd:cd05944 228 AFVAD---------GWLNTGDLGRLdADGYLFITGRAKDLI-IRgGHNIDPALIEEALLRHPAVAFAGAVGQpdaHAGEL 297
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 126789033 490 DqaiLAFVKLRDDApMVTEMQMEARLKDKLADY--MTPQVVILEHVPLLVNGKVDRQAL 546
Cdd:cd05944 298 P---VAYVQLKPGA-VVEEEELLAWARDHVPERaaVPKHIEVLEELPVTAVGKVFKPAL 352
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
32-546 |
8.00e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 75.16 E-value: 8.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 32 RHADKVALIYQPSTTgqgmapsqsSYRQMNERANRAARLLVAETHGRflqpnsdGDfIVAVCMQPSEGLVTTLLAIWKAG 111
Cdd:PRK06164 22 ARPDAVALIDEDRPL---------SRAELRALVDRLAAWLAAQGVRR-------GD-RVAVWLPNCIEWVVLFLACARLG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 112 GAYLPIDPSFPANRIHHILLEAKPTLVIRDD---DID-AGRFQGTPTLSTTELYA--------------------KSLQL 167
Cdd:PRK06164 85 ATVIAVNTRYRSHEVAHILGRGRARWLVVWPgfkGIDfAAILAAVPPDALPPLRAiavvddaadatpapapgarvQLFAL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 168 AGSNLLSEEMLRGGNDHIAIVLYT-SGSTGVPKGVrLPHESILNRLQWQWATFPYTANEAVSVFKTALTFVDSIAELWGP 246
Cdd:PRK06164 165 PDPAPPAAAGERAADPDAGALLFTtSGTTSGPKLV-LHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGFSTLLGA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 247 LMCGLAILVVPkavTKDPQRLVALLERYKIRRLVLVPTLLRSLL---------MYLKMEGGGAAQKLLYNLQIWVCsgep 317
Cdd:PRK06164 244 LAGGAPLVCEP---VFDAARTARALRRHRVTHTFGNDEMLRRILdtageradfPSARLFGFASFAPALGELAALAR---- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 318 lsvslassffdyfDEGVhRLYNFYGSTEVlgdvtyFACESKKQLSLYDNVPI---GIPLSNTV-VYLLD-ADYRPVKNGE 392
Cdd:PRK06164 317 -------------ARGV-PLTGLYGSSEV------QALVALQPATDPVSVRIeggGRPASPEArVRARDpQDGALLPDGE 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 393 IGEIFASGLNLAAGYvngrdperfLENPLAVEKKYAR--LYRTGDYGSLK-NGSIMYEGRTDSQVKIRGHRVDLSEVEKN 469
Cdd:PRK06164 377 SGEIEIRAPSLMRGY---------LDNPDATARALTDdgYFRTGDLGYTRgDGQFVYQTRMGDSLRLGGFLVNPAEIEHA 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 470 VAELPLV-DKAIVLCYHAGQVDQAilAFVKLRDDAPMVTEMQMeARLKDKLADYMTPQ-VVILEHVPLLVNG---KVDRQ 544
Cdd:PRK06164 448 LEALPGVaAAQVVGATRDGKTVPV--AFVIPTDGASPDEAGLM-AACREALAGFKVPArVQVVEAFPVTESAngaKIQKH 524
|
..
gi 126789033 545 AL 546
Cdd:PRK06164 525 RL 526
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
188-550 |
1.62e-13 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 73.96 E-value: 1.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 188 VLYTSGSTGVPKGVRlphesilnrlqwqwaTFPYTANEAVSVFKTALTFV----DSIAELWGPLM-------------CG 250
Cdd:PRK12406 157 MIYTSGTTGHPKGVR---------------RAAPTPEQAAAAEQMRALIYglkpGIRALLTGPLYhsapnayglragrLG 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 251 LAILVVPKAvtkDPQRLVALLERYKIRRLVLVPTLLRSLlmyLKMEGGGAAQKLLYNLQIWVCSGEPLSVSLASSFFDYF 330
Cdd:PRK12406 222 GVLVLQPRF---DPEELLQLIERHRITHMHMVPTMFIRL---LKLPEEVRAKYDVSSLRHVIHAAAPCPADVKRAMIEWW 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 331 DEGVhrlYNFYGSTEVlGDVTYfaCESKKQLSLYDNVpiGIPLSNTVVYLLDADYRPVKNGEIGEIFASglnlAAGYVN- 409
Cdd:PRK12406 296 GPVI---YEYYGSTES-GAVTF--ATSEDALSHPGTV--GKAAPGAELRFVDEDGRPLPQGEIGEIYSR----IAGNPDf 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 410 ---GRDPERflenpLAVEKkyARLYRTGDYGSL-KNGSIMYEGRTDSQVKIRGHRVDLSEVEKNVAELPLVDKAIVLCYH 485
Cdd:PRK12406 364 tyhNKPEKR-----AEIDR--GGFITSGDVGYLdADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIP 436
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 126789033 486 AGQVDQAILAFVKLRDDAPMvTEMQMEARLKDKLADYMTPQVV-ILEHVPLLVNGKVDRQALLKTY 550
Cdd:PRK12406 437 DAEFGEALMAVVEPQPGATL-DEADIRAQLKARLAGYKVPKHIeIMAELPREDSGKIFKRRLRDPY 501
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
86-543 |
2.09e-13 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 74.06 E-value: 2.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 86 GDfIVAVCMQPSEGLVTTLLAIWKAGGAYLPIDPSFPANRIHHILLEAKPTLVIRDDDIDagrfQGTPTLSTTELYAKSL 165
Cdd:PLN02860 57 GD-VVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFEEAKSAMLLVRPVMLVTDETCS----SWYEELQNDRLPSLMW 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 166 QL-----------AGSNLLSEEMLRG------------GNDHIAIVLYTSGSTGVPKGVRLPHESILNRLQWQWATFPYT 222
Cdd:PLN02860 132 QVflespsssvfiFLNSFLTTEMLKQralgtteldyawAPDDAVLICFTSGTTGRPKGVTISHSALIVQSLAKIAIVGYG 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 223 ANEaVSVFKTALTFVDSIAELWGPLMCGLAILVVPKAvtkDPQRLVALLERYKIRRLVLVPTLLRSLLMYLKMEGGGAAQ 302
Cdd:PLN02860 212 EDD-VYLHTAPLCHIGGLSSALAMLMVGACHVLLPKF---DAKAALQAIKQHNVTSMITVPAMMADLISLTRKSMTWKVF 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 303 KLLYNLqiwVCSGEPLSVSLASSFFDYFDEGvhRLYNFYGSTEVLGDVTYFA-----CESKKQL------------SLYD 365
Cdd:PLN02860 288 PSVRKI---LNGGGSLSSRLLPDAKKLFPNA--KLFSAYGMTEACSSLTFMTlhdptLESPKQTlqtvnqtksssvHQPQ 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 366 NVPIGIPLSNTVVYL-LDADYRpvkngeIGEIFASGLNLAAGYvngrdperFLENPLAVEKKYARLY-RTGDYGSL-KNG 442
Cdd:PLN02860 363 GVCVGKPAPHVELKIgLDESSR------VGRILTRGPHVMLGY--------WGQNSETASVLSNDGWlDTGDIGWIdKAG 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 443 SIMYEGRTDSQVKIRGHRVDLSEVEKNVAELPLVDKAIVLCYHAGQVDQAILAFVKLRD------------DAPMV---T 507
Cdd:PLN02860 429 NLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVACVRLRDgwiwsdnekenaKKNLTlssE 508
|
490 500 510
....*....|....*....|....*....|....*...
gi 126789033 508 EMQMEARLKdKLADYMTPQVVIL--EHVPLLVNGKVDR 543
Cdd:PLN02860 509 TLRHHCREK-NLSRFKIPKLFVQwrKPFPLTTTGKIRR 545
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
185-543 |
8.14e-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: 70.75 E-value: 8.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 185 IAIVLYTSGSTGVPKGVRLPHES------ILNRLQWQWatfpytANEAVSVFKTALTFvdSIAELWGPLMCGLAILVVPK 258
Cdd:cd17635 3 PLAVIFTSGTTGEPKAVLLANKTffavpdILQKEGLNW------VVGDVTYLPLPATH--IGGLWWILTCLIHGGLCVTG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 259 AVTKDPQRLVALLERYKIRRLVLVPTLLRSLLMYLKmegggAAQKLLYNLQIWVCSGEpLSVSLASSFFDYFdeGVHRLY 338
Cdd:cd17635 75 GENTTYKSLFKILTTNAVTTTCLVPTLLSKLVSELK-----SANATVPSLRLIGYGGS-RAIAADVRFIEAT--GLTNTA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 339 NFYGSTEvlgdvTYFACESKKQLSLYDNVPIGIPLSNTVVYLLDADYRPVKNGEIGEIFASGLNLAAGYVNG--RDPERF 416
Cdd:cd17635 147 QVYGLSE-----TGTALCLPTDDDSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNpeRTAEVL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 417 LENPLavekkyarlyRTGDYGSLKNGSIMY-EGRTDSQVKIRGHRVDLSEVEKNVAELPLVDKAIvlCY-----HAGQVd 490
Cdd:cd17635 222 IDGWV----------NTGDLGERREDGFLFiTGRSSESINCGGVKIAPDEVERIAEGVSGVQECA--CYeisdeEFGEL- 288
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 126789033 491 qAILAFVKLRDDAPMVTEMQMEaRLKDKLADYMTPQ-VVILEHVPLLVNGKVDR 543
Cdd:cd17635 289 -VGLAVVASAELDENAIRALKH-TIRRELEPYARPStIVIVTDIPRTQSGKVKR 340
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
136-546 |
1.12e-12 |
|
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: 71.40 E-value: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 136 TLVIRDDDIDAGRFQGTPTLSTTELYAKslqLAGSNLLSEEMLRggNDHIAIVLYTSGSTGVPKGVRLPHESILNRLQWQ 215
Cdd:cd17642 142 TIIILDSKEDYKGYQCLYTFITQNLPPG---FNEYDFKPPSFDR--DEQVALIMNSSGSTGLPKGVQLTHKNIVARFSHA 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 216 W-ATFPYTANEAVSVFkTALTFVDSIA--ELWGPLMCGLAILVVPKAvtkDPQRLVALLERYKIRRLVLVPTLLRSLLMY 292
Cdd:cd17642 217 RdPIFGNQIIPDTAIL-TVIPFHHGFGmfTTLGYLICGFRVVLMYKF---EEELFLRSLQDYKVQSALLVPTLFAFFAKS 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 293 LKMEgggaaQKLLYNLQIWVCSGEPLSVSLASSFFDYFdeGVHRLYNFYGSTEVLGDVTYFACESKKQLSLYDNVPIgip 372
Cdd:cd17642 293 TLVD-----KYDLSNLHEIASGGAPLSKEVGEAVAKRF--KLPGIRQGYGLTETTSAILITPEGDDKPGAVGKVVPF--- 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 373 LSNTVVyllDADY-RPVKNGEIGEIFASGLNLAAGYVNgrDPERflENPLAVEKKYarlYRTGDYGSL-KNGSIMYEGRT 450
Cdd:cd17642 363 FYAKVV---DLDTgKTLGPNERGELCVKGPMIMKGYVN--NPEA--TKALIDKDGW---LHSGDIAYYdEDGHFFIVDRL 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 451 DSQVKIRGHRVDLSEVEKNVAELPLVDKAIVlcyhAGQVDQAI----LAFVKLRDDAPMVtemqmEARLKDKLADYMTPQ 526
Cdd:cd17642 433 KSLIKYKGYQVPPAELESILLQHPKIFDAGV----AGIPDEDAgelpAAVVVLEAGKTMT-----EKEVMDYVASQVSTA 503
|
410 420
....*....|....*....|....*.
gi 126789033 527 ------VVILEHVPLLVNGKVDRQAL 546
Cdd:cd17642 504 krlrggVKFVDEVPKGLTGKIDRRKI 529
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
181-494 |
1.56e-12 |
|
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: 70.85 E-value: 1.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 181 GNDHIAIVLYTSGSTGVPKGVRLPHESILNRLQWQWATFPYTANEAV--------SVFKTALTFVdsiaelwgpLMCGLA 252
Cdd:cd17640 86 DSDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQPGDRFlsilpiwhSYERSAEYFI---------FACGCS 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 253 ILVV-PKAVTKDpqrlvalLERYKIRRLVLVPTLLRSLL--MYLKMEGGGAAQKLLY-------NLQIWVCSGEPLSVSL 322
Cdd:cd17640 157 QAYTsIRTLKDD-------LKRVKPHYIVSVPRLWESLYsgIQKQVSKSSPIKQFLFlfflsggIFKFGISGGGALPPHV 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 323 assffDYFDE--GVHrLYNFYGSTEVLGDVTyfACESKKQLslydNVPIGIPLSNTVVYLLDADYR-PVKNGEIGEIFAS 399
Cdd:cd17640 230 -----DTFFEaiGIE-VLNGYGLTETSPVVS--ARRLKCNV----RGSVGRPLPGTEIKIVDPEGNvVLPPGEKGIVWVR 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 400 GLNLAAGYvngrdperfLENPLAVEKKYAR--LYRTGDYGSL-KNGSIMYEGRT-DSQVKIRGHRVDLSEVEKNVAELPL 475
Cdd:cd17640 298 GPQVMKGY---------YKNPEATSKVLDSdgWFNTGDLGWLtCGGELVLTGRAkDTIVLSNGENVEPQPIEEALMRSPF 368
|
330
....*....|....*....
gi 126789033 476 VDKAIVLcyhaGQvDQAIL 494
Cdd:cd17640 369 IEQIMVV----GQ-DQKRL 382
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
20-546 |
1.80e-12 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 70.87 E-value: 1.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 20 RALHRIFEEQQLRHADKVALIYQPSTtgqGMApSQSSYRQMNERANRAARLlvaethgrFLQPNSDGDFIVAVCMQPSEG 99
Cdd:PRK08008 7 QHLRQMWDDLADVYGHKTALIFESSG---GVV-RRYSYLELNEEINRTANL--------FYSLGIRKGDKVALHLDNCPE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 100 LVTTLLAIWKAGGAYLPIDPSFPANRIHHILLEAKPTLV------------IRDDD---------IDAGRFQGTPTLSTT 158
Cdd:PRK08008 75 FIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLvtsaqfypmyrqIQQEDatplrhiclTRVALPADDGVSSFT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 159 ELYAK-SLQLAGSNLLSeemlrggNDHIAIVLYTSGSTGVPKGVRLPHESIL---NRLQWQWA---------TFP----- 220
Cdd:PRK08008 155 QLKAQqPATLCYAPPLS-------TDDTAEILFTSGTTSRPKGVVITHYNLRfagYYSAWQCAlrdddvyltVMPafhid 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 221 YTANEAVSVFKTALTFVdsiaelwgplmcglailvvpkavtkdpqrlvaLLERYKIRRL------------VLVPTLLRS 288
Cdd:PRK08008 228 CQCTAAMAAFSAGATFV--------------------------------LLEKYSARAFwgqvckyratitECIPMMIRT 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 289 LLMYLKM--EGGGAAQKLLYNLqiwvcsgePLSVSLASSFFDYFdeGVhRLYNFYGSTE----VLGDvtyFACESKKQLS 362
Cdd:PRK08008 276 LMVQPPSanDRQHCLREVMFYL--------NLSDQEKDAFEERF--GV-RLLTSYGMTEtivgIIGD---RPGDKRRWPS 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 363 lydnvpIGIPLSNTVVYLLDADYRPVKNGEIGEIFASGlnlaagyVNGRDP-ERFLENPLAVEKKYAR---LYrTGDYGS 438
Cdd:PRK08008 342 ------IGRPGFCYEAEIRDDHNRPLPAGEIGEICIKG-------VPGKTIfKEYYLDPKATAKVLEAdgwLH-TGDTGY 407
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 439 L-KNGSIMYEGRTDSQVKIRGHRVDLSEVEKNVAELPLVDKAIVLCYHAGQVDQAILAFVKLRDDApMVTEMQMEARLKD 517
Cdd:PRK08008 408 VdEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGE-TLSEEEFFAFCEQ 486
|
570 580 590
....*....|....*....|....*....|
gi 126789033 518 KLADYMTPQVV-ILEHVPLLVNGKVDRQAL 546
Cdd:PRK08008 487 NMAKFKVPSYLeIRKDLPRNCSGKIIKKNL 516
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
56-546 |
1.84e-12 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 70.29 E-value: 1.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 56 SYRQMNERANRAARLLVAETHGRflqpnsdGDFIVAVCMQPSEgLVTTLLAIWKAGGAYLPIDPSFPANRIHHILLEAKP 135
Cdd:cd05974 2 SFAEMSARSSRVANFLRSIGVGR-------GDRILLMLGNVVE-LWEAMLAAMKLGAVVIPATTLLTPDDLRDRVDRGGA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 136 TLVIRDDDIDAgrfqgtptlsttelyakslqlagsnllSEEMLrggndhiaiVLYTSGSTGVPKGVRLPHESI----LNR 211
Cdd:cd05974 74 VYAAVDENTHA---------------------------DDPML---------LYFTSGTTSKPKLVEHTHRSYpvghLST 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 212 LQW--------QW-ATFPYTANEAVSVFktaltfvdsiaelWGPLMCGLAILVVPKAvTKDPQRLVALLERYKIRRLVLV 282
Cdd:cd05974 118 MYWiglkpgdvHWnISSPGWAKHAWSCF-------------FAPWNAGATVFLFNYA-RFDAKRVLAALVRYGVTTLCAP 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 283 PTLLRsllMYLKMEGGGAAQKLlynlQIWVCSGEPLSVSLAssffdyfdEGVHRLYNF-----YGSTEVLGDVTYFACES 357
Cdd:cd05974 184 PTVWR---MLIQQDLASFDVKL----REVVGAGEPLNPEVI--------EQVRRAWGLtirdgYGQTETTALVGNSPGQP 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 358 KKQLSLydnvpiGIPLSNTVVYLLDADYRPVKNGEIGEIFASG--LNLAAGYVNgrDPERFLEnplAVEKKYarlYRTGD 435
Cdd:cd05974 249 VKAGSM------GRPLPGYRVALLDPDGAPATEGEVALDLGDTrpVGLMKGYAG--DPDKTAH---AMRGGY---YRTGD 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 436 YGSL-KNGSIMYEGRTDSQVKIRGHRVDLSEVEKNVAELPLVDKAIVLCYHAGQVDQAILAFVKLRDDAPMVTEMQME-- 512
Cdd:cd05974 315 IAMRdEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGYEPSPETALEif 394
|
490 500 510
....*....|....*....|....*....|....
gi 126789033 513 ARLKDKLADYMTPQVVILEHVPLLVNGKVDRQAL 546
Cdd:cd05974 395 RFSRERLAPYKRIRRLEFAELPKTISGKIRRVEL 428
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
33-541 |
2.00e-12 |
|
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: 70.41 E-value: 2.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 33 HADKVALIYqpsttgqgmAPSQSSYRQMNERANRAARLLVAETHGRflqpnsdGDfIVAVCMQPSEGLVTTLLAIWKAGG 112
Cdd:cd12118 17 YPDRTSIVY---------GDRRYTWRQTYDRCRRLASALAALGISR-------GD-TVAVLAPNTPAMYELHFGVPMAGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 113 AYLPIDPSFPANRIHHILLEAKPTLVIRD-----DDIDAGrfqGTPtlsttelyakslqlagsnllSEEMLRGGNDHIAI 187
Cdd:cd12118 80 VLNALNTRLDAEEIAFILRHSEAKVLFVDrefeyEDLLAE---GDP--------------------DFEWIPPADEWDPI 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 188 VL-YTSGSTGVPKGVRLPHE-----SILNRLQWQ--------WaTFP-YTANeavsvfktALTFVdsiaelWGPLMCGLA 252
Cdd:cd12118 137 ALnYTSGTTGRPKGVVYHHRgaylnALANILEWEmkqhpvylW-TLPmFHCN--------GWCFP------WTVAAVGGT 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 253 ILVVPKAvtkDPQRLVALLERYKIRRLVLVPTLLRSLLMYLKMEgggaAQKLLYNLQIWVCSGEPLSVSLASsffdyFDE 332
Cdd:cd12118 202 NVCLRKV---DAKAIYDLIEKHKVTHFCGAPTVLNMLANAPPSD----ARPLPHRVHVMTAGAPPPAAVLAK-----MEE 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 333 GVHRLYNFYGSTEVLGDVTyfACESKKQlslYDNVPI----------GIP-LSNTVVYLLDAD-YRPV-KNGE-IGEIFA 398
Cdd:cd12118 270 LGFDVTHVYGLTETYGPAT--VCAWKPE---WDELPTeerarlkarqGVRyVGLEEVDVLDPEtMKPVpRDGKtIGEIVF 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 399 SGLNLAAGYvngrdperfLENPLAVEKKYAR-LYRTGDYGSLK-NGSIMYEGRTDSQVKIRGHRVDLSEVEKNVAELPLV 476
Cdd:cd12118 345 RGNIVMKGY---------LKNPEATAEAFRGgWFHSGDLAVIHpDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAV 415
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 126789033 477 DKAIVLCY---HAGQVdqaILAFVKLRDDApMVTEMQMEARLKDKLADYMTPQVVILEHVPLLVNGKV 541
Cdd:cd12118 416 LEAAVVARpdeKWGEV---PCAFVELKEGA-KVTEEEIIAFCREHLAGFMVPKTVVFGELPKTSTGKI 479
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
176-557 |
2.19e-12 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 70.45 E-value: 2.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 176 EMLRGGNDHIAIVLYTSGSTGVPKGVRLPHESILNR--LQWQWAtfpYTANEAVSVFKTALTF-----VDSIAELwgPLM 248
Cdd:PRK06710 199 EVPCDPENDLALLQYTGGTTGFPKGVMLTHKNLVSNtlMGVQWL---YNCKEGEEVVLGVLPFfhvygMTAVMNL--SIM 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 249 CGLAILVVPKAvtkDPQRLVALLERYKIRRLVLVPTLLRSLLMYLKMEgggaaQKLLYNLQIWVCSGEPLSVSLASSfFD 328
Cdd:PRK06710 274 QGYKMVLIPKF---DMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLK-----EYDISSIRACISGSAPLPVEVQEK-FE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 329 YFDEGvhRLYNFYGSTEVlGDVTY--FACESKkqlslydnVP--IGIPLSNTVVYLLDADYRPV-KNGEIGEIFASGLNL 403
Cdd:PRK06710 345 TVTGG--KLVEGYGLTES-SPVTHsnFLWEKR--------VPgsIGVPWPDTEAMIMSLETGEAlPPGEIGEIVVKGPQI 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 404 AAGYVNgrDPErflENPLAVEKKYarlYRTGDYGSLKNGSIMY-EGRTDSQVKIRGHRVDLSEVEKNVAELPLVDKAIVL 482
Cdd:PRK06710 414 MKGYWN--KPE---ETAAVLQDGW---LHTGDVGYMDEDGFFYvKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTI 485
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 126789033 483 CYHAGQVDQAILAFVKLRDDApMVTEMQMEARLKDKLADYMTPQVV-ILEHVPLLVNGKVDRQALLKTYETANNNE 557
Cdd:PRK06710 486 GVPDPYRGETVKAFVVLKEGT-ECSEEELNQFARKYLAAYKVPKVYeFRDELPKTTVGKILRRVLIEEEKRKNEDE 560
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
32-415 |
2.75e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 70.11 E-value: 2.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 32 RHADKVALIyqpsttgqgMAPSQSS--YRQMNERANRAARLLvaETHGrfLQPnsdGDFiVAVCMQPSEGLVTTLLAIWK 109
Cdd:PRK13391 9 TTPDKPAVI---------MASTGEVvtYRELDERSNRLAHLF--RSLG--LKR---GDH-VAIFMENNLRYLEVCWAAER 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 110 AGGAYLPIDPSFPANRIHHILLEAKPTLVI---RDDDIDAGRFQGTPTLSTTELYAKSLQLAGSNLLSEEMLRGGNDHIA 186
Cdd:PRK13391 72 SGLYYTCVNSHLTPAEAAYIVDDSGARALItsaAKLDVARALLKQCPGVRHRLVLDGDGELEGFVGYAEAVAGLPATPIA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 187 ------IVLYTSGSTGVPKGVR--LPHESILNRLqwqwatfPYTAneavsVFKTALTFVD-----SIAELW--GPL-MCG 250
Cdd:PRK13391 152 deslgtDMLYSSGTTGRPKGIKrpLPEQPPDTPL-------PLTA-----FLQRLWGFRSdmvylSPAPLYhsAPQrAVM 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 251 LAILVVPKAV---TKDPQRLVALLERYKIRRLVLVPTllrsllMYLKMEGGGAAQKLLYN---LQIWVCSGEPLSVSLAS 324
Cdd:PRK13391 220 LVIRLGGTVIvmeHFDAEQYLALIEEYGVTHTQLVPT------MFSRMLKLPEEVRDKYDlssLEVAIHAAAPCPPQVKE 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 325 SFFDYFDEGVHRlynFYGSTEVLGdVTyfACESKKQLSLYDNVpiGIPLSNtVVYLLDADYRPVKNGEIGEI-FASGLNL 403
Cdd:PRK13391 294 QMIDWWGPIIHE---YYAATEGLG-FT--ACDSEEWLAHPGTV--GRAMFG-DLHILDDDGAELPPGEPGTIwFEGGRPF 364
|
410
....*....|..
gi 126789033 404 AagYVNgrDPER 415
Cdd:PRK13391 365 E--YLN--DPAK 372
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
181-546 |
3.20e-12 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 69.84 E-value: 3.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 181 GNDHIAIVLYTSGSTGVPKGVRLPHESILNRLQWQWATFPYTANEAVSVFKT---ALTFvDSIAELwgPLMCGLAilVVP 257
Cdd:PRK06334 181 DPEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLPpfhAYGF-NSCTLF--PLLSGVP--VVF 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 258 KAVTKDPQRLVALLERYKIRRLVLVPTLLRSLLMYLKMEGGGaaqklLYNLQIWVCSGEPLSVSLASSFFDYFDEGVhrL 337
Cdd:PRK06334 256 AYNPLYPKKIVEMIDEAKVTFLGSTPVFFDYILKTAKKQESC-----LPSLRFVVIGGDAFKDSLYQEALKTFPHIQ--L 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 338 YNFYGSTEVLGDVTYFACESKKQLSLydnvpIGIPLSNTVVYLLDAD-YRPVKNGEIGEIFASGLNLAAGYVnGRDPERF 416
Cdd:PRK06334 329 RQGYGTTECSPVITINTVNSPKHESC-----VGMPIRGMDVLIVSEEtKVPVSSGETGLVLTRGTSLFSGYL-GEDFGQG 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 417 LenplaVEKKYARLYRTGDYGSL-KNGSIMYEGRTDSQVKIRGHRVDLSEVEKNVAE---LPLVDKAI--VLCYHAGQVD 490
Cdd:PRK06334 403 F-----VELGGETWYVTGDLGYVdRHGELFLKGRLSRFVKIGAEMVSLEALESILMEgfgQNAADHAGplVVCGLPGEKV 477
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 126789033 491 QAILaFVKLRDDAPMVTEMQMEARLKDKLADYMTPQVvilEHVPLLVNGKVDRQAL 546
Cdd:PRK06334 478 RLCL-FTTFPTSISEVNDILKNSKTSSILKISYHHQV---ESIPMLGTGKPDYCSL 529
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
56-546 |
3.20e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 69.84 E-value: 3.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 56 SYRQMNERANRAARLLvaETHGrflqpNSDGDFIvAVCMQPSEGLVTTLLAIWKAGGAYLPIDPSFPANRIHHILLEAKP 135
Cdd:PRK09088 24 TYAELDALVGRLAAVL--RRRG-----CVDGERL-AVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 136 TLVIRDDDIDAGRFQGTpTLSTTELYAKSLQLAgsnllseEMLRGGNDHIAIVLYTSGSTGVPKGVRLPHESilnrLQWQ 215
Cdd:PRK09088 96 RLLLGDDAVAAGRTDVE-DLAAFIASADALEPA-------DTPSIPPERVSLILFTSGTSGQPKGVMLSERN----LQQT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 216 WATFPYTAN-EAVSVFKT-ALTF--VDSIAELWGPLMCGLAILVVPKAvtkDPQRLVALL--ERYKIRRLVLVPTLLRsl 289
Cdd:PRK09088 164 AHNFGVLGRvDAHSSFLCdAPMFhiIGLITSVRPVLAVGGSILVSNGF---EPKRTLGRLgdPALGITHYFCVPQMAQ-- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 290 lMYLKMEGGGAAQklLYNLQIWVCSGEPlsvSLASSFFDYFDEGVhRLYNFYGSTE---VLG---DVTYFACESKKQlsl 363
Cdd:PRK09088 239 -AFRAQPGFDAAA--LRHLTALFTGGAP---HAAEDILGWLDDGI-PMVDGFGMSEagtVFGmsvDCDVIRAKAGAA--- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 364 ydnvpiGIPLSNTVVYLLDADYRPVKNGEIGEIFASGLNLAAGYvnGRDPERFLENPLAvekkyARLYRTGDYGSLK-NG 442
Cdd:PRK09088 309 ------GIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGY--WRRPQATARAFTG-----DGWFRTGDIARRDaDG 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 443 SIMYEGRTDSQVKIRGHRVDLSEVEKNVAELPLVDKAIVLCYHAGQVDQAILAFVKLRDDAPMVTEmQMEARLKDKLADY 522
Cdd:PRK09088 376 FFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAPLDLE-RIRSHLSTRLAKY 454
|
490 500
....*....|....*....|....*
gi 126789033 523 MTPQ-VVILEHVPLLVNGKVDRQAL 546
Cdd:PRK09088 455 KVPKhLRLVDALPRTASGKLQKARL 479
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
19-214 |
1.22e-11 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 68.36 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 19 PRALHRIFEEQQLRHADKVALIYQPSTTgqgmapsqsSYRQMNERANRAARLLVAETHGRflqpnsdGDfIVAVCMQPSE 98
Cdd:PRK08279 36 KRSLGDVFEEAAARHPDRPALLFEDQSI---------SYAELNARANRYAHWAAARGVGK-------GD-VVALLMENRP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 99 GLVTTLLAIWKAGGAYLPIDPSFPANRIHHILLEAKPTLVIRDDDID------------------AGRFQGTPTLSTTEL 160
Cdd:PRK08279 99 EYLAAWLGLAKLGAVVALLNTQQRGAVLAHSLNLVDAKHLIVGEELVeafeearadlarpprlwvAGGDTLDDPEGYEDL 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 126789033 161 YAKSLQLAGSNLLSEEMLRGgnDHIAIVLYTSGSTGVPKGVRLPHESILNRLQW 214
Cdd:PRK08279 179 AAAAAGAPTTNPASRSGVTA--KDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGG 230
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
35-548 |
2.82e-11 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 66.91 E-value: 2.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 35 DKVALIYQPSttgqgmapsQSSYRQMNERANRAArllvaethGRFLQPNSDGDFIVAVCMQPSEGLVTTLLAIWKAGGAY 114
Cdd:PRK03640 17 DRTAIEFEEK---------KVTFMELHEAVVSVA--------GKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 115 LPIDPSFPANRIHHILLEAKPTLVIRDDDIDAGRFQGTPTLsTTELYAKSLQLAgsNLLSEEMLrggnDHIAIVLYTSGS 194
Cdd:PRK03640 80 VLLNTRLSREELLWQLDDAEVKCLITDDDFEAKLIPGISVK-FAELMNGPKEEA--EIQEEFDL----DEVATIMYTSGT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 195 TGVPKGVRLPHE--------SILNrlqwqwatFPYTANE----AVSVFKtaltfVDSIAELWGPLMCGLAILVVPKAvtk 262
Cdd:PRK03640 153 TGKPKGVIQTYGnhwwsavgSALN--------LGLTEDDcwlaAVPIFH-----ISGLSILMRSVIYGMRVVLVEKF--- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 263 DPQRLVALLERYKIRRLVLVPTLLRSLLMYLKME-----------GGGAAQKLLynLQIWVCSGEPLsvslassffdyfd 331
Cdd:PRK03640 217 DAEKINKLLQTGGVTIISVVSTMLQRLLERLGEGtypssfrcmllGGGPAPKPL--LEQCKEKGIPV------------- 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 332 egvhrlYNFYGSTEVLGDVTYFACES--KKQLSlydnvpIGIPLSNTVVYLLDaDYRPVKNGEIGEIFASGLNLAAGYVN 409
Cdd:PRK03640 282 ------YQSYGMTETASQIVTLSPEDalTKLGS------AGKPLFPCELKIEK-DGVVVPPFEEGEIVVKGPNVTKGYLN 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 410 GRDPER--FLENPLavekkyarlyRTGDYGSLKNGSIMYegrtdsqvkIRGHRVDL----------SEVEKNVAELPLVD 477
Cdd:PRK03640 349 REDATRetFQDGWF----------KTGDIGYLDEEGFLY---------VLDRRSDLiisggeniypAEIEEVLLSHPGVA 409
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 126789033 478 KAIVlcyhAGQVD----QAILAFVKLrdDAPmVTEMQMEARLKDKLADYMTP-QVVILEHVPLLVNGKVDRQALLK 548
Cdd:PRK03640 410 EAGV----VGVPDdkwgQVPVAFVVK--SGE-VTEEELRHFCEEKLAKYKVPkRFYFVEELPRNASGKLLRHELKQ 478
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
178-553 |
7.50e-11 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 64.68 E-value: 7.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 178 LRGG---NDHIAIVLYTSGSTGVPKGVRLP-----------HESILNRLQWQWATFPYtaneavsvfktaltfvdSIAel 243
Cdd:PRK07824 27 LRVGepiDDDVALVVATSGTTGTPKGAMLTaaaltasadatHDRLGGPGQWLLALPAH-----------------HIA-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 244 wgplmcGLAILV-------VPKAVTK----DPQRLVALLERYKI-RRLV-LVPTLLrsllmyLKMEGGGAAQKLLYNLQI 310
Cdd:PRK07824 88 ------GLQVLVrsviagsEPVELDVsagfDPTALPRAVAELGGgRRYTsLVPMQL------AKALDDPAATAALAELDA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 311 WVCSGEPLSVSLASSffdYFDEGVhRLYNFYGSTEVLGdvtyfACeskkqlsLYDnvpiGIPLSNTVVYLLDadyrpvkn 390
Cdd:PRK07824 156 VLVGGGPAPAPVLDA---AAAAGI-NVVRTYGMSETSG-----GC-------VYD----GVPLDGVRVRVED-------- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 391 geiGEIFASGLNLAAGYVNGRDPERFLEnplavekkyARLYRTGDYGSLKNGSIMYEGRTDSQVKIRGHRVDLSEVEKNV 470
Cdd:PRK07824 208 ---GRIALGGPTLAKGYRNPVDPDPFAE---------PGWFRTDDLGALDDGVLTVLGRADDAISTGGLTVLPQVVEAAL 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 471 AELPLVDKAIVLCYHAGQVDQAILAFVkLRDDAPMVTEMQMEARLKDKLADYMTP-QVVILEHVPLLVNGKVDRQALLKT 549
Cdd:PRK07824 276 ATHPAVADCAVFGLPDDRLGQRVVAAV-VGDGGPAPTLEALRAHVARTLDRTAAPrELHVVDELPRRGIGKVDRRALVRR 354
|
....
gi 126789033 550 YETA 553
Cdd:PRK07824 355 FAGE 358
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
336-543 |
1.45e-10 |
|
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: 63.83 E-value: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 336 RLYNFYGSTEVLGDVTyfaceskkqLSLYDNVP--IGIPLSNTVVYLLDADYRPVKNGEIGEIFASGLNLAAGYVNGRDp 413
Cdd:cd17637 138 TFWSLYGQTETSGLVT---------LSPYRERPgsAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPE- 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 414 erflENplavekkyARLYR-----TGDYGSL-KNGSIMYEGRTDSQ--VKIRGHRVDLSEVEKNVAELPLVDKAIVLCYH 485
Cdd:cd17637 208 ----LT--------AYTFRngwhhTGDLGRFdEDGYLWYAGRKPEKelIKPGGENVYPAEVEKVILEHPAIAEVCVIGVP 275
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 126789033 486 AGQVDQAILAFVKLRDDApMVTEMQMEARLKDKLADYMTPQ-VVILEHVPLLVNGKVDR 543
Cdd:cd17637 276 DPKWGEGIKAVCVLKPGA-TLTADELIEFVGSRIARYKKPRyVVFVEALPKTADGSIDR 333
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
183-548 |
2.11e-10 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 64.38 E-value: 2.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 183 DHIAIVLYTSGSTGVPKGVRLPHESILnrlqwqwatfpytANEAVSVFKTALTFVDSIaelWGPLMCGLA---------- 252
Cdd:PRK06087 187 DELAAVLFTSGTEGLPKGVMLTHNNIL-------------ASERAYCARLNLTWQDVF---MMPAPLGHAtgflhgvtap 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 253 ILVVPKAVTKD---PQRLVALLERYKIRRLVLVPTLLRSLLMYLKmegggAAQKLLYNLQIWVCSGEPLSVSLASsffDY 329
Cdd:PRK06087 251 FLIGARSVLLDiftPDACLALLEQQRCTCMLGATPFIYDLLNLLE-----KQPADLSALRFFLCGGTTIPKKVAR---EC 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 330 FDEGVhRLYNFYGSTEvlgDVTYFACESKKQLSLYDNVPiGIPLSNTVVYLLDADYRPVKNGEIGEIFASGLNLAAGYVN 409
Cdd:PRK06087 323 QQRGI-KLLSVYGSTE---SSPHAVVNLDDPLSRFMHTD-GYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLD 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 410 grDPERflenplavekkYARL------YRTGDYGSL-KNGSIMYEGRTdSQVKIR-GHRVDLSEVEKNVAELPLVDKAIV 481
Cdd:PRK06087 398 --EPEL-----------TARAldeegwYYSGDLCRMdEAGYIKITGRK-KDIIVRgGENISSREVEDILLQHPKIHDACV 463
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 126789033 482 LCYHAGQVDQAILAFVKLRDDAPMVTEMQMEARL-KDKLADYMTPQ-VVILEHVPLLVNGKVDRQALLK 548
Cdd:PRK06087 464 VAMPDERLGERSCAYVVLKAPHHSLTLEEVVAFFsRKRVAKYKYPEhIVVIDKLPRTASGKIQKFLLRK 532
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
181-546 |
3.30e-10 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 63.50 E-value: 3.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 181 GNDHIAIVLYTSGSTGVPKGVRLPHESIL-NRLQ---WQWATFPYTANEAVSVFKTAL----TFVDSIAELWGPLMCGLA 252
Cdd:PRK07059 202 GPDDVAFLQYTGGTTGVSKGATLLHRNIVaNVLQmeaWLQPAFEKKPRPDQLNFVCALplyhIFALTVCGLLGMRTGGRN 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 253 ILVvpkAVTKDPQRLVALLERYKIRRLVLVPTLLRSLL------------MYLKMEGGGAAQKLLYNLqiWV-CSGEPLS 319
Cdd:PRK07059 282 ILI---PNPRDIPGFIKELKKYQVHIFPAVNTLYNALLnnpdfdkldfskLIVANGGGMAVQRPVAER--WLeMTGCPIT 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 320 vslassffdyfdEGvhrlynfYGSTEVLGDVTYFACESKKQlslydNVPIGIPLSNTVVYLLDADYRPVKNGEIGEIFAS 399
Cdd:PRK07059 357 ------------EG-------YGLSETSPVATCNPVDATEF-----SGTIGLPLPSTEVSIRDDDGNDLPLGEPGEICIR 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 400 GLNLAAGYVNGRDperflENPLAVEKKyaRLYRTGDYGSL-KNGSIMYEGRTDSQVKIRGHRVDLSEVEKNVAELPLVDK 478
Cdd:PRK07059 413 GPQVMAGYWNRPD-----ETAKVMTAD--GFFRTGDVGVMdERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLE 485
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 126789033 479 AIVLCYHAGQVDQAILAFVKLRDdaPMVTEMQMEARLKDKLADYMTPQVV-ILEHVPLLVNGKVDRQAL 546
Cdd:PRK07059 486 VAAVGVPDEHSGEAVKLFVVKKD--PALTEEDVKAFCKERLTNYKRPKFVeFRTELPKTNVGKILRREL 552
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
184-562 |
4.15e-10 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 63.61 E-value: 4.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 184 HIAIVLYTSGSTGVPKGVRLPHESILNRLQWQWATFPYTANEAVSVFKTALTFVDSIAELWGPLMCGLAILVVPKAVTKD 263
Cdd:PTZ00237 255 HPLYILYTSGTTGNSKAVVRSNGPHLVGLKYYWRSIIEKDIPTVVFSHSSIGWVSFHGFLYGSLSLGNTFVMFEGGIIKN 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 264 PQ---RLVALLERYKIRRLVLVPTLLRSLLmylKMEGGGAAQKLLYNL----QIWvCSGEPLSVSLAssffDYFDEGVH- 335
Cdd:PTZ00237 335 KHiedDLWNTIEKHKVTHTLTLPKTIRYLI---KTDPEATIIRSKYDLsnlkEIW-CGGEVIEESIP----EYIENKLKi 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 336 RLYNFYGSTEvlGDVTYFACESKKQLSLYdnvPIGIPLSNTVVYLLDADYRPVKNGEIGEIfASGLNLAAGYVNgrdpeR 415
Cdd:PTZ00237 407 KSSRGYGQTE--IGITYLYCYGHINIPYN---ATGVPSIFIKPSILSEDGKELNVNEIGEV-AFKLPMPPSFAT-----T 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 416 FLENPLAVEK---KYARLYRTGDYG-SLKNGSIMYEGRTDSQVKIRGHRVDLSEVEKNVAELPLVdkaIVLC----YHAG 487
Cdd:PTZ00237 476 FYKNDEKFKQlfsKFPGYYNSGDLGfKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLV---LECCsigiYDPD 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 488 QVDQAI-LAFVKLRDDAPMVTEMQMEARLKDKLADYMTP-----QVVILEHVPLLVNGKVDRQALLKTYETAN----NNE 557
Cdd:PTZ00237 553 CYNVPIgLLVLKQDQSNQSIDLNKLKNEINNIITQDIESlavlrKIIIVNQLPKTKTGKIPRQIISKFLNDSNyqlpDNV 632
|
....*
gi 126789033 558 GDSSI 562
Cdd:PTZ00237 633 NDSEI 637
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
32-541 |
5.12e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 62.75 E-value: 5.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 32 RHADKVALIyqpsttgqgMAPSQSSYRQMNERANRAARLLVAethgRFLQPnsdGDFIV---AVCMQpsegLVTTLLAIW 108
Cdd:PRK07470 19 RFPDRIALV---------WGDRSWTWREIDARVDALAAALAA----RGVRK---GDRILvhsRNCNQ----MFESMFAAF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 109 KAGGAYLPIDPSFPANRIHHILLEAKPTLVIRDDDidagrFQGtptlsttelYAKSLQLAGSNL---LSEEMLRGGNDHI 185
Cdd:PRK07470 79 RLGAVWVPTNFRQTPDEVAYLAEASGARAMICHAD-----FPE---------HAAAVRAASPDLthvVAIGGARAGLDYE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 186 AIV---------------------LYTSGSTGVPKGVRLPHES----ILNRLQwqwATFPYTANEAVSVFKTALTFVDSI 240
Cdd:PRK07470 145 ALVarhlgarvanaavdhddpcwfFFTSGTTGRPKAAVLTHGQmafvITNHLA---DLMPGTTEQDASLVVAPLSHGAGI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 241 AELwgplmCGLA---ILVVPKAVTKDPQRLVALLERYKIRRLVLVPTLLRSLLmylkmEGGGAAQKLLYNLQIWVCSGEP 317
Cdd:PRK07470 222 HQL-----CQVArgaATVLLPSERFDPAEVWALVERHRVTNLFTVPTILKMLV-----EHPAVDRYDHSSLRYVIYAGAP 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 318 LsvslassffdYFDEGVHRL-------YNFYGSTEVLGDVTYFAceskKQLSLYDNVP------IGIPLSNTVVYLLDAD 384
Cdd:PRK07470 292 M----------YRADQKRALaklgkvlVQYFGLGEVTGNITVLP----PALHDAEDGPdarigtCGFERTGMEVQIQDDE 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 385 YRPVKNGEIGEIFASGLNLAAGYVNgrdperfleNPLAVEKKYAR-LYRTGDYGSLKNGSIMY-EGRTdSQVKIR-GHRV 461
Cdd:PRK07470 358 GRELPPGETGEICVIGPAVFAGYYN---------NPEANAKAFRDgWFRTGDLGHLDARGFLYiTGRA-SDMYISgGSNV 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 462 DLSEVEKNVAELPLVDKAIVLCYHAGQVDQAILAFVKLRDDAPmVTEMQMEARLKDKLADYMTPQ-VVILEHVPLLVNGK 540
Cdd:PRK07470 428 YPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARDGAP-VDEAELLAWLDGKVARYKLPKrFFFWDALPKSGYGK 506
|
.
gi 126789033 541 V 541
Cdd:PRK07470 507 I 507
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
90-547 |
5.50e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 62.70 E-value: 5.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 90 VAVCMQPSeglVTTLLAI---WKAGGAYLPIDP-SFPANRiHHILLEAKPTLVIRDDDIDAGrfqGTPTLsTTELYAKSl 165
Cdd:PRK07787 48 VAVLATPT---LATVLAVvgaLIAGVPVVPVPPdSGVAER-RHILADSGAQAWLGPAPDDPA---GLPHV-PVRLHARS- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 166 qlagSNLLSEEmlrgGNDHIAIVLYTSGSTGVPKGVRLPHESI---LNRLQ--WQWatfpyTANEaVSVFKTALTFVDS- 239
Cdd:PRK07787 119 ----WHRYPEP----DPDAPALIVYTSGTTGPPKGVVLSRRAIaadLDALAeaWQW-----TADD-VLVHGLPLFHVHGl 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 240 IAELWGPLMCG--LAILVVPKavtkdPQRLVALLERyKIRRLVLVPTllrsllMYLKMEGGGAAQKLLYNLQIWVCSGEP 317
Cdd:PRK07787 185 VLGVLGPLRIGnrFVHTGRPT-----PEAYAQALSE-GGTLYFGVPT------VWSRIAADPEAARALRGARLLVSGSAA 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 318 LSVSLassfFDYFDEGV-HRLYNFYGSTEVLGDVTYFAceskkqlslyDNVP----IGIPLSNTVVYLLDADYRPV-KNG 391
Cdd:PRK07787 253 LPVPV----FDRLAALTgHRPVERYGMTETLITLSTRA----------DGERrpgwVGLPLAGVETRLVDEDGGPVpHDG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 392 E-IGEIFASGLNLAAGYVNgrdperfleNPLAVEKKYAR--LYRTGDYGSLK-NGSIMYEGR--TDsQVKIRGHRVDLSE 465
Cdd:PRK07787 319 EtVGELQVRGPTLFDGYLN---------RPDATAAAFTAdgWFRTGDVAVVDpDGMHRIVGResTD-LIKSGGYRIGAGE 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 466 VEKNVAELPLVDKAIVLcyhaGQVD----QAILAFVKLRDDAPmvtemqmEARLKDKLADYMTP-----QVVILEHVPLL 536
Cdd:PRK07787 389 IETALLGHPGVREAAVV----GVPDddlgQRIVAYVVGADDVA-------ADELIDFVAQQLSVhkrprEVRFVDALPRN 457
|
490
....*....|.
gi 126789033 537 VNGKVDRQALL 547
Cdd:PRK07787 458 AMGKVLKKQLL 468
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
32-561 |
5.61e-10 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 62.99 E-value: 5.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 32 RHA-----DKVALIYQPSTTGQgmapsQSSYRQMNERANRAARLLVAETHGRflqpnsdGD--FIVavcMQPSEGLVTTL 104
Cdd:PRK04319 51 RHAdggrkDKVALRYLDASRKE-----KYTYKELKELSNKFANVLKELGVEK-------GDrvFIF---MPRIPELYFAL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 105 LAIWKAGGAYLPIDPSF---P-ANRIHH----------ILLEAKP--------TLVIRDDDIDAGrfqgTPTLSttelYA 162
Cdd:PRK04319 116 LGALKNGAIVGPLFEAFmeeAvRDRLEDseakvlittpALLERKPaddlpslkHVLLVGEDVEEG----PGTLD----FN 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 163 KSLQLAGSNLLSEEMLRggnDHIAIVLYTSGSTGVPKGVRLPHESILnrLQWQwatfpyTAneavsvfKTALTF-VDSI- 240
Cdd:PRK04319 188 ALMEQASDEFDIEWTDR---EDGAILHYTSGSTGKPKGVLHVHNAML--QHYQ------TG-------KYVLDLhEDDVy 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 241 ---AE----------LWGPLMCGLAILVVpkAVTKDPQRLVALLERYKIRRLVLVPTLLRsllMYLKMeGGGAAQKllYN 307
Cdd:PRK04319 250 wctADpgwvtgtsygIFAPWLNGATNVID--GGRFSPERWYRILEDYKVTVWYTAPTAIR---MLMGA-GDDLVKK--YD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 308 LQI--WVCS-GEPLSvslassffdyfDEGVHrlynfYGStEVLG----DvTYFACESKKQL-SLYDNVPI-----GIPLS 374
Cdd:PRK04319 322 LSSlrHILSvGEPLN-----------PEVVR-----WGM-KVFGlpihD-NWWMTETGGIMiANYPAMDIkpgsmGKPLP 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 375 NTVVYLLDADYRPVKNGEIGeifasglNLAA---------GYVNgrDPERFlenplaveKKYAR--LYRTGDygSLK--- 440
Cdd:PRK04319 384 GIEAAIVDDQGNELPPNRMG-------NLAIkkgwpsmmrGIWN--NPEKY--------ESYFAgdWYVSGD--SAYmde 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 441 NGSIMYEGRTDSQVKIRGHRVDLSEVEKNVAELPLVDKAIVLcyhaGQVD----QAILAFVKLRDDAPMVTEMQMEARL- 515
Cdd:PRK04319 445 DGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVI----GKPDpvrgEIIKAFVALRPGYEPSEELKEEIRGf 520
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 126789033 516 -KDKLADYMTP-QVVILEHVPLLVNGKVDRQaLLKTYETaNNNEGDSS 561
Cdd:PRK04319 521 vKKGLGAHAAPrEIEFKDKLPKTRSGKIMRR-VLKAWEL-GLPEGDLS 566
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
11-546 |
8.13e-10 |
|
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: 62.47 E-value: 8.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 11 KGLQQDfvpRALHRIFEEQQLRHADKVALIYqpsttgqgmAPSQSSYRQMNERANRAARLLVAetHGrfLQPnsdGDfiV 90
Cdd:COG1021 19 AGYWRG---ETLGDLLRRRAERHPDRIAVVD---------GERRLSYAELDRRADRLAAGLLA--LG--LRP---GD--R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 91 AVCMQP-SEGLVTTLLAIWKAGGAylpidPSF--PANRIH---HILLEAKPTLVIRDDDID-------AGRFQ-GTPTLS 156
Cdd:COG1021 78 VVVQLPnVAEFVIVFFALFRAGAI-----PVFalPAHRRAeisHFAEQSEAVAYIIPDRHRgfdyralARELQaEVPSLR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 157 T-------------TELYAKSLQLAGSNLLSEEmlrggndhIAIVLYTSGSTGVPKGVRLPHESILnrlqwqwatfpYTA 223
Cdd:COG1021 153 HvlvvgdageftslDALLAAPADLSEPRPDPDD--------VAFFQLSGGTTGLPKLIPRTHDDYL-----------YSV 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 224 NEAV--------SVFKTALT----FVDSIAELWGPLMCGlAILVVpkAVTKDPQRLVALLERYKIRRLVLVPTLLrsLLM 291
Cdd:COG1021 214 RASAeicgldadTVYLAALPaahnFPLSSPGVLGVLYAG-GTVVL--APDPSPDTAFPLIERERVTVTALVPPLA--LLW 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 292 ylkMEGGGAAQKLLYNLQIWVCSGEPLSVSLASSFFDYFDegvHRLYNFYGSTEvlGDVTYfaceskkqLSLYDNVPI-- 369
Cdd:COG1021 289 ---LDAAERSRYDLSSLRVLQVGGAKLSPELARRVRPALG---CTLQQVFGMAE--GLVNY--------TRLDDPEEVil 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 370 ---GIPLS-NTVVYLLDADYRPVKNGEIGEIFASGLNLAAGY-----VNGR--DPERFlenplavekkyarlYRTGDYGS 438
Cdd:COG1021 353 ttqGRPISpDDEVRIVDEDGNPVPPGEVGELLTRGPYTIRGYyrapeHNARafTPDGF--------------YRTGDLVR 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 439 L-KNGSIMYEGRTDSQVkIR-GHRVDLSEVEKNVAELPLV-DKAIVlcyhaGQVDQA----ILAFVKLRDDAPMVTEMQ- 510
Cdd:COG1021 419 RtPDGYLVVEGRAKDQI-NRgGEKIAAEEVENLLLAHPAVhDAAVV-----AMPDEYlgerSCAFVVPRGEPLTLAELRr 492
|
570 580 590
....*....|....*....|....*....|....*...
gi 126789033 511 -MEARlkdKLADYMTP-QVVILEHVPLLVNGKVDRQAL 546
Cdd:COG1021 493 fLRER---GLAAFKLPdRLEFVDALPLTAVGKIDKKAL 527
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
4-641 |
2.11e-09 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 61.72 E-value: 2.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 4 LPqLSIVKGLQQdfvpRALHRifeeqqlrhADKVALIYQPSTTGQGMapsQSSYRQMNERANRAARLLvaETHGRFlqpn 83
Cdd:PRK05691 7 LP-LTLVQALQR----RAAQT---------PDRLALRFLADDPGEGV---VLSYRDLDLRARTIAAAL--QARASF---- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 84 sdGDfiVAVCMQPS-EGLVTTLLAIWKAGGAYLPIDPSfPANRIHH------ILLEAKPTLVIRDDD-------IDAGRF 149
Cdd:PRK05691 64 --GD--RAVLLFPSgPDYVAAFFGCLYAGVIAVPAYPP-ESARRHHqerllsIIADAEPRLLLTVADlrdsllqMEELAA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 150 QGTPTLstteLYAKSLQLAGSNLLSEEMLRGgnDHIAIVLYTSGSTGVPKGVRLPHESILNRLQWQWATFPYTANEAVSV 229
Cdd:PRK05691 139 ANAPEL----LCVDTLDPALAEAWQEPALQP--DDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGIDLNPDDVI 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 230 FKTALTFVDS--IAELWGPLMCGL-AILVVPKAVTKDPQRLVALLERYKiRRLVLVPTLLRSLLMYLKMEggGAAQKLly 306
Cdd:PRK05691 213 VSWLPLYHDMglIGGLLQPIFSGVpCVLMSPAYFLERPLRWLEAISEYG-GTISGGPDFAYRLCSERVSE--SALERL-- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 307 NLQIW--VCSG-EPLSVSLASSFFDYFDEGVHRLYNFYGSTEvLGDVTYFACESKK-----QLSLYDN------------ 366
Cdd:PRK05691 288 DLSRWrvAYSGsEPIRQDSLERFAEKFAACGFDPDSFFASYG-LAEATLFVSGGRRgqgipALELDAEalarnraepgtg 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 367 ---VPIGIPLSNTVVYLLDADYRPV-KNGEIGEIFASGLNLAAGYvngrdperfLENPLAVEKKYARL-----YRTGDYG 437
Cdd:PRK05691 367 svlMSCGRSQPGHAVLIVDPQSLEVlGDNRVGEIWASGPSIAHGY---------WRNPEASAKTFVEHdgrtwLRTGDLG 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 438 SLKNGSIMYEGRTDSQVKIRGHRVDLSEVEKNV-AELPLVDKAIVLCY---HAGQVDQAILAFVKlRDDAPMVTEMQMEA 513
Cdd:PRK05691 438 FLRDGELFVTGRLKDMLIVRGHNLYPQDIEKTVeREVEVVRKGRVAAFavnHQGEEGIGIAAEIS-RSVQKILPPQALIK 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 514 RLKDKLAD--YMTPQVVILEH---VPLLVNGKVDRQAllktyetANNNEGDSSivLDfDYSQVPEdLKLTARDLFETVGG 588
Cdd:PRK05691 517 SIRQAVAEacQEAPSVVLLLNpgaLPKTSSGKLQRSA-------CRLRLADGS--LD-SYALFPA-LQAVEAAQTAASGD 585
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 126789033 589 VIGRSTRA---------TLAPHSNFYELGGNSLNSIFTVTLLREK-GYNIGISEFIAAKNLGE 641
Cdd:PRK05691 586 ELQARIAAiwceqlkveQVAADDHFFLLGGNSIAATQVVARLRDElGIDLNLRQLFEAPTLAA 648
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
105-546 |
2.39e-09 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 60.80 E-value: 2.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 105 LAIWKAGGAYLPIDPSFPANRIHHILLEAKPTLVIRDDDIDA---------GRFQGTPTL---------STTELYAKSLQ 166
Cdd:PLN03102 82 FAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFVDRSFEPlarevlhllSSEDSNLNLpvifiheidFPKRPSSEELD 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 167 LAG-------SNLLSEEMLRGGNDHIAIVL-YTSGSTGVPKGVRLPHE-SILNRLQ----WQWATFPYTANEAVSVFKTA 233
Cdd:PLN03102 162 YECliqrgepTPSLVARMFRIQDEHDPISLnYTSGTTADPKGVVISHRgAYLSTLSaiigWEMGTCPVYLWTLPMFHCNG 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 234 LTFVDSIAELWGPLMCgLAILVVPKaVTKDpqrlvalLERYKIRRLVLVPTLLRSLLmylkmEGGGAAQKLLYNLQIWVC 313
Cdd:PLN03102 242 WTFTWGTAARGGTSVC-MRHVTAPE-IYKN-------IEMHNVTHMCCVPTVFNILL-----KGNSLDLSPRSGPVHVLT 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 314 SGEPLSVSLASSffdyfdegVHRL----YNFYGSTEVLGDVTYfaCESKKQLS-LYDNVPIGIPLSNTVVYLLDADYrPV 388
Cdd:PLN03102 308 GGSPPPAALVKK--------VQRLgfqvMHAYGLTEATGPVLF--CEWQDEWNrLPENQQMELKARQGVSILGLADV-DV 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 389 KNGE-----------IGEIFASGLNLAAGYvngrdperfLENPLAVEKKYARLY-RTGDYGSLK-NGSIMYEGRTDSQVK 455
Cdd:PLN03102 377 KNKEtqesvprdgktMGEIVIKGSSIMKGY---------LKNPKATSEAFKHGWlNTGDVGVIHpDGHVEIKDRSKDIII 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 456 IRGHRVDLSEVEKNVAELPLVDKAIVLCYHAGQVDQAILAFVKL---------RDDAPMVTEMQMEARLKDKLADYMTP- 525
Cdd:PLN03102 448 SGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLekgettkedRVDKLVTRERDLIEYCRENLPHFMCPr 527
|
490 500
....*....|....*....|.
gi 126789033 526 QVVILEHVPLLVNGKVDRQAL 546
Cdd:PLN03102 528 KVVFLQELPKNGNGKILKPKL 548
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
51-546 |
3.07e-09 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 60.82 E-value: 3.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 51 APSQSSYRQMNERANRAARLLvaetHGRFLqpnSDGDFIVaVCMQPSEGLVTTLLAIWKAGGAYLPIDPSFPANRIHHIL 130
Cdd:PRK06060 27 AADVVTHGQIHDGAARLGEVL----RNRGL---SSGDRVL-LCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 131 LEAKPTLVIRDDDIdAGRFQGTPTLSTTELYAKSLQLAGSNLlseEMLRGgnDHIAIVLYTSGSTGVPKGVRLPHESiln 210
Cdd:PRK06060 99 RNTEPALVVTSDAL-RDRFQPSRVAEAAELMSEAARVAPGGY---EPMGG--DALAYATYTSGTTGPPKAAIHRHAD--- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 211 rlqwqwatfPYTANEAVSVFKTALTFVD---SIAEL----------WGPLMCGLAILVVPKAVTKDPQRLVAllERYKIR 277
Cdd:PRK06060 170 ---------PLTFVDAMCRKALRLTPEDtglCSARMyfayglgnsvWFPLATGGSAVINSAPVTPEAAAILS--ARFGPS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 278 RLVLVPTLLRSLLmylkmegGGAAQKLLYNLQIWVCSGEPLSVSLASSFFDYFdeGVHRLYNFYGSTEVLGDVTYFACES 357
Cdd:PRK06060 239 VLYGVPNFFARVI-------DSCSPDSFRSLRCVVSAGEALELGLAERLMEFF--GGIPILDGIGSTEVGQTFVSNRVDE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 358 KKQLSLYDNVPigiPLSNTVVyllDADYRPVKNGEIGEIFASGLNLAAGYVNGrdPERFLENPLAVEKKyARLYRTGDyg 437
Cdd:PRK06060 310 WRLGTLGRVLP---PYEIRVV---APDGTTAGPGVEGDLWVRGPAIAKGYWNR--PDSPVANEGWLDTR-DRVCIDSD-- 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 438 slknGSIMYEGRTDSQVKIRGHRVDLSEVEKNVAELPLVDKAIVLCYHAGQVDQAILAFVklrddAPMVTEM-------Q 510
Cdd:PRK06060 379 ----GWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFL-----VATSGATidgsvmrD 449
|
490 500 510
....*....|....*....|....*....|....*..
gi 126789033 511 MEARLKDKLADYMTP-QVVILEHVPLLVNGKVDRQAL 546
Cdd:PRK06060 450 LHRGLLNRLSAFKVPhRFAVVDRLPRTPNGKLVRGAL 486
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
17-563 |
1.02e-08 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 58.62 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 17 FVP--RALHRIFEEQQLRHADKVALIYqpsttgqgmAPSQSSYRQMNERANRAARLLVAetHGrfLQPnsdGDFIVAVCM 94
Cdd:PRK06155 16 LPPseRTLPAMLARQAERYPDRPLLVF---------GGTRWTYAEAARAAAAAAHALAA--AG--VKR---GDRVALMCG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 95 QPSEGLVTTLLAIWkAGGAYLPIDPSFPANRIHHILLEAKPTLVIRD-------DDIDAGR--------FQGTPTLSTTE 159
Cdd:PRK06155 80 NRIEFLDVFLGCAW-LGAIAVPINTALRGPQLEHILRNSGARLLVVEaallaalEAADPGDlplpavwlLDAPASVSVPA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 160 LYAKSLQLAGSNLLSEEMLRGGNdhIAIVLYTSGSTGVPKGVRLPHEsilnrlQWQW------------------ATFPY 221
Cdd:PRK06155 159 GWSTAPLPPLDAPAPAAAVQPGD--TAAILYTSGTTGPSKGVCCPHA------QFYWwgrnsaedleigaddvlyTTLPL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 222 TANEAVSVFKTALtfvdsiaeLWGplmcglAILVVPKAVTKdpQRLVALLERYKirrlVLVPTLLRSLLMYLKMEGGGAA 301
Cdd:PRK06155 231 FHTNALNAFFQAL--------LAG------ATYVLEPRFSA--SGFWPAVRRHG----ATVTYLLGAMVSILLSQPARES 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 302 QKllynlqiwvcsGEPLSVSLA----SSFFDYFDE--GVhRLYNFYGSTEVlgdvtyfaceskkqlslydNVPIGIPLSN 375
Cdd:PRK06155 291 DR-----------AHRVRVALGpgvpAALHAAFRErfGV-DLLDGYGSTET-------------------NFVIAVTHGS 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 376 ----TVVYL--------LDADYRPVKNGEIGEI-------FAsglnLAAGYVNgrDPERflenplAVEKKYARLYRTGDY 436
Cdd:PRK06155 340 qrpgSMGRLapgfearvVDEHDQELPDGEPGELllradepFA----FATGYFG--MPEK------TVEAWRNLWFHTGDR 407
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 437 GSLK-NGSIMYEGRTDSQVKIRGHRVDLSEVEKNVAELPLVDKAIVLCYHAGQVDQAILAFVKLRDDapMVTEMQMEARL 515
Cdd:PRK06155 408 VVRDaDGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDG--TALEPVALVRH 485
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 126789033 516 -KDKLADYMTPQVV-ILEHVPLLVNGKVDRQALLKTYETANNNEGDSSIV 563
Cdd:PRK06155 486 cEPRLAYFAVPRYVeFVAALPKTENGKVQKFVLREQGVTADTWDREAAGV 535
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
191-532 |
1.55e-08 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 57.85 E-value: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 191 TSGSTGVPKGVRL-PHEsiLNRLQWQWA----------------TFPYtaneavSVFKTALTFVDSiAELWGplmcglaI 253
Cdd:COG1541 91 SSGTTGKPTVVGYtRKD--LDRWAELFArslraagvrpgdrvqnAFGY------GLFTGGLGLHYG-AERLG-------A 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 254 LVVPKAVTkDPQRLVALLERYKIRRLVLVPTLLRSLLMYLKMEGGGAAQkllYNLQIWVCSGEPLSVSLASSFFDYFdeG 333
Cdd:COG1541 155 TVIPAGGG-NTERQLRLMQDFGPTVLVGTPSYLLYLAEVAEEEGIDPRD---LSLKKGIFGGEPWSEEMRKEIEERW--G 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 334 VhRLYNFYGSTEVlGdvTYFACESKKQLSLY---DNVpigIPlsnTVVylldaDY---RPVKNGEIGEIFASGLNlaagy 407
Cdd:COG1541 229 I-KAYDIYGLTEV-G--PGVAYECEAQDGLHiweDHF---LV---EII-----DPetgEPVPEGEEGELVVTTLT----- 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 408 vngrdPERFlenPLAvekkyaRlYRTGDYGSLKNGS------------IMyeGRTDSQVKIRGHRVDLSEVEKNVAELP- 474
Cdd:COG1541 289 -----KEAM---PLI------R-YRTGDLTRLLPEPcpcgrthprigrIL--GRADDMLIIRGVNVFPSQIEEVLLRIPe 351
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 126789033 475 LVDKAIVLCYHAGQVDQAILaFVKLRDDAPMVT-EMQMEARLKDKLAdyMTPQVVILEH 532
Cdd:COG1541 352 VGPEYQIVVDREGGLDELTV-RVELAPGASLEAlAEAIAAALKAVLG--LRAEVELVEP 407
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
181-546 |
2.99e-08 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 57.16 E-value: 2.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 181 GNDHIAIVLYTSGSTGVPKGVRLPHESILNRLQ----WQWATFPYTANEAVSVFKTALTFVDSIAEL-WGPLMCGLAILV 255
Cdd:PLN02574 196 KQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVElfvrFEASQYEYPGSDNVYLAALPMFHIYGLSLFvVGLLSLGSTIVV 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 256 VPKAvtkDPQRLVALLERYKIRRLVLVPTLLRSLLMYLKMEGGGAAQKLlynlqIWVCSG-EPLSVSLASSFFDYFDegv 334
Cdd:PLN02574 276 MRRF---DASDMVKVIDRFKVTHFPVVPPILMALTKKAKGVCGEVLKSL-----KQVSCGaAPLSGKFIQDFVQTLP--- 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 335 H-RLYNFYGSTE--VLGDVTYfaceSKKQLSLYDNVPIGIP-LSNTVVYLLDADYRPvkNGEIGEIFASGLNLAAGYVNG 410
Cdd:PLN02574 345 HvDFIQGYGMTEstAVGTRGF----NTEKLSKYSSVGLLAPnMQAKVVDWSTGCLLP--PGNCGELWIQGPGVMKGYLNN 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 411 RDperfLENPLAVEKKYarlYRTGDYGSL-KNGSIMYEGRTDSQVKIRGHRVDLSEVEKNVAELPLVDKAIVLCYHAGQV 489
Cdd:PLN02574 419 PK----ATQSTIDKDGW---LRTGDIAYFdEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKEC 491
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 126789033 490 DQAILAFVkLRDDAPMVTEMQMEARLKDKLADY-MTPQVVILEHVPLLVNGKVDRQAL 546
Cdd:PLN02574 492 GEIPVAFV-VRRQGSTLSQEAVINYVAKQVAPYkKVRKVVFVQSIPKSPAGKILRREL 548
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
90-546 |
3.51e-08 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 57.20 E-value: 3.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 90 VAVCMQPSEGLVTTLLAIWKAGGAYLPIDPSFPAN--RIHHILLEAKPTLVIRDDDIDAgrfqgtpTLSTTELYAKSLQL 167
Cdd:PRK05852 71 VALRMGSNAEFVVALLAASRADLVVVPLDPALPIAeqRVRSQAAGARVVLIDADGPHDR-------AEPTTRWWPLTVNV 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 168 AGSNLLSEEML-----------------RGGNDHIAIVLYTSGSTGVPKGVRLPHESILNRLQWQWATF---PYTANEAV 227
Cdd:PRK05852 144 GGDSGPSGGTLsvhldaateptpatstpEGLRPDDAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYrlsPRDATVAV 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 228 SVFKTALTFvdsIAELWGPLMCGLAILVVPKAvtkdpqRLVALLERYKIRRL-----VLVPTLLRSLLMYLKMEGGGAAQ 302
Cdd:PRK05852 224 MPLYHGHGL---IAALLATLASGGAVLLPARG------RFSAHTFWDDIKAVgatwyTAVPTIHQILLERAATEPSGRKP 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 303 KLLYNlqIWVCSGePLSVSLASSFFDYFDEGVhrlYNFYGSTEVLGDVTYFACESKKQlSLYDNVPIGIPLSNTV--VYL 380
Cdd:PRK05852 295 AALRF--IRSCSA-PLTAETAQALQTEFAAPV---VCAFGMTEATHQVTTTQIEGIGQ-TENPVVSTGLVGRSTGaqIRI 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 381 LDADYRPVKNGEIGEIFASGLNLAAGYVNgrDPE----RFLENPLavekkyarlyRTGDYGSLK-NGSIMYEGRTDSQVK 455
Cdd:PRK05852 368 VGSDGLPLPAGAVGEVWLRGTTVVRGYLG--DPTitaaNFTDGWL----------RTGDLGSLSaAGDLSIRGRIKELIN 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 456 IRGHRVDLSEVEKNVAELPLVDKAIVLCYHAGQVDQAILAFVKLRDDAPmVTEMQMEARLKDKLADYMTP-QVVILEHVP 534
Cdd:PRK05852 436 RGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPRESAP-PTAEELVQFCRERLAAFEIPaSFQEASGLP 514
|
490
....*....|..
gi 126789033 535 LLVNGKVDRQAL 546
Cdd:PRK05852 515 HTAKGSLDRRAV 526
|
|
| AcpA |
COG3433 |
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ... |
365-653 |
3.89e-08 |
|
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442659 [Multi-domain] Cd Length: 295 Bit Score: 55.91 E-value: 3.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 365 DNVPIGIPLSNtVVYLLDADYRPVKNGEIGEIFASGLNLAAGYVNGRDPERFLENPLAVEKKYARLYRTGDYGSLKNGSI 444
Cdd:COG3433 14 DEPPPVIPPAI-VQARALLLIVDLQGYFGGFGGEGGLLGAGLLLRIRLLAAAARAPFIPVPYPAQPGRQADDLRLLLRRG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 445 MYEGRTDSQVKI-------RGHRVDLSEVEKNVAELPLVDKAIVLcyHAGQVDQAILAFVKLRDDapMVTEMQMEARLKD 517
Cdd:COG3433 93 LGPGGGLERLVQqvviraeRGEEEELLLVLRAAAVVRVAVLAALR--GAGVGLLLIVGAVAALDG--LAAAAALAALDKV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 518 KLADYMTPQVVILEHVPLLVNGKVDRQALLKTYETANnnegdssivLDFDYSQVPEDLKLTARDLFETVGGVIGRStRAT 597
Cdd:COG3433 169 PPDVVAASAVVALDALLLLALKVVARAAPALAAAEAL---------LAAASPAPALETALTEEELRADVAELLGVD-PEE 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 126789033 598 LAPHSNFYELGGNSLNSIFTVTLLREKGYNIGISEFIAAKNLGEIIEKMAANHDAV 653
Cdd:COG3433 239 IDPDDNLFDLGLDSIRLMQLVERWRKAGLDVSFADLAEHPTLAAWWALLAAAQAAA 294
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
188-565 |
6.67e-08 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 56.44 E-value: 6.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 188 VLYTSGSTGVPKGVrlphesilnrLQWQWATFPYTAneavSVFKTALTFVDS-----IAE----------LWGPLMCGLA 252
Cdd:PLN02654 280 LLYTSGSTGKPKGV----------LHTTGGYMVYTA----TTFKYAFDYKPTdvywcTADcgwitghsyvTYGPMLNGAT 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 253 ILVVPKAVT-KDPQRLVALLERYKIRRLVLVPTLLRSLlmylkMEGGG--AAQKLLYNLQIWVCSGEPLSVSLASSFFDY 329
Cdd:PLN02654 346 VLVFEGAPNyPDSGRCWDIVDKYKVTIFYTAPTLVRSL-----MRDGDeyVTRHSRKSLRVLGSVGEPINPSAWRWFFNV 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 330 FDEGVHRLYNFYGSTEVLGdvtyfaceskkqlSLYDNVPIGIPLSNTVVYLLDADYRPV----KNGEI-GEifASGLNLA 404
Cdd:PLN02654 421 VGDSRCPISDTWWQTETGG-------------FMITPLPGAWPQKPGSATFPFFGVQPVivdeKGKEIeGE--CSGYLCV 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 405 AGYVNGR------DPERFLENPLaveKKYARLYRTGDYGSL-KNGSIMYEGRTDSQVKIRGHRVDLSEVEKNVAELPLVD 477
Cdd:PLN02654 486 KKSWPGAfrtlygDHERYETTYF---KPFAGYYFSGDGCSRdKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCA 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 478 KAIVLCYHAGQVDQAILAFVKLRDDAPMVTEMQ--MEARLKDKLADYMTPQVVileH----VPLLVNGKVDRQALLKTYE 551
Cdd:PLN02654 563 EAAVVGIEHEVKGQGIYAFVTLVEGVPYSEELRksLILTVRNQIGAFAAPDKI---HwapgLPKTRSGKIMRRILRKIAS 639
|
410
....*....|....
gi 126789033 552 TANNNEGDSSIVLD 565
Cdd:PLN02654 640 RQLDELGDTSTLAD 653
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
56-210 |
9.28e-08 |
|
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: 55.68 E-value: 9.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 56 SYRQMNERANRAARLLVAEthgrfLQPNSDGDFIvAVCMQPSEGLVTTLLAIWKAGGAYLPIDPSFPANRIHHILLEAKP 135
Cdd:cd05927 7 SYKEVAERADNIGSALRSL-----GGKPAPASFV-GIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEI 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 126789033 136 TLVIRDDDIdagrfqgtptlsTTELYAKSLQLAGSNLLSEEmlRGGNDHIAIVLYTSGSTGVPKGVRLPHESILN 210
Cdd:cd05927 81 SIVFCDAGV------------KVYSLEEFEKLGKKNKVPPP--PPKPEDLATICYTSGTTGNPKGVMLTHGNIVS 141
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
56-203 |
2.41e-07 |
|
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: 54.40 E-value: 2.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 56 SYRQMNERANRAARLLVAEThgrfLQPNSDGDFIVAVCMQpsegLVTTLLAIWKAGGAYLPIDPSFPANRIHHIL--LEA 133
Cdd:cd05932 8 TWGEVADKARRLAAALRALG----LEPGSKIALISKNCAE----WFITDLAIWMAGHISVPLYPTLNPDTIRYVLehSES 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 126789033 134 KPTLVIRDDDIDA---GRFQGTPTLSTTELYAKSLQLAGSNLL-----SEEMLRGGNDHIAIVLYTSGSTGVPKGVRL 203
Cdd:cd05932 80 KALFVGKLDDWKAmapGVPEGLISISLPPPSAANCQYQWDDLIaqhppLEERPTRFPEQLATLIYTSGTTGQPKGVML 157
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
182-546 |
2.73e-07 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 54.29 E-value: 2.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 182 NDHIAIVLYTSGSTGVPKGVRLPHESIL-NRLQWQWATFPY---------TANEAVSVFktALT-----FVDsiaelwgp 246
Cdd:PRK08974 205 PEDLAFLQYTGGTTGVAKGAMLTHRNMLaNLEQAKAAYGPLlhpgkelvvTALPLYHIF--ALTvncllFIE-------- 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 247 lMCGLAILVV-PKavtkDPQRLVALLERYKIRRLVLVPTLLRSLL------------MYLKMEGGGAAQKllynlqiwvc 313
Cdd:PRK08974 275 -LGGQNLLITnPR----DIPGFVKELKKYPFTAITGVNTLFNALLnneefqeldfssLKLSVGGGMAVQQ---------- 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 314 sgeplsvSLASSFFDYfdEGVHrLYNFYGSTEVLGDVTyfACESkkQLSLYdNVPIGIPLSNTVVYLLDADYRPVKNGEI 393
Cdd:PRK08974 340 -------AVAERWVKL--TGQY-LLEGYGLTECSPLVS--VNPY--DLDYY-SGSIGLPVPSTEIKLVDDDGNEVPPGEP 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 394 GEIFASGLNLAAGYVNgrdperfleNPLAVEKKYARLY-RTGDYGSL-KNGSIMYEGRTDSQVKIRGHRVDLSEVEKNVA 471
Cdd:PRK08974 405 GELWVKGPQVMLGYWQ---------RPEATDEVIKDGWlATGDIAVMdEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVM 475
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 126789033 472 ELPLVDKAIVLCYHAGQVDQAILAFVKLRDdaPMVTEMQMEARLKDKLADYMTPQVV-ILEHVPLLVNGKVDRQAL 546
Cdd:PRK08974 476 LHPKVLEVAAVGVPSEVSGEAVKIFVVKKD--PSLTEEELITHCRRHLTGYKVPKLVeFRDELPKSNVGKILRREL 549
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
4-543 |
5.17e-07 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 53.24 E-value: 5.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 4 LPQLSIVKG-----LQQDFVPRALHRIFEeqqlRHADKVALIYQPsttgQGMapsQSSYRQMNERANRAARLLVAethgR 78
Cdd:PRK12583 1 MPQPSYYQGggdkpLLTQTIGDAFDATVA----RFPDREALVVRH----QAL---RYTWRQLADAVDRLARGLLA----L 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 79 FLQPnsdGDFIVAVCMQPSEGLVTTLlAIWKAGGAYLPIDPSFPANRIHHILLEAKPTLVIRDDdidagRFQGTPTLSTT 158
Cdd:PRK12583 66 GVQP---GDRVGIWAPNCAEWLLTQF-ATARIGAILVNINPAYRASELEYALGQSGVRWVICAD-----AFKTSDYHAML 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 159 ELYAKSLQLAGSNLLSEE---MLRG--------------------------------------GNDHIAIvLYTSGSTGV 197
Cdd:PRK12583 137 QELLPGLAEGQPGALACErlpELRGvvslapapppgflawhelqargetvsrealaerqasldRDDPINI-QYTSGTTGF 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 198 PKGVRLPHESILNrlqwqwatfpytaNEAVSVFKTALTFVDSIA------ELWGPLMCGLAILVVPKAVTK-----DPQR 266
Cdd:PRK12583 216 PKGATLSHHNILN-------------NGYFVAESLGLTEHDRLCvpvplyHCFGMVLANLGCMTVGACLVYpneafDPLA 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 267 LVALLERYKIRRLVLVPTllrsllMYL-KMEGGGAAQKLLYNLQIWVCSGEPLSVSLASSFFDyfDEGVHRLYNFYGSTE 345
Cdd:PRK12583 283 TLQAVEEERCTALYGVPT------MFIaELDHPQRGNFDLSSLRTGIMAGAPCPIEVMRRVMD--EMHMAEVQIAYGMTE 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 346 VlGDVTYfaceskkQLSLYDNVP-----IGIPLSNTVVYLLDADYRPVKNGEIGEIFASGLNLAAGYVNgrDPERFLEnp 420
Cdd:PRK12583 355 T-SPVSL-------QTTAADDLErrvetVGRTQPHLEVKVVDPDGATVPRGEIGELCTRGYSVMKGYWN--NPEATAE-- 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 421 lAVEKKyARLYrTGDYGSL-KNGSIMYEGRTDSQVkIR-GHRVDLSEVEKNVAELPLVDKAIVLCYHAGQVDQAILAFVK 498
Cdd:PRK12583 423 -SIDED-GWMH-TGDLATMdEQGYVRIVGRSKDMI-IRgGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVR 498
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 126789033 499 LRDDApMVTEMQMEARLKDKLADYMTPQVV-ILEHVPLLVNGKVDR 543
Cdd:PRK12583 499 LHPGH-AASEEELREFCKARIAHFKVPRYFrFVDEFPMTVTGKVQK 543
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
183-543 |
1.15e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 52.31 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 183 DHIAIVLYTSGSTGVPKGVRLPHESIL-NRLQWQ-W----ATFPYTANEAVSVFKT-ALTFVDSIAelwgpLMCGLAILV 255
Cdd:PRK05605 219 DDVALILYTSGTTGKPKGAQLTHRNLFaNAAQGKaWvpglGDGPERVLAALPMFHAyGLTLCLTLA-----VSIGGELVL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 256 VPKAvtkDPQRLVALLERYKIRRLVLVPTLlrsllmYLKMEGGGAAQKL-LYNLQIWVCSGEPLSVSLASSFfdyfdEGV 334
Cdd:PRK05605 294 LPAP---DIDLILDAMKKHPPTWLPGVPPL------YEKIAEAAEERGVdLSGVRNAFSGAMALPVSTVELW-----EKL 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 335 H--RLYNFYGSTE----VLGD-VTyfacESKKQLSlydnvpIGIPLSNTVVYLLDAD--YRPVKNGEIGEIFASGLNLAA 405
Cdd:PRK05605 360 TggLLVEGYGLTEtspiIVGNpMS----DDRRPGY------VGVPFPDTEVRIVDPEdpDETMPDGEEGELLVRGPQVFK 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 406 GYVNgrDPErflENPLAVEKKYarlYRTGDYGslkngsIMYEgrtDSQVKIR----------GHRVDLSEVEKNVAELPL 475
Cdd:PRK05605 430 GYWN--RPE---ETAKSFLDGW---FRTGDVV------VMEE---DGFIRIVdrikeliitgGFNVYPAEVEEVLREHPG 492
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 126789033 476 VDKAIVLCYHAGQVDQAILAFVKLRDDApMVTEMQMEARLKDKLADYMTPQ-VVILEHVPLLVNGKVDR 543
Cdd:PRK05605 493 VEDAAVVGLPREDGSEEVVAAVVLEPGA-ALDPEGLRAYCREHLTRYKVPRrFYHVDELPRDQLGKVRR 560
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
183-548 |
1.28e-06 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 52.28 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 183 DHIAIVLYTSGSTGVPKGVRLPHESIL-NRLQWQwATFPYTANEAV----SVFKT-ALTfvdsiAELWGPLMCGLAILVV 256
Cdd:PRK06814 793 DDPAVILFTSGSEGTPKGVVLSHRNLLaNRAQVA-ARIDFSPEDKVfnalPVFHSfGLT-----GGLVLPLLSGVKVFLY 866
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 257 PKAVTkdpQRLVALLeRYKIRRLVLVPTllRSLLM-YLKMegggAAQKLLYNLQIWVCSGEPLSvslASSFFDYFDEGVH 335
Cdd:PRK06814 867 PSPLH---YRIIPEL-IYDTNATILFGT--DTFLNgYARY----AHPYDFRSLRYVFAGAEKVK---EETRQTWMEKFGI 933
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 336 RLYNFYGSTE---VLgdvtyfACESkkqlslydnvpigiPLSN---TVVYLLDA-DYR--PVKN-GEIGEIFASGLNLAA 405
Cdd:PRK06814 934 RILEGYGVTEtapVI------ALNT--------------PMHNkagTVGRLLPGiEYRlePVPGiDEGGRLFVRGPNVML 993
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 406 GYVNgrdperfLENPLAVEKKYARLYRTGDYGSL-KNGSIMYEGRTDSQVKIRGHRVDLSEVEKNVAEL-PLVDKAIVLC 483
Cdd:PRK06814 994 GYLR-------AENPGVLEPPADGWYDTGDIVTIdEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELwPDALHAAVSI 1066
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 126789033 484 YHAGQVDQAILAfvklrDDAPMVTEMQMEARLKDK-LADYMTPQVVI-LEHVPLLVNGKVDRQALLK 548
Cdd:PRK06814 1067 PDARKGERIILL-----TTASDATRAAFLAHAKAAgASELMVPAEIItIDEIPLLGTGKIDYVAVTK 1128
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
180-497 |
5.72e-06 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.
Pssm-ID: 341294 [Multi-domain] Cd Length: 507 Bit Score: 49.91 E-value: 5.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 180 GGNDHIAIVLYTSGSTGVPKGVRLPHESILNRLqwqwATFPYTANEAVSVFKTALTF----------VDSIAELWG---- 245
Cdd:cd17639 85 GKPDDLACIMYTSGSTGNPKGVMLTHGNLVAGI----AGLGDRVPELLGPDDRYLAYlplahifelaAENVCLYRGgtig 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 246 ---PLMCGLAILVVPK--AVTKDPQRLV---ALLERykIRRLVL-----VPTLLRSL---LMYLKME------GGGAAQK 303
Cdd:cd17639 161 ygsPRTLTDKSKRGCKgdLTEFKPTLMVgvpAIWDT--IRKGVLaklnpMGGLKRTLfwtAYQSKLKalkegpGTPLLDE 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 304 LLYN---------LQIWVCSGEPLSVS---LASSFFDYFDEGvhrlynfYGSTE--------VLGDVTYFAceskkqlsl 363
Cdd:cd17639 239 LVFKkvraalggrLRYMLSGGAPLSADtqeFLNIVLCPVIQG-------YGLTEtcaggtvqDPGDLETGR--------- 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 364 ydnvpIGIPLSNTVVYLLDAD---YRPVKNGEIGEIFASGLNLAAGYVNgrdperfleNPLAVEKKYA--RLYRTGDYGS 438
Cdd:cd17639 303 -----VGPPLPCCEIKLVDWEeggYSTDKPPPRGEILIRGPNVFKGYYK---------NPEKTKEAFDgdGWFHTGDIGE 368
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 126789033 439 L-KNGSIMYEGRTDSQVKIR-GHRVDLSEVEKNVAELPLVDKaivLCYHAGQVDQAILAFV 497
Cdd:cd17639 369 FhPDGTLKIIDRKKDLVKLQnGEYIALEKLESIYRSNPLVNN---ICVYADPDKSYPVAIV 426
|
|
| PaaK |
cd05913 |
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ... |
191-548 |
7.97e-06 |
|
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic degradation pathway, by converting phenylacetic acid (PA) into phenylacetyl-CoA (PA-CoA). Phenylacetate-CoA ligase has been found in proteobacteria as well as gram positive prokaryotes. The enzyme is specifically induced after aerobic growth in a chemically defined medium containing PA or phenylalanine (Phe) as the sole carbon source. PaaKs are members of the adenylate-forming enzyme (AFE) family. However, sequence comparison reveals divergent features of PaaK with respect to the superfamily, including a novel N-terminal sequence.
Pssm-ID: 341239 [Multi-domain] Cd Length: 425 Bit Score: 49.16 E-value: 7.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 191 TSGSTGVPKGVRLPHESIlNRLQWQWATFPYTANeavsvFKTALTFvdSIAELWGPLMCGLAI---------LVVPkAVT 261
Cdd:cd05913 86 SSGTTGKPTVVGYTKNDL-DVWAELVARCLDAAG-----VTPGDRV--QNAYGYGLFTGGLGFhygaerlgaLVIP-AGG 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 262 KDPQRLVALLERYKIRRLVLVPTLLRSLLMYLKMEGGGAAQkllYNLQIWVCSGEPLSVSLASSFFDYFDEGVhrlYNFY 341
Cdd:cd05913 157 GNTERQLQLIKDFGPTVLCCTPSYALYLAEEAEEEGIDPRE---LSLKVGIFGAEPWTEEMRKRIERRLGIKA---YDIY 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 342 GSTEVLGDVTYFACESKKQLSLY-DNVPIGIplsntvvyLLDADYRPVKNGEIGEIFASGLNLAAGyvngrdperflenP 420
Cdd:cd05913 231 GLTEIIGPGVAFECEEKDGLHIWeDHFIPEI--------IDPETGEPVPPGEVGELVFTTLTKEAM-------------P 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 421 LavekkyaRLYRTGDYGSLKNGS------------IMyeGRTDSQVKIRGhrvdlseveKNVaelplvdkaivlcyHAGQ 488
Cdd:cd05913 290 L-------IRYRTRDITRLLPGPcpcgrthrridrIT--GRSDDMLIIRG---------VNV--------------FPSQ 337
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 489 VDQAILAFvklrddAPMVTEMQMEARLKDKLaDYMTpqvVILEHVPLLVNGKvDRQALLK 548
Cdd:cd05913 338 IEDVLLKI------PGLGPHYQLILTRQEHL-DELT---IKVEVRPEADDDE-KLEALKQ 386
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
56-444 |
4.41e-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: 46.96 E-value: 4.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 56 SYRQMNERANRAARLLvaETHGRfLQPnsdGDFIVAVCMQPSEgLVTTLLAIWKAGGAYLPIDPSFPANRIHHIL----- 130
Cdd:cd05905 16 TWGKLLSRAEKIAAVL--QKKVG-LKP---GDRVALMYPDPLD-FVAAFYGCLYAGVVPIPIEPPDISQQLGFLLgtckv 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 131 ---LEAKPTLVIRDDDIDAGRFQGT-------PTLSTTELYAKSLQLagSNLLSEEMLRGGNDHIAIVLYTSGSTGVPKG 200
Cdd:cd05905 89 rvaLTVEACLKGLPKKLLKSKTAAEiakkkgwPKILDFVKIPKSKRS--KLKKWGPHPPTRDGDTAYIEYSFSSDGSLSG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 201 VRLPHESILNRLQWQWATFPYTANEAVSV---FKTALTFVDSIaeLWGpLMCGL-AILVVPKAVTKDPQRLVALLERYKI 276
Cdd:cd05905 167 VAVSHSSLLAHCRALKEACELYESRPLVTvldFKSGLGLWHGC--LLS-VYSGHhTILIPPELMKTNPLLWLQTLSQYKV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 277 RRLVLvptLLRSLLMYLKMEGGGAAQKLLYNL------QIWVCSGEPLSVSLASSFFDYFdeGVHRLYNFYGSTEVLGDV 350
Cdd:cd05905 244 RDAYV---KLRTLHWCLKDLSSTLASLKNRDVnlsslrMCMVPCENRPRISSCDSFLKLF--QTLGLSPRAVSTEFGTRV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 351 TYFACE-------------SKKQLSlYDNVPIGIPLSNTVVYLLDADYRPV---------------KNGEIGEIFASGLN 402
Cdd:cd05905 319 NPFICWqgtsgpepsrvylDMRALR-HGVVRLDERDKPNSLPLQDSGKVLPgaqvaivnpetkglcKDGEIGEIWVNSPA 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 126789033 403 LAAGY--VNG------RDPERFLENPLAVEKKYArlyRTGDYGSLKNGSI 444
Cdd:cd05905 398 NASGYflLDGetndtfKVFPSTRLSTGITNNSYA---RTGLLGFLRPTKC 444
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
34-458 |
4.69e-05 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 47.03 E-value: 4.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 34 ADKVALIYQPSTTGQGMAPSQSSYRQMNERaNRAarllVAethGRFLQPNSDGDFIVAVCMQPSEGLVTTLLAIWkAGGA 113
Cdd:PRK07769 35 GDKLAYRFLDFSTERDGVARDLTWSQFGAR-NRA----VG---ARLQQVTKPGDRVAILAPQNLDYLIAFFGALY-AGRI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 114 YLPI-DPSFP--ANRIHHILLEAKPTLVIRDDDIDAGR---FQGTPTLSTTELYAKSL--QLAGSNLLSEEMLRggnDHI 185
Cdd:PRK07769 106 AVPLfDPAEPghVGRLHAVLDDCTPSAILTTTDSAEGVrkfFRARPAKERPRVIAVDAvpDEVGATWVPPEANE---DTI 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 186 AIVLYTSGSTGVPKGVRLPHESIL-NRLQWQWATFPYTANEAVSvfktaltfvdsiaelWGPL-------------MCGL 251
Cdd:PRK07769 183 AYLQYTSGSTRIPAGVQITHLNLPtNVLQVIDALEGQEGDRGVS---------------WLPFfhdmglitvllpaLLGH 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 252 AI-LVVPKAVTKDPQRLvallerykIRRLVLVPTllrsllmylkmEGGG-------------AAQKL---------LYNL 308
Cdd:PRK07769 248 YItFMSPAAFVRRPGRW--------IRELARKPG-----------GTGGtfsaapnfafehaAARGLpkdgeppldLSNV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 309 QIWVCSGEPLSVSLASSFFDYFDEgvhrlYNF--------YGstevLGDVTYFACESKkqlslYDNVPigiplsnTVVYL 380
Cdd:PRK07769 309 KGLLNGSEPVSPASMRKFNEAFAP-----YGLpptaikpsYG----MAEATLFVSTTP-----MDEEP-------TVIYV 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 381 ----LDADyRPVK-----------------------------------NGEIGEIFASGLNLAAGYVNGRDPERF----- 416
Cdd:PRK07769 368 drdeLNAG-RFVEvpadapnavaqvsagkvgvsewavivdpetaselpDGQIGEIWLHGNNIGTGYWGKPEETAAtfqni 446
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 126789033 417 LENPLAVE-----KKYARLYRTGDYGSLKNGSIMYEGRTDSQVKIRG 458
Cdd:PRK07769 447 LKSRLSEShaegaPDDALWVRTGDYGVYFDGELYITGRVKDLVIIDG 493
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
188-514 |
4.96e-05 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 47.06 E-value: 4.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 188 VLYTSGSTGVPKGVRlpHES------ILNRLQWqwaTFPYTANEavsVF--------KTALTFVdsiaeLWGPLMCGLAI 253
Cdd:PRK00174 250 ILYTSGSTGKPKGVL--HTTggylvyAAMTMKY---VFDYKDGD---VYwctadvgwVTGHSYI-----VYGPLANGATT 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 254 LV---VPKavTKDPQRLVALLERYKIRRLVLVPTLLRSLlmylkMEGGGAAQKL--LYNLQIWVCSGEPLsvslassffd 328
Cdd:PRK00174 317 LMfegVPN--YPDPGRFWEVIDKHKVTIFYTAPTAIRAL-----MKEGDEHPKKydLSSLRLLGSVGEPI---------- 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 329 yfdegvhrlyN------FYgstEVLGDvtyfaceskkqlslyDNVPI----------GI---PL---------SNT---- 376
Cdd:PRK00174 380 ----------NpeawewYY---KVVGG---------------ERCPIvdtwwqtetgGImitPLpgatplkpgSATrplp 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 377 --VVYLLDADYRPVKNGEIGeifasglNLA--------AGYVNGrDPERFLENPLaveKKYARLYRTGDyGSLK--NGSI 444
Cdd:PRK00174 432 giQPAVVDEEGNPLEGGEGG-------NLVikdpwpgmMRTIYG-DHERFVKTYF---STFKGMYFTGD-GARRdeDGYY 499
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 126789033 445 MYEGRTDSQVKIRGHRVDLSEVEKNVAELPLVDKAIVLcyhaGQVD----QAILAFVKLRDDAPMVTEMQMEAR 514
Cdd:PRK00174 500 WITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVV----GRPDdikgQGIYAFVTLKGGEEPSDELRKELR 569
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
181-546 |
7.67e-05 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 46.29 E-value: 7.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 181 GNDHIAIVLYTSGSTGVPKGVRLPHESIL-NRLQWQwATFPYTANEAVSVFKTALTFVDSIAelwGPLMCGLAILVVPKA 259
Cdd:PRK05677 205 QADDVAVLQYTGGTTGVAKGAMLTHRNLVaNMLQCR-ALMGSNLNEGCEILIAPLPLYHIYA---FTFHCMAMMLIGNHN 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 260 V----TKDPQRLVALLERYKIRRLVLVPTLLRSLL------------MYLKMEGGGAAQklLYNLQIW-------VCSGe 316
Cdd:PRK05677 281 IlisnPRDLPAMVKELGKWKFSGFVGLNTLFVALCnneafrkldfsaLKLTLSGGMALQ--LATAERWkevtgcaICEG- 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 317 plsvslassffdyfdegvhrlynfYGSTEVLGDVTyfaceskkqLSLYDNV---PIGIPLSNTVVYLLDADYRPVKNGEI 393
Cdd:PRK05677 358 ------------------------YGMTETSPVVS---------VNPSQAIqvgTIGIPVPSTLCKVIDDDGNELPLGEV 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 394 GEIFASGLNLAAGYvngrdperfLENPLAVEKKYAR--LYRTGDYGSLK-NGSIMYEGRTDSQVKIRGHRVDLSEVEKNV 470
Cdd:PRK05677 405 GELCVKGPQVMKGY---------WQRPEATDEILDSdgWLKTGDIALIQeDGYMRIVDRKKDMILVSGFNVYPNELEDVL 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 471 AELPLVdkaiVLCYHAGQVD----QAILAFVKLRdDAPMVTEMQMEARLKDKLADYMTPQVV-ILEHVPLLVNGKVDRQA 545
Cdd:PRK05677 476 AALPGV----LQCAAIGVPDeksgEAIKVFVVVK-PGETLTKEQVMEHMRANLTGYKVPKAVeFRDELPTTNVGKILRRE 550
|
.
gi 126789033 546 L 546
Cdd:PRK05677 551 L 551
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
190-546 |
1.16e-04 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 45.61 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 190 YTSGSTGVPKGVRLPHE-----SILNRLQWQwatfpytANE-AVSVFKTALTFVDSIAELWG-PLMCGLAIL---VVPKA 259
Cdd:PLN02479 202 YTSGTTASPKGVVLHHRgaylmALSNALIWG-------MNEgAVYLWTLPMFHCNGWCFTWTlAALCGTNIClrqVTAKA 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 260 VtkdpqrlVALLERYKIRRLVLVPTLLRSLLMYLKMEgggAAQKLLYNLQIWVCSGEPLSVSLASsffdyFDEGVHRLYN 339
Cdd:PLN02479 275 I-------YSAIANYGVTHFCAAPVVLNTIVNAPKSE---TILPLPRVVHVMTAGAAPPPSVLFA-----MSEKGFRVTH 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 340 FYGSTEVLGDVTyfACESKKQlslYDNVP---------------IGIPLSNtVVYLLDADYRPVKNGEIGEIFASGLNLA 404
Cdd:PLN02479 340 TYGLSETYGPST--VCAWKPE---WDSLPpeeqarlnarqgvryIGLEGLD-VVDTKTMKPVPADGKTMGEIVMRGNMVM 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 405 AGYvngrdperfLENPLAVEKKYAR-LYRTGDYGsLKN--GSIMYEGRTDSQVKIRGHRVDLSEVEKNVAELPLVDKAIV 481
Cdd:PLN02479 414 KGY---------LKNPKANEEAFANgWFHSGDLG-VKHpdGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASV 483
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 126789033 482 LCYHAGQVDQAILAFVKLRDDAPMVTEMQMEARL----KDKLADYMTPQVVILEHVPLLVNGKVDRQAL 546
Cdd:PLN02479 484 VARPDERWGESPCAFVTLKPGVDKSDEAALAEDImkfcRERLPAYWVPKSVVFGPLPKTATGKIQKHVL 552
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
177-557 |
1.16e-04 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 45.86 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 177 MLRGGNDHIAIVLYTSGSTGVPKGVRLPHESILNRLQWQWATFPYTANEAvsvFKTALTFVDSIA---ELWGPLMCGLAI 253
Cdd:PRK08043 359 QVKQQPEDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDR---FMSALPLFHSFGltvGLFTPLLTGAEV 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 254 LVVPKAVtkdpqrlvalleRYKIrrlvlVP--------TLLRSLLMYLKMEGGGAAQKLLYNLQIWVCSGEPLSVSLASS 325
Cdd:PRK08043 436 FLYPSPL------------HYRI-----VPelvydrncTVLFGTSTFLGNYARFANPYDFARLRYVVAGAEKLQESTKQL 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 326 FFDYFdeGVhRLYNFYGSTEvlgdvtyfaCESKkqlslydnVPIGIPLS---NTVVYLL---DADYRPV---KNGeiGEI 396
Cdd:PRK08043 499 WQDKF--GL-RILEGYGVTE---------CAPV--------VSINVPMAakpGTVGRILpgmDARLLSVpgiEQG--GRL 556
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 397 FASGLNLAAGYVNGRDPERfLENPLAVE---KKYARLYRTGDYGSL-KNGSIMYEGRTDSQVKIRGHRVDLSEVEKnvae 472
Cdd:PRK08043 557 QLKGPNIMNGYLRVEKPGV-LEVPTAENargEMERGWYDTGDIVRFdEQGFVQIQGRAKRFAKIAGEMVSLEMVEQ---- 631
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 473 lpLVDKAIVLCYHAGQVDQAIL---AFVKLRDDAPMVTEMQMEARLKDKLADYMTPQ-VVILEHVPLLVNGKVDRQALLK 548
Cdd:PRK08043 632 --LALGVSPDKQHATAIKSDASkgeALVLFTTDSELTREKLQQYAREHGVPELAVPRdIRYLKQLPLLGSGKPDFVTLKS 709
|
....*....
gi 126789033 549 TYETANNNE 557
Cdd:PRK08043 710 MVDEPEQHD 718
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
128-229 |
1.18e-04 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 45.81 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 128 HILLEAKPTLVIRDDDIDagrfqGTPTLSTTELYAKSLQLAgsnlLSEEMLRGGNDHIAIVLYTSGSTGVPKGVRLPHES 207
Cdd:PRK12582 174 AALDLLDVTVVHVTGPGE-----GIASIAFADLAATPPTAA----VAAAIAAITPDTVAKYLFTSGSTGMPKAVINTQRM 244
|
90 100
....*....|....*....|..
gi 126789033 208 ILNRLQWQWATFPYTANEAVSV 229
Cdd:PRK12582 245 MCANIAMQEQLRPREPDPPPPV 266
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
185-209 |
3.77e-04 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 44.34 E-value: 3.77e-04
10 20
....*....|....*....|....*
gi 126789033 185 IAIVLYTSGSTGVPKGVRLPHESIL 209
Cdd:PLN02387 252 IAVIMYTSGSTGLPKGVMMTHGNIV 276
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
56-225 |
5.89e-04 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 43.33 E-value: 5.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 56 SYRQMNERANRAARLLvaetHGRFLQPnsdgDFIVAVCMQPS-EGLVTTLLAIWkAGGAYLPIDP-----SFPANRIHHI 129
Cdd:PRK08180 71 TYAEALERVRAIAQAL----LDRGLSA----ERPLMILSGNSiEHALLALAAMY-AGVPYAPVSPayslvSQDFGKLRHV 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 130 LLEAKPTLVIRDDD------IDAGRFQGTPTLSTTELYAKSLQLAGSNLL--------SEEMLRGGNDHIAIVLYTSGST 195
Cdd:PRK08180 142 LELLTPGLVFADDGaafaraLAAVVPADVEVVAVRGAVPGRAATPFAALLatpptaavDAAHAAVGPDTIAKFLFTSGST 221
|
170 180 190
....*....|....*....|....*....|
gi 126789033 196 GVPKGVRLPHESILNRLQWQWATFPYTANE 225
Cdd:PRK08180 222 GLPKAVINTHRMLCANQQMLAQTFPFLAEE 251
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
105-225 |
6.26e-04 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 43.19 E-value: 6.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 105 LAIWKAGGAYLPIDPSFPA-----NRIHHILLEAKPTLVIRDDD------IDAGRFQGTPTLSTTELYAKSLQLAGSNLL 173
Cdd:cd05921 68 LAAMYAGVPAAPVSPAYSLmsqdlAKLKHLFELLKPGLVFAQDAapfaraLAAIFPLGTPLVVSRNAVAGRGAISFAELA 147
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 174 SEEML--------RGGNDHIAIVLYTSGSTGVPKGVRLPHESILNRLQWQWATFPYTANE 225
Cdd:cd05921 148 ATPPTaavdaafaAVGPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEE 207
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
32-201 |
9.80e-04 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 42.55 E-value: 9.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 32 RHADKVALIYQPSTTgqgmapsqsSYRQMNERANRAARLLVAethgrflQPNSDGDfIVAVCMQPSEGLVTTLLAIWKAG 111
Cdd:PRK09029 15 VRPQAIALRLNDEVL---------TWQQLCARIDQLAAGFAQ-------QGVVEGS-GVALRGKNSPETLLAYLALLQCG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 112 GAYLPIDPSFPANRIHHILleakPTLVIR--DDDIDAGRFQGTPTLSTTELYAK-SLQLAGSNLLSeemlrggndhiaIV 188
Cdd:PRK09029 78 ARVLPLNPQLPQPLLEELL----PSLTLDfaLVLEGENTFSALTSLHLQLVEGAhAVAWQPQRLAT------------MT 141
|
170
....*....|...
gi 126789033 189 LyTSGSTGVPKGV 201
Cdd:PRK09029 142 L-TSGSTGLPKAA 153
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
388-552 |
1.17e-03 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 42.29 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 388 VKNGEIGEIFASGLNLAAGYVngrdPErFLENPlavekkyaRLYRTGDYGSL-KNGSIMYEGRtDSQVKIRG-HRVDLSE 465
Cdd:PRK07445 296 IPANQTGNITIQAQSLALGYY----PQ-ILDSQ--------GIFETDDLGYLdAQGYLHILGR-NSQKIITGgENVYPAE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 466 VEKNVAELPLVDKAIVLcyhaGQVD----QAILAFVKLRDDAPmvTEMQMEARLKDKLADYMTP-QVVILEHVPLLVNGK 540
Cdd:PRK07445 362 VEAAILATGLVQDVCVL----GLPDphwgEVVTAIYVPKDPSI--SLEELKTAIKDQLSPFKQPkHWIPVPQLPRNPQGK 435
|
170
....*....|..
gi 126789033 541 VDRQALLKTYET 552
Cdd:PRK07445 436 INRQQLQQIAVQ 447
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
56-208 |
1.57e-03 |
|
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: 41.96 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 56 SYRQMNERANRAAR----LLVAETHG-RFLQPNSDGDFIVAVCmqpseglvttllAIWkAGGAYLPIDPSFPANRIHHIL 130
Cdd:cd05933 10 TYKEYYEACRQAAKaflkLGLERFHGvGILGFNSPEWFIAAVG------------AIF-AGGIAVGIYTTNSPEACQYVA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 131 LEAKPTLVIRDDD-----IDAGRFQgTPTLSTTELYAKSLQLAGSNLLS-EEMLRGGND----------------HIAIV 188
Cdd:cd05933 77 ETSEANILVVENQkqlqkILQIQDK-LPHLKAIIQYKEPLKEKEPNLYSwDEFMELGRSipdeqldaiissqkpnQCCTL 155
|
170 180
....*....|....*....|
gi 126789033 189 LYTSGSTGVPKGVRLPHESI 208
Cdd:cd05933 156 IYTSGTTGMPKGVMLSHDNI 175
|
|
| PP-binding |
pfam00550 |
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
580-641 |
1.90e-03 |
|
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: 37.54 E-value: 1.90e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 126789033 580 RDLFETVGGVIGRSTrATLAPHSNFYELGGNSLNSI-FTVTLLREKGYNIGISEFIAAKNLGE 641
Cdd:pfam00550 1 ERLRELLAEVLGVPA-EEIDPDTDLFDLGLDSLLAVeLIARLEEEFGVEIPPSDLFEHPTLAE 62
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
6-210 |
3.30e-03 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 40.95 E-value: 3.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 6 QLSIVKGLQ-QDFVPRALHRIFEEQQLRHADKVALIYQPsttgQGMapsQSSYRQMNERANRAARLLVAethgRFLQPns 84
Cdd:PRK08315 1 GLSYVRGPTdVPLLEQTIGQLLDRTAARYPDREALVYRD----QGL---RWTYREFNEEVDALAKGLLA----LGIEK-- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 85 dGDFiVAVCMQPSEGLVTTLLAIWKAGGAYLPIDPSFPANRIHHIL--LEAKpTLVIrdddidAGRFQGT---------- 152
Cdd:PRK08315 68 -GDR-VGIWAPNVPEWVLTQFATAKIGAILVTINPAYRLSELEYALnqSGCK-ALIA------ADGFKDSdyvamlyela 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126789033 153 PTLSTTE---LYAKSL------------QLAGSNLLSEEMLRGGNDHIAIVL---------------YTSGSTGVPKGVR 202
Cdd:PRK08315 139 PELATCEpgqLQSARLpelrrviflgdeKHPGMLNFDELLALGRAVDDAELAarqatldpddpiniqYTSGTTGFPKGAT 218
|
....*...
gi 126789033 203 LPHESILN 210
Cdd:PRK08315 219 LTHRNILN 226
|
|
| |
