|
Name |
Accession |
Description |
Interval |
E-value |
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
23-620 |
0e+00 |
|
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: 1053.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 23 KKDGKWEILSFNQYYEASRKAAKAMIKLGLEPFHSVGILGFNSVEWFIAALGAILAGGLCVGIYATNSADACQYAIAHSK 102
Cdd:cd05933 1 KRGDKWHTLTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 103 VNILVVENELQLQKIFSIpKNRIQTLKAIIQYRLPVKEtKNYDLYSWDDFMELGNSIPDSQLDQIIGSQKANQCAVIIYT 182
Cdd:cd05933 81 ANILVVENQKQLQKILQI-QDKLPHLKAIIQYKEPLKE-KEPNLYSWDEFMELGRSIPDEQLDAIISSQKPNQCCTLIYT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 183 SGTTGHPKGAMLSHDNITWMAGAAAMECNLSLAPKKQEVVVSYLPLSHIAAQMMDVWIPMKVGASIYFAQPDALKGTLVN 262
Cdd:cd05933 159 SGTTGMPKGVMLSHDNITWTAKAASQHMDLRPATVGQESVVSYLPLSHIAAQILDIWLPIKVGGQVYFAQPDALKGTLVK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 263 TLQEVKPTAFMGVPRIWEKMHEKIKEAASKSSSLRKKVFSWARNVGLKINTKRMLGAHDTPMSYRMAKALVFSKVKSSLG 342
Cdd:cd05933 239 TLREVRPTAFMGVPRVWEKIQEKMKAVGAKSGTLKRKIASWAKGVGLETNLKLMGGESPSPLFYRLAKKLVFKKVRKALG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 343 LDHCHIFISGAAPLNQETSEFFLSLDIPIGEVYGLSESTGPHSMSTPENYRILSSGKVMTGCKNMLYQQNKEGIGEVCLW 422
Cdd:cd05933 319 LDRCQKFFTGAAPISRETLEFFLSLNIPIMELYGMSETSGPHTISNPQAYRLLSCGKALPGCKTKIHNPDADGIGEICFW 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 423 GRHVFMGYLGSEDATTEAIDKEGWLHSGDLGRVDNKGFLYITGRIKEIIITAGGENVAPIPIENLVKEKLPIISNAMLVG 502
Cdd:cd05933 399 GRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITAGGENVPPVPIEDAVKKELPIISNAMLIG 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 503 DKAKFLSVLLTLKCEVDKTSGEPLDNLTWEAIKFCRDVGSQASTVTEIVELQDPLVYMAIQKGINAVNQQAISNAQKIQK 582
Cdd:cd05933 479 DKRKFLSMLLTLKCEVNPETGEPLDELTEEAIEFCRKLGSQATRVSEIAGGKDPKVYEAIEEGIKRVNKKAISNAQKIQK 558
|
570 580 590
....*....|....*....|....*....|....*...
gi 1811029393 583 WVILEKDFSIGGGELGPTTKMKRHFIIQKYKRQIENLY 620
Cdd:cd05933 559 WVILEKDFSVPGGELGPTMKLKRPVVAKKYKDEIDKLY 596
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
1-620 |
0e+00 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 593.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 1 MTIPEFFQESVNRFGIYPALASKKDGKWEILSFNQYYEASRKAAKAMIKLGLEPFHSVGILGFNSVEWFIAALGAILAGG 80
Cdd:COG1022 11 DTLPDLLRRRAARFPDRVALREKEDGIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 81 LCVGIYATNSADACQYAIAHSKVNILVVENELQLQKIFSIpKNRIQTLKAIIQYRlPVKETKNYDLYSWDDFMELGNSI- 159
Cdd:COG1022 91 VTVPIYPTSSAEEVAYILNDSGAKVLFVEDQEQLDKLLEV-RDELPSLRHIVVLD-PRGLRDDPRLLSLDELLALGREVa 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 160 PDSQLDQIIGSQKANQCAVIIYTSGTTGHPKGAMLSHDNITWMAgAAAMECnlsLAPKKQEVVVSYLPLSHIAAQMMDVW 239
Cdd:COG1022 169 DPAELEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNA-RALLER---LPLGPGDRTLSFLPLAHVFERTVSYY 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 240 IpMKVGASIYFAQ-PDalkgTLVNTLQEVKPTAFMGVPRIWEKMHEKIKEAASKSSSLRKKVFSWARNVGLKINTKRMLG 318
Cdd:COG1022 245 A-LAAGATVAFAEsPD----TLAEDLREVKPTFMLAVPRVWEKVYAGIQAKAEEAGGLKRKLFRWALAVGRRYARARLAG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 319 AHDTP---MSYRMAKALVFSKVKSSLGlDHCHIFISGAAPLNQETSEFFLSLDIPIGEVYGLSESTGPHSMSTPENYRIL 395
Cdd:COG1022 320 KSPSLllrLKHALADKLVFSKLREALG-GRLRFAVSGGAALGPELARFFRALGIPVLEGYGLTETSPVITVNRPGDNRIG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 396 SSGKVMTGCKNMLYQQnkegiGEVCLWGRHVFMGYLGSEDATTEAIDKEGWLHSGDLGRVDNKGFLYITGRIKEIIITAG 475
Cdd:COG1022 399 TVGPPLPGVEVKIAED-----GEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGELDEDGFLRITGRKKDLIVTSG 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 476 GENVAPIPIENLVKEkLPIISNAMLVGDKAKFLSVLLTLKcevdktsgepldnltWEAI-KFCRDVGSQASTVTEIVelQ 554
Cdd:COG1022 474 GKNVAPQPIENALKA-SPLIEQAVVVGDGRPFLAALIVPD---------------FEALgEWAEENGLPYTSYAELA--Q 535
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1811029393 555 DPLVYMAIQKGINAVNQQaISNAQKIQKWVILEKDFSIGGGELGPTTKMKRHFIIQKYKRQIENLY 620
Cdd:COG1022 536 DPEVRALIQEEVDRANAG-LSRAEQIKRFRLLPKEFTIENGELTPTLKLKRKVILEKYADLIEALY 600
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
26-608 |
2.14e-155 |
|
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: 454.36 E-value: 2.14e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 26 GKWEILSFNQYYEASRKAAKAMIKLGLEPFHSVGILGFNSVEWFIAALGAILAGGLCVGIYATNSADACQYAIAHSKVNI 105
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 106 LVVENelqlqkifsipknriqtlkaiiqyrlpvketknydlyswddfmelgnsiPDsqldqiigsqkanQCAVIIYTSGT 185
Cdd:cd05907 81 LFVED-------------------------------------------------PD-------------DLATIIYTSGT 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 186 TGHPKGAMLSHDNITWMAGAAAmecnLSLAPKKQEVVVSYLPLSHIAAQMMDVWIPMKVGASIYFAQPDAlkgTLVNTLQ 265
Cdd:cd05907 99 TGRPKGVMLSHRNILSNALALA----ERLPATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFASSAE---TLLDDLS 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 266 EVKPTAFMGVPRIWEKMHEKIKeaASKSSSLRKKVFSWARnvglkintkrmlgahdtpmsyrmakalvfskvksslgLDH 345
Cdd:cd05907 172 EVRPTVFLAVPRVWEKVYAAIK--VKAVPGLKRKLFDLAV-------------------------------------GGR 212
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 346 CHIFISGAAPLNQETSEFFLSLDIPIGEVYGLSESTGPHSMSTPENYRILSSGKVMTGCKNMLYQQnkegiGEVCLWGRH 425
Cdd:cd05907 213 LRFAASGGAPLPAELLHFFRALGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVEVRIADD-----GEILVRGPN 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 426 VFMGYLGSEDATTEAIDKEGWLHSGDLGRVDNKGFLYITGRIKEIIITAGGENVAPIPIENLVKEKlPIISNAMLVGDKA 505
Cdd:cd05907 288 VMLGYYKNPEATAEALDADGWLHTGDLGEIDEDGFLHITGRKKDLIITSGGKNISPEPIENALKAS-PLISQAVVIGDGR 366
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 506 KFLSVLLTLKCEVdktsgepldnltweAIKFCRDVGSQASTVTEIVElqDPLVYMAIQKGINAVNQQAiSNAQKIQKWVI 585
Cdd:cd05907 367 PFLVALIVPDPEA--------------LEAWAEEHGIAYTDVAELAA--NPAVRAEIEAAVEAANARL-SRYEQIKKFLL 429
|
570 580
....*....|....*....|...
gi 1811029393 586 LEKDFSIGGGELGPTTKMKRHFI 608
Cdd:cd05907 430 LPEPFTIENGELTPTLKLKRPVI 452
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
26-620 |
3.30e-95 |
|
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: 302.60 E-value: 3.30e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 26 GKWEILSFNQYYEASRKAAKAMIKLGLEPF--HSVGILGFNSVEWFIAALGAILAGGLCVGIYATNSADACQYAIAHSKV 103
Cdd:cd05927 1 GPYEWISYKEVAERADNIGSALRSLGGKPApaSFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 104 NILVVEnelqlqkifsipknriqtlkaiiqyrlpvketKNYDLYSWDDFMELGNSIPdsqLDQIIGsqKANQCAVIIYTS 183
Cdd:cd05927 81 SIVFCD--------------------------------AGVKVYSLEEFEKLGKKNK---VPPPPP--KPEDLATICYTS 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 184 GTTGHPKGAMLSHDNItwMAGAAAMECNLSLAPK--KQEVVVSYLPLSHIAAQMMdVWIPMKVGASIYFAQPDALKgtLV 261
Cdd:cd05927 124 GTTGNPKGVMLTHGNI--VSNVAGVFKILEILNKinPTDVYISYLPLAHIFERVV-EALFLYHGAKIGFYSGDIRL--LL 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 262 NTLQEVKPTAFMGVPRIWEKMHEKIKEAASKSSSLRKKVFSWARNvgLKINTKRMLGAHDTPMSYRmakaLVFSKVKSSL 341
Cdd:cd05927 199 DDIKALKPTVFPGVPRVLNRIYDKIFNKVQAKGPLKRKLFNFALN--YKLAELRSGVVRASPFWDK----LVFNKIKQAL 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 342 GLdHCHIFISGAAPLNQETSEFFLS-LDIPIGEVYGLSESTGPHSMSTPENYRILSSGKVMTGCK-------NMLYQQNK 413
Cdd:cd05927 273 GG-NVRLMLTGSAPLSPEVLEFLRVaLGCPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCAEvklvdvpEMNYDAKD 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 414 E-GIGEVCLWGRHVFMGYLGSEDATTEAIDKEGWLHSGDLGRVDNKGFLYITGRIKEIIITAGGENVAPIPIENLVKeKL 492
Cdd:cd05927 352 PnPRGEVCIRGPNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLSQGEYVAPEKIENIYA-RS 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 493 PIISNAMLVGDKAKflSVLLTLKCeVDKTSGEPldnltWEAikfcrdvgSQASTVTEIVEL-QDPLVYMAIQKGINAVNQ 571
Cdd:cd05927 431 PFVAQIFVYGDSLK--SFLVAIVV-PDPDVLKE-----WAA--------SKGGGTGSFEELcKNPEVKKAILEDLVRLGK 494
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 1811029393 572 QAISNAQKIQKWVILEKD-FSIGGGELGPTTKMKRHFIIQKYKRQIENLY 620
Cdd:cd05927 495 ENGLKGFEQVKAIHLEPEpFSVENGLLTPTFKLKRPQLKKYYKKQIDEMY 544
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
7-474 |
4.97e-93 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 292.68 E-value: 4.97e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 7 FQESVNRFGIYPALAskkDGKWEILSFNQYYEASRKAAKAMIKLGLEPFHSVGILGFNSVEWFIAALGAILAGGLCVGIY 86
Cdd:pfam00501 1 LERQAARTPDKTALE---VGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 87 ATNSADACQYAIAHSKVNILVVENELQLQKIFSIPKNRIQTLKAIIQYRLPVKETKNYDlyswddfmelGNSIPDSQLDQ 166
Cdd:pfam00501 78 PRLPAEELAYILEDSGAKVLITDDALKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLP----------EEAKPADVPPP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 167 IIGSQKANQCAVIIYTSGTTGHPKGAMLSHDNITWMAGAAAMECNLSLAPKKQEVVVSYLPLSHIAAQMMDVWIPMKVGA 246
Cdd:pfam00501 148 PPPPPDPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 247 SIYFAQPDALK--GTLVNTLQEVKPTAFMGVPRIWEKMHEKIKEAASKSSSLRkkvfswarnvglkintkrmlgahdtpm 324
Cdd:pfam00501 228 TVVLPPGFPALdpAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLR--------------------------- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 325 syrmakalvfskvksslgldhchIFISGAAPLNQETSEFFLS-LDIPIGEVYGLSESTGPHSMSTPENYR---ILSSGKV 400
Cdd:pfam00501 281 -----------------------LVLSGGAPLPPELARRFRElFGGALVNGYGLTETTGVVTTPLPLDEDlrsLGSVGRP 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 401 MTGC-------KNMLYQQNKEgIGEVCLWGRHVFMGYLGSEDATTEAIDKEGWLHSGDLGRVDNKGFLYITGRIKEIIIT 473
Cdd:pfam00501 338 LPGTevkivddETGEPVPPGE-PGELCVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKL 416
|
.
gi 1811029393 474 A 474
Cdd:pfam00501 417 G 417
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
20-612 |
1.35e-85 |
|
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341296 [Multi-domain] Cd Length: 569 Bit Score: 278.15 E-value: 1.35e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 20 LASKKDGKWEILSFNQYYEASRKAAKAMIKLGLEPFHSVGILGFNSVEWFIAALGAILAGGLCVGIYATNSADACQYAIA 99
Cdd:cd17641 1 LREKDFGIWQEFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 100 HSKVNILVVENELQLQKIFSIpKNRIQTLKAIIqYRLPvKETKNYD---LYSWDDFMELGNSIP---DSQLDQIIGSQKA 173
Cdd:cd17641 81 YTGARVVIAEDEEQVDKLLEI-ADRIPSVRYVI-YCDP-RGMRKYDdprLISFEDVVALGRALDrrdPGLYEREVAAGKG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 174 NQCAVIIYTSGTTGHPKGAMLSHDNITWMAGAAamecnLSLAPKKQ-EVVVSYLPLSHIAAQMMDVWIPMKVGASIYFAQ 252
Cdd:cd17641 158 EDVAVLCTTSGTTGKPKLAMLSHGNFLGHCAAY-----LAADPLGPgDEYVSVLPLPWIGEQMYSVGQALVCGFIVNFPE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 253 PDAlkgTLVNTLQEVKPTAFMGVPRIWEKMHEKIKEAASKSSSLRKKVFSWARNVGLKINTKRMLGAHDT---PMSYRMA 329
Cdd:cd17641 233 EPE---TMMEDLREIGPTFVLLPPRVWEGIAADVRARMMDATPFKRFMFELGMKLGLRALDRGKRGRPVSlwlRLASWLA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 330 KALVFSKVKSSLGLDHCHIFISGAAPLNQETSEFFLSLDIPIGEVYGLSESTGPHSMSTPENYRILSSGKVMTGCknmly 409
Cdd:cd17641 310 DALLFRPLRDRLGFSRLRSAATGGAALGPDTFRFFHAIGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGT----- 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 410 QQNKEGIGEVCLWGRHVFMGYLGSEDATTEAIDKEGWLHSGDLGRVDNKGFLYITGRIKEIIITAGGENVAPIPIENLVK 489
Cdd:cd17641 385 EVRIDEVGEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTTSDGTRFSPQFIENKLK 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 490 EKlPIISNAMLVGDKAKFLSVLLtlkcevdktsgepldNLTWEAI-KFCRDVGSQASTVTEIVelQDPLVYMAIQKGINA 568
Cdd:cd17641 465 FS-PYIAEAVVLGAGRPYLTAFI---------------CIDYAIVgKWAEQRGIAFTTYTDLA--SRPEVYELIRKEVEK 526
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1811029393 569 VNqQAISNAQKIQKWVILEKDFSIGGGELGPTTKMKRHFIIQKY 612
Cdd:cd17641 527 VN-ASLPEAQRIRRFLLLYKELDADDGELTRTRKVRRGVIAEKY 569
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
25-612 |
2.16e-72 |
|
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: 241.60 E-value: 2.16e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 25 DGKWEILSFNQYYEASRKAAKAMIKLGLEPFHSVGILGFNSVEWFIAALGAILAGGLCVGIYATNSADACQYAIAHSKVN 104
Cdd:cd05932 1 GGQVVEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 105 ILVVenelqlQKIFSIPKNRIQTLKAIIQYRLPVKETKNYDlYSWDDFMELGNSIPDSQLdqiigsQKANQCAVIIYTSG 184
Cdd:cd05932 81 ALFV------GKLDDWKAMAPGVPEGLISISLPPPSAANCQ-YQWDDLIAQHPPLEERPT------RFPEQLATLIYTSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 185 TTGHPKGAMLSHDNITWmAGAAAMEcnlSLAPKKQEVVVSYLPLSHIAAQMMDVWIPMKVGASIYFAQpdALKgTLVNTL 264
Cdd:cd05932 148 TTGQPKGVMLTFGSFAW-AAQAGIE---HIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAE--SLD-TFVEDV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 265 QEVKPTAFMGVPRIWEKMHEKIKEaaskssslrkkvfswarnvglKINTKRMlgahDTPMSYRMAKALVFSKVKSSLGLD 344
Cdd:cd05932 221 QRARPTLFFSVPRLWTKFQQGVQD---------------------KIPQQKL----NLLLKIPVVNSLVKRKVLKGLGLD 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 345 HCHIFISGAAPLNQETSEFFLSLDIPIGEVYGLSESTGPHSMSTPENYRILSSGKVMTGCKNMLYQQnkegiGEVCLWGR 424
Cdd:cd05932 276 QCRLAGCGSAPVPPALLEWYRSLGLNILEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRISED-----GEILVRSP 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 425 HVFMGYLGSEDATTEAIDKEGWLHSGDLGRVDNKGFLYITGRIKEIIITAGGENVAPIPIENlvkeKLPIISNAMLVgdk 504
Cdd:cd05932 351 ALMMGYYKDPEATAEAFTADGFLRTGDKGELDADGNLTITGRVKDIFKTSKGKYVAPAPIEN----KLAEHDRVEMV--- 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 505 akflsvlltlkCEVDKTSGEPLdnltweAIKFCRDVGSQASTVTEIVELQDPLvymaiQKGINAVNQQAISNAQkIQKWV 584
Cdd:cd05932 424 -----------CVIGSGLPAPL------ALVVLSEEARLRADAFARAELEASL-----RAHLARVNSTLDSHEQ-LAGIV 480
|
570 580
....*....|....*....|....*...
gi 1811029393 585 ILEKDFSIGGGELGPTTKMKRHFIIQKY 612
Cdd:cd05932 481 VVKDPWSIDNGILTPTLKIKRNVLEKAY 508
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
3-502 |
1.28e-71 |
|
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: 237.79 E-value: 1.28e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 3 IPEFFQESVNRFGIYPALASKkdgkWEILSFNQYYEASRKAAKAMIKLGLEPFHSVGILGFNSVEWFIAALGAILAGGLC 82
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFG----GRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 83 VGIYATNSADACQYAIAHSKVNILVvenelqlqkifsipknriqtlkaiiqyrlpvketknydlyswddfmelgnsipds 162
Cdd:COG0318 77 VPLNPRLTAEELAYILEDSGARALV------------------------------------------------------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 163 qldqiigsqkanqCAVIIYTSGTTGHPKGAMLSHDNITWMAGAAAMECNLSlapkKQEVVVSYLPLSHIAAQMMDVWIPM 242
Cdd:COG0318 102 -------------TALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLT----PGDVVLVALPLFHVFGLTVGLLAPL 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 243 KVGASIYFA-QPDAlkGTLVNTLQEVKPTAFMGVPRIWEKMHEKIKEAASKSSSLRkkvfswarnvglkintkrmlgahd 321
Cdd:COG0318 165 LAGATLVLLpRFDP--ERVLELIERERVTVLFGVPTMLARLLRHPEFARYDLSSLR------------------------ 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 322 tpmsyrmakalvfskvksslgldhchIFISGAAPLNQETSEFFLS-LDIPIGEVYGLSEsTGPHSMSTPENY---RILSS 397
Cdd:COG0318 219 --------------------------LVVSGGAPLPPELLERFEErFGVRIVEGYGLTE-TSPVVTVNPEDPgerRPGSV 271
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 398 GKVMTGCKNMLYqqNKEG-------IGEVCLWGRHVFMGYLGSEDATTEAIdKEGWLHSGDLGRVDNKGFLYITGRIKEI 470
Cdd:COG0318 272 GRPLPGVEVRIV--DEDGrelppgeVGEIVVRGPNVMKGYWNDPEATAEAF-RDGWLRTGDLGRLDEDGYLYIVGRKKDM 348
|
490 500 510
....*....|....*....|....*....|..
gi 1811029393 471 IITaGGENVAPIPIENLVKEkLPIISNAMLVG 502
Cdd:COG0318 349 IIS-GGENVYPAEVEEVLAA-HPGVAEAAVVG 378
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
35-554 |
1.13e-70 |
|
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: 235.80 E-value: 1.13e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 35 QYYEASRKAAKAMIKL---GLEPFHSVGILGFNSVEWFIAALGAILAGGLCVGIYATNSADACQYAIAHSKVNILVVENE 111
Cdd:cd05914 9 TYKDLADNIAKFALLLkinGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFVSDE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 112 lqlqkifsipknriqtlkaiiqyrlpvketknydlyswDDFmelgnsipdsqldqiigsqkanqcAVIIYTSGTTGHPKG 191
Cdd:cd05914 89 --------------------------------------DDV------------------------ALINYTSGTTGNSKG 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 192 AMLSHDNITW-MAGAAAMEcnlslAPKKQEVVVSYLPLSHIAAQMMDVWIPMKVGASIYFAqpDALKGTLVNTLQEVKPT 270
Cdd:cd05914 107 VMLTYRNIVSnVDGVKEVV-----LLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFL--DKIPSAKIIALAFAQVT 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 271 AFMGVPRIWEKMHEKIKEAASKSSslrKKVFSWARNVglKINTKRMlgahdtpmsyrmaKALVFSKVKSSLGlDHCHIFI 350
Cdd:cd05914 180 PTLGVPVPLVIEKIFKMDIIPKLT---LKKFKFKLAK--KINNRKI-------------RKLAFKKVHEAFG-GNIKEFV 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 351 SGAAPLNQETSEFFLSLDIPIGEVYGLSEsTGPH-SMSTPENYRILSSGKVMTGCKNMLYQQN-KEGIGEVCLWGRHVFM 428
Cdd:cd05914 241 IGGAKINPDVEEFLRTIGFPYTIGYGMTE-TAPIiSYSPPNRIRLGSAGKVIDGVEVRIDSPDpATGEGEIIVRGPNVMK 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 429 GYLGSEDATTEAIDKEGWLHSGDLGRVDNKGFLYITGRIKEIIITAGGENVAPIPIEN-LVKEKLPIISnamLVGDKAKF 507
Cdd:cd05914 320 GYYKNPEATAEAFDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSSGKNIYPEEIEAkINNMPFVLES---LVVVQEKK 396
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1811029393 508 LSVLLTLKCEVDKTSG----EPLDNLTWEAIKfcrDVGSQASTVTEIVELQ 554
Cdd:cd05914 397 LVALAYIDPDFLDVKAlkqrNIIDAIKWEVRD---KVNQKVPNYKKISKVK 444
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
2-620 |
3.16e-66 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 228.83 E-value: 3.16e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 2 TIPEFFQESVNRFGIYPALASK--KDG-----KWeiLSFNQYYEASRKAAKAMIKLGLEPFHSVGILGFNSVEWFIAALG 74
Cdd:PLN02736 45 TLHDNFVYAVETFRDYKYLGTRirVDGtvgeyKW--MTYGEAGTARTAIGSGLVQHGIPKGACVGLYFINRPEWLIVDHA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 75 AILAGGLCVGIYATNSADACQYAIAHSKVN-ILVVENELQ--LQKIFSIPKNRIQTLKAIIQYRLP-VKETKNYDLYSWD 150
Cdd:PLN02736 123 CSAYSYVSVPLYDTLGPDAVKFIVNHAEVAaIFCVPQTLNtlLSCLSEIPSVRLIVVVGGADEPLPsLPSGTGVEIVTYS 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 151 DFMELGNSIPdsqldQIIGSQKANQCAVIIYTSGTTGHPKGAMLSHDNItwMAGAAAMECNLSLAPkkQEVVVSYLPLSH 230
Cdd:PLN02736 203 KLLAQGRSSP-----QPFRPPKPEDVATICYTSGTTGTPKGVVLTHGNL--IANVAGSSLSTKFYP--SDVHISYLPLAH 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 231 IAaQMMDVWIPMKVGASIYFAQPDALKgtLVNTLQEVKPTAFMGVPRIWEKMHEKIKEAASKSSSLRKKVFSWArnvglk 310
Cdd:PLN02736 274 IY-ERVNQIVMLHYGVAVGFYQGDNLK--LMDDLAALRPTIFCSVPRLYNRIYDGITNAVKESGGLKERLFNAA------ 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 311 INTKRMLGAHDTPMSyRMAKALVFSKVKSSLGlDHCHIFISGAAPLNQETSEFflsLDIPIG----EVYGLSESTGPHSM 386
Cdd:PLN02736 345 YNAKKQALENGKNPS-PMWDRLVFNKIKAKLG-GRVRFMSSGASPLSPDVMEF---LRICFGgrvlEGYGMTETSCVISG 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 387 STPENYRILSSGKVMTGCK-------NMLYQQNKEGI--GEVCLWGRHVFMGYLGSEDATTEAIDKEGWLHSGDLGRVDN 457
Cdd:PLN02736 420 MDEGDNLSGHVGSPNPACEvklvdvpEMNYTSEDQPYprGEICVRGPIIFKGYYKDEVQTREVIDEDGWLHTGDIGLWLP 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 458 KGFLYITGRIKEIIITAGGENVAPIPIENlVKEKLPIISNAMLVGDkaKFLSVLltlkceVDKTSGEPLDNLTWEAikfc 537
Cdd:PLN02736 500 GGRLKIIDRKKNIFKLAQGEYIAPEKIEN-VYAKCKFVAQCFVYGD--SLNSSL------VAVVVVDPEVLKAWAA---- 566
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 538 rdvgSQASTVTEIVEL-QDPLVYMAIQKGINAVNQQAISNAQKIQKWVILEKD-FSIGGGELGPTTKMKRHFIIQKYKRQ 615
Cdd:PLN02736 567 ----SEGIKYEDLKQLcNDPRVRAAVLADMDAVGREAQLRGFEFAKAVTLVPEpFTVENGLLTPTFKVKRPQAKAYFAKA 642
|
....*
gi 1811029393 616 IENLY 620
Cdd:PLN02736 643 ISDMY 647
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
31-608 |
7.62e-64 |
|
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: 218.62 E-value: 7.62e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 31 LSFNQYYEASRKAAKAMIKLGLEPFHSVGILGFNSVEWFIAALGAILAGGLCVGIYATNSADACQYAIAHSKVNIlvven 110
Cdd:cd17639 6 MSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECSA----- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 111 elqlqkifsipknriqtlkaiiqyrlpvketknydlyswddfmelgnsipdsqldqIIGSQKANQCAVIIYTSGTTGHPK 190
Cdd:cd17639 81 --------------------------------------------------------IFTDGKPDDLACIMYTSGSTGNPK 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 191 GAMLSHDNITwmAGAAAMECNLSLAPKKQEVVVSYLPLSHI---AAQMmdvwIPMKVGASIYFAQPDalkgTLVNT---- 263
Cdd:cd17639 105 GVMLTHGNLV--AGIAGLGDRVPELLGPDDRYLAYLPLAHIfelAAEN----VCLYRGGTIGYGSPR----TLTDKskrg 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 264 ----LQEVKPTAFMGVPRIWEKMHEKIKEAASKSSSLRKKVFSWARNVGLKintkRMLGAHDTPMsyrmAKALVFSKVKS 339
Cdd:cd17639 175 ckgdLTEFKPTLMVGVPAIWDTIRKGVLAKLNPMGGLKRTLFWTAYQSKLK----ALKEGPGTPL----LDELVFKKVRA 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 340 SLGlDHCHIFISGAAPLNQETSEFFLSLDIPIGEVYGLSESTGPHSMSTPENYRILSSGKVMTGCKNML--------YQQ 411
Cdd:cd17639 247 ALG-GRLRYMLSGGAPLSADTQEFLNIVLCPVIQGYGLTETCAGGTVQDPGDLETGRVGPPLPCCEIKLvdweeggySTD 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 412 NKEGIGEVCLWGRHVFMGYLGSEDATTEAIDKEGWLHSGDLGRVDNKGFLYITGRIKEIIITAGGENVAPIPIENLVKEk 491
Cdd:cd17639 326 KPPPRGEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQNGEYIALEKLESIYRS- 404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 492 LPIISNAMLVGDKAKFLSVLLTLKCEVdktsgepldnltwEAIKFCRDVGSQASTVTEIVElqDPLVYMAIQKGINAV-N 570
Cdd:cd17639 405 NPLVNNICVYADPDKSYPVAIVVPNEK-------------HLTKLAEKHGVINSEWEELCE--DKKLQKAVLKSLAETaR 469
|
570 580 590
....*....|....*....|....*....|....*...
gi 1811029393 571 QQAISNAQKIQKWVILEKDFSIGGGELGPTTKMKRHFI 608
Cdd:cd17639 470 AAGLEKFEIPQGVVLLDEEWTPENGLVTAAQKLKRKEI 507
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
7-620 |
1.06e-62 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 219.30 E-value: 1.06e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 7 FQESVNRFGIYPALASKK--DGK-----WEilSFNQYYEASRKAAKAMIKLGLEPFHSVGILGFNSVEWfIAALGAILAG 79
Cdd:PLN02430 48 FSKSVEKYPDNKMLGWRRivDGKvgpymWK--TYKEVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQW-IVAMEACAAH 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 80 GL-CVGIYATNSADACQYAIAHSKVNILVVENElQLQKIFSIPKNRIQTLKAIIQYRLPVKETKN------YDLYSWDDF 152
Cdd:PLN02430 125 SLiCVPLYDTLGPGAVDYIVDHAEIDFVFVQDK-KIKELLEPDCKSAKRLKAIVSFTSVTEEESDkasqigVKTYSWIDF 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 153 MELGNSIPDSqldqiIGSQKANQCAVIIYTSGTTGHPKGAMLSHDNI-TWMAGAAAMECNLSLAPKKQEVVVSYLPLSHI 231
Cdd:PLN02430 204 LHMGKENPSE-----TNPPKPLDICTIMYTSGTSGDPKGVVLTHEAVaTFVRGVDLFMEQFEDKMTHDDVYLSFLPLAHI 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 232 AAQMMDVWIPMKvGASI--YFAQPDALKgtlvNTLQEVKPTAFMGVPRIWEKMHEKIKEAASKSSSLRKKVFswarNVGL 309
Cdd:PLN02430 279 LDRMIEEYFFRK-GASVgyYHGDLNALR----DDLMELKPTLLAGVPRVFERIHEGIQKALQELNPRRRLIF----NALY 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 310 KINTKRMLGAHDTPMSYRMAKALVFSKVKSSLGlDHCHIFISGAAPLNQETSEFF-LSLDIPIGEVYGLSESTGPHSMST 388
Cdd:PLN02430 350 KYKLAWMNRGYSHKKASPMADFLAFRKVKAKLG-GRLRLLISGGAPLSTEIEEFLrVTSCAFVVQGYGLTETLGPTTLGF 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 389 PENYRILSSGKVMTGCKNMLYQQNKE---------GIGEVCLWGRHVFMGYLGSEDATTEAIdKEGWLHSGDLGRVDNKG 459
Cdd:PLN02430 429 PDEMCMLGTVGAPAVYNELRLEEVPEmgydplgepPRGEICVRGKCLFSGYYKNPELTEEVM-KDGWFHTGDIGEILPNG 507
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 460 FLYITGRIKEIIITAGGENVAPIPIENlVKEKLPIISNAMLVGDKAKFLSVLLTLKCEvdktsgeplDNLTweaiKFCRD 539
Cdd:PLN02430 508 VLKIIDRKKNLIKLSQGEYVALEYLEN-VYGQNPIVEDIWVYGDSFKSMLVAVVVPNE---------ENTN----KWAKD 573
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 540 VGSQAStVTEIVELqdPLVYMAIQKGINAVNQQAISNAQKIQKWVILE-KDFSIGGGELGPTTKMKRHFIIQKYKRQIEN 618
Cdd:PLN02430 574 NGFTGS-FEELCSL--PELKEHILSELKSTAEKNKLRGFEYIKGVILEtKPFDVERDLVTATLKKRRNNLLKYYQVEIDE 650
|
..
gi 1811029393 619 LY 620
Cdd:PLN02430 651 MY 652
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
5-620 |
3.59e-62 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 217.79 E-value: 3.59e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 5 EFFQESVNRFGIYPALASK-----KDGKWEILSFNQYYEASRKAAKAMIKLGLEPFHSVGILGFNSVEWfIAALGAILAG 79
Cdd:PLN02861 47 QFFSDAVKKYPNNQMLGRRqvtdsKVGPYVWLTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEW-IIAMEACNSQ 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 80 GLC-VGIYATNSADACQYAIAHSKVNILVVEnELQLQKIFSIPKNRIQTLKAIIQY----RLPVKETKNY--DLYSWDDF 152
Cdd:PLN02861 126 GITyVPLYDTLGANAVEFIINHAEVSIAFVQ-ESKISSILSCLPKCSSNLKTIVSFgdvsSEQKEEAEELgvSCFSWEEF 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 153 MELGNSipDSQLDQiigSQKANQCAvIIYTSGTTGHPKGAMLSHDNItwMAGAAAMECNLSLAPK---KQEVVVSYLPLS 229
Cdd:PLN02861 205 SLMGSL--DCELPP---KQKTDICT-IMYTSGTTGEPKGVILTNRAI--IAEVLSTDHLLKVTDRvatEEDSYFSYLPLA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 230 HIAAQMMDVWIPMKvGASIYFAQPDALkgTLVNTLQEVKPTAFMGVPRIWEKMHEKIKEAASKSSSLRKKVFSWARNVGL 309
Cdd:PLN02861 277 HVYDQVIETYCISK-GASIGFWQGDIR--YLMEDVQALKPTIFCGVPRVYDRIYTGIMQKISSGGMLRKKLFDFAYNYKL 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 310 KINTKRMLGAHDTPMSYRmakaLVFSKVKSSLGlDHCHIFISGAAPLNQETSEFFLSLDIP-IGEVYGLSESTGPHSMST 388
Cdd:PLN02861 354 GNLRKGLKQEEASPRLDR----LVFDKIKEGLG-GRVRLLLSGAAPLPRHVEEFLRVTSCSvLSQGYGLTESCGGCFTSI 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 389 PENYRILSS-GKVMTGCKNMLYQQNKEGI--------GEVCLWGRHVFMGYLGSEDATTEAIdKEGWLHSGDLGRVDNKG 459
Cdd:PLN02861 429 ANVFSMVGTvGVPMTTIEARLESVPEMGYdalsdvprGEICLRGNTLFSGYHKRQDLTEEVL-IDGWFHTGDIGEWQPNG 507
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 460 FLYITGRIKEIIITAGGENVAPIPIENlVKEKLPIISNAMLVGDkaKFLSVLLTLKCEvDKTSGEpldnltweaikfcrD 539
Cdd:PLN02861 508 AMKIIDRKKNIFKLSQGEYVAVENLEN-TYSRCPLIASIWVYGN--SFESFLVAVVVP-DRQALE--------------D 569
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 540 VGSQASTVTEIVEL-QDPLVYMAIQKGINAVNQQAISNAQKIQKWVILEKD-FSIGGGELGPTTKMKRHFIIQKYKRQIE 617
Cdd:PLN02861 570 WAANNNKTGDFKSLcKNLKARKYILDELNSTGKKLQLRGFEMLKAIHLEPNpFDIERDLITPTFKLKRPQLLKYYKDCID 649
|
...
gi 1811029393 618 NLY 620
Cdd:PLN02861 650 QLY 652
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
5-620 |
2.58e-61 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 215.65 E-value: 2.58e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 5 EFFQESVNRFGIYPALASK-----KDGKWEILSFNQYYEASRKAAKAMIKLGLEPFHSVGILGFNSVEWFIAALGAILAG 79
Cdd:PLN02614 49 DVFRMSVEKYPNNPMLGRReivdgKPGKYVWQTYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHG 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 80 GLCVGIYATNSADACQYAIAHSKVNILVVEnELQLQKIFSIPKNRIQTLKAIIQY----RLPVKETKNYDL--YSWDDFM 153
Cdd:PLN02614 129 LYCVPLYDTLGAGAVEFIISHSEVSIVFVE-EKKISELFKTCPNSTEYMKTVVSFggvsREQKEEAETFGLviYAWDEFL 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 154 ELGNSipdSQLDQIIgsQKANQCAVIIYTSGTTGHPKGAMLSHDNI-TWMAGAAAMECNLSLAPKKQEVVVSYLPLSHIA 232
Cdd:PLN02614 208 KLGEG---KQYDLPI--KKKSDICTIMYTSGTTGDPKGVMISNESIvTLIAGVIRLLKSANAALTVKDVYLSYLPLAHIF 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 233 AQMMDVWIpMKVGASIYFAQPDAlkGTLVNTLQEVKPTAFMGVPRIWEKMHEKIKEAASKSSSLRKKVFSWARNVGLKIN 312
Cdd:PLN02614 283 DRVIEECF-IQHGAAIGFWRGDV--KLLIEDLGELKPTIFCAVPRVLDRVYSGLQKKLSDGGFLKKFVFDSAFSYKFGNM 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 313 TKRMLGAHDTPMSYRmakaLVFSKVKSSLGlDHCHIFISGAAPLNQETSEFFLSLD-IPIGEVYGLSESTGPHSMSTPEN 391
Cdd:PLN02614 360 KKGQSHVEASPLCDK----LVFNKVKQGLG-GNVRIILSGAAPLASHVESFLRVVAcCHVLQGYGLTESCAGTFVSLPDE 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 392 YRILssGKVMTGCKNM------LYQQNKEGI-----GEVCLWGRHVFMGYLGSEDATTEAIdKEGWLHSGDLGRVDNKGF 460
Cdd:PLN02614 435 LDML--GTVGPPVPNVdirlesVPEMEYDALastprGEICIRGKTLFSGYYKREDLTKEVL-IDGWLHTGDVGEWQPNGS 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 461 LYITGRIKEIIITAGGENVAPIPIENLVKEkLPIISNAMLVGDkaKFLSVLLTL----KCEVDKTSGEPLDNLTWEAIkf 536
Cdd:PLN02614 512 MKIIDRKKNIFKLSQGEYVAVENIENIYGE-VQAVDSVWVYGN--SFESFLVAIanpnQQILERWAAENGVSGDYNAL-- 586
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 537 CRDVGSQASTVTEivelqdpLVYMAIQKGINAVnqqaisnaqKIQKWVILEK-DFSIGGGELGPTTKMKRHFIIQKYKRQ 615
Cdd:PLN02614 587 CQNEKAKEFILGE-------LVKMAKEKKMKGF---------EIIKAIHLDPvPFDMERDLLTPTFKKKRPQLLKYYQSV 650
|
....*
gi 1811029393 616 IENLY 620
Cdd:PLN02614 651 IDEMY 655
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
29-608 |
8.11e-61 |
|
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: 209.52 E-value: 8.11e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 29 EILSFNQYYEASRKAAKAMIKLGLEPFHSVGILGFNSVEWFIAALGAILAGGLCVGIYATNSADACQYAIAHSKVNILVV 108
Cdd:cd17640 4 KRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 109 ENElqlqkifsipknriqtlkaiiqyrlpvketknydlyswddfmelGNSIpdsqldqiigsqkanqcAVIIYTSGTTGH 188
Cdd:cd17640 84 END--------------------------------------------SDDL-----------------ATIIYTSGTTGN 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 189 PKGAMLSHDNITW-MAGAAAMecnlsLAPKKQEVVVSYLPLSHIAAQMMDVWIPMKvGASIYFAQPDALKgtlvNTLQEV 267
Cdd:cd17640 103 PKGVMLTHANLLHqIRSLSDI-----VPPQPGDRFLSILPIWHSYERSAEYFIFAC-GCSQAYTSIRTLK----DDLKRV 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 268 KPTAFMGVPRIWEKMHEKIKEAASKSSSLRKKVFSWArnvgLKINTKRMLgahdtpmsyrmakalvfskvksslgldhch 347
Cdd:cd17640 173 KPHYIVSVPRLWESLYSGIQKQVSKSSPIKQFLFLFF----LSGGIFKFG------------------------------ 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 348 ifISGAAPLNQETSEFFLSLDIPIGEVYGLSESTGPHSMSTPENYRILSSGKVMTGCKNMLYQQNKEGI------GEVCL 421
Cdd:cd17640 219 --ISGGGALPPHVDTFFEAIGIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIVDPEGNVVlppgekGIVWV 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 422 WGRHVFMGYLGSEDATTEAIDKEGWLHSGDLGRVDNKGFLYITGRIKEIIITAGGENVAPIPIENlVKEKLPIISNAMLV 501
Cdd:cd17640 297 RGPQVMKGYYKNPEATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSNGENVEPQPIEE-ALMRSPFIEQIMVV 375
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 502 GDKAKFLSVL-LTLKCEVDKTSGEpldnltwEAIKFCRDVGSQASTVTEIVELQDplvymAIQKGINavNQQAISNAQKI 580
Cdd:cd17640 376 GQDQKRLGALiVPNFEELEKWAKE-------SGVKLANDRSQLLASKKVLKLYKN-----EIKDEIS--NRPGFKSFEQI 441
|
570 580
....*....|....*....|....*...
gi 1811029393 581 QKWVILEKDFsIGGGELGPTTKMKRHFI 608
Cdd:cd17640 442 APFALLEEPF-IENGEMTQTMKIKRNVV 468
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
175-490 |
2.62e-60 |
|
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: 204.44 E-value: 2.62e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 175 QCAVIIYTSGTTGHPKGAMLSHDNitWMAGAAAMECNLSLAPkkQEVVVSYLPLSHIAaQMMDVWIPMKVGASIYFAQPD 254
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRN--LLAAAAALAASGGLTE--GDVFLSTLPLFHIG-GLFGLLGALLAGGTVVLLPKF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 255 aLKGTLVNTLQEVKPTAFMGVPRIWEKMHEKIKEAASKSSSLRkkvfswarnvglkintkrmlgahdtpmsyrmakalvf 334
Cdd:cd04433 76 -DPEAALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLR------------------------------------- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 335 skvksslgldhchIFISGAAPLNQETSEFFLSL-DIPIGEVYGLSESTGPHSMSTPEN--YRILSSGKVMTGCKNMLYQQ 411
Cdd:cd04433 118 -------------ALVSGGAPLPPELLERFEEApGIKLVNGYGLTETGGTVATGPPDDdaRKPGSVGRPVPGVEVRIVDP 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 412 NKE-----GIGEVCLWGRHVFMGYLGsEDATTEAIDKEGWLHSGDLGRVDNKGFLYITGRIKEIIITaGGENVAPIPIEN 486
Cdd:cd04433 185 DGGelppgEIGELVVRGPSVMKGYWN-NPEATAAVDEDGWYRTGDLGRLDEDGYLYIVGRLKDMIKS-GGENVYPAEVEA 262
|
....
gi 1811029393 487 LVKE 490
Cdd:cd04433 263 VLLG 266
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
31-502 |
3.89e-56 |
|
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: 197.44 E-value: 3.89e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 31 LSFNQYYEASRKAAKAMIKLGLEPFHSVGILGFNSVEWFIAALGAILAGGLCVGIYATNSADACQYAIAHSKVNILVVEN 110
Cdd:cd05911 11 LTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTDP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 111 ELqLQKI-----FSIPKNRIQTLKAIIQYRLPVKETknydlyswdDFMELGNSIPDSQLDQIIGsqkANQCAVIIYTSGT 185
Cdd:cd05911 91 DG-LEKVkeaakELGPKDKIIVLDDKPDGVLSIEDL---------LSPTLGEEDEDLPPPLKDG---KDDTAAILYSSGT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 186 TGHPKGAMLSHDNITwmagAAAMECNLSLAP--KKQEVVVSYLPLSHIAAQMMDVWIPMKvGASIY-FAQPDALkgTLVN 262
Cdd:cd05911 158 TGLPKGVCLSHRNLI----ANLSQVQTFLYGndGSNDVILGFLPLYHIYGLFTTLASLLN-GATVIiMPKFDSE--LFLD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 263 TLQEVKPT-AFMgVPRIWEKMhekikeaaSKSSSLRKkvfswarnvglkintkrmlgaHDTpmsyrmakalvfskvkSSL 341
Cdd:cd05911 231 LIEKYKITfLYL-VPPIAAAL--------AKSPLLDK---------------------YDL----------------SSL 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 342 gldhcHIFISGAAPLNQETSEFFLSLDIP--IGEVYGLSESTGPHSMSTPENYRILSSGKVMTGCKNMLyqQNKEG---- 415
Cdd:cd05911 265 -----RVILSGGAPLSKELQELLAKRFPNatIKQGYGMTETGGILTVNPDGDDKPGSVGRLLPNVEAKI--VDDDGkdsl 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 416 ----IGEVCLWGRHVFMGYLGSEDATTEAIDKEGWLHSGDLGRVDNKGFLYITGRIKEiIITAGGENVAPIPIENLVKEk 491
Cdd:cd05911 338 gpnePGEICVRGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKKE-LIKYKGFQVAPAELEAVLLE- 415
|
490
....*....|.
gi 1811029393 492 LPIISNAMLVG 502
Cdd:cd05911 416 HPGVADAAVIG 426
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
1-502 |
7.53e-56 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 197.43 E-value: 7.53e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 1 MTIPEFFQESVNRFGIYPALAskkDGKwEILSFNQYYEASRKAAKAMIKLGLEPFHSVGILGFNSVEWFIAALGAILAGG 80
Cdd:PRK07656 5 MTLPELLARAARRFGDKEAYV---FGD-QRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 81 LCVGIYATNSADACQYAIAHSKVNILVVENELqLQKIFSIPKnRIQTLKAIIQYRLPVKETKNYDLYSWDDFMELGNSip 160
Cdd:PRK07656 81 VVVPLNTRYTADEAAYILARGDAKALFVLGLF-LGVDYSATT-RLPALEHVVICETEEDDPHTEKMKTFTDFLAAGDP-- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 161 dsqlDQIIGSQKANQCAVIIYTSGTTGHPKGAMLSHDNItwMAGAAAMECNLSLAPKKQEVVVsyLPLSHIAAQMMDVWI 240
Cdd:PRK07656 157 ----AERAPEVDPDDVADILFTSGTTGRPKGAMLTHRQL--LSNAADWAEYLGLTEGDRYLAA--NPFFHVFGYKAGVNA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 241 PMKVGASIY----FaQPDAlkgtLVNTLQEVKPTAFMGVPRIWEKMHEKIKEAASKSSSLRkkvfswarnvglkintkrm 316
Cdd:PRK07656 229 PLMRGATILplpvF-DPDE----VFRLIETERITVLPGPPTMYNSLLQHPDRSAEDLSSLR------------------- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 317 lgahdtpmsyrmakalvfskvksslgldhchIFISGAAPLNQETSEFFLS-LDIP-IGEVYGLSESTGPHSMSTPENYRI 394
Cdd:PRK07656 285 -------------------------------LAVTGAASMPVALLERFESeLGVDiVLTGYGLSEASGVTTFNRLDDDRK 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 395 L---SSGKVMTGCKNMLYQQNKEGI-----GEVCLWGRHVFMGYLGSEDATTEAIDKEGWLHSGDLGRVDNKGFLYITGR 466
Cdd:PRK07656 334 TvagTIGTAIAGVENKIVNELGEEVpvgevGELLVRGPNVMKGYYDDPEATAAAIDADGWLHTGDLGRLDEEGYLYIVDR 413
|
490 500 510
....*....|....*....|....*....|....*.
gi 1811029393 467 IKEIIITaGGENVAPIPIENLVKEkLPIISNAMLVG 502
Cdd:PRK07656 414 KKDMFIV-GGFNVYPAEVEEVLYE-HPAVAEAAVIG 447
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
31-487 |
3.46e-52 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 190.96 E-value: 3.46e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 31 LSFNQYYEASRKAAKAMIKLGLEPFHSVGILGFNSVEWFIAALGAILAGGLCVGIYATNSADACQYAIAHSKVNILV--- 107
Cdd:PTZ00216 122 ITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAIVcng 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 108 --VENELQLQKIFSIPKnriqtlkAIIQY--RLPVK-ETKNYDLYSWDDFMELGNSIPdSQLdQIIGSQKANQCAVIIYT 182
Cdd:PTZ00216 202 knVPNLLRLMKSGGMPN-------TTIIYldSLPASvDTEGCRLVAWTDVVAKGHSAG-SHH-PLNIPENNDDLALIMYT 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 183 SGTTGHPKGAMLSHDNITwmAGAAAMECNLS--LAPKK-QEVVVSYLPLSHIaaqmMD---VWIPMKVGASIYFAQPDal 256
Cdd:PTZ00216 273 SGTTGDPKGVMHTHGSLT--AGILALEDRLNdlIGPPEeDETYCSYLPLAHI----MEfgvTNIFLARGALIGFGSPR-- 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 257 kgTLVNT-------LQEVKPTAFMGVPRIWEKMHEKIKEAASKSSSLRKKVFSWARNVGLKINTKRMlgahDTPmsYRMA 329
Cdd:PTZ00216 345 --TLTDTfarphgdLTEFRPVFLIGVPRIFDTIKKAVEAKLPPVGSLKRRVFDHAYQSRLRALKEGK----DTP--YWNE 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 330 KalVFSKVKSSLGlDHCHIFISGAAPLNQETSEFFLSLDIPIGEVYGLSESTGPHSMSTPENYRILSSGKVMTGCKNML- 408
Cdd:PTZ00216 417 K--VFSAPRAVLG-GRVRAMLSGGGPLSAATQEFVNVVFGMVIQGWGLTETVCCGGIQRTGDLEPNAVGQLLKGVEMKLl 493
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 409 ----YQQNK--EGIGEVCLWGRHVFMGYLGSEDATTEAIDKEGWLHSGDLGRVDNKGFLYITGRIKEIIITAGGENVApi 482
Cdd:PTZ00216 494 dteeYKHTDtpEPRGEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVKALAKNCLGEYIA-- 571
|
....*
gi 1811029393 483 pIENL 487
Cdd:PTZ00216 572 -LEAL 575
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
3-539 |
9.11e-51 |
|
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: 182.38 E-value: 9.11e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 3 IPEFFQESVNRFGIYPALASkkDGKWeiLSFNQYYEASRKAAKAMIKLGLEPFHSVGILGFNSVEWFIAALGAILAGGLC 82
Cdd:cd05936 1 LADLLEEAARRFPDKTALIF--MGRK--LTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 83 VgiyatnsadacqyaiahsKVNILVVENELQLQkifsipknriqtlkaiiqyrlpVKETKNYDLYSWDDFMELGNSIPDS 162
Cdd:cd05936 77 V------------------PLNPLYTPRELEHI----------------------LNDSGAKALIVAVSFTDLLAAGAPL 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 163 QLDQIIgsqKANQCAVIIYTSGTTGHPKGAMLSHDNITwmagAAAMECNLSLAP--KKQEVVVSYLPLSHIAAQMMDVWI 240
Cdd:cd05936 117 GERVAL---TPEDVAVLQYTSGTTGVPKGAMLTHRNLV----ANALQIKAWLEDllEGDDVVLAALPLFHVFGLTVALLL 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 241 PMKVGASIYF-AQPDALkgTLVNTLQEVKPTAFMGVPRIWEKMhekikeaaskssslrkkvfswarnvglkintkrmLGA 319
Cdd:cd05936 190 PLALGATIVLiPRFRPI--GVLKEIRKHRVTIFPGVPTMYIAL----------------------------------LNA 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 320 HDtpmsyrmAKALVFSKVKSSlgldhchifISGAAPLNQETSEFFLSL-DIPIGEVYGLSESTGPHSMSTPENYRILSS- 397
Cdd:cd05936 234 PE-------FKKRDFSSLRLC---------ISGGAPLPVEVAERFEELtGVPIVEGYGLTETSPVVAVNPLDGPRKPGSi 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 398 GKVMTGCKNMLYqqNKEG-------IGEVCLWGRHVFMGYLGSEDATTEAIdKEGWLHSGDLGRVDNKGFLYITGRIKEI 470
Cdd:cd05936 298 GIPLPGTEVKIV--DDDGeelppgeVGELWVRGPQVMKGYWNRPEETAEAF-VDGWLRTGDIGYMDEDGYFFIVDRKKDM 374
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1811029393 471 IItAGGENVAPIPIEnLVKEKLPIISNAMLVGDKakflsvlltlkcevDKTSGE---------PLDNLTWEAI-KFCRD 539
Cdd:cd05936 375 II-VGGFNVYPREVE-EVLYEHPAVAEAAVVGVP--------------DPYSGEavkafvvlkEGASLTEEEIiAFCRE 437
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
1-488 |
4.59e-50 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 181.54 E-value: 4.59e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 1 MTIPEFFQESVNRFGIYPALASKKDGkweiLSFNQYYEASRKAAKAMIKLGLEPFHSVGILGFNSVEWFIAALGAILAGG 80
Cdd:PRK06187 6 LTIGRILRHGARKHPDKEAVYFDGRR----TTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 81 lcvgIYAT-N---SADACQYAIAHSKVNILVVENEL--QLQKIfsipKNRIQTLKAIIQYR-LPVKETKNYdlysWDDFM 153
Cdd:PRK06187 82 ----VLHPiNirlKPEEIAYILNDAEDRVVLVDSEFvpLLAAI----LPQLPTVRTVIVEGdGPAAPLAPE----VGEYE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 154 ELGNSIPDSQLDQIIGsqkANQCAVIIYTSGTTGHPKGAMLSHDNITWMAGAAAMECNLSlapkKQEVVVSYLPLSHIAA 233
Cdd:PRK06187 150 ELLAAASDTFDFPDID---ENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLS----RDDVYLVIVPMFHVHA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 234 qmmdvW----IPMKVGASIYFA---QPDalkgTLVNTLQEVKPTAFMGVPRIWekmhekikeaaskssslrkkvfswarn 306
Cdd:PRK06187 223 -----WglpyLALMAGAKQVIPrrfDPE----NLLDLIETERVTFFFAVPTIW--------------------------- 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 307 vglkintkRMLGAHdtPMSYRMAkalvFSKVKsslgldhchIFISGAAPLNQETSEFFLS-LDIPIGEVYGLSESTGPHS 385
Cdd:PRK06187 267 --------QMLLKA--PRAYFVD----FSSLR---------LVIYGGAALPPALLREFKEkFGIDLVQGYGMTETSPVVS 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 386 MSTPE------NYRILSSGKVMTGCK--------NMLYQQNKEgIGEVCLWGRHVFMGYLGSEDATTEAIDKeGWLHSGD 451
Cdd:PRK06187 324 VLPPEdqlpgqWTKRRSAGRPLPGVEarivdddgDELPPDGGE-VGEIIVRGPWLMQGYWNRPEATAETIDG-GWLHTGD 401
|
490 500 510
....*....|....*....|....*....|....*..
gi 1811029393 452 LGRVDNKGFLYITGRIKEIIITaGGENVAPIPIENLV 488
Cdd:PRK06187 402 VGYIDEDGYLYITDRIKDVIIS-GGENIYPRELEDAL 437
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
29-502 |
1.72e-49 |
|
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.
Pssm-ID: 341286 [Multi-domain] Cd Length: 435 Bit Score: 178.19 E-value: 1.72e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 29 EILSFNQYYEASRKAAKAMIKLGLEPFHSVGILGFNSVEWFIAALGAILAGGLCVGIYATNSADACQYAIAHSKVNILVv 108
Cdd:cd17631 19 RSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAYILADSGAKVLF- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 109 enelqlqkifsipknriqtlkaiiqyrlpvketknydlyswDDFmelgnsipdsqldqiigsqkanqcAVIIYTSGTTGH 188
Cdd:cd17631 98 -----------------------------------------DDL------------------------ALLMYTSGTTGR 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 189 PKGAMLSHDNITWMAgaaaMECNLSLAPKKQEVVVSYLPLSHIAAqmMDVWIP--MKVGASIYF-AQPDAlkGTLVNTLQ 265
Cdd:cd17631 113 PKGAMLTHRNLLWNA----VNALAALDLGPDDVLLVVAPLFHIGG--LGVFTLptLLRGGTVVIlRKFDP--ETVLDLIE 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 266 EVKPTAFMGVPRIWEKM--HEKIKEAASksSSLRKkvfswarnvglkintkrmlgahdtpmsyrmakalvfskvksslgl 343
Cdd:cd17631 185 RHRVTSFFLVPTMIQALlqHPRFATTDL--SSLRA--------------------------------------------- 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 344 dhchiFISGAAPLNQETSEFFLSLDIPIGEVYGLSESTGPHSMSTPENYR--ILSSGKVMTGCKNMLYQQNKE-----GI 416
Cdd:cd17631 218 -----VIYGGAPMPERLLRALQARGVKFVQGYGMTETSPGVTFLSPEDHRrkLGSAGRPVFFVEVRIVDPDGRevppgEV 292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 417 GEVCLWGRHVFMGYLGSEDATTEAIdKEGWLHSGDLGRVDNKGFLYITGRIKEIIITaGGENVAPIPIENLVKEkLPIIS 496
Cdd:cd17631 293 GEIVVRGPHVMAGYWNRPEATAAAF-RDGWFHTGDLGRLDEDGYLYIVDRKKDMIIS-GGENVYPAEVEDVLYE-HPAVA 369
|
....*.
gi 1811029393 497 NAMLVG 502
Cdd:cd17631 370 EVAVIG 375
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
2-485 |
2.49e-46 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 171.88 E-value: 2.49e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 2 TIPEFFQESVNRFGIYPALASKKDGKWeiLSFNQYYEASRKAAKAMIKLGLEPFHSVGILGFNSVEWFI-----AALGAI 76
Cdd:PRK12583 19 TIGDAFDATVARFPDREALVVRHQALR--YTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLtqfatARIGAI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 77 LagglcVGIYATNSADACQYAIAHSKVNILVVENELQ-------LQKIfsIPKNRIQTLKAIIQYRLP-VKETKNYD--- 145
Cdd:PRK12583 97 L-----VNINPAYRASELEYALGQSGVRWVICADAFKtsdyhamLQEL--LPGLAEGQPGALACERLPeLRGVVSLApap 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 146 ---LYSWDDFMELGNSIPDSQLDQIIGSQKANQCAVIIYTSGTTGHPKGAMLSHDNI---TWMAGAaamecnlSLAPKKQ 219
Cdd:PRK12583 170 ppgFLAWHELQARGETVSREALAERQASLDRDDPINIQYTSGTTGFPKGATLSHHNIlnnGYFVAE-------SLGLTEH 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 220 EVVVSYLPLSHIAAQMMDVWIPMKVGASIYFAQ----PDAlkgTLvNTLQEVKPTAFMGVPRIWEKMHEKIKEAASKSSS 295
Cdd:PRK12583 243 DRLCVPVPLYHCFGMVLANLGCMTVGACLVYPNeafdPLA---TL-QAVEEERCTALYGVPTMFIAELDHPQRGNFDLSS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 296 LRkkvfswarnvglkinTKRMLGAHDTPMsyrmakalVFSKVKSSLgldHCHifisgaaplnqetsefflslDIPIGevY 375
Cdd:PRK12583 319 LR---------------TGIMAGAPCPIE--------VMRRVMDEM---HMA--------------------EVQIA--Y 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 376 GLSEsTGPHSMST----PENYRILSSGKVMTgcknmlYQQNK----EG-------IGEVCLWGRHVFMGYLGSEDATTEA 440
Cdd:PRK12583 351 GMTE-TSPVSLQTtaadDLERRVETVGRTQP------HLEVKvvdpDGatvprgeIGELCTRGYSVMKGYWNNPEATAES 423
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1811029393 441 IDKEGWLHSGDLGRVDNKGFLYITGRIKEIIITaGGENVAPIPIE 485
Cdd:PRK12583 424 IDEDGWMHTGDLATMDEQGYVRIVGRSKDMIIR-GGENIYPREIE 467
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
2-480 |
6.77e-42 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 161.44 E-value: 6.77e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 2 TIPEFFQESVNRFGIYPALASKK----------DGK---------WEILSFNQYYEASRKAAKAMIKLGLEPFHSVGILG 62
Cdd:PLN02387 59 TLAALFEQSCKKYSDKRLLGTRKlisrefetssDGRkfeklhlgeYEWITYGQVFERVCNFASGLVALGHNKEERVAIFA 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 63 FNSVEWFIAALGAILAGGLCVGIYATNSADACQYAIAHSKVNILVVENElQLQKIFSIpKNRIQTLKAIIQYR------- 135
Cdd:PLN02387 139 DTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICDSK-QLKKLIDI-SSQLETVKRVIYMDdegvdsd 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 136 LPVKETKNYDLYSWDDFMELGNSIP-DSQLdqiigsQKANQCAVIIYTSGTTGHPKGAMLSHDNItwMAGAAAMecnLSL 214
Cdd:PLN02387 217 SSLSGSSNWTVSSFSEVEKLGKENPvDPDL------PSPNDIAVIMYTSGSTGLPKGVMMTHGNI--VATVAGV---MTV 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 215 APK--KQEVVVSYLPLSHI---AAQMmdvwIPMKVGASIYFAQPDAL--------KGTLvNTLQEVKPTAFMGVPRIWEK 281
Cdd:PLN02387 286 VPKlgKNDVYLAYLPLAHIlelAAES----VMAAVGAAIGYGSPLTLtdtsnkikKGTK-GDASALKPTLMTAVPAILDR 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 282 MHEKIKEAASKSSSLRKKVFSWArnvglkinTKRMLGAHDTpmSYRMA--------KALVFSKVKSSLGlDHCHIFISGA 353
Cdd:PLN02387 361 VRDGVRKKVDAKGGLAKKLFDIA--------YKRRLAAIEG--SWFGAwglekllwDALVFKKIRAVLG-GRIRFMLSGG 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 354 APLNQETSEFF-LSLDIPIGEVYGLSESTGPHSMSTPENYRILSSGKVMTGCKNMLYQQNKEGI---------GEVCLWG 423
Cdd:PLN02387 430 APLSGDTQRFInICLGAPIGQGYGLTETCAGATFSEWDDTSVGRVGPPLPCCYVKLVSWEEGGYlisdkpmprGEIVIGG 509
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1811029393 424 RHVFMGYLGSEDATTEA--IDKEG--WLHSGDLGRVDNKGFLYITGRIKEIIITAGGENVA 480
Cdd:PLN02387 510 PSVTLGYFKNQEKTDEVykVDERGmrWFYTGDIGQFHPDGCLEIIDRKKDIVKLQHGEYVS 570
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
1-502 |
1.11e-40 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 156.12 E-value: 1.11e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 1 MTIPEFFQESVNRFGIYPALASKKDG-KWeilSFNQYYEASRKAAKAMIKLGLEPFHSVGILGFNSVEWFI-----AALG 74
Cdd:PRK08315 16 QTIGQLLDRTAARYPDREALVYRDQGlRW---TYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLtqfatAKIG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 75 AILagglcVGI----------YATNSADaCQYAIAHSK------VNIL-VVENELQLQKIFSIPKNRIQTLKAIIQyrlp 137
Cdd:PRK08315 93 AIL-----VTInpayrlseleYALNQSG-CKALIAADGfkdsdyVAMLyELAPELATCEPGQLQSARLPELRRVIF---- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 138 VKETKNYDLYSWDDFMELGNSIPDSQLDQIIGSQKANQCAVIIYTSGTTGHPKGAMLSHDNIT---WMAGAAameCNLSl 214
Cdd:PRK08315 163 LGDEKHPGMLNFDELLALGRAVDDAELAARQATLDPDDPINIQYTSGTTGFPKGATLTHRNILnngYFIGEA---MKLT- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 215 apkKQEVVVSYLPLSHIAAQMMDVWIPMKVGASIYFAQP--DALKgTLvNTLQEVKPTAFMGVPR--IWEKMHekiKEAA 290
Cdd:PRK08315 239 ---EEDRLCIPVPLYHCFGMVLGNLACVTHGATMVYPGEgfDPLA-TL-AAVEEERCTALYGVPTmfIAELDH---PDFA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 291 SKS-SSLRKKVfswarnvglkintkrmlgahdtpmsyrMAKAL----VFSKVKSSLGLdhchifisgaaplnqetSEffl 365
Cdd:PRK08315 311 RFDlSSLRTGI---------------------------MAGSPcpieVMKRVIDKMHM-----------------SE--- 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 366 sldIPIgeVYGLSEsTGPHSMST----PENYRILSSGKVM-----------TGCKNMLYQQnkegiGEVCLWGRHVFMGY 430
Cdd:PRK08315 344 ---VTI--AYGMTE-TSPVSTQTrtddPLEKRVTTVGRALphlevkivdpeTGETVPRGEQ-----GELCTRGYSVMKGY 412
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1811029393 431 LGSEDATTEAIDKEGWLHSGDLGRVDNKGFLYITGRIKEIIITaGGENVAPIPIEnlvkEKL---PIISNAMLVG 502
Cdd:PRK08315 413 WNDPEKTAEAIDADGWMHTGDLAVMDEEGYVNIVGRIKDMIIR-GGENIYPREIE----EFLythPKIQDVQVVG 482
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
18-486 |
1.57e-39 |
|
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: 151.70 E-value: 1.57e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 18 PALASKKDGKWeiLSFNQYYEASRKAAKAMIKLGLEPFHSVGILGFNSVEWFIAALGAILAGGLCVGIYATNSADACQYA 97
Cdd:cd05926 4 PALVVPGSTPA--LTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 98 IAHSKVNILVVENELQLqkifSIPKNRIQTLKAIIQYRLPVKETKNYDLYSwddfmELGNSIPDSQLDQIIGSQKANQCA 177
Cdd:cd05926 82 LADLGSKLVLTPKGELG----PASRAASKLGLAILELALDVGVLIRAPSAE-----SLSNLLADKKNAKSEGVPLPDDLA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 178 VIIYTSGTTGHPKGAMLSHDNITwmAGAAAMECNLSLAPKKQEVVVsyLPLSHIAAQMM----------DVWIPMKVGAS 247
Cdd:cd05926 153 LILHTSGTTGRPKGVPLTHRNLA--ASATNITNTYKLTPDDRTLVV--MPLFHVHGLVAsllstlaaggSVVLPPRFSAS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 248 IYFAQpdalkgtlvntLQEVKPTAFMGVP---RIWEKMHEKIKEaaSKSSSLRkkvfswarnvglkintkrmlgahdtpm 324
Cdd:cd05926 229 TFWPD-----------VRDYNATWYTAVPtihQILLNRPEPNPE--SPPPKLR--------------------------- 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 325 syrmakalvfskvksslgldhchiFI-SGAAPLNQET-SEFFLSLDIPIGEVYGLSESTgpHSMST----PENYRILSSG 398
Cdd:cd05926 269 ------------------------FIrSCSASLPPAVlEALEATFGAPVLEAYGMTEAA--HQMTSnplpPGPRKPGSVG 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 399 KVmTGCKNMLYQQNKE-----GIGEVCLWGRHVFMGYLGSEDATTEAIDKEGWLHSGDLGRVDNKGFLYITGRIKEIIIT 473
Cdd:cd05926 323 KP-VGVEVRILDEDGEilppgVVGEICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADGYLFLTGRIKELINR 401
|
490
....*....|...
gi 1811029393 474 aGGENVAPIPIEN 486
Cdd:cd05926 402 -GGEKISPLEVDG 413
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
29-502 |
8.56e-39 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 149.63 E-value: 8.56e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 29 EILSFNQYYEASRKAAKAMI-KLGLEPFHSVGILGFNSVEWFIAALGAILAGGLCVGIYATNSADACQYAIAHSKVNILV 107
Cdd:PRK06839 26 EEMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTTVLF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 108 VENELQlqkifsipkNRIQTLKAIIQYRLPVKET--KNYDLYSWDDFMELGNSIPdsqldqiigsqkanqcAVIIYTSGT 185
Cdd:PRK06839 106 VEKTFQ---------NMALSMQKVSYVQRVISITslKEIEDRKIDNFVEKNESAS----------------FIICYTSGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 186 TGHPKGAMLSHDNITWmagaAAMECNLSLAPKKQEVVVSYLPLSHIAAQMMDVWIPMKVGASIYFA---QPDalkgTLVN 262
Cdd:PRK06839 161 TGKPKGAVLTQENMFW----NALNNTFAIDLTMHDRSIVLLPLFHIGGIGLFAFPTLFAGGVIIVPrkfEPT----KALS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 263 TLQEVKPTAFMGVPRIwekmHEKIKEAASKSSSlrkkvfswarnvglkintkrmlgahdtpmsyrmakalvfskvksslG 342
Cdd:PRK06839 233 MIEKHKVTVVMGVPTI----HQALINCSKFETT----------------------------------------------N 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 343 LDHCHIFISGAAPLNQETSEFFLSLDIPIGEVYGLSESTGPHSMSTPENYR--ILSSGKVMTGCKNMLYQQNKE-----G 415
Cdd:PRK06839 263 LQSVRWFYNGGAPCPEELMREFIDRGFLFGQGFGMTETSPTVFMLSEEDARrkVGSIGKPVLFCDYELIDENKNkvevgE 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 416 IGEVCLWGRHVFMGYLGSEDATTEAIdKEGWLHSGDLGRVDNKGFLYITGRIKEIIITaGGENVAPIPIENLVkEKLPII 495
Cdd:PRK06839 343 VGELLIRGPNVMKEYWNRPDATEETI-QDGWLCTGDLARVDEDGFVYIVGRKKEMIIS-GGENIYPLEVEQVI-NKLSDV 419
|
....*..
gi 1811029393 496 SNAMLVG 502
Cdd:PRK06839 420 YEVAVVG 426
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
18-471 |
1.06e-37 |
|
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.
Pssm-ID: 341230 [Multi-domain] Cd Length: 505 Bit Score: 146.61 E-value: 1.06e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 18 PALASKKDGKweILSFNQYYEASRKAAKAMIKLGLEPFHSVGILGFNSVEWFIAALGAILAGGLCVGIYATNSADACQYA 97
Cdd:cd05904 22 PALIDAATGR--ALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 98 IAHSKVNILVVENELqlqkifsIPKnriqtlkaIIQYRLPV----KETKNYDLYSWDDFMELGNSIPDSQLDQiigsqka 173
Cdd:cd05904 100 VKDSGAKLAFTTAEL-------AEK--------LASLALPVvlldSAEFDSLSFSDLLFEADEAEPPVVVIKQ------- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 174 NQCAVIIYTSGTTGHPKGAMLSHDNITwmAGAAAMECNLSLAPKKQEVVVSYLPLSHIAAQMMDVWIPMKVGASIyFAQP 253
Cdd:cd05904 158 DDVAALLYSSGTTGRSKGVMLTHRNLI--AMVAQFVAGEGSNSDSEDVFLCVLPMFHIYGLSSFALGLLRLGATV-VVMP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 254 DALKGTLVNTLQEVKPTAFMGVPriwekmhekikeaaskssslrkkvfswarnvglkintkrmlgahdtPMSYRMAK-AL 332
Cdd:cd05904 235 RFDLEELLAAIERYKVTHLPVVP----------------------------------------------PIVLALVKsPI 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 333 VFSKVKSSLgldhcHIFISGAAPLNQETSEFFLSL--DIPIGEVYGLSESTGP-HSMSTPE--NYRILSSGKVMTGCK-- 405
Cdd:cd05904 269 VDKYDLSSL-----RQIMSGAAPLGKELIEAFRAKfpNVDLGQGYGMTESTGVvAMCFAPEkdRAKYGSVGRLVPNVEak 343
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1811029393 406 ------NMLYQQNKEGigEVCLWGRHVFMGYLGSEDATTEAIDKEGWLHSGDLGRVDNKGFLYITGRIKEII 471
Cdd:cd05904 344 ivdpetGESLPPNQTG--ELWIRGPSIMKGYLNNPEATAATIDKEGWLHTGDLCYIDEDGYLFIVDRLKELI 413
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
179-502 |
2.56e-33 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 130.86 E-value: 2.56e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 179 IIYTSGTTGHPKGAMLSHDNI---TWMAGaaamECNLSLapkKQEVVVSYLPLSHIAAQMMDVWIPMKVGASIYFAQP-- 253
Cdd:cd05917 7 IQFTSGTTGSPKGATLTHHNIvnnGYFIG----ERLGLT---EQDRLCIPVPLFHCFGSVLGVLACLTHGATMVFPSPsf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 254 DALkgTLVNTLQEVKPTAFMGVPRIWEKMHEKIKEAASKSSSLRKKVfswarnvglkintkrMLGAhDTPMSyrmakalV 333
Cdd:cd05917 80 DPL--AVLEAIEKEKCTALHGVPTMFIAELEHPDFDKFDLSSLRTGI---------------MAGA-PCPPE-------L 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 334 FSKVKSSLGLDHCHIfisgaaplnqetsefflsldipigeVYGLSESTGPHSMSTPEN---YRILSSGKVM--------- 401
Cdd:cd05917 135 MKRVIEVMNMKDVTI-------------------------AYGMTETSPVSTQTRTDDsieKRVNTVGRIMphteakivd 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 402 --TGCKNMLYQQnkegiGEVCLWGRHVFMGYLGSEDATTEAIDKEGWLHSGDLGRVDNKGFLYITGRIKEIIITaGGENV 479
Cdd:cd05917 190 peGGIVPPVGVP-----GELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLAVMDEDGYCRIVGRIKDMIIR-GGENI 263
|
330 340
....*....|....*....|...
gi 1811029393 480 APIPIENLVkEKLPIISNAMLVG 502
Cdd:cd05917 264 YPREIEEFL-HTHPKVSDVQVVG 285
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
173-502 |
7.51e-33 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 132.95 E-value: 7.51e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 173 ANQCAVIIYTSGTTGHPKGAMLSHDNITWMAGAAAMECNLSlapkKQEVVVSYLPLSHIAAQMMDVWIPMKVGASIYFaq 252
Cdd:PRK06087 186 GDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLT----WQDVFMMPAPLGHATGFLHGVTAPFLIGARSVL-- 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 253 pdalkgtlvntLQEVKPTAFMGVpriwekmhekikeaasksssLRKKVFSWarnvglkintkrMLGAhdTPMSYRMAKAL 332
Cdd:PRK06087 260 -----------LDIFTPDACLAL--------------------LEQQRCTC------------MLGA--TPFIYDLLNLL 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 333 VFSKVK-SSLGLdhchiFISGAAPLNQETSEFFLSLDIPIGEVYGLSESTgPHSMSTPEN---YRILSSGKVMTGCKNML 408
Cdd:PRK06087 295 EKQPADlSALRF-----FLCGGTTIPKKVARECQQRGIKLLSVYGSTESS-PHAVVNLDDplsRFMHTDGYAAAGVEIKV 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 409 YQQNKEGI-----GEVCLWGRHVFMGYLGSEDATTEAIDKEGWLHSGDLGRVDNKGFLYITGRIKEIIITaGGENVAPIP 483
Cdd:PRK06087 369 VDEARKTLppgceGEEASRGPNVFMGYLDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVR-GGENISSRE 447
|
330
....*....|....*....
gi 1811029393 484 IENLVKeKLPIISNAMLVG 502
Cdd:PRK06087 448 VEDILL-QHPKIHDACVVA 465
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
32-488 |
1.16e-32 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 130.49 E-value: 1.16e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 32 SFNQYYEASRKAAKAMIKLGLEPFHSVGILGFNSVEWFIAALGAILAGGLCVGIYATNSADACQYAIAHSKVNILVVene 111
Cdd:cd05934 5 TYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 112 lqlqkifsipknriqtlkaiiqyrlpvketknyDLYSwddfmelgnsipdsqldqiigsqkanqcavIIYTSGTTGHPKG 191
Cdd:cd05934 82 ---------------------------------DPAS------------------------------ILYTSGTTGPPKG 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 192 AMLSHDNITWMAGAAAMECNLSlapkKQEVVVSYLPLSHIAAQMMDVWIPMKVGASIyfaqpdalkgtlvnTLQE-VKPT 270
Cdd:cd05934 99 VVITHANLTFAGYYSARRFGLG----EDDVYLTVLPLFHINAQAVSVLAALSVGATL--------------VLLPrFSAS 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 271 AFmgvpriWekmhekikeaasksSSLRKKVFSWARNVGLkintkrmlgahdtPMSYRMAKAlvfskvKSSLGLDHCHIFI 350
Cdd:cd05934 161 RF------W--------------SDVRRYGATVTNYLGA-------------MLSYLLAQP------PSPDDRAHRLRAA 201
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 351 SGAAPLNQETSEFFLSLDIPIGEVYGLSESTGPHSMSTPENYRILSSGKVMTGCKNMLY----QQNKEG-IGEVCL---- 421
Cdd:cd05934 202 YGAPNPPELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIVdddgQELPAGePGELVIrglr 281
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1811029393 422 -WGRhvFMGYLGSEDATTEAIdKEGWLHSGDLGRVDNKGFLYITGRIKEiIITAGGENVAPIPIENLV 488
Cdd:cd05934 282 gWGF--FKGYYNMPEATAEAM-RNGWFHTGDLGYRDADGFFYFVDRKKD-MIRRRGENISSAEVERAI 345
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
158-502 |
3.59e-32 |
|
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: 129.33 E-value: 3.59e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 158 SIPDSQLDQIIGSQKAN---QCAVIIYTSGTTGHPKGAMLSHDNITWMAGAAAMECNLSlapkKQEVVVSYLPLSHIAAQ 234
Cdd:cd05941 70 SYPLAELEYVITDSEPSlvlDPALILYTSGTTGRPKGVVLTHANLAANVRALVDAWRWT----EDDVLLHVLPLHHVHGL 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 235 MMDVWIPMKVGASIYF-AQPDAlkgTLVNTLQEVKP-TAFMGVPRIWEKMhekikeaaskssslrkkvfswarnvglkIN 312
Cdd:cd05941 146 VNALLCPLFAGASVEFlPKFDP---KEVAISRLMPSiTVFMGVPTIYTRL----------------------------LQ 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 313 TKRmlgAHDTPMSYRMAKALvfskvkSSLGLdhchiFISGAAPLNQETSEFFLSLD-IPIGEVYGLSEsTGpHSMSTP-E 390
Cdd:cd05941 195 YYE---AHFTDPQFARAAAA------ERLRL-----MVSGSAALPVPTLEEWEAITgHTLLERYGMTE-IG-MALSNPlD 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 391 NYRILSS-GKVMTGCKNMLYQQN------KEGIGEVCLWGRHVFMGYLGSEDATTEAIDKEGWLHSGDLGRVDNKGFLYI 463
Cdd:cd05941 259 GERRPGTvGMPLPGVQARIVDEEtgeplpRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGWFKTGDLGVVDEDGYYWI 338
|
330 340 350
....*....|....*....|....*....|....*....
gi 1811029393 464 TGRIKEIIITAGGENVAPIPIENLVKEkLPIISNAMLVG 502
Cdd:cd05941 339 LGRSSVDIIKSGGYKVSALEIERVLLA-HPGVSECAVIG 376
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
2-480 |
3.69e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 130.82 E-value: 3.69e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 2 TIPEFFQESVNRFGIYPALASKkDGKWeilSFNQYYEASRKAAKAMIKLGLEPFHSVGILGFNSVEWFIAALGAILAGGL 81
Cdd:PRK08316 12 TIGDILRRSARRYPDKTALVFG-DRSW---TYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 82 CVGI-YATNSADACqYAIAHSKVNILVVENEL--QLQKIFSIPKNRIQTLKAIIQYRLPVKetknydlySWDDFMELGNS 158
Cdd:PRK08316 88 HVPVnFMLTGEELA-YILDHSGARAFLVDPALapTAEAALALLPVDTLILSLVLGGREAPG--------GWLDFADWAEA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 159 IPDSQLDQIIGSqkaNQCAVIIYTSGTTGHPKGAMLSHDNITWMAGAAAMECNLSlapkKQEVVVSYLPLSHIAAqmMDV 238
Cdd:PRK08316 159 GSVAEPDVELAD---DDLAQILYTSGTESLPKGAMLTHRALIAEYVSCIVAGDMS----ADDIPLHALPLYHCAQ--LDV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 239 W-IP-MKVGA-SIYFAQPDAlkGTLVNTLQEVKPTAFMGVPRIWEKMhekikeaasksssLRKKVFSWARNVGLkinTKR 315
Cdd:PRK08316 230 FlGPyLYVGAtNVILDAPDP--ELILRTIEAERITSFFAPPTVWISL-------------LRHPDFDTRDLSSL---RKG 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 316 MLGAHDTPMSY--RMAKALvfskvkSSLGLDHChifisgaaplnqetsefflsldipigevYGLSEsTGP-HSMSTPENY 392
Cdd:PRK08316 292 YYGASIMPVEVlkELRERL------PGLRFYNC----------------------------YGQTE-IAPlATVLGPEEH 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 393 --RILSSGK----VMTGCKNMLYQQNKEG-IGEVCLWGRHVFMGYLGSEDATTEAIdKEGWLHSGDLGRVDNKGFLYITG 465
Cdd:PRK08316 337 lrRPGSAGRpvlnVETRVVDDDGNDVAPGeVGEIVHRSPQLMLGYWDDPEKTAEAF-RGGWFHSGDLGVMDEEGYITVVD 415
|
490
....*....|....*
gi 1811029393 466 RIKEIIITaGGENVA 480
Cdd:PRK08316 416 RKKDMIKT-GGENVA 429
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
1-502 |
8.77e-32 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 130.12 E-value: 8.77e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 1 MTIPEFFQESVNRFGIYPAL----ASKkdgkweilSFNQYYEASRKAAKAMIKLGLEPFHSVGILGFNSVEwFIAALGAI 76
Cdd:PRK05605 32 TTLVDLYDNAVARFGDRPALdffgATT--------TYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQ-HIVAFYAV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 77 LAGGLCV-------------GIYATNSAdacQYAIAHSKVNILVVE--NELQLQKIFSIpkNRIQTLKAIIQY--RLPVK 139
Cdd:PRK05605 103 LRLGAVVvehnplytaheleHPFEDHGA---RVAIVWDKVAPTVERlrRTTPLETIVSV--NMIAAMPLLQRLalRLPIP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 140 ETKNY---------DLYSWDDFmeLGNSIPDsqLDQIIGSQKANQ--CAVIIYTSGTTGHPKGAMLSHDNItwMAGAAAM 208
Cdd:PRK05605 178 ALRKAraaltgpapGTVPWETL--VDAAIGG--DGSDVSHPRPTPddVALILYTSGTTGKPKGAQLTHRNL--FANAAQG 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 209 ECNLSLAPKKQEVVVSYLPLSHIAAQMMDVWIPMKVGAS-IYFAQPDAlkGTLVNTLQEVKPTAFMGVPRIWEKmhekIK 287
Cdd:PRK05605 252 KAWVPGLGDGPERVLAALPMFHAYGLTLCLTLAVSIGGElVLLPAPDI--DLILDAMKKHPPTWLPGVPPLYEK----IA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 288 EAASKssslrkkvfswaRNVGLKintkrmlgahdtpmSYRMAkalvfskvksslgldhchifISGAAPLNQETSEFFLSL 367
Cdd:PRK05605 326 EAAEE------------RGVDLS--------------GVRNA--------------------FSGAMALPVSTVELWEKL 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 368 dipIG----EVYGLSEsTGPHSMSTP--ENYRI------LSSGKVMTGCKNMLYQQNKEG-IGEVCLWGRHVFMGYLGSE 434
Cdd:PRK05605 360 ---TGgllvEGYGLTE-TSPIIVGNPmsDDRRPgyvgvpFPDTEVRIVDPEDPDETMPDGeEGELLVRGPQVFKGYWNRP 435
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1811029393 435 DATTEAIdKEGWLHSGDLGRVDNKGFLYITGRIKEIIITaGGENVAPIPIENLVKEkLPIISNAMLVG 502
Cdd:PRK05605 436 EETAKSF-LDGWFRTGDVVVMEEDGFIRIVDRIKELIIT-GGFNVYPAEVEEVLRE-HPGVEDAAVVG 500
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
32-502 |
6.94e-30 |
|
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: 124.18 E-value: 6.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 32 SFNQYYEASRKAAKAMIKLGLEPFHSVGILGFNSVEWFIAALGAILAGglcVGIYATN---SADACQYAIAHSKVNILVV 108
Cdd:cd17642 46 SYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIG---VGVAPTNdiyNERELDHSLNISKPTIVFC 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 109 eNELQLQKIFSIPKnRIQTLKAIIQYRLpvketkNYDL--YSWDDFMELGNSIPDSQLDQII--GSQKANQCAVIIYTSG 184
Cdd:cd17642 123 -SKKGLQKVLNVQK-KLKIIKTIIILDS------KEDYkgYQCLYTFITQNLPPGFNEYDFKppSFDRDEQVALIMNSSG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 185 TTGHPKGAMLSHDNITwMAGAAAMECNLSLAPKKQEVVVSYLPLSHiAAQMMDVWIPMKVGASIYFaQPDALKGTLVNTL 264
Cdd:cd17642 195 STGLPKGVQLTHKNIV-ARFSHARDPIFGNQIIPDTAILTVIPFHH-GFGMFTTLGYLICGFRVVL-MYKFEEELFLRSL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 265 QEVKPTAFMGVPriwekmhekikeaaskssslrkkvfswarnvglkintkrmlgahdTPMSYrMAKALVFSKVKsslgLD 344
Cdd:cd17642 272 QDYKVQSALLVP---------------------------------------------TLFAF-FAKSTLVDKYD----LS 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 345 HCHIFISGAAPLNQETSEFFLS-LDIP-IGEVYGLSESTGPHSMSTPENYRILSSGKVMTGCKNMLYQQNKEGI------ 416
Cdd:cd17642 302 NLHEIASGGAPLSKEVGEAVAKrFKLPgIRQGYGLTETTSAILITPEGDDKPGAVGKVVPFFYAKVVDLDTGKTlgpner 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 417 GEVCLWGRHVFMGYLGSEDATTEAIDKEGWLHSGDLGRVDNKGFLYITGRIKEiIITAGGENVAPIPIENLVKEKlPIIS 496
Cdd:cd17642 382 GELCVKGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKS-LIKYKGYQVPPAELESILLQH-PKIF 459
|
....*.
gi 1811029393 497 NAMLVG 502
Cdd:cd17642 460 DAGVAG 465
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
177-485 |
7.66e-30 |
|
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: 121.05 E-value: 7.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 177 AVIIYTSGTTGHPKGAMLSHDNITWMAGAAAmecnLSLAPKKQEVVVSYLPLSHIAAQMMDVWIPMKVGASIYFAQPDAL 256
Cdd:cd05944 5 AAYFHTGGTTGTPKLAQHTHSNEVYNAWMLA----LNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLAGPAGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 257 KG-TLVNTL----QEVKPTAFMGVPRIWEKMhekikeaaskssslrkkvfsWARNVGLKINtkrmlgahdtpmSYRMAka 331
Cdd:cd05944 81 RNpGLFDNFwklvERYRITSLSTVPTVYAAL--------------------LQVPVNADIS------------SLRFA-- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 332 lvfskvksslgldhchifISGAAPLNQET-SEFFLSLDIPIGEVYGLSESTGPHSMSTPEN-YRILSSGKVMTGCKNMLY 409
Cdd:cd05944 127 ------------------MSGAAPLPVELrARFEDATGLPVVEGYGLTEATCLVAVNPPDGpKRPGSVGLRLPYARVRIK 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 410 QQNKEG----------IGEVCLWGRHVFMGYLGSEDATTEAIDkEGWLHSGDLGRVDNKGFLYITGRIKEIIITaGGENV 479
Cdd:cd05944 189 VLDGVGrllrdcapdeVGEICVAGPGVFGGYLYTEGNKNAFVA-DGWLNTGDLGRLDADGYLFITGRAKDLIIR-GGHNI 266
|
....*.
gi 1811029393 480 APIPIE 485
Cdd:cd05944 267 DPALIE 272
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
154-502 |
1.25e-29 |
|
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: 121.30 E-value: 1.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 154 ELGNSIPDSQLDQiigsqkaNQCAVIIYTSGTTGHPKGAMLSHDNITWMAGAAAMecNLSLAPKKQEVVVsyLPLSHIAa 233
Cdd:cd05912 64 ELAFQLKDSDVKL-------DDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSAL--NLGLTEDDNWLCA--LPLFHIS- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 234 qmmdvwipmkvGASIYFAQpdALKGTLVNTLQEVKPtafmgvpriwEKMHEKIKEAASKSSSLRKKVFSWarnvglkint 313
Cdd:cd05912 132 -----------GLSILMRS--VIYGMTVYLVDKFDA----------EQVLHLINSGKVTIISVVPTMLQR---------- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 314 krMLGAHDTPMSYRMAKALVfskvksslgldhchifisGAAPLNQETSEFFLSLDIPIGEVYGLSESTGPHSMSTPENY- 392
Cdd:cd05912 179 --LLEILGEGYPNNLRCILL------------------GGGPAPKPLLEQCKEKGIPVYQSYGMTETCSQIVTLSPEDAl 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 393 -RILSSGKVMTGCKNMLYQ--QNKEGIGEVCLWGRHVFMGYLGSEDATTEAIdKEGWLHSGDLGRVDNKGFLYITGRIKE 469
Cdd:cd05912 239 nKIGSAGKPLFPVELKIEDdgQPPYEVGEILLKGPNVTKGYLNRPDATEESF-ENGWFKTGDIGYLDEEGFLYVLDRRSD 317
|
330 340 350
....*....|....*....|....*....|...
gi 1811029393 470 IIItAGGENVAPIPIENLVKEkLPIISNAMLVG 502
Cdd:cd05912 318 LII-SGGENIYPAEIEEVLLS-HPAIKEAGVVG 348
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
177-485 |
1.58e-29 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 123.91 E-value: 1.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 177 AVIIYTSGTTGHPKGAMLSHDNITWMAGAAAMecNLSLAPkkQEVVVSYLPLSHIAAQMMDVWIPMKVGASIYFAQPDAL 256
Cdd:PRK07529 216 AAYFHTGGTTGMPKLAQHTHGNEVANAWLGAL--LLGLGP--GDTVFCGLPLFHVNALLVTGLAPLARGAHVVLATPQGY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 257 KG-TLVNTLQEV----KPTAFMGVPRIWekmhekikeaaskSSSLRKKVfswarnvglkintkrmlGAHDTpmsyrmaka 331
Cdd:PRK07529 292 RGpGVIANFWKIveryRINFLSGVPTVY-------------AALLQVPV-----------------DGHDI--------- 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 332 lvfskvkSSLgldhcHIFISGAAPLNQETSEFFLS-LDIPIGEVYGLSESTGPHSMSTPEN-YRILSSG--------KVM 401
Cdd:PRK07529 333 -------SSL-----RYALCGAAPLPVEVFRRFEAaTGVRIVEGYGLTEATCVSSVNPPDGeRRIGSVGlrlpyqrvRVV 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 402 TGCKNMLYQQN--KEGIGEVCLWGRHVFMGYLGSEDATTEAIDkEGWLHSGDLGRVDNKGFLYITGRIKEIIITaGGENV 479
Cdd:PRK07529 401 ILDDAGRYLRDcaVDEVGVLCIAGPNVFSGYLEAAHNKGLWLE-DGWLNTGDLGRIDADGYFWLTGRAKDLIIR-GGHNI 478
|
....*.
gi 1811029393 480 APIPIE 485
Cdd:PRK07529 479 DPAAIE 484
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
41-506 |
5.73e-29 |
|
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: 120.90 E-value: 5.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 41 RKAAKAMIKLG--LEPFHS----VGILGFNSVEWFIAALGAILAGGLCVGIYATNSADACQYAIAHSKVNILVVENELqL 114
Cdd:cd05909 11 RKLLTGAIALArkLAKMTKegenVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLTSKQF-I 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 115 QKIFSIPKNRIQTLKAIIqYRLPVKETknydlYSWDD--FMELGNSIPDSQLDQIIGS--QKANQCAVIIYTSGTTGHPK 190
Cdd:cd05909 90 EKLKLHHLFDVEYDARIV-YLEDLRAK-----ISKADkcKAFLAGKFPPKWLLRIFGVapVQPDDPAVILFTSGSEGLPK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 191 GAMLSHDNITwmagAAAMECNLSLAPKKQEVVVSYLPLSHIAAQMMDVWIPMKVGASIYFAqPDALKG-TLVNTLQEVKP 269
Cdd:cd05909 164 GVVLSHKNLL----ANVEQITAIFDPNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVVFH-PNPLDYkKIPELIYDKKA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 270 TAFMGVPriwekmhekikeaaskssslrkkVFswarnvgLKINTKRmlgAHDTPMsyrmakalvfskvkSSLGLdhchiF 349
Cdd:cd05909 239 TILLGTP-----------------------TF-------LRGYARA---AHPEDF--------------SSLRL-----V 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 350 ISGAAPLNQETSEFFLSL-DIPIGEVYGLSESTGPHSMSTPE---------------NYRILSsgkVMTGCKnmlYQQNK 413
Cdd:cd05909 267 VAGAEKLKDTLRQEFQEKfGIRILEGYGTTECSPVISVNTPQspnkegtvgrplpgmEVKIVS---VETHEE---VPIGE 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 414 EGIgeVCLWGRHVFMGYLGSEDATTEAIdKEGWLHSGDLGRVDNKGFLYITGRIKEiIITAGGENVAPIPIENLVKEKLP 493
Cdd:cd05909 341 GGL--LLVRGPNVMLGYLNEPELTSFAF-GDGWYDTGDIGKIDGEGFLTITGRLSR-FAKIAGEMVSLEAIEDILSEILP 416
|
490
....*....|....*
gi 1811029393 494 IISN--AMLVGDKAK 506
Cdd:cd05909 417 EDNEvaVVSVPDGRK 431
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
2-488 |
1.39e-28 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 120.37 E-value: 1.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 2 TIPEFFQESVNRFGIYPALASKkdGKweILSFNQYYEASRK-AAKAMIKLGLEPFHSVGILGFNSVEWFIAALGAILAGG 80
Cdd:PRK08751 26 TVAEVFATSVAKFADRPAYHSF--GK--TITYREADQLVEQfAAYLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 81 LCVGIYATNSADACQYAIAHSKVNILVVENELQL---QKIFSIPKNRIQTL----------KAIIQYRLPV--KETKNYD 145
Cdd:PRK08751 102 TVVNVNPLYTPRELKHQLIDSGASVLVVIDNFGTtvqQVIADTPVKQVITTglgdmlgfpkAALVNFVVKYvkKLVPEYR 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 146 LYSWDDFME---LG--NSIPDSQLDqiigsqkANQCAVIIYTSGTTGHPKGAMLSHDNIT--------WMAGAAAMEcnl 212
Cdd:PRK08751 182 INGAIRFREalaLGrkHSMPTLQIE-------PDDIAFLQYTGGTTGVAKGAMLTHRNLVanmqqahqWLAGTGKLE--- 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 213 slapKKQEVVVSYLPLSHIAAQMMDVWIPMKVGASIYF-AQPDALKGtLVNTLQEVKPTAFMGVPRIWEKMhekikeaas 291
Cdd:PRK08751 252 ----EGCEVVITALPLYHIFALTANGLVFMKIGGCNHLiSNPRDMPG-FVKELKKTRFTAFTGVNTLFNGL--------- 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 292 kssslrkkvfswarnvglkINTKRMlgahdtpmsyrmaKALVFSKVKSSLGldhchifisGAAPLNQETSEFFLSLD-IP 370
Cdd:PRK08751 318 -------------------LNTPGF-------------DQIDFSSLKMTLG---------GGMAVQRSVAERWKQVTgLT 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 371 IGEVYGLSEsTGPHSMSTPENYR---------ILSSGKVMTGCKNMLYQQNKegIGEVCLWGRHVFMGYLGSEDATTEAI 441
Cdd:PRK08751 357 LVEAYGLTE-TSPAACINPLTLKeyngsiglpIPSTDACIKDDAGTVLAIGE--IGELCIKGPQVMKGYWKRPEETAKVM 433
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1811029393 442 DKEGWLHSGDLGRVDNKGFLYITGRIKEIIITAGGeNVAPIPIENLV 488
Cdd:PRK08751 434 DADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGF-NVYPNEIEDVI 479
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
31-539 |
4.21e-28 |
|
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: 118.24 E-value: 4.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 31 LSFNQYYEASRKAAKAMIKLGLEPFHSVGILGFNSVEWFIAALGAILAGGLCVGIYATNSADACQYAIAHSKVNILVVEN 110
Cdd:cd05959 30 LTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVVSG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 111 ELqLQKIFSIPKNRIQTLKAIIQYRlpvketknyDLYSWDDFMELGNSIPDSQLDQIIGSQKANQCAVIIYTSGTTGHPK 190
Cdd:cd05959 110 EL-APVLAAALTKSEHTLVVLIVSG---------GAGPEAGALLLAELVAAEAEQLKPAATHADDPAFWLYSSGSTGRPK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 191 GAMLSHDNITWMAGAAAMECnlsLAPKKQEVVVSYLPLSHIAAQMMDVWIPMKVGAS--IYFAQPDAlkGTLVNTLQEVK 268
Cdd:cd05959 180 GVVHLHADIYWTAELYARNV---LGIREDDVCFSAAKLFFAYGLGNSLTFPLSVGATtvLMPERPTP--AAVFKRIRRYR 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 269 PTAFMGVPRIWEKM----------HEKIKEAASKSSSLRKKVF-SWARNVGLKIntkrMLGAHDTPMsyrmakalvfskv 337
Cdd:cd05959 255 PTVFFGVPTLYAAMlaapnlpsrdLSSLRLCVSAGEALPAEVGeRWKARFGLDI----LDGIGSTEM------------- 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 338 ksslgldhCHIFISgaaplnqetsefflsldipigevyglsestgphsmSTPENYRILSSGKVMTGcknmlYQ---QNKE 414
Cdd:cd05959 318 --------LHIFLS-----------------------------------NRPGRVRYGTTGKPVPG-----YEvelRDED 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 415 G-------IGEVCLWGRHVFMGYLGSEDATTEAIdKEGWLHSGDLGRVDNKGFLYITGRIKEiIITAGGENVAPIPIENL 487
Cdd:cd05959 350 GgdvadgePGELYVRGPSSATMYWNNRDKTRDTF-QGEWTRTGDKYVRDDDGFYTYAGRADD-MLKVSGIWVSPFEVESA 427
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1811029393 488 VKEKlPIISNAMLVGdkAKFLSVLLTLK-CEVDKTSGEPLDNLTWEAIKFCRD 539
Cdd:cd05959 428 LVQH-PAVLEAAVVG--VEDEDGLTKPKaFVVLRPGYEDSEALEEELKEFVKD 477
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
25-488 |
6.12e-28 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.
Pssm-ID: 341284 [Multi-domain] Cd Length: 518 Bit Score: 118.12 E-value: 6.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 25 DGKWEILSFNQYYEASRKAAKAMIKLGLEPFHSVGILGFNSVEWFIAALGAILAGGLCVGIYATNSADACQYAIAHSKVN 104
Cdd:cd12119 20 EGEVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 105 ILVVENELQ--LQKIfsipKNRIQTLKAIIQY--RLPVKETKNYDLYSWDDFMELGNsiPDSQLDQIigsqKANQCAVII 180
Cdd:cd12119 100 VVFVDRDFLplLEAI----APRLPTVEHVVVMtdDAAMPEPAGVGVLAYEELLAAES--PEYDWPDF----DENTAAAIC 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 181 YTSGTTGHPKGAMLSHDNITWMAGAAAMECNLSLAPKkqEVVVSYLPLSHIAAQMMDVWIPMkVGASIYFAQPDALKGTL 260
Cdd:cd12119 170 YTSGTTGNPKGVVYSHRSLVLHAMAALLTDGLGLSES--DVVLPVVPMFHVNAWGLPYAAAM-VGAKLVLPGPYLDPASL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 261 VNTLQEVKPTAFMGVPRIWEKMHEKIKEAASKSSSLRKKVfswarnVGlkintkrmlGAhdtPMSYRMAKALvfskvkSS 340
Cdd:cd12119 247 AELIEREGVTFAAGVPTVWQGLLDHLEANGRDLSSLRRVV------IG---------GS---AVPRSLIEAF------EE 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 341 LGLDHCHIFisGAAplnqETSefflsldiPIGEVYGLSESTGPHSMSTPENYRIlSSGKVMTGCKnmLYQQNKEG----- 415
Cdd:cd12119 303 RGVRVIHAW--GMT----ETS--------PLGTVARPPSEHSNLSEDEQLALRA-KQGRPVPGVE--LRIVDDDGrelpw 365
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1811029393 416 ----IGEVCLWGRHVFMGYLGSeDATTEAIDKEGWLHSGDLGRVDNKGFLYITGRIKEiIITAGGENVAPIPIENLV 488
Cdd:cd12119 366 dgkaVGELQVRGPWVTKSYYKN-DEESEALTEDGWLRTGDVATIDEDGYLTITDRSKD-VIKSGGEWISSVELENAI 440
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
31-502 |
4.57e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 115.47 E-value: 4.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 31 LSFNQYYEASRKAAKAMIKLGLEPFHSVGILGFNSVEWFIAALGAILAGGLCVGIYATNSADACQYAIAHSKVNILVVEN 110
Cdd:PRK06188 38 LTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLDDHAYVLEDAGISTLIVDP 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 111 ELQLQKIFSIpKNRIQTLKAIIQYRlPVKETKnyDLYSWDDFMELGNSIPDSQLDQIIGsqkanqcavIIYTSGTTGHPK 190
Cdd:PRK06188 118 APFVERALAL-LARVPSLKHVLTLG-PVPDGV--DLLAAAAKFGPAPLVAAALPPDIAG---------LAYTGGTTGKPK 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 191 GAMLSHDNITWMAGAAAMECNLSLAPKkqevvvsYL---PLSHIAAQMMdvwIP--MKVGASIYFAQPDAlkGTLVNTLQ 265
Cdd:PRK06188 185 GVMGTHRSIATMAQIQLAEWEWPADPR-------FLmctPLSHAGGAFF---LPtlLRGGTVIVLAKFDP--AEVLRAIE 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 266 EVKPTAFMGVPRIWEKMHEKIKEAASKSSSLrkkvfswarnvglkintkrmlgahDTpMSYrmakalvfskvksslgldh 345
Cdd:PRK06188 253 EQRITATFLVPTMIYALLDHPDLRTRDLSSL------------------------ET-VYY------------------- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 346 chifisGAAPLN----QETSEFFLsldiPI-GEVYGLSE--------STGPHSMSTPEnyRILSSGKVMTGCKNMLYQQN 412
Cdd:PRK06188 289 ------GASPMSpvrlAEAIERFG----PIfAQYYGQTEapmvitylRKRDHDPDDPK--RLTSCGRPTPGLRVALLDED 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 413 KEGI-----GEVCLWGRHVFMGYLGSEDATTEAIdKEGWLHSGDLGRVDNKGFLYITGRIKEIIITaGGENVAPIPIENL 487
Cdd:PRK06188 357 GREVaqgevGEICVRGPLVMDGYWNRPEETAEAF-RDGWLHTGDVAREDEDGFYYIVDRKKDMIVT-GGFNVFPREVEDV 434
|
490
....*....|....*
gi 1811029393 488 VKEkLPIISNAMLVG 502
Cdd:PRK06188 435 LAE-HPAVAQVAVIG 448
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
175-502 |
5.18e-26 |
|
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: 111.32 E-value: 5.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 175 QCAVIIYTSGTTGHPKGAMLSHDNItwMAGAAAMECNLSLAPkkQEVVVSYLPLSHIAAQMMDVWIPMKVGASIYFAQP- 253
Cdd:cd05903 94 AVALLLFTSGTTGEPKGVMHSHNTL--SASIRQYAERLGLGP--GDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIw 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 254 DALKGtlVNTLQEVKPTAFMGVPRIWEKMHEKIKEAASKSSSLRKkvfswarnvglkintkrmlgahdtpmsyrmakalv 333
Cdd:cd05903 170 DPDKA--LALMREHGVTFMMGATPFLTDLLNAVEEAGEPLSRLRT----------------------------------- 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 334 fskvksslgldhchiFISGAAP----LNQETSEFFLSLdipIGEVYGLSESTGPHSMSTP--ENYRILSSGKVMTGCKNM 407
Cdd:cd05903 213 ---------------FVCGGATvprsLARRAAELLGAK---VCSAYGSTECPGAVTSITPapEDRRLYTDGRPLPGVEIK 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 408 LYQQNKEG-----IGEVCLWGRHVFMGYLGSEDATTEAiDKEGWLHSGDLGRVDNKGFLYITGRIKEIIITaGGENVAPI 482
Cdd:cd05903 275 VVDDTGATlapgvEGELLSRGPSVFLGYLDRPDLTADA-APEGWFRTGDLARLDEDGYLRITGRSKDIIIR-GGENIPVL 352
|
330 340
....*....|....*....|
gi 1811029393 483 PIENLVKeKLPIISNAMLVG 502
Cdd:cd05903 353 EVEDLLL-GHPGVIEAAVVA 371
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
31-502 |
5.59e-26 |
|
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: 111.62 E-value: 5.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 31 LSFNQYYEASRKAAKAMIKLGLEPFHSVGILGFNSVEWFIAALGAILAGGLCVGIYATNSADACQYAIAHSKVNILVVEN 110
Cdd:cd12118 30 YTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVLFVDR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 111 ELQlqkifsipknriqtlkaiiqyrlpvketknydlysWDDFMELGNSIPDSQldqiigsQKANQCAVII--YTSGTTGH 188
Cdd:cd12118 110 EFE-----------------------------------YEDLLAEGDPDFEWI-------PPADEWDPIAlnYTSGTTGR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 189 PKGAMLSHDNITWMAGAAAMECNLSLAPkkqeVVVSYLPLSHiAAQMMDVWIPMKVGasiyfaqpdalkGTLVnTLQEVK 268
Cdd:cd12118 148 PKGVVYHHRGAYLNALANILEWEMKQHP----VYLWTLPMFH-CNGWCFPWTVAAVG------------GTNV-CLRKVD 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 269 PTAfmgvprIWEkmhekikeaaskssSLRK-KVfswarnvglkintKRMLGAhdtPMSYRMakaLVFSKVKSSLGLDH-C 346
Cdd:cd12118 210 AKA------IYD--------------LIEKhKV-------------THFCGA---PTVLNM---LANAPPSDARPLPHrV 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 347 HIFISGAAP----LNQETSefflsLDIPIGEVYGLSESTGPH----------SMSTPENYRILSSGKVMTGCKNMLYQQN 412
Cdd:cd12118 251 HVMTAGAPPpaavLAKMEE-----LGFDVTHVYGLTETYGPAtvcawkpewdELPTEERARLKARQGVRYVGLEEVDVLD 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 413 KEG----------IGEVCLWGRHVFMGYLGSEDATTEAIdKEGWLHSGDLGRVDNKGFLYITGRIKEIIITaGGENVAPI 482
Cdd:cd12118 326 PETmkpvprdgktIGEIVFRGNIVMKGYLKNPEATAEAF-RGGWFHSGDLAVIHPDGYIEIKDRSKDIIIS-GGENISSV 403
|
490 500
....*....|....*....|
gi 1811029393 483 PIENlVKEKLPIISNAMLVG 502
Cdd:cd12118 404 EVEG-VLYKHPAVLEAAVVA 422
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
9-504 |
7.34e-25 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 108.91 E-value: 7.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 9 ESVNRFGIYPALASKKDGkwEILSFNQYYEASRKAAKAMIKLGLEPFHSVGILGFNSVEWFIAALGAILAGGLcvgIYAT 88
Cdd:PLN02246 31 ERLSEFSDRPCLIDGATG--RVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAV---TTTA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 89 N----SADACQYAIAhSKVNILVVENeLQLQKIFSIPKNRIQTLKAIIQYRlpvketKNYdLYSWDDFMELGNSIPDSQL 164
Cdd:PLN02246 106 NpfytPAEIAKQAKA-SGAKLIITQS-CYVDKLKGLAEDDGVTVVTIDDPP------EGC-LHFSELTQADENELPEVEI 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 165 DqiigsqkANQCAVIIYTSGTTGHPKGAMLSHDN-ITWMAGAAAMEcNLSLAPKKQEVVVSYLPLSHIAAQMMDVWIPMK 243
Cdd:PLN02246 177 S-------PDDVVALPYSSGTTGLPKGVMLTHKGlVTSVAQQVDGE-NPNLYFHSDDVILCVLPMFHIYSLNSVLLCGLR 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 244 VGASIYFAQPDALkGTLVNTLQEVKPTAFMGVPRIwekmhekikeaaskssslrkkVFSWARNvglkintkRMLGAHDTP 323
Cdd:PLN02246 249 VGAAILIMPKFEI-GALLELIQRHKVTIAPFVPPI---------------------VLAIAKS--------PVVEKYDLS 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 324 mSYRMAKalvfskvksslgldhchifiSGAAPLNQETSEFFLSlDIP---IGEVYGLSEStGP-HSMS-----TPENYRI 394
Cdd:PLN02246 299 -SIRMVL--------------------SGAAPLGKELEDAFRA-KLPnavLGQGYGMTEA-GPvLAMClafakEPFPVKS 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 395 LSSGKVM-----------TGCkNMLYQQNkegiGEVCLWGRHVFMGYLGSEDATTEAIDKEGWLHSGDLGRVDNKGFLYI 463
Cdd:PLN02246 356 GSCGTVVrnaelkivdpeTGA-SLPRNQP----GEICIRGPQIMKGYLNDPEATANTIDKDGWLHTGDIGYIDDDDELFI 430
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1811029393 464 TGRIKEIIITAGGEnVAPIPIENLVKEKlPIISNAMLVGDK 504
Cdd:PLN02246 431 VDRLKELIKYKGFQ-VAPAELEALLISH-PSIADAAVVPMK 469
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
3-557 |
1.38e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 108.31 E-value: 1.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 3 IPEFFQESVNRFGIYPALASKkdGKweILSFNQYYEASRK-AAKAMIKLGLEPFHSVGILGFNSVEWFIAALGAILAGGL 81
Cdd:PRK05677 26 IQAVLKQSCQRFADKPAFSNL--GK--TLTYGELYKLSGAfAAWLQQHTDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 82 CVGIYATNSADACQYAIAHSKVNILVVENEL--QLQKIfsIPKNRIQ-----------------TLKAIIQYrlpVKE-T 141
Cdd:PRK05677 102 VVNTNPLYTAREMEHQFNDSGAKALVCLANMahLAEKV--LPKTGVKhvivtevadmlpplkrlLINAVVKH---VKKmV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 142 KNYDL---YSWDDFMELGNSIPDSQLDQiigsqKANQCAVIIYTSGTTGHPKGAMLSHDNI--TWMAGAAAMECNLSlap 216
Cdd:PRK05677 177 PAYHLpqaVKFNDALAKGAGQPVTEANP-----QADDVAVLQYTGGTTGVAKGAMLTHRNLvaNMLQCRALMGSNLN--- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 217 KKQEVVVSYLPLSHIAAQMMDVWIPMKVGA-SIYFAQPDALKGtLVNTLQEVKPTAFMGVPRIWEkmhekikeAASKSSS 295
Cdd:PRK05677 249 EGCEILIAPLPLYHIYAFTFHCMAMMLIGNhNILISNPRDLPA-MVKELGKWKFSGFVGLNTLFV--------ALCNNEA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 296 LRKKVFSwarnvGLKINtkrmlgahdtpmsyrmakalvfskvksslgldhchifISGAAPLNQETSEFFLSLD-IPIGEV 374
Cdd:PRK05677 320 FRKLDFS-----ALKLT-------------------------------------LSGGMALQLATAERWKEVTgCAICEG 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 375 YGLSESTGPHSMSTPENYRILSSGKVM--TGCKNMlyqqNKEG-------IGEVCLWGRHVFMGYLGSEDATTEAIDKEG 445
Cdd:PRK05677 358 YGMTETSPVVSVNPSQAIQVGTIGIPVpsTLCKVI----DDDGnelplgeVGELCVKGPQVMKGYWQRPEATDEILDSDG 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 446 WLHSGDLGRVDNKGFLYITGRIKEIIITAGGeNVAPIPIENLVkeklpiisnAMLVGdkakflsvllTLKCEV----DKT 521
Cdd:PRK05677 434 WLKTGDIALIQEDGYMRIVDRKKDMILVSGF-NVYPNELEDVL---------AALPG----------VLQCAAigvpDEK 493
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 1811029393 522 SGE---------PLDNLTWEAIK-FCRDvGSQASTVTEIVELQDPL 557
Cdd:PRK05677 494 SGEaikvfvvvkPGETLTKEQVMeHMRA-NLTGYKVPKAVEFRDEL 538
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
179-502 |
2.43e-24 |
|
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.
Pssm-ID: 341293 [Multi-domain] Cd Length: 330 Bit Score: 104.51 E-value: 2.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 179 IIYTSGTTGHPKGAMLSHDNiTWMAGAAAMECNlSLAPKKQEVVVSylPLSHIAAQMMDVWIPMKVGASIY-FAQPDALK 257
Cdd:cd17638 5 IMFTSGTTGRSKGVMCAHRQ-TLRAAAAWADCA-DLTEDDRYLIIN--PFFHTFGYKAGIVACLLTGATVVpVAVFDVDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 258 gtLVNTLQEVKPTAFMGVPRIWEKMHEKIKEAASKSSSLRKKVfswarnvglkintkrmLGAHDTPMSyrmakalVFSKV 337
Cdd:cd17638 81 --ILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAV----------------TGAATVPVE-------LVRRM 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 338 KSSLGLDHchifisgaaplnqetsefflsldipIGEVYGLSEStGPHSMSTPENYRILSSGKVMTGCKNMlyQQNKEGIG 417
Cdd:cd17638 136 RSELGFET-------------------------VLTAYGLTEA-GVATMCRPGDDAETVATTCGRACPGF--EVRIADDG 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 418 EVCLWGRHVFMGYLGSEDATTEAIDKEGWLHSGDLGRVDNKGFLYITGRIKEIIItAGGENVAPIPIENLVKEkLPIISN 497
Cdd:cd17638 188 EVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGELDERGYLRITDRLKDMYI-VGGFNVYPAEVEGALAE-HPGVAQ 265
|
....*
gi 1811029393 498 AMLVG 502
Cdd:cd17638 266 VAVIG 270
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
26-620 |
5.48e-24 |
|
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: 106.36 E-value: 5.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 26 GKWEILSFNQYYEASRKAAKAMIKLGLEPFHSVGILGFNSVEWFIAALGAILAGGLCVGI---YATNSAD--ACQYAIAH 100
Cdd:cd05921 21 GGWRRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVspaYSLMSQDlaKLKHLFEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 101 SKVNILVVENELQLQKifsipknriqTLKAIIQYRLPVKETKNY-DLYSWDDFMELGNSIPDSQLDQIIGSQKANQCAVI 179
Cdd:cd05921 101 LKPGLVFAQDAAPFAR----------ALAAIFPLGTPLVVSRNAvAGRGAISFAELAATPPTAAVDAAFAAVGPDTVAKF 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 180 IYTSGTTGHPKGAMLSHDNITwmAGAAAMECNLSLAPKKQEVVVSYLPLSHIAAQMMDVWIPMKVGASIYF--AQPDA-L 256
Cdd:cd05921 171 LFTSGSTGLPKAVINTQRMLC--ANQAMLEQTYPFFGEEPPVLVDWLPWNHTFGGNHNFNLVLYNGGTLYIddGKPMPgG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 257 KGTLVNTLQEVKPTAFMGVPRIWEKMhekiKEAASKSSSLRKKVFswarnvglkintKRMlgahdtpmsyrmakalvfsk 336
Cdd:cd05921 249 FEETLRNLREISPTVYFNVPAGWEML----VAALEKDEALRRRFF------------KRL-------------------- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 337 vksslgldhcHIFISGAAPLNQETSEfflSLD----------IPIGEVYGLSESTGPHSMSTPENYRILSSGKVMTGCKN 406
Cdd:cd05921 293 ----------KLMFYAGAGLSQDVWD---RLQalavatvgerIPMMAGLGATETAPTATFTHWPTERSGLIGLPAPGTEL 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 407 MLYQQNkeGIGEVCLWGRHVFMGYLGSEDATTEAIDKEGWLHSGDLGR-VD----NKGfLYITGRIKEIIITAGGENVAP 481
Cdd:cd05921 360 KLVPSG--GKYEVRVKGPNVTPGYWRQPELTAQAFDEEGFYCLGDAAKlADpddpAKG-LVFDGRVAEDFKLASGTWVSV 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 482 IPIEN-LVKEKLPIISNAMLVGDKAKFLSVLLtlkcevdktsgepldnltWEAIKFCRD-VGSQASTVTEIVELqdPLVY 559
Cdd:cd05921 437 GPLRArAVAACAPLVHDAVVAGEDRAEVGALV------------------FPDLLACRRlVGLQEASDAEVLRH--AKVR 496
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1811029393 560 MAIQKGINAVNQQAISNAQKIQKWVILEKDFSIGGGELGPTTKMKRHFIIQKYKRQIENLY 620
Cdd:cd05921 497 AAFRDRLAALNGEATGSSSRIARALLLDEPPSIDKGEITDKGYINQRAVLERRAALVERLY 557
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
181-502 |
5.60e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 105.89 E-value: 5.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 181 YTSGTTGHPKGAMLSHDNITW---------MAGAAAMECNLSLAPkkqevvvsylpLSHIAA--QMMDVwipmKVGASIY 249
Cdd:PRK07470 170 FTSGTTGRPKAAVLTHGQMAFvitnhladlMPGTTEQDASLVVAP-----------LSHGAGihQLCQV----ARGAATV 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 250 FAQPDALKGTLVNTL-QEVKPTAFMGVPRIWEKMHEKIKEAASKSSSLRKKVFSwarnvglkintkrmlGAhdtPMsYRM 328
Cdd:PRK07470 235 LLPSERFDPAEVWALvERHRVTNLFTVPTILKMLVEHPAVDRYDHSSLRYVIYA---------------GA---PM-YRA 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 329 AKALVFSKvksslgldhchifisgaaplnqetsefflsldipIGEV----YGLSESTG-----PHSMSTPE---NYRILS 396
Cdd:PRK07470 296 DQKRALAK----------------------------------LGKVlvqyFGLGEVTGnitvlPPALHDAEdgpDARIGT 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 397 SGKVMTGcknMLYQ-QNKEG-------IGEVCLWGRHVFMGYLGSEDATTEAIdKEGWLHSGDLGRVDNKGFLYITGRIK 468
Cdd:PRK07470 342 CGFERTG---MEVQiQDDEGrelppgeTGEICVIGPAVFAGYYNNPEANAKAF-RDGWFRTGDLGHLDARGFLYITGRAS 417
|
330 340 350
....*....|....*....|....*....|....*..
gi 1811029393 469 EIIITaGGENVAPIPIEnlvkEKL---PIISNAMLVG 502
Cdd:PRK07470 418 DMYIS-GGSNVYPREIE----EKLlthPAVSEVAVLG 449
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
1-485 |
7.10e-24 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 105.83 E-value: 7.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 1 MTIPEFFQESVNRFGIYPALASKKDGKweILSFNQYYEASRKAAKAMIKLGLEPFHSVGILGFNSVEWFIAALGAILAGG 80
Cdd:PLN02330 28 LTLPDFVLQDAELYADKVAFVEAVTGK--AVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 81 LCVGIYAT--NSADACQYAIAHSKvniLVVENELQLQKIFSIpknriqtlkaiiqyRLPV---KETKNYDLYSWDDFMEL 155
Cdd:PLN02330 106 VFSGANPTalESEIKKQAEAAGAK---LIVTNDTNYGKVKGL--------------GLPVivlGEEKIEGAVNWKELLEA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 156 GNSIPDSQLDQIIgsQKANQCAvIIYTSGTTGHPKGAMLSHDNITwmagaaAMECN--LSLAPKK--QEVVVSYLPLSHI 231
Cdd:PLN02330 169 ADRAGDTSDNEEI--LQTDLCA-LPFSSGTTGISKGVMLTHRNLV------ANLCSslFSVGPEMigQVVTLGLIPFFHI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 232 AAQMMDVWIPMKVGASIYFAQPDALKgTLVNTL--QEVKPTAFmgVPRIWEKMhekIKEAASKSSSLRKkvfswarnvgL 309
Cdd:PLN02330 240 YGITGICCATLRNKGKVVVMSRFELR-TFLNALitQEVSFAPI--VPPIILNL---VKNPIVEEFDLSK----------L 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 310 KINTKRMLGAHDTP-MSYRMAKALVFSKVKSSLGL-DHCHIFISGAAP-----LNQETSEFFLsldIPIGEVYGLSESTG 382
Cdd:PLN02330 304 KLQAIMTAAAPLAPeLLTAFEAKFPGVQVQEAYGLtEHSCITLTHGDPekghgIAKKNSVGFI---LPNLEVKFIDPDTG 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 383 phsMSTPENYRilssgkvmtgcknmlyqqnkegiGEVCLWGRHVFMGYLGSEDATTEAIDKEGWLHSGDLGRVDNKGFLY 462
Cdd:PLN02330 381 ---RSLPKNTP-----------------------GELCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIGYIDDDGDIF 434
|
490 500
....*....|....*....|...
gi 1811029393 463 ITGRIKEIIITAGGEnVAPIPIE 485
Cdd:PLN02330 435 IVDRIKELIKYKGFQ-VAPAELE 456
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
25-495 |
1.54e-23 |
|
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: 104.67 E-value: 1.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 25 DGKWEILSFNQYYEASRKAAKAMIKLGLEPFHSVgILGFNSVEWFIAAL-GAILAGGLcvgiyATNSADACQYAIAHSKV 103
Cdd:cd05906 34 DGSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSV-ILQFDDNEDFIPAFwACVLAGFV-----PAPLTVPPTYDEPNARL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 104 NILvveneLQLQKIFSIPknRIQTLKAIIQYRLPVKETKNYDLYSWDDFMELGNSIPDSQLDQiigsQKANQCAVIIYTS 183
Cdd:cd05906 108 RKL-----RHIWQLLGSP--VVLTDAELVAEFAGLETLSGLPGIRVLSIEELLDTAADHDLPQ----SRPDDLALLMLTS 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 184 GTTGHPKGAMLSHDNITWMAGAAAMECNLSlapkKQEVVVSYLPLSHIAAQMMDVWIPMKVGASIYFAQPDALkgtlvnt 263
Cdd:cd05906 177 GSTGFPKAVPLTHRNILARSAGKIQHNGLT----PQDVFLNWVPLDHVGGLVELHLRAVYLGCQQVHVPTEEI------- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 264 LQEvkptafmgvPRIWEKMHEKikeaaskssslRKKVFSWARNVGL-KINTkrmLGAHDTPMSYRMakalvfskvkSSLG 342
Cdd:cd05906 246 LAD---------PLRWLDLIDR-----------YRVTITWAPNFAFaLLND---LLEEIEDGTWDL----------SSLR 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 343 LdhchiFISGAAPLNQETSEFFLSLDIPIG-------EVYGLSE-------STGPHSMSTPENYRILSSGKVMTGCKNML 408
Cdd:cd05906 293 Y-----LVNAGEAVVAKTIRRLLRLLEPYGlppdairPAFGMTEtcsgviySRSFPTYDHSQALEFVSLGRPIPGVSMRI 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 409 YQQNKEG-----IGEVCLWGRHVFMGYLGSEDATTEAIDKEGWLHSGDLGRVDNkGFLYITGRIKEIIITaGGENVAPIP 483
Cdd:cd05906 368 VDDEGQLlpegeVGRLQVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLGFLDN-GNLTITGRTKDTIIV-NGVNYYSHE 445
|
490
....*....|..
gi 1811029393 484 IENLVkEKLPII 495
Cdd:cd05906 446 IEAAV-EEVPGV 456
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
25-502 |
2.21e-23 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 104.42 E-value: 2.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 25 DGKWEILSFNQYYEASRKAAKAMIKLGLEPFHSVGILGFNSVEWFIAALGAILAGGLCVGIYATNSADACQYAIAHSKVN 104
Cdd:COG0365 34 DGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 105 ILVVENEL-------QLQKIFSIPKNRIQTLKAIIQYRLPVKETKNYDLYSWDDFMELGNS-IPDSQLDqiigsqkANQC 176
Cdd:COG0365 114 VLITADGGlrggkviDLKEKVDEALEELPSLEHVIVVGRTGADVPMEGDLDWDELLAAASAeFEPEPTD-------ADDP 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 177 AVIIYTSGTTGHPKGAMLSHdniTWMAGAAAMECNLSLAPKKQEVV-----------VSYL---PLSHIAAQ-MMDvwip 241
Cdd:COG0365 187 LFILYTSGTTGKPKGVVHTH---GGYLVHAATTAKYVLDLKPGDVFwctadigwatgHSYIvygPLLNGATVvLYE---- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 242 mkvGASIYfaqPDAlkGTLVNTLQEVKPTAFMGVPRIWEKMHEKIKEAASKS--SSLRK----------KVFSWAR-NVG 308
Cdd:COG0365 260 ---GRPDF---PDP--GRLWELIEKYGVTVFFTAPTAIRALMKAGDEPLKKYdlSSLRLlgsageplnpEVWEWWYeAVG 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 309 LKIntkrmlgaHDTpmsyrmakalvfskvksSLGLDHCHIFISGaaplnqetsefflsldIPIGEVYglsestgPHSMst 388
Cdd:COG0365 332 VPI--------VDG-----------------WGQTETGGIFISN----------------LPGLPVK-------PGSM-- 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 389 penyrilssGKVMTGCKNMLYqqNKEG-------IGEVCL---W-GrhVFMGYLGSEDATTEAI--DKEGWLHSGDLGRV 455
Cdd:COG0365 362 ---------GKPVPGYDVAVV--DEDGnpvppgeEGELVIkgpWpG--MFRGYWNDPERYRETYfgRFPGWYRTGDGARR 428
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1811029393 456 DNKGFLYITGRIKEIIITAgGENVAPIPIENLVkEKLPIISNAMLVG 502
Cdd:COG0365 429 DEDGYFWILGRSDDVINVS-GHRIGTAEIESAL-VSHPAVAEAAVVG 473
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
177-502 |
2.53e-23 |
|
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: 101.25 E-value: 2.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 177 AVIIYTSGTTGHPKGAMLSHDNITwmagAAAMECNLSLAPKKQEVVVSYLPLSHIAAQMMdVWIPMKVGASIYFAQPDAL 256
Cdd:cd17630 3 ATVILTSGSTGTPKAVVHTAANLL----ASAAGLHSRLGFGGGDSWLLSLPLYHVGGLAI-LVRSLLAGAELVLLERNQA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 257 kgtLVNTLQEVKPTAFMGVPRiwekmhekikeaaskssSLRkkvfswarnvglkintkRMLGAHDTPmsyrmakalvfsk 336
Cdd:cd17630 78 ---LAEDLAPPGVTHVSLVPT-----------------QLQ-----------------RLLDSGQGP------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 337 vKSSLGLDHchIFIsGAAPLNQETSEFFLSLDIPIGEVYGLSESTGPHSMSTPENYRILSSGKVMTGCKNMLYQQnkegi 416
Cdd:cd17630 108 -AALKSLRA--VLL-GGAPIPPELLERAADRGIPLYTTYGMTETASQVATKRPDGFGRGGVGVLLPGRELRIVED----- 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 417 GEVCLWGRHVFMGYLGSEdaTTEAIDKEGWLHSGDLGRVDNKGFLYITGRIKEIIITaGGENVAPIPIENLVkEKLPIIS 496
Cdd:cd17630 179 GEIWVGGASLAMGYLRGQ--LVPEFNEDGWFTTKDLGELHADGRLTVLGRADNMIIS-GGENIQPEEIEAAL-AAHPAVR 254
|
....*.
gi 1811029393 497 NAMLVG 502
Cdd:cd17630 255 DAFVVG 260
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
178-490 |
4.14e-23 |
|
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: 100.81 E-value: 4.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 178 VIIYTSGTTGHPKGAMLSHDNITwmagAAAMECNLSLAPKKQEVVVSYLPLSHIAAQMMDVWIPMKVGASIYFAQPDALK 257
Cdd:cd17637 4 VIIHTAAVAGRPRGAVLSHGNLI----AANLQLIHAMGLTEADVYLNMLPLFHIAGLNLALATFHAGGANVVMEKFDPAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 258 GtlVNTLQEVKPTAFMGVPRIWEKMHEKIKEAASKSSSLRkkvfswarNV-GLkintkrmlgahDTPMSyrmakalvfsk 336
Cdd:cd17637 80 A--LELIEEEKVTLMGSFPPILSNLLDAAEKSGVDLSSLR--------HVlGL-----------DAPET----------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 337 vksslgldhchifisgAAPLNQETSEFFLSLdipigevYGLSESTGPHSMStPENYRILSSGKVMTGCKNMLYQQNKEGI 416
Cdd:cd17637 128 ----------------IQRFEETTGATFWSL-------YGQTETSGLVTLS-PYRERPGSAGRPGPLVRVRIVDDNDRPV 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 417 -----GEVCLWGRHVFMGYLGsEDATTEAIDKEGWLHSGDLGRVDNKGFLYITGRI--KEIIITaGGENVAPIPIENLVK 489
Cdd:cd17637 184 pagetGEIVVRGPLVFQGYWN-LPELTAYTFRNGWHHTGDLGRFDEDGYLWYAGRKpeKELIKP-GGENVYPAEVEKVIL 261
|
.
gi 1811029393 490 E 490
Cdd:cd17637 262 E 262
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
31-490 |
6.53e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 102.80 E-value: 6.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 31 LSFNQYYEASRKAAKAMIKLGLEPFHSVGILGFNSVEWFIAALGAILAGGLCVGIYATNSADACQYAIAHSKVNILV--- 107
Cdd:PRK06710 50 ITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILcld 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 108 --------VENELQLQKI--------FSIPKNRIQTLKAIIQYRLPVKETKNYDLYSWDDFMELGNSIPDSQLDqiigsq 171
Cdd:PRK06710 130 lvfprvtnVQSATKIEHVivtriadfLPFPKNLLYPFVQKKQSNLVVKVSESETIHLWNSVEKEVNTGVEVPCD------ 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 172 KANQCAVIIYTSGTTGHPKGAMLSHDNI---TWMAGAAAMECNlslapKKQEVVVSYLPLSHIAAQmmdvwipmkvgasi 248
Cdd:PRK06710 204 PENDLALLQYTGGTTGFPKGVMLTHKNLvsnTLMGVQWLYNCK-----EGEEVVLGVLPFFHVYGM-------------- 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 249 yfaqpdalkgTLVNTLQEVKPTAFMGVPRIWEKMhekIKEAASKSsslRKKVFSWARNVGLKINTKRMLGAHDtpmsyrm 328
Cdd:PRK06710 265 ----------TAVMNLSIMQGYKMVLIPKFDMKM---VFEAIKKH---KVTLFPGAPTIYIALLNSPLLKEYD------- 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 329 akalvFSKVKSSlgldhchifISGAAPLNQETSEFFLSLDI-PIGEVYGLSESTG------------PHSMSTP---ENY 392
Cdd:PRK06710 322 -----ISSIRAC---------ISGSAPLPVEVQEKFETVTGgKLVEGYGLTESSPvthsnflwekrvPGSIGVPwpdTEA 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 393 RILS--SGKVMTGCKnmlyqqnkegIGEVCLWGRHVFMGYLGSEDATTeAIDKEGWLHSGDLGRVDNKGFLYITGRIKEI 470
Cdd:PRK06710 388 MIMSleTGEALPPGE----------IGEIVVKGPQIMKGYWNKPEETA-AVLQDGWLHTGDVGYMDEDGFFYVKDRKKDM 456
|
490 500
....*....|....*....|
gi 1811029393 471 IItAGGENVAPIPIENLVKE 490
Cdd:PRK06710 457 IV-ASGFNVYPREVEEVLYE 475
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
177-490 |
1.18e-21 |
|
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: 98.85 E-value: 1.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 177 AVIIYTSGTTGHPKGAMLSHDNItwMAGAAAMECNLSLAPKkqEVVVSYLPLSHIAAQMMDVWIPMKVGASIYFAQPdal 256
Cdd:cd05931 152 AYLQYTSGSTGTPKGVVVTHRNL--LANVRQIRRAYGLDPG--DVVVSWLPLYHDMGLIGGLLTPLYSGGPSVLMSP--- 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 257 kgtlvntlqevkpTAFMGVPRIWekmhekIKEAASkssslRKKVFSWARNVGLKINTKRMLGAHDTPmsyrmakalvfsk 336
Cdd:cd05931 225 -------------AAFLRRPLRW------LRLISR-----YRATISAAPNFAYDLCVRRVRDEDLEG------------- 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 337 vkssLGLDHCHIFISGAAPLNQETSEFFLSLDIPIG---EV----YGLSESTGPHSMSTPEN------------------ 391
Cdd:cd05931 268 ----LDLSSWRVALNGAEPVRPATLRRFAEAFAPFGfrpEAfrpsYGLAEATLFVSGGPPGTgpvvlrvdrdalagrava 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 392 --------YRILSSGKVMTGCknmlyqqnkE---------------GIGEVCLWGRHVFMGYLGSEDATTE------AID 442
Cdd:cd05931 344 vaaddpaaRELVSCGRPLPDQ---------EvrivdpetgrelpdgEVGEIWVRGPSVASGYWGRPEATAEtfgalaATD 414
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1811029393 443 KEGWLHSGDLGRVdNKGFLYITGRIKEIIITAgGENVAPIPIENLVKE 490
Cdd:cd05931 415 EGGWLRTGDLGFL-HDGELYITGRLKDLIIVR-GRNHYPQDIEATAEE 460
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
31-502 |
1.28e-21 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 98.50 E-value: 1.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 31 LSFNQYYEASRKAAKAMIKLGLEPFHSVGILGFNSVEWFIAALGAILAGGLCVGIYATNSADACQYAIAHSKVNILVVEN 110
Cdd:PRK03640 28 VTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKCLITDD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 111 ELQlqkifsipknriQTLKAIIQYRlpvketknydlysWDDFMELGNSIPDSQ----LDQIigsqkanqcAVIIYTSGTT 186
Cdd:PRK03640 108 DFE------------AKLIPGISVK-------------FAELMNGPKEEAEIQeefdLDEV---------ATIMYTSGTT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 187 GHPKGAMLSHDNITWMAGAAAMecNLSLAPKKQEVVVsyLPLSHIAAqmmdVWIPMK---VGASIYFAQP-DALKGTlvN 262
Cdd:PRK03640 154 GKPKGVIQTYGNHWWSAVGSAL--NLGLTEDDCWLAA--VPIFHISG----LSILMRsviYGMRVVLVEKfDAEKIN--K 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 263 TLQEVKPTAFMGVPRIWEKMHEKIKEAaSKSSSLRKKvfswarnvglkintkrMLGAHDTPmsyrmaKALvfskvksslg 342
Cdd:PRK03640 224 LLQTGGVTIISVVSTMLQRLLERLGEG-TYPSSFRCM----------------LLGGGPAP------KPL---------- 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 343 LDHChifisgaaplnQETsefflslDIPIGEVYGLSESTGPHSMSTPEN--YRILSSGKVMTGC-----KNMLYQQNKEg 415
Cdd:PRK03640 271 LEQC-----------KEK-------GIPVYQSYGMTETASQIVTLSPEDalTKLGSAGKPLFPCelkieKDGVVVPPFE- 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 416 IGEVCLWGRHVFMGYLGSEDATTEAIdKEGWLHSGDLGRVDNKGFLYITGRIKEIIITaGGENVAPIPIENlVKEKLPII 495
Cdd:PRK03640 332 EGEIVVKGPNVTKGYLNREDATRETF-QDGWFKTGDIGYLDEEGFLYVLDRRSDLIIS-GGENIYPAEIEE-VLLSHPGV 408
|
....*..
gi 1811029393 496 SNAMLVG 502
Cdd:PRK03640 409 AEAGVVG 415
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
182-485 |
1.53e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 98.53 E-value: 1.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 182 TSGTTGHPKGAMLSHDNItwMAGAAAMECNLSLAPKKqEVVVSYLPLSHIAAQMMDVWIPMKVGAsiyfaqpDALKGTlv 261
Cdd:PRK07768 160 TSGSTGSPKAVQITHGNL--YANAEAMFVAAEFDVET-DVMVSWLPLFHDMGMVGFLTVPMYFGA-------ELVKVT-- 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 262 ntlqevkPTAFMGVPRIWEKMHEKikeaaskssslRKKVFSWARNVGLKINTKRMLGAhDTPMSYRMakalvfskvkSSL 341
Cdd:PRK07768 228 -------PMDFLRDPLLWAELISK-----------YRGTMTAAPNFAYALLARRLRRQ-AKPGAFDL----------SSL 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 342 gldhcHIFISGAAPLNQETSEFFLSLDIPIG-------EVYGLSESTGPHSMS-------------------------TP 389
Cdd:PRK07768 279 -----RFALNGAEPIDPADVEDLLDAGARFGlrpeailPAYGMAEATLAVSFSpcgaglvvdevdadllaalrravpaTK 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 390 ENYRILSS-GKVMTGCKNMLYQQNKE-----GIGEVCLWGRHVFMGYLgSEDATTEAIDKEGWLHSGDLGRVDNKGFLYI 463
Cdd:PRK07768 354 GNTRRLATlGPPLPGLEVRVVDEDGQvlpprGVGVIELRGESVTPGYL-TMDGFIPAQDADGWLDTGDLGYLTEEGEVVV 432
|
330 340
....*....|....*....|..
gi 1811029393 464 TGRIKEIIITaGGENVAPIPIE 485
Cdd:PRK07768 433 CGRVKDVIIM-AGRNIYPTDIE 453
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
64-504 |
4.30e-21 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 97.22 E-value: 4.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 64 NSVEWFIAALGAILAGGlcvgIYATNSADACQYAIAHSkvnilVVENELQLqkIFSIPKNrIQTLKAIIQYRLPVKETKN 143
Cdd:PLN02574 101 NSVYFPVIFLAVLSLGG----IVTTMNPSSSLGEIKKR-----VVDCSVGL--AFTSPEN-VEKLSPLGVPVIGVPENYD 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 144 YDLYSWDD--FMELGNSIPDSQLDQIIGSQKAnqcAVIIYTSGTTGHPKGAMLSHDN-ITWMAGAAAMECNLSLAPKKQE 220
Cdd:PLN02574 169 FDSKRIEFpkFYELIKEDFDFVPKPVIKQDDV---AAIMYSSGTTGASKGVVLTHRNlIAMVELFVRFEASQYEYPGSDN 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 221 VVVSYLPLSHIAAQMMDVWIPMKVGASIYFAQP-DAlkGTLVNTLQEVKPTAFMGVPRIWEKMHEKIKEAASKSSSLRKK 299
Cdd:PLN02574 246 VYLAALPMFHIYGLSLFVVGLLSLGSTIVVMRRfDA--SDMVKVIDRFKVTHFPVVPPILMALTKKAKGVCGEVLKSLKQ 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 300 VfswarnvglkintkrmlgahdtpmsyrmakalvfskvksslgldhchifISGAAPLNQETSEFFLS----LDIPIGevY 375
Cdd:PLN02574 324 V-------------------------------------------------SCGAAPLSGKFIQDFVQtlphVDFIQG--Y 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 376 GLSEST--GPHSMSTPENYRILSSG--------KVM---TGCknMLYQQNKegiGEVCLWGRHVFMGYLGSEDATTEAID 442
Cdd:PLN02574 353 GMTESTavGTRGFNTEKLSKYSSVGllapnmqaKVVdwsTGC--LLPPGNC---GELWIQGPGVMKGYLNNPKATQSTID 427
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1811029393 443 KEGWLHSGDLGRVDNKGFLYITGRIKEIIITAGGEnVAPIPIENLVKEKLPIISNAML-VGDK 504
Cdd:PLN02574 428 KDGWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQ-IAPADLEAVLISHPEIIDAAVTaVPDK 489
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
177-502 |
4.63e-21 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 97.20 E-value: 4.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 177 AVIIYTSGTTGHPKGAMLSHDNItwMAGAAAMECNLS--------LAPKKQEVVVSYLPLSHIAAQMMDVWIPMKVGA-S 247
Cdd:PRK12492 210 AVLQYTGGTTGLAKGAMLTHGNL--VANMLQVRACLSqlgpdgqpLMKEGQEVMIAPLPLYHIYAFTANCMCMMVSGNhN 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 248 IYFAQPDALKGtLVNTLQEVKPTAFMGVPRIWekmhekikeaaskssslrkkvfswarnVGLkintkrmlgahdtpMSYR 327
Cdd:PRK12492 288 VLITNPRDIPG-FIKELGKWRFSALLGLNTLF---------------------------VAL--------------MDHP 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 328 MAKALVFSKVKSSlgldhchifISGAAPLNQETSEFFLSLD-IPIGEVYGLSEsTGPHSMSTP--ENYRILSSGKVMTGc 404
Cdd:PRK12492 326 GFKDLDFSALKLT---------NSGGTALVKATAERWEQLTgCTIVEGYGLTE-TSPVASTNPygELARLGTVGIPVPG- 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 405 kNMLYQQNKEGI-------GEVCLWGRHVFMGYLGSEDATTEAIDKEGWLHSGDLGRVDNKGFLYITGRIKEIIITAGGe 477
Cdd:PRK12492 395 -TALKVIDDDGNelplgerGELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGF- 472
|
330 340
....*....|....*....|....*
gi 1811029393 478 NVAPIPIENLVKEKlPIISNAMLVG 502
Cdd:PRK12492 473 NVYPNEIEDVVMAH-PKVANCAAIG 496
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
177-486 |
1.85e-20 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 94.43 E-value: 1.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 177 AVIIYTSGTTGHPKGAMLSHDNItwMAGAAAMECNLSLAPKkqEVVVSYLPLSHIAAqMMDVWIPMKVGASIYFAQPDAL 256
Cdd:cd05922 120 ALLLYTSGSTGSPKLVRLSHQNL--LANARSIAEYLGITAD--DRALTVLPLSYDYG-LSVLNTHLLRGATLVLTNDGVL 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 257 KGTLVNTLQEVKPTAFMGVPRIWEkMHEKIKEAASKSSSLrkkvfswarnvglkintkRMLgahdTPMSYRMAKALVfsk 336
Cdd:cd05922 195 DDAFWEDLREHGATGLAGVPSTYA-MLTRLGFDPAKLPSL------------------RYL----TQAGGRLPQETI--- 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 337 vksslgldhchifisgaaplnQETSEFFLSLDIPIgeVYGLSESTGPHSMSTPEnyRIL----SSGKVMTGCKnmLYQQN 412
Cdd:cd05922 249 ---------------------ARLRELLPGAQVYV--MYGQTEATRRMTYLPPE--RILekpgSIGLAIPGGE--FEILD 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 413 KEG-------IGEVCLWGRHVFMGYLGSEDATTEAIDKEGWLHSGDLGRVDNKGFLYITGRIKEIIITAgGENVAPIPIE 485
Cdd:cd05922 302 DDGtptppgePGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLF-GNRISPTEIE 380
|
.
gi 1811029393 486 N 486
Cdd:cd05922 381 A 381
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
31-502 |
2.29e-20 |
|
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: 94.85 E-value: 2.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 31 LSFNQYYEASRKAAKAMIKLGLEPFHSVGILGFNSVEWFIAALGAILAGGLCVGIYATNSADACQYAIAHSKVNILVVEN 110
Cdd:TIGR03098 26 LTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQVAHILADCNVRLLVTSS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 111 ELqLQKIFSIPKNrIQTLKAIIQYRLPVKETKNY---DLYSWDDFMELGNSIP-----DSQLdqiigsqkanqcAVIIYT 182
Cdd:TIGR03098 106 ER-LDLLHPALPG-CHDLRTLIIVGDPAHASEGHpgeEPASWPKLLALGDADPphpviDSDM------------AAILYT 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 183 SGTTGHPKGAMLSHDNItwMAGAAAMECNLSLAPKKQevVVSYLPLSHIAA--QMMDVWIpmkVGASI----YFAQPDAL 256
Cdd:TIGR03098 172 SGSTGRPKGVVLSHRNL--VAGAQSVATYLENRPDDR--LLAVLPLSFDYGfnQLTTAFY---VGATVvlhdYLLPRDVL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 257 KgtlvnTLQEVKPTAFMGVPRIWEKMHE-KIKEAASKssSLRkkvfsWARNVGlkintkrmlGahdtpmsyRMAKALVfS 335
Cdd:TIGR03098 245 K-----ALEKHGITGLAAVPPLWAQLAQlDWPESAAP--SLR-----YLTNSG---------G--------AMPRATL-S 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 336 KVKSSLGLdhchifisgaaplnqetSEFFLsldipigeVYGLSESTgphsMST---PE--NYRILSSGKVMTGCKNMLYq 410
Cdd:TIGR03098 295 RLRSFLPN-----------------ARLFL--------MYGLTEAF----RSTylpPEevDRRPDSIGKAIPNAEVLVL- 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 411 qNKEG-------IGEVCLWGRHVFMGYLGSEDATTEAIDK----EGWLH-------SGDLGRVDNKGFLYITGRIKEIII 472
Cdd:TIGR03098 345 -REDGsecapgeEGELVHRGALVAMGYWNDPEKTAERFRPlppfPGELHlpelavwSGDTVRRDEEGFLYFVGRRDEMIK 423
|
490 500 510
....*....|....*....|....*....|
gi 1811029393 473 TAgGENVAPIPIENlVKEKLPIISNAMLVG 502
Cdd:TIGR03098 424 TS-GYRVSPTEVEE-VAYATGLVAEAVAFG 451
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
25-597 |
2.80e-20 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 94.95 E-value: 2.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 25 DGKWEILSFNQYYEASRKAAKAMIKLGLEPFHSVGILGFNSVEWFIAALGAILAGGLCVGI---YATNSADacqYA-IAH 100
Cdd:PRK08180 64 DGGWRRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAMYAGVPYAPVspaYSLVSQD---FGkLRH 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 101 skvnilVVEnELQLQKIFSIPKNRIQT-LKAIIQYRLPVKETKNYD----LYSWDDFMElgnSIPDSQLDQIIGSQKANQ 175
Cdd:PRK08180 141 ------VLE-LLTPGLVFADDGAAFARaLAAVVPADVEVVAVRGAVpgraATPFAALLA---TPPTAAVDAAHAAVGPDT 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 176 CAVIIYTSGTTGHPKGAMLSHDNITwmAGAAAMEcnLSLAPKKQE--VVVSYLPLSHIAAQMMDVWIPMKVGASIY---- 249
Cdd:PRK08180 211 IAKFLFTSGSTGLPKAVINTHRMLC--ANQQMLA--QTFPFLAEEppVLVDWLPWNHTFGGNHNLGIVLYNGGTLYiddg 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 250 ------FAQpdalkgTLVNtLQEVKPTAFMGVPRIWEKmhekIKEAASKSSSLRKKVFSwarnvGLKIntkrmlgahdtp 323
Cdd:PRK08180 287 kptpggFDE------TLRN-LREISPTVYFNVPKGWEM----LVPALERDAALRRRFFS-----RLKL------------ 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 324 msyrmakalvfskvksslgldhchIFISGAApLNQETSEfflSLD----------IPIGEVYGLSEsTGPHSMSTpeNYR 393
Cdd:PRK08180 339 ------------------------LFYAGAA-LSQDVWD---RLDrvaeatcgerIRMMTGLGMTE-TAPSATFT--TGP 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 394 ILSSGKV---MTGCKNMLYQQNkeGIGEVCLWGRHVFMGYLGSEDATTEAIDKEGWLHSGDLGR-VD----NKGFLYiTG 465
Cdd:PRK08180 388 LSRAGNIglpAPGCEVKLVPVG--GKLEVRVKGPNVTPGYWRAPELTAEAFDEEGYYRSGDAVRfVDpadpERGLMF-DG 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 466 RIKEIIITAGGE--NVAPIPIEnLVKEKLPIISNAMLVGDKAKFLSVLLtlkcevdktsgepldnltWEAIKFCRDVGSQ 543
Cdd:PRK08180 465 RIAEDFKLSSGTwvSVGPLRAR-AVSAGAPLVQDVVITGHDRDEIGLLV------------------FPNLDACRRLAGL 525
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 1811029393 544 ASTVTEIVELQDPLVYMAIQKGINAVNQQAISNAQKIQKWVILEKDFSIGGGEL 597
Cdd:PRK08180 526 LADASLAEVLAHPAVRAAFRERLARLNAQATGSSTRVARALLLDEPPSLDAGEI 579
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
31-467 |
1.79e-19 |
|
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: 91.54 E-value: 1.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 31 LSFNQYYEASRKAAKAMIKLGLEPFHSVGILGFNSVEWFIAALGAILAGglcvgiyatnsadacqyaiaHSKVNIlvven 110
Cdd:cd05945 17 LTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAG--------------------HAYVPL----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 111 elqlqkIFSIPKNRIQTLKAIIQyrlpvketknydlyswddfmelgnsiPDSqldqIIGSQKANqcAVIIYTSGTTGHPK 190
Cdd:cd05945 72 ------DASSPAERIREILDAAK--------------------------PAL----LIADGDDN--AYIIFTSGSTGRPK 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 191 GAMLSHDNIT----WMAGAAAMEcnlslapkKQEVVVSYLPLSHIAAqMMDVWIPMKVGASIYFAQPDALK--GTLVNTL 264
Cdd:cd05945 114 GVQISHDNLVsftnWMLSDFPLG--------PGDVFLNQAPFSFDLS-VMDLYPALASGATLVPVPRDATAdpKQLFRFL 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 265 QEVKPTAFMGVPRIWE--KMHEKIkeAASKSSSLRKKVFSwarnvglkintkrmlGahdTPMSYRMAKALVfskvksslg 342
Cdd:cd05945 185 AEHGITVWVSTPSFAAmcLLSPTF--TPESLPSLRHFLFC---------------G---EVLPHKTARALQ--------- 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 343 ldhchifisGAAPlnqetsefflslDIPIGEVYGLSESTG--------PHSMstpENYRILSSGKVMTGCKNMLYQQNKE 414
Cdd:cd05945 236 ---------QRFP------------DARIYNTYGPTEATVavtyievtPEVL---DGYDRLPIGYAKPGAKLVILDEDGR 291
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1811029393 415 -----GIGEVCLWGRHVFMGYLGSEDATTEA---IDKEGWLHSGDLGRVDNKGFLYITGRI 467
Cdd:cd05945 292 pvppgEKGELVISGPSVSKGYLNNPEKTAAAffpDEGQRAYRTGDLVRLEADGLLFYRGRL 352
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
31-502 |
1.84e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 92.30 E-value: 1.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 31 LSFNQYYEASRKAAKAMIKLGLEPFHSVGILGFNSVeWFIAALGAilAGGLCVGIYATN---SADACQYAIAHSKVNILV 107
Cdd:PRK07788 75 LTYAELDEQSNALARGLLALGVRAGDGVAVLARNHR-GFVLALYA--AGKVGARIILLNtgfSGPQLAEVAAREGVKALV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 108 VENELQlqKIFSIPKNRIQTLKAIIQYRlpvketknydlyswDDFMELGNSIPDsqLDQIIGSQKAN-------QCAVII 180
Cdd:PRK07788 152 YDDEFT--DLLSALPPDLGRLRAWGGNP--------------DDDEPSGSTDET--LDDLIAGSSTAplpkppkPGGIVI 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 181 YTSGTTGHPKGAMLSHDNitwmagaaamecnlSLAPkkqevvvsylplshiAAQMMDvWIPMKVGASIYFAQP------- 253
Cdd:PRK07788 214 LTSGTTGTPKGAPRPEPS--------------PLAP---------------LAGLLS-RVPFRAGETTLLPAPmfhatgw 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 254 ------DALKGTLV--------NTLQEV---KPTAFMGVPriweKMHEKIKEAASKssslrkkvfswarnvglkintkrM 316
Cdd:PRK07788 264 ahltlaMALGSTVVlrrrfdpeATLEDIakhKATALVVVP----VMLSRILDLGPE-----------------------V 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 317 LGAHDTpmsyrmakalvfskvkSSLGLdhchIFISGAApLNQETSEFFLSLdipIGEV-YGLSEST--GPHSMSTPENYR 393
Cdd:PRK07788 317 LAKYDT----------------SSLKI----IFVSGSA-LSPELATRALEA---FGPVlYNLYGSTevAFATIATPEDLA 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 394 ILSS--GKVMTGCKNMLYQQNKEGI--GEVclwGR------HVFMGYLGseDATTEAIDkeGWLHSGDLGRVDNKGFLYI 463
Cdd:PRK07788 373 EAPGtvGRPPKGVTVKILDENGNEVprGVV---GRifvgngFPFEGYTD--GRDKQIID--GLLSSGDVGYFDEDGLLFV 445
|
490 500 510
....*....|....*....|....*....|....*....
gi 1811029393 464 TGRIKEIIITaGGENVAPIPIENLVKEkLPIISNAMLVG 502
Cdd:PRK07788 446 DGRDDDMIVS-GGENVFPAEVEDLLAG-HPDVVEAAVIG 482
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
177-488 |
3.92e-19 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 91.27 E-value: 3.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 177 AVIIYTSGTTGHPKGAMLSHDNITwmagAAAMECNLSLAP---KKQEVVVSYLPLSHIAAQMMDVWIPMKVGA-SIYFAQ 252
Cdd:PRK08974 209 AFLQYTGGTTGVAKGAMLTHRNML----ANLEQAKAAYGPllhPGKELVVTALPLYHIFALTVNCLLFIELGGqNLLITN 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 253 PDALKGtLVNTLQEVKPTAFMGVPRIWEKMhekikeaaskssslrkkvfswarnvglkINTKRMlgahdtpmsyrmaKAL 332
Cdd:PRK08974 285 PRDIPG-FVKELKKYPFTAITGVNTLFNAL----------------------------LNNEEF-------------QEL 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 333 VFSKVKSSLGldhchifisGAAPLNQETSEFFLSL-DIPIGEVYGLSESTgPHSMSTPENYRILSSG----------KVM 401
Cdd:PRK08974 323 DFSSLKLSVG---------GGMAVQQAVAERWVKLtGQYLLEGYGLTECS-PLVSVNPYDLDYYSGSiglpvpsteiKLV 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 402 TGCKNMLYQQNkegIGEVCLWGRHVFMGYLGSEDATTEAIdKEGWLHSGDLGRVDNKGFLYITGRIKEIIITAGGeNVAP 481
Cdd:PRK08974 393 DDDGNEVPPGE---PGELWVKGPQVMLGYWQRPEATDEVI-KDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGF-NVYP 467
|
....*..
gi 1811029393 482 IPIENLV 488
Cdd:PRK08974 468 NEIEDVV 474
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
177-490 |
5.03e-19 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 90.32 E-value: 5.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 177 AVIIYTSGTTGHPKGAMLSHDNITWMAgaaamecnLSLAP----KKQEVVVSYLPLSHIAAQMMDVWIPMKVGASIYFAQ 252
Cdd:PRK07514 159 AAILYTSGTTGRSKGAMLSHGNLLSNA--------LTLVDywrfTPDDVLIHALPIFHTHGLFVATNVALLAGASMIFLP 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 253 ---PDALKGTLVNTlqevkpTAFMGVPRIWekmhekikeaaskssslrkkvfswarnvglkintKRMLGahdtpmSYRMA 329
Cdd:PRK07514 231 kfdPDAVLALMPRA------TVMMGVPTFY----------------------------------TRLLQ------EPRLT 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 330 KALVfskvksslglDHCHIFISGAAPLNQET-SEFFLSLDIPIGEVYGLSEsTGphsMSTPENY---------------- 392
Cdd:PRK07514 265 REAA----------AHMRLFISGSAPLLAEThREFQERTGHAILERYGMTE-TN---MNTSNPYdgerragtvgfplpgv 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 393 --RILS--SGKVMTgcknmlyqqnKEGIGEVCLWGRHVFMGYLGSEDATTEAIDKEGWLHSGDLGRVDNKGFLYITGRIK 468
Cdd:PRK07514 331 slRVTDpeTGAELP----------PGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGFFITGDLGKIDERGYVHIVGRGK 400
|
330 340
....*....|....*....|..
gi 1811029393 469 EIIITaGGENVAPIPIENLVKE 490
Cdd:PRK07514 401 DLIIS-GGYNVYPKEVEGEIDE 421
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
177-502 |
5.04e-19 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 90.61 E-value: 5.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 177 AVIIYTSGTTGHPKGAMLSHDNITwmagAAAMECNLSL-APKKQEVVVSYLPLSHIAAqMMDVWIPMKVGASIYFAQPDA 255
Cdd:PRK07786 177 ALIMYTSGTTGRPKGAVLTHANLT----GQAMTCLRTNgADINSDVGFVGVPLFHIAG-IGSMLPGLLLGAPTVIYPLGA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 256 LK-GTLVNTLQEVKPTAFMGVPRIWEKMhekIKEAASKSSSLRKKVFSWarnvglkintkrmlgahdtpmsyrmakalvf 334
Cdd:PRK07786 252 FDpGQLLDVLEAEKVTGIFLVPAQWQAV---CAEQQARPRDLALRVLSW------------------------------- 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 335 skvksslgldhchifisGAAP----LNQETSEFFLslDIPIGEVYGLSESTGPHSMSTPEN--YRILSSGKVMTGCKNML 408
Cdd:PRK07786 298 -----------------GAAPasdtLLRQMAATFP--EAQILAAFGQTEMSPVTCMLLGEDaiRKLGSVGKVIPTVAARV 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 409 YQQNKEG-----IGEVCLWGRHVFMGYLGSEDATTEAIDKeGWLHSGDLGRVDNKGFLYITGRIKEIIITaGGENVAPIP 483
Cdd:PRK07786 359 VDENMNDvpvgeVGEIVYRAPTLMSGYWNNPEATAEAFAG-GWFHSGDLVRQDEEGYVWVVDRKKDMIIS-GGENIYCAE 436
|
330
....*....|....*....
gi 1811029393 484 IENLVKEKlPIISNAMLVG 502
Cdd:PRK07786 437 VENVLASH-PDIVEVAVIG 454
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
168-493 |
5.80e-19 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 91.52 E-value: 5.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 168 IGSQKANQCAVIIYTSGTTGHPKGAMLSHDNItwMAGAAAMecNLSLAPKKQEVVVSYLPLSHIAAQMMDVWIPMKVG-A 246
Cdd:PRK08633 776 GPTFKPDDTATIIFSSGSEGEPKGVMLSHHNI--LSNIEQI--SDVFNLRNDDVILSSLPFFHSFGLTVTLWLPLLEGiK 851
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 247 SIYFAQP-DAlkgtlvntlqevkptafmgvpriwekmhEKIKEAASKssslrkkvfswaRNVGLKINTKRMLGAHdtpMS 325
Cdd:PRK08633 852 VVYHPDPtDA----------------------------LGIAKLVAK------------HRATILLGTPTFLRLY---LR 888
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 326 YRMAKALVFSKVksslgldhcHIFISGAAPLNQETSEFF-LSLDIPIGEVYGLSESTGPHSMSTPEnyrILSSG-KVMTG 403
Cdd:PRK08633 889 NKKLHPLMFASL---------RLVVAGAEKLKPEVADAFeEKFGIRILEGYGATETSPVASVNLPD---VLAADfKRQTG 956
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 404 CKN-----------------MLYQQNKEGI-GEVCLWGRHVFMGYLGSEDATTEAI---DKEGWLHSGDLGRVDNKGFLY 462
Cdd:PRK08633 957 SKEgsvgmplpgvavrivdpETFEELPPGEdGLILIGGPQVMKGYLGDPEKTAEVIkdiDGIGWYVTGDKGHLDEDGFLT 1036
|
330 340 350
....*....|....*....|....*....|....
gi 1811029393 463 ITGRIK---EIiitaGGENVAPIPIENLVKEKLP 493
Cdd:PRK08633 1037 ITDRYSrfaKI----GGEMVPLGAVEEELAKALG 1066
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
171-496 |
9.43e-19 |
|
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: 89.47 E-value: 9.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 171 QKANQCAVIIYTSGTTGHPKGAMLSHDNITWMAGAaameCNLSLAPKKQEVVVSYLPLSH----IAAQMmdvwIPMKVGA 246
Cdd:cd05908 103 ELADELAFIQFSSGSTGDPKGVMLTHENLVHNMFA----ILNSTEWKTKDRILSWMPLTHdmglIAFHL----APLIAGM 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 247 SIYFAqpdalkgtlvntlqevkPTA-FMGVPRIWEKMHEKIKeaASKSSSlrkkvfswaRNVGLKINTKRmlgahdtpms 325
Cdd:cd05908 175 NQYLM-----------------PTRlFIRRPILWLKKASEHK--ATIVSS---------PNFGYKYFLKT---------- 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 326 YRMAKAlvfskvkSSLGLDHCHIFISGAAPLNQETSEFFLSLDIPIG-------EVYGLSEST--------GPH------ 384
Cdd:cd05908 217 LKPEKA-------NDWDLSSIRMILNGAEPIDYELCHEFLDHMSKYGlkrnailPVYGLAEASvgaslpkaQSPfktitl 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 385 --------------SMSTPENYRILSSGKVMTGCK-NMLYQQNKE----GIGEVCLWGRHVFMGYLGSEDATTEAIDKEG 445
Cdd:cd05908 290 grrhvthgepepevDKKDSECLTFVEVGKPIDETDiRICDEDNKIlpdgYIGHIQIRGKNVTPGYYNNPEATAKVFTDDG 369
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1811029393 446 WLHSGDLGRVDNkGFLYITGRIKEIIITaGGENVAPIPIENLVKEKLPIIS 496
Cdd:cd05908 370 WLKTGDLGFIRN-GRLVITGREKDIIFV-NGQNVYPHDIERIAEELEGVEL 418
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
31-502 |
1.52e-18 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 89.47 E-value: 1.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 31 LSFNQYYEASRKAAKAMIKLGLEPFHSVGILGFNS---VEWFIAAlgaILAGGLCVGIYATNSADACQYAIAHSKVNILV 107
Cdd:PLN02860 33 RTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSdlyLEWLLAV---ACAGGIVAPLNYRWSFEEAKSAMLLVRPVMLV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 108 VENELQ----LQKIFSIPKNRIQTLkaiiqyrlpvketknYDLYSWDDFMELGNSI-PDSQLDQIIGSQKANQC------ 176
Cdd:PLN02860 110 TDETCSswyeELQNDRLPSLMWQVF---------------LESPSSSVFIFLNSFLtTEMLKQRALGTTELDYAwapdda 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 177 AVIIYTSGTTGHPKGAMLSHDNITWMagaaamecnlSLAP------KKQEVVVSYLPLSHIA------AQMM----DVWI 240
Cdd:PLN02860 175 VLICFTSGTTGRPKGVTISHSALIVQ----------SLAKiaivgyGEDDVYLHTAPLCHIGglssalAMLMvgacHVLL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 241 PmKVGASIYFaqpDALKGTLVntlqevkpTAFMGVPRIwekMHEKIKEAASKSSSlrkKVFSWAR---NVGLKINTKRML 317
Cdd:PLN02860 245 P-KFDAKAAL---QAIKQHNV--------TSMITVPAM---MADLISLTRKSMTW---KVFPSVRkilNGGGSLSSRLLP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 318 GAHDTPMSYRMAKALVFSKVKSSLgldhchIFIsgaaPLNQETSEFFLSLDIPIGEVYGLSestGPHSMSTpenyrilSS 397
Cdd:PLN02860 307 DAKKLFPNAKLFSAYGMTEACSSL------TFM----TLHDPTLESPKQTLQTVNQTKSSS---VHQPQGV-------CV 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 398 GKVMTGCKNMLYQQNKEGIGEVCLWGRHVFMGYLGSEDATTEAIDKEGWLHSGDLGRVDNKGFLYITGRIKEIIITaGGE 477
Cdd:PLN02860 367 GKPAPHVELKIGLDESSRVGRILTRGPHVMLGYWGQNSETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKT-GGE 445
|
490 500
....*....|....*....|....*
gi 1811029393 478 NVAPIPIENLVKEKlPIISNAMLVG 502
Cdd:PLN02860 446 NVYPEEVEAVLSQH-PGVASVVVVG 469
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
31-502 |
1.94e-18 |
|
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: 88.30 E-value: 1.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 31 LSFNQYYEASRKAAKAMIKLGLEPFHSVGILGFNSVEWFIAALGAILAGGLCVGIYATNSADACQYAIAHSKVNILVVEN 110
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 111 ELqlqkifsipknriqtlkaiiqyrlpvketknydlyswDDFmelgnsipdsqldqiigsqkanqcAVIIYTSGTTGHPK 190
Cdd:cd05935 82 EL-------------------------------------DDL------------------------ALIPYTSGTTGLPK 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 191 GAMLSHDNItwMAGAAAMECNLSLAPkkQEVVVSYLPLSHIAAQMMDVWIPMKVGASIYF-AQPDalKGTLVNTLQEVKP 269
Cdd:cd05935 101 GCMHTHFSA--AANALQSAVWTGLTP--SDVILACLPLFHVTGFVGSLNTAVYVGGTYVLmARWD--RETALELIEKYKV 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 270 TAFMGVPRIWEKMHEKIKEAASKSSSLRkkvfswarnvglkintkrMLGAHDTPMsyrmAKALVfSKVKSSLGLDHChif 349
Cdd:cd05935 175 TFWTNIPTMLVDLLATPEFKTRDLSSLK------------------VLTGGGAPM----PPAVA-EKLLKLTGLRFV--- 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 350 isgaaplnqetsefflsldipigEVYGLSESTGPHSMSTPENYRILSSG--------KVMTGCKNMLYQQNKEGigEVCL 421
Cdd:cd05935 229 -----------------------EGYGLTETMSQTHTNPPLRPKLQCLGip*fgvdaRVIDIETGRELPPNEVG--EIVV 283
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 422 WGRHVFMGYLGSEDATTEA---IDKEGWLHSGDLGRVDNKGFLYITGRIKEIIITAGGEnVAPIPIENLVkEKLPIISNA 498
Cdd:cd05935 284 RGPQIFKGYWNRPEETEESfieIKGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFK-VWPAEVEAKL-YKHPAI*EV 361
|
....
gi 1811029393 499 MLVG 502
Cdd:cd05935 362 CVIS 365
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
31-502 |
3.64e-18 |
|
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: 87.52 E-value: 3.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 31 LSFNQYYEASRKAAKAMIKLGLEPFHSVGILGFNSVEWFIAALGAILAGGLCVGIYATNSADACQYAIAHSKVNILVVEN 110
Cdd:cd05919 11 VTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVTSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 111 ElqlqkifsipknriqtlkaiiqyrlpvketknyDLYSWddfmelgnsipdsqldqiigsqkanqcaviIYTSGTTGHPK 190
Cdd:cd05919 91 D---------------------------------DIAYL------------------------------LYSSGTTGPPK 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 191 GAMLSHDNITWMAGAAAMECnLSLAPkkQEVVVSylplshiAAQMM-------DVWIPMKVGAS--IYFAQPDAlkGTLV 261
Cdd:cd05919 108 GVMHAHRDPLLFADAMAREA-LGLTP--GDRVFS-------SAKMFfgyglgnSLWFPLAVGASavLNPGWPTA--ERVL 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 262 NTLQEVKPTAFMGVPRIWEKMhekIKEAASKSSSLRkkvfswarnvglkintkrmlgahdtpmSYRmakalvfskvkssl 341
Cdd:cd05919 176 ATLARFRPTVLYGVPTFYANL---LDSCAGSPDALR---------------------------SLR-------------- 211
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 342 gldhchIFISGAAPLNQETSEFFLS-LDIPIGEVYGLSESTGPHSMSTPENYRILSSGKVMTGCKNMLYqqNKEG----- 415
Cdd:cd05919 212 ------LCVSAGEALPRGLGERWMEhFGGPILDGIGATEVGHIFLSNRPGAWRLGSTGRPVPGYEIRLV--DEEGhtipp 283
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 416 --IGEVCLWGRHVFMGYLGSEDaTTEAIDKEGWLHSGDLGRVDNKGFLYITGRIKEIIITaGGENVAPIPIENLVKEKLP 493
Cdd:cd05919 284 geEGDLLVRGPSAAVGYWNNPE-KSRATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKV-GGQWVSPVEVESLIIQHPA 361
|
....*....
gi 1811029393 494 iISNAMLVG 502
Cdd:cd05919 362 -VAEAAVVA 369
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
32-502 |
7.49e-18 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 87.05 E-value: 7.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 32 SFNQYYEASRKAAKAMIKLGLEPFHSVGILGFNSVE----WF-IAALGAILagglcVGIYATNSADACQYAIAHSKVNIL 106
Cdd:PRK08008 39 SYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEfifcWFgLAKIGAIM-----VPINARLLREESAWILQNSQASLL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 107 VVENELqLQKIFSIPKNRIQTLKAIIQYRLPVKETKNYDlyswdDFMELGNSIPDsQLDQIIgSQKANQCAVIIYTSGTT 186
Cdd:PRK08008 114 VTSAQF-YPMYRQIQQEDATPLRHICLTRVALPADDGVS-----SFTQLKAQQPA-TLCYAP-PLSTDDTAEILFTSGTT 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 187 GHPKGAMLSHDNITWMAGAAAMECNLslapKKQEVVVSYLPLSHIAAQMMDVWIPMKVGAsiyfaqpdalkgTLVntlqe 266
Cdd:PRK08008 186 SRPKGVVITHYNLRFAGYYSAWQCAL----RDDDVYLTVMPAFHIDCQCTAAMAAFSAGA------------TFV----- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 267 vkptafmgvpriwekMHEKikeaaskssslrkkvFSwARNVGLKINTKRMLGAHDTPMsyrMAKALVFSKVkSSLGLDHC 346
Cdd:PRK08008 245 ---------------LLEK---------------YS-ARAFWGQVCKYRATITECIPM---MIRTLMVQPP-SANDRQHC 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 347 ------HIFISgaaplNQETSEFFLSLDIPIGEVYGLSESTGPHSMSTP-ENYRILSSGKVMTGcknmlYQ------QNK 413
Cdd:PRK08008 290 lrevmfYLNLS-----DQEKDAFEERFGVRLLTSYGMTETIVGIIGDRPgDKRRWPSIGRPGFC-----YEaeirddHNR 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 414 E----GIGEVCLWG---RHVFMGYLGSEDATTEAIDKEGWLHSGDLGRVDNKGFLYITGRiKEIIITAGGENVAPIPIEN 486
Cdd:PRK08008 360 PlpagEIGEICIKGvpgKTIFKEYYLDPKATAKVLEADGWLHTGDTGYVDEEGFFYFVDR-RCNMIKRGGENVSCVELEN 438
|
490
....*....|....*.
gi 1811029393 487 LVkEKLPIISNAMLVG 502
Cdd:PRK08008 439 II-ATHPKIQDIVVVG 453
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
177-494 |
7.95e-18 |
|
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: 85.00 E-value: 7.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 177 AVIIYTSGTTGHPKGAMLSHDNitwmagAAAMECNLSLAPKK---QEVVVSYLPLSHIAAQMmdvWIPMKV---GASIYF 250
Cdd:cd17635 4 LAVIFTSGTTGEPKAVLLANKT------FFAVPDILQKEGLNwvvGDVTYLPLPATHIGGLW---WILTCLihgGLCVTG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 251 AQPDALKgTLVNTLQEVKPTAFMGVPRIWEKMHEKIKEAASKSSSLRkkvfswarnvglkintkrmlgahdtpmsyrmak 330
Cdd:cd17635 75 GENTTYK-SLFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLR--------------------------------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 331 alvfskvksslgldhcHIFISGAAPLNQETSEFFLSLDIPIGEVYGLSESTGPHSMSTPENYR-ILSSGKVMTGCKnmLY 409
Cdd:cd17635 121 ----------------LIGYGGSRAIAADVRFIEATGLTNTAQVYGLSETGTALCLPTDDDSIeINAVGRPYPGVD--VY 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 410 QQNKEGI-------GEVCLWGRHVFMGYLGSEDATTEAIdKEGWLHSGDLGRVDNKGFLYITGRIKEIIItAGGENVAPI 482
Cdd:cd17635 183 LAATDGIagpsasfGTIWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLGERREDGFLFITGRSSESIN-CGGVKIAPD 260
|
330
....*....|..
gi 1811029393 483 PIENLVKEKLPI 494
Cdd:cd17635 261 EVERIAEGVSGV 272
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
31-502 |
1.74e-17 |
|
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: 85.08 E-value: 1.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 31 LSFNQYYEASRKAAKAMIKLGLEPFHSVGILGFNSVEWFIAALGAILAGGLCVGIYATNSADACQYAIAHSKVNILVVEn 110
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 111 elqlqkifsipknriqtlkaiiqyrlpvketknydlyswddfmelgnsipdsqldqiigsqkANQCAVIIYTSGTTGHPK 190
Cdd:cd05972 80 --------------------------------------------------------------AEDPALIYFTSGTTGLPK 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 191 GAMLSHdniTWMAGA-AAMECNLSLAPKkqEVVVSYLPLSHIAAQMMDVWIPMKVGASiyfaqpdalkgTLVNTLQEVKP 269
Cdd:cd05972 98 GVLHTH---SYPLGHiPTAAYWLGLRPD--DIHWNIADPGWAKGAWSSFFGPWLLGAT-----------VFVYEGPRFDA 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 270 tafmgvpriwEKMHEKIKEaaskssslrkkvfswarnvgLKINTkrMLGAhdtPMSYRM-AKALVFSKVKSSLgldhcHI 348
Cdd:cd05972 162 ----------ERILELLER--------------------YGVTS--FCGP---PTAYRMlIKQDLSSYKFSHL-----RL 201
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 349 FISGAAPLNQETSEFFLS-LDIPIGEVYGLSESTGPHSMSTPENYRILSSGKVMTGCKNMLYQQNKEGI-----GEVCL- 421
Cdd:cd05972 202 VVSAGEPLNPEVIEWWRAaTGLPIRDGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYDVAIIDDDGRELppgeeGDIAIk 281
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 422 WGRHV-FMGYLGSEDATTEAIdKEGWLHSGDLGRVDNKGFLYITGRIKEIIITAgGENVAPIPIEN-LVKEklPIISNAM 499
Cdd:cd05972 282 LPPPGlFLGYVGDPEKTEASI-RGDYYLTGDRAYRDEDGYFWFVGRADDIIKSS-GYRIGPFEVESaLLEH--PAVAEAA 357
|
...
gi 1811029393 500 LVG 502
Cdd:cd05972 358 VVG 360
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
31-557 |
2.86e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 85.40 E-value: 2.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 31 LSFNQYYE-ASRKAAKAMIKLGLEPFHSVGILGFNSVEWFIAALGAILAGGLCVGIYATNSADACQYAIAHS--KVNILV 107
Cdd:PRK08314 36 ISYRELLEeAERLAGYLQQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSgaRVAIVG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 108 VE---------NELQLQKI----FS--IPKNRIQTLKAIIQYRLPVKETKNYDLYSWDDFMELGNSIPDSQLDqiigsqk 172
Cdd:PRK08314 116 SElapkvapavGNLRLRHVivaqYSdyLPAEPEIAVPAWLRAEPPLQALAPGGVVAWKEALAAGLAPPPHTAG------- 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 173 ANQCAVIIYTSGTTGHPKGAMLSHDNITWMAGAAAMECNLSlapkKQEVVVSYLPLSHIAAQMMDVWIPMKVGASIYFaq 252
Cdd:PRK08314 189 PDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNST----PESVVLAVLPLFHVTGMVHSMNAPIYAGATVVL-- 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 253 pdalkgtlvntlqevkptafmgVPRiWEKmhekikEAASKSSSlRKKVFSWArnvglkiNTKRMLgaHDTPMSYRMAKAl 332
Cdd:PRK08314 263 ----------------------MPR-WDR------EAAARLIE-RYRVTHWT-------NIPTMV--VDFLASPGLAER- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 333 VFSKVKSSLGldhchifisGAAPLNQETSEFFLSL-DIPIGEVYGLSESTGPHSMSTPEN--------------YRIL-- 395
Cdd:PRK08314 303 DLSSLRYIGG---------GGAAMPEAVAERLKELtGLDYVEGYGLTETMAQTHSNPPDRpklqclgiptfgvdARVIdp 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 396 SSGKVMTgcknmlyqQNKEGigEVCLWGRHVFMGYLGSEDATTEA---IDKEGWLHSGDLGRVDNKGFLYITGRIKEiII 472
Cdd:PRK08314 374 ETLEELP--------PGEVG--EIVVHGPQVFKGYWNRPEATAEAfieIDGKRFFRTGDLGRMDEEGYFFITDRLKR-MI 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 473 TAGGENVAPIPIENLVkEKLPIISNAMLV-------GDKAKFLSVlltLKCE-VDKTSGEpldnltwEAIKFCRDVGSqA 544
Cdd:PRK08314 443 NASGFKVWPAEVENLL-YKHPAIQEACVIatpdprrGETVKAVVV---LRPEaRGKTTEE-------EIIAWAREHMA-A 510
|
570
....*....|...
gi 1811029393 545 STVTEIVELQDPL 557
Cdd:PRK08314 511 YKYPRIVEFVDSL 523
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
40-487 |
6.33e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 83.99 E-value: 6.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 40 SRKAAKAMIKLGLEPFHSVGILGFNSVEWFIAALGAILAGGLCVGIYATNSADACQYAIAHSKVNILvvenelqlqkIFS 119
Cdd:PRK07008 49 AKQLAQALAALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRLFPEQIAYIVNHAEDRYV----------LFD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 120 IpknriqTLKAIIQYRLP-VKETKNYDLYSWDDFMELGnSIPDSQLDQIIGSQKA---------NQCAVIIYTSGTTGHP 189
Cdd:PRK07008 119 L------TFLPLVDALAPqCPNVKGWVAMTDAAHLPAG-STPLLCYETLVGAQDGdydwprfdeNQASSLCYTSGTTGNP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 190 KGAMLSHDNITWMAGAAAMECNLSLApkKQEVVVSYLPLSHIAAQMMDVWIPMkVGASIYFAQPDaLKGTLVNTLQEVKP 269
Cdd:PRK07008 192 KGALYSHRSTVLHAYGAALPDAMGLS--ARDAVLPVVPMFHVNAWGLPYSAPL-TGAKLVLPGPD-LDGKSLYELIEAER 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 270 TAF-MGVPRIWEKMHEKIKEAASKSSSLRKKVfswarnvglkintkrmLGAHDTPMSyrMAKALvfskvKSSLGLDHCHI 348
Cdd:PRK07008 268 VTFsAGVPTVWLGLLNHMREAGLRFSTLRRTV----------------IGGSACPPA--MIRTF-----EDEYGVEVIHA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 349 FisGAAPLNqetsefflsldiPIGEvygLSESTGPHSMSTPENYR--ILSSGKVMTGCK-NMLYQQNKE------GIGEV 419
Cdd:PRK07008 325 W--GMTEMS------------PLGT---LCKLKWKHSQLPLDEQRklLEKQGRVIYGVDmKIVGDDGRElpwdgkAFGDL 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1811029393 420 CLWGRHVFMGYLGSEDatTEAIDkeGWLHSGDLGRVDNKGFLYITGRIKEiIITAGGENVAPIPIENL 487
Cdd:PRK07008 388 QVRGPWVIDRYFRGDA--SPLVD--GWFPTGDVATIDADGFMQITDRSKD-VIKSGGEWISSIDIENV 450
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
173-502 |
3.90e-16 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 81.64 E-value: 3.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 173 ANQCAVIIYTSGTTGHPKGAMLSHDniTWMAGAAAMECNLSLapKKQEVVVSYLPLSHIAAQMMDVWIPMKVGAS-IYFA 251
Cdd:PRK13295 196 PDDVTQLIYTSGTTGEPKGVMHTAN--TLMANIVPYAERLGL--GADDVILMASPMAHQTGFMYGLMMPVMLGATaVLQD 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 252 QPDALKgtLVNTLQEVKPTAFMGVPRIWEKMHEKIKEAASKSSSLRkkVFSWArnvglkintkrmlGAHDTPMSYRMAKA 331
Cdd:PRK13295 272 IWDPAR--AAELIRTEGVTFTMASTPFLTDLTRAVKESGRPVSSLR--TFLCA-------------GAPIPGALVERARA 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 332 LVFSKVKSSLGLDHChifisGAAPLnqetsefflsldipigevyglsestgpHSMSTPENYRILSSG--------KVMTG 403
Cdd:PRK13295 335 ALGAKIVSAWGMTEN-----GAVTL---------------------------TKLDDPDERASTTDGcplpgvevRVVDA 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 404 CKNMLYQQNkegIGEVCLWGRHVFMGYLGSEDATteAIDKEGWLHSGDLGRVDNKGFLYITGRIKEIIITaGGENVAPIP 483
Cdd:PRK13295 383 DGAPLPAGQ---IGRLQVRGCSNFGGYLKRPQLN--GTDADGWFDTGDLARIDADGYIRISGRSKDVIIR-GGENIPVVE 456
|
330
....*....|....*....
gi 1811029393 484 IENLVKEKlPIISNAMLVG 502
Cdd:PRK13295 457 IEALLYRH-PAIAQVAIVA 474
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
31-541 |
5.02e-16 |
|
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: 81.02 E-value: 5.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 31 LSFNQYYEASRKAAKAMIKLGLEPFHSVGILGFNSVEWFIAALGAILAGGLCVGIYATNSADACQYAIAHSKVNILVVEN 110
Cdd:cd05923 29 LTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEMTAAVIAV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 111 ELQLQKIFSIPKNRIQTLKAIIQYRLPvketknydlYSWddfmelGNSIPDSQldqiigsQKANQCAVIIYTSGTTGHPK 190
Cdd:cd05923 109 DAQVMDAIFQSGVRVLALSDLVGLGEP---------ESA------GPLIEDPP-------REPEQPAFVFYTSGTTGLPK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 191 GAMLSHDNITwmAGAAAMECNLSLAPKKQEVVVSYLPLSH--------IAAQMMD-VWIPMKvgasiYFAQPDALKgtlv 261
Cdd:cd05923 167 GAVIPQRAAE--SRVLFMSTQAGLRHGRHNVVLGLMPLYHvigffavlVAALALDgTYVVVE-----EFDPADALK---- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 262 nTLQEVKPTAFMGVPRIWEKMHEKIKEAASKSSSLRKKVFSWARnvglkintkrmlgahdtpmsyrMAKALvfskvkssl 341
Cdd:cd05923 236 -LIEQERVTSLFATPTHLDALAAAAEFAGLKLSSLRHVTFAGAT----------------------MPDAV--------- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 342 gLDHCHIFISGaaplnqetsefflsldiPIGEVYGLSESTGPHSMSTPENYRILSSG-----KVMT--GCKNMLYQQNKE 414
Cdd:cd05923 284 -LERVNQHLPG-----------------EKVNIYGTTEAMNSLYMRDARTGTEMRPGffsevRIVRigGSPDEALANGEE 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 415 GIGEVCLWGRHVFMGYLGSEDATTEAIdKEGWLHSGDLGRVDNKGFLYITGRIKEIIITaGGENVAPIPIENLVKEKlPI 494
Cdd:cd05923 346 GELIVAAAADAAFTGYLNQPEATAKKL-QDGWYRTGDVGYVDPSGDVRILGRVDDMIIS-GGENIHPSEIERVLSRH-PG 422
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1811029393 495 ISNAMLVG--DKAKFLSVLLTLKCEVDKTSGEPLDnltweaiKFCRDVG 541
Cdd:cd05923 423 VTEVVVIGvaDERWGQSVTACVVPREGTLSADELD-------QFCRASE 464
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
177-452 |
1.42e-15 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 80.19 E-value: 1.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 177 AVIIYTSGTTGHPKGAMLSHDNITWMAGAAAMECNLSLAPkkqEVVVSYLPLSHIAAQMMDVWIPMKVGASIYFAQPDAl 256
Cdd:cd17632 226 ALLIYTSGSTGTPKGAMYTERLVATFWLKVSSIQDIRPPA---SITLNFMPMSHIAGRISLYGTLARGGTAYFAAASDM- 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 257 kGTLVNTLQEVKPTAFMGVPRIWEKMHEKIKEAASKSSSLRKKVFSWARNVGLKINtKRMLGAhdtpmsyRMAKAlvfsk 336
Cdd:cd17632 302 -STLFDDLALVRPTELFLVPRVCDMLFQRYQAELDRRSVAGADAETLAERVKAELR-ERVLGG-------RLLAA----- 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 337 vksslgldhchifISGAAPLNQETSEFFLS-LDIPIGEVYGLSESTG---PHSMSTPE--NYRILSS---GKVMTgckNM 407
Cdd:cd17632 368 -------------VCGSAPLSAEMKAFMESlLDLDLHDGYGSTEAGAvilDGVIVRPPvlDYKLVDVpelGYFRT---DR 431
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1811029393 408 LYQQnkegiGEVCLWGRHVFMGYLGSEDATTEAIDKEGWLHSGDL 452
Cdd:cd17632 432 PHPR-----GELLVKTDTLFPGYYKRPEVTAEVFDEDGFYRTGDV 471
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
150-502 |
1.53e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 79.47 E-value: 1.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 150 DDFMELGNSIPDSqLDQIIGSQKANQCA-----------VIIYTSGTTGHPKGAMLSHDNITWMAgaaameCNLSLAPK- 217
Cdd:PRK09088 101 DDAVAAGRTDVED-LAAFIASADALEPAdtpsippervsLILFTSGTSGQPKGVMLSERNLQQTA------HNFGVLGRv 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 218 -KQEVVVSYLPLSHIAAQMMDVWIPMKVGASIYFA---QPDALKGTLVNtlQEVKPTAFMGVPRIwekmhekikeaasks 293
Cdd:PRK09088 174 dAHSSFLCDAPMFHIIGLITSVRPVLAVGGSILVSngfEPKRTLGRLGD--PALGITHYFCVPQM--------------- 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 294 sslrkkvfswarnvglkintKRMLGAHDT--PMSYRMAKALVfskvksslgldhchifiSGAAPLNQETSEFFLSLDIPI 371
Cdd:PRK09088 237 --------------------AQAFRAQPGfdAAALRHLTALF-----------------TGGAPHAAEDILGWLDDGIPM 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 372 GEVYGLSESTGPHSMSTPENY---RILSSGKVMTGCKNMLYQQNKEGI-----GEVCLWGRHVFMGYLGSEDATTEAIDK 443
Cdd:PRK09088 280 VDGFGMSEAGTVFGMSVDCDViraKAGAAGIPTPTVQTRVVDDQGNDCpagvpGELLLRGPNLSPGYWRRPQATARAFTG 359
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1811029393 444 EGWLHSGDLGRVDNKGFLYITGRIKEIIITaGGENVAPIPIENLVKEKlPIISNAMLVG 502
Cdd:PRK09088 360 DGWFRTGDIARRDADGFFWVVDRKKDMFIS-GGENVYPAEIEAVLADH-PGIRECAVVG 416
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
177-485 |
1.56e-15 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 79.55 E-value: 1.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 177 AVIIYTSGTTGHPKGAMLSHDNITwmAGAAAMECNLSLAPKKQEVVVsyLPLSH----IAAQMMDVwipMKVGASIYFAQ 252
Cdd:PRK05852 179 AMIMFTGGTTGLPKMVPWTHANIA--SSVRAIITGYRLSPRDATVAV--MPLYHghglIAALLATL---ASGGAVLLPAR 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 253 PDALKGTLVNTLQEVKPTAFMGVPRIwekmHEKIKEAASKSSSLRKKvfswarnvglkintkrmlgahdtpmsyrmaKAL 332
Cdd:PRK05852 252 GRFSAHTFWDDIKAVGATWYTAVPTI----HQILLERAATEPSGRKP------------------------------AAL 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 333 VFSKvksslgldhchifiSGAAPLNQETSEF----FLSldiPIGEVYGLSE---------------------STGPHSMS 387
Cdd:PRK05852 298 RFIR--------------SCSAPLTAETAQAlqteFAA---PVVCAFGMTEathqvtttqiegigqtenpvvSTGLVGRS 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 388 TPENYRIL-SSGKVMTgcknmlyqqnKEGIGEVCLWGRHVFMGYLGsEDATTEAIDKEGWLHSGDLGRVDNKGFLYITGR 466
Cdd:PRK05852 361 TGAQIRIVgSDGLPLP----------AGAVGEVWLRGTTVVRGYLG-DPTITAANFTDGWLRTGDLGSLSAAGDLSIRGR 429
|
330
....*....|....*....
gi 1811029393 467 IKEiIITAGGENVAPIPIE 485
Cdd:PRK05852 430 IKE-LINRGGEKISPERVE 447
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
179-502 |
1.60e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 79.54 E-value: 1.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 179 IIYTSGTTGHPKGAMLSHDNITWMAgaAAMECNLSLAPKKQEVVVSylPLSHIAAQMMDVWIPMKVGASIYFAQpDALKG 258
Cdd:PRK06145 154 LMYTSGTTDRPKGVMHSYGNLHWKS--IDHVIALGLTASERLLVVG--PLYHVGAFDLPGIAVLWVGGTLRIHR-EFDPE 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 259 TLVNTLQEVKPTAFMGVPRIWEKMHEKIKEAASKSSSLRkkvfsWArnVGlkintkrmlGAHDTPMSYRMAKALVFSKVK 338
Cdd:PRK06145 229 AVLAAIERHRLTCAWMAPVMLSRVLTVPDRDRFDLDSLA-----WC--IG---------GGEKTPESRIRDFTRVFTRAR 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 339 sslgldhchiFISGaaplnqetsefflsldipigevYGLSESTGPHSM--STPENYRILSSGK--------VMTGCKNML 408
Cdd:PRK06145 293 ----------YIDA----------------------YGLTETCSGDTLmeAGREIEKIGSTGRalahveirIADGAGRWL 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 409 YQQNKegiGEVCLWGRHVFMGYLGSEDATTEAIdKEGWLHSGDLGRVDNKGFLYITGRIKEIIITaGGENVAPIPIENLV 488
Cdd:PRK06145 341 PPNMK---GEICMRGPKVTKGYWKDPEKTAEAF-YGDWFRSGDVGYLDEEGFLYLTDRKKDMIIS-GGENIASSEVERVI 415
|
330
....*....|....
gi 1811029393 489 KEkLPIISNAMLVG 502
Cdd:PRK06145 416 YE-LPEVAEAAVIG 428
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
177-486 |
2.08e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 78.88 E-value: 2.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 177 AVIIYTSGTTGHPKGAMLSHDNItwmagAAAMEcnlSLAPKKQ----EVVVSYLPLSHIAAQMMDVWIPMKVGASIY--- 249
Cdd:PRK07787 131 ALIVYTSGTTGPPKGVVLSRRAI-----AADLD---ALAEAWQwtadDVLVHGLPLFHVHGLVLGVLGPLRIGNRFVhtg 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 250 ------FAQPDALKGTLvntlqevkptaFMGVPRIWEkmhekikeaaskssslrkkvfswarnvglkintkRMLGAHDTP 323
Cdd:PRK07787 203 rptpeaYAQALSEGGTL-----------YFGVPTVWS----------------------------------RIAADPEAA 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 324 MSYRMAKALVfskvksslgldhchifiSGAAPLNQETSEFFLSLD-IPIGEVYGLSESTGPHSMSTPENYRILSSGKVMT 402
Cdd:PRK07787 238 RALRGARLLV-----------------SGSAALPVPVFDRLAALTgHRPVERYGMTETLITLSTRADGERRPGWVGLPLA 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 403 GCKNMLYQQNK-------EGIGEVCLWGRHVFMGYLGSEDATTEAIDKEGWLHSGDLGRVDNKGFLYITGRIKEIIITAG 475
Cdd:PRK07787 301 GVETRLVDEDGgpvphdgETVGELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDPDGMHRIVGRESTDLIKSG 380
|
330
....*....|.
gi 1811029393 476 GENVAPIPIEN 486
Cdd:PRK07787 381 GYRIGAGEIET 391
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
35-539 |
4.45e-15 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 78.35 E-value: 4.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 35 QYYEASRKAAKAMIKLGLEPFHSVGILGFNSVEWFIAALGAILAGGL--CVGIYAtnSADACQYAIAHSKVNILVVEnel 112
Cdd:PLN02479 50 QTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVvnCVNIRL--NAPTIAFLLEHSKSEVVMVD--- 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 113 qlQKIFSIPKN--RIQTLKAIIQYRLPV----------KETKNYDL----YSWDDFMELGN-----SIPDSQLDQIigsq 171
Cdd:PLN02479 125 --QEFFTLAEEalKILAEKKKSSFKPPLlivigdptcdPKSLQYALgkgaIEYEKFLETGDpefawKPPADEWQSI---- 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 172 kanqcaVIIYTSGTTGHPKGAMLSHDNITWMAGAAAMECNLSLAPkkqeVVVSYLPLSHIAAqmmdvWIpmkvgasiYFA 251
Cdd:PLN02479 199 ------ALGYTSGTTASPKGVVLHHRGAYLMALSNALIWGMNEGA----VYLWTLPMFHCNG-----WC--------FTW 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 252 QPDALKGTLVnTLQEVKPTAfmgvpriwekmhekikeaaskssslrkkVFSWARNVGLKintkRMLGAhdtPMSYRMaka 331
Cdd:PLN02479 256 TLAALCGTNI-CLRQVTAKA----------------------------IYSAIANYGVT----HFCAA---PVVLNT--- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 332 LVFS-KVKSSLGLDH-CHIFISGAAPlnqeTSEFFLSLDIP---IGEVYGLSESTGPHSMST--PENYRILSSGKVMTGC 404
Cdd:PLN02479 297 IVNApKSETILPLPRvVHVMTAGAAP----PPSVLFAMSEKgfrVTHTYGLSETYGPSTVCAwkPEWDSLPPEEQARLNA 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 405 KNMLYQQNKEG------------------IGEVCLWGRHVFMGYLGSEDATTEAIdKEGWLHSGDLGRVDNKGFLYITGR 466
Cdd:PLN02479 373 RQGVRYIGLEGldvvdtktmkpvpadgktMGEIVMRGNMVMKGYLKNPKANEEAF-ANGWFHSGDLGVKHPDGYIEIKDR 451
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1811029393 467 IKEIIITaGGENVAPIPIENLVKEKlPIISNAMLVGDK----AKFLSVLLTLKCEVDKTSGEPLDNltwEAIKFCRD 539
Cdd:PLN02479 452 SKDIIIS-GGENISSLEVENVVYTH-PAVLEASVVARPderwGESPCAFVTLKPGVDKSDEAALAE---DIMKFCRE 523
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
30-490 |
1.79e-14 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 76.39 E-value: 1.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 30 ILSFNQYYeasrkaaKAMIKLGLE----PFHSVGILGFNSVEWFIAALGAILAGGLCVGIYATNSADACQYAIAHSKVNI 105
Cdd:PRK06334 45 KLSYNQVR-------KAVIALATKvskyPDQHIGIMMPASAGAYIAYFATLLSGKIPVMINWSQGLREVTACANLVGVTH 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 106 LVVENELqLQKIFSIPKNRIQTLKAIIQYRLPVKEtknydlYSWDDFMELG--NSIPDSQLDQIIGSQKANQ--CAVIIY 181
Cdd:PRK06334 118 VLTSKQL-MQHLAQTHGEDAEYPFSLIYMEEVRKE------LSFWEKCRIGiyMSIPFEWLMRWFGVSDKDPedVAVILF 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 182 TSGTTGHPKGAMLSHDNItwMAGAAAmeCNLSLAPKKQEVVVSYLPLSHIAAQMMDVWIPMKVGASIYFAQPDALKGTLV 261
Cdd:PRK06334 191 TSGTEKLPKGVPLTHANL--LANQRA--CLKFFSPKEDDVMMSFLPPFHAYGFNSCTLFPLLSGVPVVFAYNPLYPKKIV 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 262 NTLQEVKPTAFMGVPRIWEKMHEKIKEAASKSSSLRKKVfswarnvglkintkrmLGAHDTPMSYRMAKALVFSKV--KS 339
Cdd:PRK06334 267 EMIDEAKVTFLGSTPVFFDYILKTAKKQESCLPSLRFVV----------------IGGDAFKDSLYQEALKTFPHIqlRQ 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 340 SLGLDHCHIFISgaapLNQETSEFFLS-LDIPIG--EVYGLSEstgphsmstpENYRILSSGKVmtgcknmlyqqnkegi 416
Cdd:PRK06334 331 GYGTTECSPVIT----INTVNSPKHEScVGMPIRgmDVLIVSE----------ETKVPVSSGET---------------- 380
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1811029393 417 GEVCLWGRHVFMGYLGsEDATTEAI--DKEGWLHSGDLGRVDNKGFLYITGRIKEiIITAGGENVAPIPIENLVKE 490
Cdd:PRK06334 381 GLVLTRGTSLFSGYLG-EDFGQGFVelGGETWYVTGDLGYVDRHGELFLKGRLSR-FVKIGAEMVSLEALESILME 454
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
25-502 |
2.90e-14 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 75.16 E-value: 2.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 25 DGKWEILSFNQYYEASRKAAKAMIKLGLEPFHSVGILGFNSVEWFIAALGAILAGGLCVGIYATNSADACQYAIAHSKVN 104
Cdd:cd05971 1 KGTPEKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 105 ILVVEnelqlqkifsipknriqtlkaiiqyrlpvketknydlyswddfmelgnsipdsqldqiigsqKANQCAVIIYTSG 184
Cdd:cd05971 81 ALVTD--------------------------------------------------------------GSDDPALIIYTSG 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 185 TTGHPKGAMLSHdnitwmagaaamecnlslapkkqEVVVSYLPLSHIAAQMMdvwiPMKvgASIYFAQPD-ALKGTLVNT 263
Cdd:cd05971 99 TTGPPKGALHAH-----------------------RVLLGHLPGVQFPFNLF----PRD--GDLYWTPADwAWIGGLLDV 149
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 264 LQevkPTAFMGVPRIWEKMHEKIKEAASKSSSlRKKVfswaRNVGLKINTKRMLGAHDTPMSYRMAKALVFSKVKSSLGl 343
Cdd:cd05971 150 LL---PSLYFGVPVLAHRMTKFDPKAALDLMS-RYGV----TTAFLPPTALKMMRQQGEQLKHAQVKLRAIATGGESLG- 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 344 dhchifisgaAPLNQETSEFFlslDIPIGEVYGLSE------------STGPHSMSTP---ENYRILSSgkvmtgcKNML 408
Cdd:cd05971 221 ----------EELLGWAREQF---GVEVNEFYGQTEcnlvigncsalfPIKPGSMGKPipgHRVAIVDD-------NGTP 280
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 409 YQQNKEGIGEVCLWGRHVFMGYLGSEDATtEAIDKEGWLHSGDLGRVDNKGFLYITGRIKEiIITAGGENVAPIPIENLV 488
Cdd:cd05971 281 LPPGEVGEIAVELPDPVAFLGYWNNPSAT-EKKMAGDWLLTGDLGRKDSDGYFWYVGRDDD-VITSSGYRIGPAEIEECL 358
|
490
....*....|....
gi 1811029393 489 KeKLPIISNAMLVG 502
Cdd:cd05971 359 L-KHPAVLMAAVVG 371
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
181-502 |
4.53e-14 |
|
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: 73.59 E-value: 4.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 181 YTSGTTGHPKGAMLSHDniTWMAgaaAMECNLSL-APKKQEVVVSYLPLSH---IAAQMMDVWIPmkvGASIYFAQPDAL 256
Cdd:cd17633 7 FTSGTTGLPKAYYRSER--SWIE---SFVCNEDLfNISGEDAILAPGPLSHslfLYGAISALYLG---GTFIGQRKFNPK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 257 KGtlVNTLQEVKPTAFMGVPRIWEkmhekikeaaskssslrkkvfswarnvglkintkrMLGAHDTPMSyrmakalvfsK 336
Cdd:cd17633 79 SW--IRKINQYNATVIYLVPTMLQ-----------------------------------ALARTLEPES----------K 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 337 VKSslgldhchiFISGAAPLNQETSEFF--LSLDIPIGEVYGLSESTGPHSMSTPENYRILSSGKVMTGCKNMLYQQNKE 414
Cdd:cd17633 112 IKS---------IFSSGQKLFESTKKKLknIFPKANLIEFYGTSELSFITYNFNQESRPPNSVGRPFPNVEIEIRNADGG 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 415 GIGEVCLWGRHVFMGYLgsedaTTEAIDKEGWLHSGDLGRVDNKGFLYITGRIKEIIITaGGENVAPIPIENLVKeKLPI 494
Cdd:cd17633 183 EIGKIFVKSEMVFSGYV-----RGGFSNPDGWMSVGDIGYVDEEGYLYLVGRESDMIII-GGINIFPTEIESVLK-AIPG 255
|
....*...
gi 1811029393 495 ISNAMLVG 502
Cdd:cd17633 256 IEEAIVVG 263
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
25-597 |
4.75e-14 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 75.08 E-value: 4.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 25 DGKWEILSfnqYYEASRKA---AKAMIKLGLEPFHSVGILGFNSVEWFIAALGAILAGGLCVGI---YATNSADacqyai 98
Cdd:PRK12582 75 HGQWRKVT---YGEAKRAVdalAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVspaYSLMSHD------ 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 99 aHSKvnilvvenelqLQKIFSIPKNRI-------QTLKAIIQYRLP----VKETKNYDLYSWDDFMELGNSIPDSQLDQI 167
Cdd:PRK12582 146 -HAK-----------LKHLFDLVKPRVvfaqsgaPFARALAALDLLdvtvVHVTGPGEGIASIAFADLAATPPTAAVAAA 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 168 IGSQKANQCAVIIYTSGTTGHPKGAMLSHdniTWMAGAAAMECNLSLAPKKQE--VVVSYLPLSHIAAQMMDVWIPMKVG 245
Cdd:PRK12582 214 IAAITPDTVAKYLFTSGSTGMPKAVINTQ---RMMCANIAMQEQLRPREPDPPppVSLDWMPWNHTMGGNANFNGLLWGG 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 246 ASIYFAQ----PDALKGTLVNtLQEVKPTAFMGVPrIWEKMhekIKEAASKSSSLRKKVFSwarNVGLkintkrmlgahd 321
Cdd:PRK12582 291 GTLYIDDgkplPGMFEETIRN-LREISPTVYGNVP-AGYAM---LAEAMEKDDALRRSFFK---NLRL------------ 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 322 tpMSYrmakalvfskvksslgldhchifisGAAPLNQETSEFFLSL-------DIPIGEVYGLSEsTGPHSMST---PEn 391
Cdd:PRK12582 351 --MAY-------------------------GGATLSDDLYERMQALavrttghRIPFYTGYGATE-TAPTTTGThwdTE- 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 392 yRILSSGKVMTGCK-NMLYQQNKEgigEVCLWGRHVFMGYLGSEDATTEAIDKEGWLHSGDLGR-VD----NKGfLYITG 465
Cdd:PRK12582 402 -RVGLIGLPLPGVElKLAPVGDKY---EVRVKGPNVTPGYHKDPELTAAAFDEEGFYRLGDAARfVDpddpEKG-LIFDG 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 466 RIKEIIITAGGE--NVAPIPIeNLVKEKLPIISNAMLVGDKAKFLSVLLtlkcevdktsgepldnltWEAIKFCRDVGSQ 543
Cdd:PRK12582 477 RVAEDFKLSTGTwvSVGTLRP-DAVAACSPVIHDAVVAGQDRAFIGLLA------------------WPNPAACRQLAGD 537
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 1811029393 544 ASTVTEIVeLQDPLVYMAIQKGINAVNQQAISNAQKIQKWVILEKDFSIGGGEL 597
Cdd:PRK12582 538 PDAAPEDV-VKHPAVLAILREGLSAHNAEAGGSSSRIARALLMTEPPSIDAGEI 590
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
152-503 |
1.04e-13 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 74.37 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 152 FMELGNSIPDSQLDQIIGSQKANQCAVIIYTSGTTGHPKGAMLSHDNITWMAGAAameCNLSLAPK-KQEVVVSYLPLSH 230
Cdd:PTZ00342 282 IILFDDMTKNKTTNYKIQNEDPDFITSIVYTSGTSGKPKGVMLSNKNLYNTVVPL---CKHSIFKKyNPKTHLSYLPISH 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 231 IAAQMMdVWIPMKVGASI--------YFAQpdalkgTLVNTLQEVkptaFMGVPRIWEKMHEKIKEAASKSSSLRKkvfs 302
Cdd:PTZ00342 359 IYERVI-AYLSFMLGGTIniwskdinYFSK------DIYNSKGNI----LAGVPKVFNRIYTNIMTEINNLPPLKR---- 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 303 waRNVGLKINTKRmlGAHDTPMSYRMAKAL-VFSKVKSSLG--LDhchIFISGAAPLNQE-TSEFFLSLDIPIGEVYGLS 378
Cdd:PTZ00342 424 --FLVKKILSLRK--SNNNGGFSKFLEGIThISSKIKDKVNpnLE---VILNGGGKLSPKiAEELSVLLNVNYYQGYGLT 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 379 ESTGPHSMSTPENYRILSSGKVMtgCKNMLYQ-------QNKEGI--GEVCLWGRHVFMGYLGSEDATTEAIDKEGWLHS 449
Cdd:PTZ00342 497 ETTGPIFVQHADDNNTESIGGPI--SPNTKYKvrtwetyKATDTLpkGELLIKSDSIFSGYFLEKEQTKNAFTEDGYFKT 574
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1811029393 450 GDLGRVDNKGFLYITGRIKEIIITAGGENVAPIPIENLVKEkLPIISNAMLVGD 503
Cdd:PTZ00342 575 GDIVQINKNGSLTFLDRSKGLVKLSQGEYIETDMLNNLYSQ-ISFINFCVVYGD 627
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
181-485 |
2.05e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 73.06 E-value: 2.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 181 YTSGTTGHPKGAMLSHDNITWMAGAAAMECNLslapKKQEVVVSYLPLSHIAAqmmdvW-IPMKVGASIyfaqpdalkGT 259
Cdd:PRK08162 189 YTSGTTGNPKGVVYHHRGAYLNALSNILAWGM----PKHPVYLWTLPMFHCNG-----WcFPWTVAARA---------GT 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 260 LVnTLQEVKPTAfmgvprIWEKMHEKikeaaskssslrkKVfswarnvglkintKRMLGAhdtPMSYRMakaLVFSKVKS 339
Cdd:PRK08162 251 NV-CLRKVDPKL------IFDLIREH-------------GV-------------THYCGA---PIVLSA---LINAPAEW 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 340 SLGLDH-CHIFISGAAPLNQ--ETSEfflSLDIPIGEVYGLSESTGP----------HSMSTPENYRIlssgKVMTGCKN 406
Cdd:PRK08162 292 RAGIDHpVHAMVAGAAPPAAviAKME---EIGFDLTHVYGLTETYGPatvcawqpewDALPLDERAQL----KARQGVRY 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 407 MLYQQ--------------NKEGIGEVCLWGRHVFMGYLGSEDATTEAIdKEGWLHSGDLGRVDNKGFLYITGRIKEIII 472
Cdd:PRK08162 365 PLQEGvtvldpdtmqpvpaDGETIGEIMFRGNIVMKGYLKNPKATEEAF-AGGWFHTGDLAVLHPDGYIKIKDRSKDIII 443
|
330
....*....|...
gi 1811029393 473 TaGGENVAPIPIE 485
Cdd:PRK08162 444 S-GGENISSIEVE 455
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
181-490 |
2.13e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 73.05 E-value: 2.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 181 YTSGTTGHPKGAMLSHDNIT-----WMAGAAAMECNlslAPKKQEVVVSYLPLSHIAAQMMDVWIPMKVGASIYFaqpda 255
Cdd:PRK05850 167 YTSGSTRTPAGVMVSHRNVIanfeqLMSDYFGDTGG---VPPPDTTVVSWLPFYHDMGLVLGVCAPILGGCPAVL----- 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 256 lkgtlvntlqeVKPTAFMGVPRIWekMHekikeAASKSSSlrkkVFSWARNVGLKINTKRmlgAHDTPMSyrmakalvfs 335
Cdd:PRK05850 239 -----------TSPVAFLQRPARW--MQ-----LLASNPH----AFSAAPNFAFELAVRK---TSDDDMA---------- 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 336 kvksslGLD--HCHIFISGAAPLNQET--------SEFFLSlDIPIGEVYGLSEST----GPHSMSTPE----NYRILSS 397
Cdd:PRK05850 284 ------GLDlgGVLGIISGSERVHPATlkrfadrfAPFNLR-ETAIRPSYGLAEATvyvaTREPGQPPEsvrfDYEKLSA 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 398 GKVM-----TGCKNMLYQ----------------QNKEG-IGEVCLWGRHVFMGYLGSEDAT-----------TEAIDKE 444
Cdd:PRK05850 357 GHAKrcetgGGTPLVSYGsprsptvrivdpdtciECPAGtVGEIWVHGDNVAAGYWQKPEETertfgatlvdpSPGTPEG 436
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1811029393 445 GWLHSGDLGRVDNkGFLYITGRIKEIIITAgGENVAPIPIENLVKE 490
Cdd:PRK05850 437 PWLRTGDLGFISE-GELFIVGRIKDLLIVD-GRNHYPDDIEATIQE 480
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
177-502 |
4.36e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 72.00 E-value: 4.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 177 AVIIYTSGTTGHPKGAMLSHDNITWMAGAAameCNLSLAPKKQEVVVSYLPLSHIAAQMMDVWIPMKVGAS-IYFAQPDA 255
Cdd:PRK06178 212 AALNYTGGTTGMPKGCEHTQRDMVYTAAAA---YAVAVVGGEDSVFLSFLPEFWIAGENFGLLFPLFSGATlVLLARWDA 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 256 LkgTLVNTLQEVKPT-AFMGVPRIWEKMhEKIKEAASKSSSLRK-KVFSWARnvglKINtkrmlgahdtPMSYRMAKALV 333
Cdd:PRK06178 289 V--AFMAAVERYRVTrTVMLVDNAVELM-DHPRFAEYDLSSLRQvRVVSFVK----KLN----------PDYRQRWRALT 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 334 FSKV-KSSLGLDHCHI---FISGaaplnQETSEF-------FLSLDIPIGEVYGLSESTGphsmstpenyRILSSGkvmt 402
Cdd:PRK06178 352 GSVLaEAAWGMTETHTcdtFTAG-----FQDDDFdllsqpvFVGLPVPGTEFKICDFETG----------ELLPLG---- 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 403 gcknmlyqqnkeGIGEVCLWGRHVFMGYLGSEDATTEAIdKEGWLHSGDLGRVDNKGFLYITGRIKEIIITAgGENVAPI 482
Cdd:PRK06178 413 ------------AEGEIVVRTPSLLKGYWNKPEATAEAL-RDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVN-GMSVFPS 478
|
330 340
....*....|....*....|
gi 1811029393 483 PIENLVKEKlPIISNAMLVG 502
Cdd:PRK06178 479 EVEALLGQH-PAVLGSAVVG 497
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
177-539 |
5.21e-13 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 71.98 E-value: 5.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 177 AVIIYTSGTTGHPKGAMLSHDNI--------TWMAGAaamecnLSLAPK-KQEVVVSYLPLSHIAAQMMDVWIPMKVGA- 246
Cdd:PRK07059 207 AFLQYTGGTTGVSKGATLLHRNIvanvlqmeAWLQPA------FEKKPRpDQLNFVCALPLYHIFALTVCGLLGMRTGGr 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 247 SIYFAQPDALKGtLVNTLQEVKPTAFMGVPRIWEKMhekikeaaskssslrkkvfswarnvglkintkrmlgahdtpMSY 326
Cdd:PRK07059 281 NILIPNPRDIPG-FIKELKKYQVHIFPAVNTLYNAL-----------------------------------------LNN 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 327 RMAKALVFSKVKSSLGldhchifisGAAPLNQETSEFFLSLD-IPIGEVYGLSEsTGPHSMSTPenyrilSSGKVMTGCK 405
Cdd:PRK07059 319 PDFDKLDFSKLIVANG---------GGMAVQRPVAERWLEMTgCPITEGYGLSE-TSPVATCNP------VDATEFSGTI 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 406 NM------LYQQNKEG-------IGEVCLWGRHVFMGYLGSEDATTEAIDKEGWLHSGDLGRVDNKGFLYITGRIKEIII 472
Cdd:PRK07059 383 GLplpsteVSIRDDDGndlplgePGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKDMIL 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 473 TAGGeNVAPIPIENLVkeklpiisnAMLVGdkakflsvllTLKCEV----DKTSGEPL--------DNLTWEAIK-FCRD 539
Cdd:PRK07059 463 VSGF-NVYPNEIEEVV---------ASHPG----------VLEVAAvgvpDEHSGEAVklfvvkkdPALTEEDVKaFCKE 522
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
375-488 |
1.02e-12 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 70.82 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 375 YGLSESTGP--------HSMSTPEN----------YRILSSGKVMTGCKNMLYQQNKEG--IGEVCLWGRHVFMGYLGSE 434
Cdd:PLN03102 331 YGLTEATGPvlfcewqdEWNRLPENqqmelkarqgVSILGLADVDVKNKETQESVPRDGktMGEIVIKGSSIMKGYLKNP 410
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1811029393 435 DATTEAIdKEGWLHSGDLGRVDNKGFLYITGRIKEIIITaGGENVAPIPIENLV 488
Cdd:PLN03102 411 KATSEAF-KHGWLNTGDVGVIHPDGHVEIKDRSKDIIIS-GGENISSVEVENVL 462
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
5-200 |
1.20e-12 |
|
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: 70.43 E-value: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 5 EFFQESVNRFGIYPALASKKdgkwEILSFNQYYEASRKAAKAMIKLGLEPFHSVGILGFNSVEWFIAALGAILAGGLCVG 84
Cdd:cd17655 1 ELFEEQAEKTPDHTAVVFED----QTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 85 IYATNSADACQYAIAHSKVNILVVENELQLQKIFSipknriqtlKAIIQyrlpvkeTKNYDLYSWDDfmelGNSIPDSQL 164
Cdd:cd17655 77 IDPDYPEERIQYILEDSGADILLTQSHLQPPIAFI---------GLIDL-------LDEDTIYHEES----ENLEPVSKS 136
|
170 180 190
....*....|....*....|....*....|....*.
gi 1811029393 165 DQIigsqkanqcAVIIYTSGTTGHPKGAMLSHDNIT 200
Cdd:cd17655 137 DDL---------AYVIYTSGSTGKPKGVMIEHRGVV 163
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
31-557 |
2.82e-12 |
|
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: 69.07 E-value: 2.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 31 LSFNQYYEASRKAAKAMIKLGLEPFHSVGILGFNSVEWFIAALGAILAGGLCVGIYATNSADACQYAIAHSKVNILVVEN 110
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 111 ELqlqkifsipknriqtlkaiiqYRLPVKETKNYdlyswddfmelgnsipdsqldqiigsqkanqcavIIYTSGTTGHPK 190
Cdd:cd05969 81 EL---------------------YERTDPEDPTL----------------------------------LHYTSGTTGTPK 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 191 GAMLSHDNIT--WMAGAaamecnLSLAPKKQEVVVSYLPLSHIAAQMMDVWIPMKVGASIYFAQPDALKGTLVNTLQEVK 268
Cdd:cd05969 106 GVLHVHDAMIfyYFTGK------YVLDLHPDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVVYEGRFDAESWYGIIERVK 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 269 PTAFMGVPriwekmhekikeaaskssslrkkvfswarnvglkINTKRMLGAHDTPMSyrmakalvfskvksSLGLDHCHI 348
Cdd:cd05969 180 VTVWYTAP----------------------------------TAIRMLMKEGDELAR--------------KYDLSSLRF 211
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 349 FISGAAPLNQETSEFFLS-LDIPIGEVYGLSEsTGPHSMStpeNY-----RILSSGKVMTGCKNMLYQQNKEGI-----G 417
Cdd:cd05969 212 IHSVGEPLNPEAIRWGMEvFGVPIHDTWWQTE-TGSIMIA---NYpcmpiKPGSMGKPLPGVKAAVVDENGNELppgtkG 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 418 EVCL---WGRhVFMGYLGSEDATTEAIdKEGWLHSGDLGRVDNKGFLYITGRIKEIIITAgGENVAPIPIENLVKEKlPI 494
Cdd:cd05969 288 ILALkpgWPS-MFRGIWNDEERYKNSF-IDGWYLTGDLAYRDEDGYFWFVGRADDIIKTS-GHRVGPFEVESALMEH-PA 363
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1811029393 495 ISNAMLVGDKAKFLSVLltLKCEVDKTSG-EPLDNLTWEAIKFCRdVGSQASTVTEIVELQDPL 557
Cdd:cd05969 364 VAEAGVIGKPDPLRGEI--IKAFISLKEGfEPSDELKEEIINFVR-QKLGAHVAPREIEFVDNL 424
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
31-485 |
1.10e-11 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 67.42 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 31 LSFNQYYEASRKAAKAMIKLGLEPFHSVGILGFNSVEWFIAALGAILAGGLCVGIYATNSADACQYAIAHSKVNILVVEN 110
Cdd:PRK12406 12 RSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAHA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 111 ELQLQKIFSIPKN----RIQTLKAIIQ-YRL-PVKETKNYDLYSWDDFMELGNSIpdsqlDQIIGSQKANqcavIIYTSG 184
Cdd:PRK12406 92 DLLHGLASALPAGvtvlSVPTPPEIAAaYRIsPALLTPPAGAIDWEGWLAQQEPY-----DGPPVPQPQS----MIYTSG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 185 TTGHPKGamLSHDNITWMAGAAAM---ECNLSLAPkkQEVVVSYLPLSHIAaqmmdvwipmkvgASIYFAQPDALKGTLV 261
Cdd:PRK12406 163 TTGHPKG--VRRAAPTPEQAAAAEqmrALIYGLKP--GIRALLTGPLYHSA-------------PNAYGLRAGRLGGVLV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 262 ntLQ-EVKPTAFMGVpriwekmhekikeaaskssslrkkvfswarnvglkINTKRMLGAHDTP-MSYRMAKalVFSKVKS 339
Cdd:PRK12406 226 --LQpRFDPEELLQL-----------------------------------IERHRITHMHMVPtMFIRLLK--LPEEVRA 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 340 SLGLDHCHIFISGAAPLNQETSEFFLSLDIP-IGEVYGLSEsTGPHSMSTPENY--RILSSGKVMTGCKNMLYQQNKE-- 414
Cdd:PRK12406 267 KYDVSSLRHVIHAAAPCPADVKRAMIEWWGPvIYEYYGSTE-SGAVTFATSEDAlsHPGTVGKAAPGAELRFVDEDGRpl 345
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1811029393 415 GIGEVclwgRHVFM--------GYLGSEDATTEaIDKEGWLHSGDLGRVDNKGFLYITGRIKEIIITaGGENVAPIPIE 485
Cdd:PRK12406 346 PQGEI----GEIYSriagnpdfTYHNKPEKRAE-IDRGGFITSGDVGYLDADGYLFLCDRKRDMVIS-GGVNIYPAEIE 418
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
32-502 |
1.16e-11 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 67.46 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 32 SFNQYYEASRKAAKAMIKLGLEPFHSVGILGFNSVEWFIAALGAILAGGLCVGIYATNSADACQYAIAHSKVNILVVENE 111
Cdd:cd05915 26 TYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLLFDPN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 112 LqlqkiFSIPKNRIQTLKAIIQYrlPVKETKnYDLYswDDFMELGNsiPDSQldqiiGSQKANQCAVII--YTSGTTGHP 189
Cdd:cd05915 106 L-----LPLVEAIRGELKTVQHF--VVMDEK-APEG--YLAYEEAL--GEEA-----DPVRVPERAACGmaYTTGTTGLP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 190 KGAMLSHDNITWMAGAAAMECNLSLAPkkQEVVVSYLPLSHIAAQMMdVWIPMKVGASIYFAQPDALKGTLVNTLQEVKP 269
Cdd:cd05915 169 KGVVYSHRALVLHSLAASLVDGTALSE--KDVVLPVVPMFHVNAWCL-PYAATLVGAKQVLPGPRLDPASLVELFDGEGV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 270 TAFMGVPRIwekmhekIKEAASKSSSLrKKVFSWARNVglkintkrMLGAHDTPMSYRMAKALVFSKVKSSLGLDHCH-- 347
Cdd:cd05915 246 TFTAGVPTV-------WLALADYLEST-GHRLKTLRRL--------VVGGSAAPRSLIARFERMGVEVRQGYGLTETSpv 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 348 ----IFISGAAPLNQETSEFFLSLDiPIGEVYGLSESTGPHSMSTPENyrilssGKVmtgcknmlyqqnkegIGEVCLWG 423
Cdd:cd05915 310 vvqnFVKSHLESLSEEEKLTLKAKT-GLPIPLVRLRVADEEGRPVPKD------GKA---------------LGEVQLKG 367
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1811029393 424 RHVFMGYLGSEDATTEAIDKEGWLHSGDLGRVDNKGFLYITGRIKEiIITAGGENVAPIPIENLVKEKlPIISNAMLVG 502
Cdd:cd05915 368 PWITGGYYGNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKD-LIKSGGEWISSVDLENALMGH-PKVKEAAVVA 444
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
172-495 |
2.13e-11 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 67.50 E-value: 2.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 172 KANQCAVIIYTSGTTGHPKGAMLSHDNItwMAGAAAMECNLSLAPKKQEVVVSYLPLSHiaaqmmDVWIPMKVGASIYFA 251
Cdd:PRK05691 164 QPDDIAFLQYTSGSTALPKGVQVSHGNL--VANEQLIRHGFGIDLNPDDVIVSWLPLYH------DMGLIGGLLQPIFSG 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 252 QPDALkgtlvntlqeVKPTAFMGVPRIWekmHEKIKEAASKSSslrkkvfswarnvglkintkrmlGAHDtpMSYRMAKA 331
Cdd:PRK05691 236 VPCVL----------MSPAYFLERPLRW---LEAISEYGGTIS-----------------------GGPD--FAYRLCSE 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 332 LVFSKVKSSLGLDHCHIFISGAAPLNQETSEFFLSLDIPIG-------EVYGLSEST-----GPHSMSTP---------- 389
Cdd:PRK05691 278 RVSESALERLDLSRWRVAYSGSEPIRQDSLERFAEKFAACGfdpdsffASYGLAEATlfvsgGRRGQGIPaleldaeala 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 390 ENYRILSSGKVMTGCKnmlYQQNKEG----------------IGEVCLWGRHVFMGYLGSEDATTEAI---DKEGWLHSG 450
Cdd:PRK05691 358 RNRAEPGTGSVLMSCG---RSQPGHAvlivdpqslevlgdnrVGEIWASGPSIAHGYWRNPEASAKTFvehDGRTWLRTG 434
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1811029393 451 DLGRVdNKGFLYITGRIKEIIITAgGENVAPIPIENLVKEKLPII 495
Cdd:PRK05691 435 DLGFL-RDGELFVTGRLKDMLIVR-GHNLYPQDIEKTVEREVEVV 477
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
29-488 |
2.55e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 66.24 E-value: 2.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 29 EILSFNQYYEASRKAAKAMIKLgLE---PFHsVGILGFNSVEWFIAALGAILAGGLCVGIYATNSADACQYAIAHSKVNI 105
Cdd:PRK07867 27 SFTSWREHIRGSAARAAALRAR-LDptrPPH-VGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDIAHADCQL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 106 LVVENelqlqkifsipkNRIQTLKAiiqyRLPVKETKNYDLYSWDDFM--ELGNSIPDSQLDqiigsqkANQCAVIIYTS 183
Cdd:PRK07867 105 VLTES------------AHAELLDG----LDPGVRVINVDSPAWADELaaHRDAEPPFRVAD-------PDDLFMLIFTS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 184 GTTGHPKGAMLSHDNItwmAGAAAMecnlsLAPK----KQEVVVSYLPLSHIAAqMMDVWIP-MKVGASIyfaqpdALKg 258
Cdd:PRK07867 162 GTSGDPKAVRCTHRKV---ASAGVM-----LAQRfglgPDDVCYVSMPLFHSNA-VMAGWAVaLAAGASI------ALR- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 259 tlvntlQEVKPTAFMgvpriwekmhekikeaasksSSLRKKVFSWARNVGlkintkrmlgahdTPMSYRMAKALVFSKVK 338
Cdd:PRK07867 226 ------RKFSASGFL--------------------PDVRRYGATYANYVG-------------KPLSYVLATPERPDDAD 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 339 SSLGLdhchIFISGAAPlnQETSEFFLSLDIPIGEVYGLSE---------STGPHSMST-PENYRILSsgkVMTG--CKN 406
Cdd:PRK07867 267 NPLRI----VYGNEGAP--GDIARFARRFGCVVVDGFGSTEggvaitrtpDTPPGALGPlPPGVAIVD---PDTGteCPP 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 407 MLYQQN-----KEGIGE-VCLWGRHVFMGYLGSEDATTEAIdKEGWLHSGDLGRVDNKGFLYITGRIKEiIITAGGENVA 480
Cdd:PRK07867 338 AEDADGrllnaDEAIGElVNTAGPGGFEGYYNDPEADAERM-RGGVYWSGDLAYRDADGYAYFAGRLGD-WMRVDGENLG 415
|
....*...
gi 1811029393 481 PIPIENLV 488
Cdd:PRK07867 416 TAPIERIL 423
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
160-467 |
2.89e-11 |
|
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: 66.01 E-value: 2.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 160 PDSQLDQIIGSQKA-------NQCAVIIYTSGTTGHPKGAMLSHDNItwMAGAAAMECNLSLAPkkQEVVVSYLPLSHIA 232
Cdd:cd05930 72 PAERLAYILEDSGAklvltdpDDLAYVIYTSGSTGKPKGVMVEHRGL--VNLLLWMQEAYPLTP--GDRVLQFTSFSFDV 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 233 AqMMDVWIPMKVGASIYFAQPDALK--GTLVNTLQEVKPTAFMGVPRIWekmhekikeaaskssslrkkvfswarnvglk 310
Cdd:cd05930 148 S-VWEIFGALLAGATLVVLPEEVRKdpEALADLLAEEGITVLHLTPSLL------------------------------- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 311 intkRMLGAHDTPMSYrmakalvfskvkSSLGldhcHIFISGAAPLNQETSEFFLSL-DIPIGEVYGLSESTGphsMST- 388
Cdd:cd05930 196 ----RLLLQELELAAL------------PSLR----LVLVGGEALPPDLVRRWRELLpGARLVNLYGPTEATV---DATy 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 389 ------PENYRILSSGKVMTGCKnmLY---QQNKE----GIGEVCLWGRHVFMGYLGSEDATTEAI-----DKEGWLH-S 449
Cdd:cd05930 253 yrvppdDEEDGRVPIGRPIPNTR--VYvldENLRPvppgVPGELYIGGAGLARGYLNRPELTAERFvpnpfGPGERMYrT 330
|
330
....*....|....*...
gi 1811029393 450 GDLGRVDNKGFLYITGRI 467
Cdd:cd05930 331 GDLVRWLPDGNLEFLGRI 348
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
38-485 |
3.12e-11 |
|
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: 65.96 E-value: 3.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 38 EASRKAAKAMIKLGLEPFHSVGILGFNSVEWFIAALGAILAGGLCVGIYatnsadacqyaiahskvnilvvenelqlqki 117
Cdd:cd05958 19 LANRIANVLVGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATM------------------------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 118 fsiPKNRIQTLKAIIQYRLPVKETKNYDLYSWDDFmelgnsipdsqldqiigsqkanqcAVIIYTSGTTGHPKGAMLSHD 197
Cdd:cd05958 68 ---PLLRPKELAYILDKARITVALCAHALTASDDI------------------------CILAFTSGTTGAPKATMHFHR 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 198 NITWMAGAAAMECnlsLAPKKQEVVVSYLPLSHIAAQMMDVWIPMKVGASIyFAQPDALKGTLVNTLQEVKPTAFMGVPR 277
Cdd:cd05958 121 DPLASADRYAVNV---LRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASG-VLLEEATPDLLLSAIARYKPTVLFTAPT 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 278 IWEKMHEKIKEAASKSSSLRKKVFSwarnvglkintkrmlGAHDTPMSYRMAKALVFSKVKSSLG-LDHCHIFISgaapl 356
Cdd:cd05958 197 AYRAMLAHPDAAGPDLSSLRKCVSA---------------GEALPAALHRAWKEATGIPIIDGIGsTEMFHIFIS----- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 357 nqetsefflsldipigevyglsestgphsmSTPENYRILSSGKVMTGCKNMLYqqNKEG-------IGEVCLWGRhvfMG 429
Cdd:cd05958 257 ------------------------------ARPGDARPGATGKPVPGYEAKVV--DDEGnpvpdgtIGRLAVRGP---TG 301
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1811029393 430 YLGSEDATTEAIDKEGWLHSGDLGRVDNKGFLYITGRIKEIIITaGGENVAPIPIE 485
Cdd:cd05958 302 CRYLADKRQRTYVQGGWNITGDTYSRDPDGYFRHQGRSDDMIVS-GGYNIAPPEVE 356
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
32-502 |
7.13e-11 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 65.16 E-value: 7.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 32 SFNQYYEASRKAAKAMIKLGLEPFHSVGILGFNSVEWFIAALGAILAGGLCVGIYATNSADACQYAIAHSKVNILVVEne 111
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVITD-- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 112 LQLQKIFSIPKNRIQTLKAIIQY--RLPVKETKNYDLYSWDDFMElgnsipDSQLDQIIGSQKANQCAVIIYTSGTTGHP 189
Cdd:PRK06018 119 LTFVPILEKIADKLPSVERYVVLtdAAHMPQTTLKNAVAYEEWIA------EADGDFAWKTFDENTAAGMCYTSGTTGDP 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 190 KGAMLSHDN------ITWMAGAAAMECnlslapkkQEVVVSYLPLSH-------IAAQMMDVWIPM---KV-GASIYfaq 252
Cdd:PRK06018 193 KGVLYSHRSnvlhalMANNGDALGTSA--------ADTMLPVVPLFHanswgiaFSAPSMGTKLVMpgaKLdGASVY--- 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 253 pdalkgTLVNTlQEVKPTAfmGVPRIWEKMHEKIKEAASKSSSLRKKVfswarnvglkintkrmLGAHDTPMSyrMAKAL 332
Cdd:PRK06018 262 ------ELLDT-EKVTFTA--GVPTVWLMLLQYMEKEGLKLPHLKMVV----------------CGGSAMPRS--MIKAF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 333 V--FSKVKSSLGLdhchifisgaaplnQETSefflsldiPIGEVYGLSestgPHSMSTPENYRI---LSSG--------K 399
Cdd:PRK06018 315 EdmGVEVRHAWGM--------------TEMS--------PLGTLAALK----PPFSKLPGDARLdvlQKQGyppfgvemK 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 400 VMTGCKNMLYQQNKeGIGEVCLWGRHVFMGYLGSEDattEAIDKEGWLHSGDLGRVDNKGFLYITGRIKEiIITAGGENV 479
Cdd:PRK06018 369 ITDDAGKELPWDGK-TFGRLKVRGPAVAAAYYRVDG---EILDDDGFFDTGDVATIDAYGYMRITDRSKD-VIKSGGEWI 443
|
490 500
....*....|....*....|...
gi 1811029393 480 APIPIENLVKEKlPIISNAMLVG 502
Cdd:PRK06018 444 SSIDLENLAVGH-PKVAEAAVIG 465
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
416-502 |
1.12e-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: 64.40 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 416 IGEVCLWGRHVFMGYLGSEDATTEAIDKEGWLHSGDLGRVDNKGFLYITGRIKEIIITaGGENVAPIPIENLVKEkLPII 495
Cdd:COG1021 380 VGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRAKDQINR-GGEKIAAEEVENLLLA-HPAV 457
|
....*..
gi 1811029393 496 SNAMLVG 502
Cdd:COG1021 458 HDAAVVA 464
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
177-490 |
1.12e-10 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 64.99 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 177 AVIIYTSGTTGHPKGAMLSHDNItwMAGAAAMECNLSLAPkkQEVVVSYLPLSH---IAAQMMdvwIPMKVGASIYFaQP 253
Cdd:PRK06814 796 AVILFTSGSEGTPKGVVLSHRNL--LANRAQVAARIDFSP--EDKVFNALPVFHsfgLTGGLV---LPLLSGVKVFL-YP 867
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 254 DALKgtlvntlqevkptafmgvPRIwekmhekIKEAAskssslrkkvfsWARNVGLKINTKRMLgahdtpMSY-RMAKAL 332
Cdd:PRK06814 868 SPLH------------------YRI-------IPELI------------YDTNATILFGTDTFL------NGYaRYAHPY 904
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 333 VFSKVKsslgldhcHIFiSGAAPLNQETSEFFLS-LDIPIGEVYGLSEsTGP-HSMSTPENYRILSSGKVMTGcknMLYQ 410
Cdd:PRK06814 905 DFRSLR--------YVF-AGAEKVKEETRQTWMEkFGIRILEGYGVTE-TAPvIALNTPMHNKAGTVGRLLPG---IEYR 971
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 411 QNK-EGI---GEVCLWGRHVFMGYLGSEDATTEAIDKEGWLHSGDLGRVDNKGFLYITGRIK---EIiitaGGENVAPIP 483
Cdd:PRK06814 972 LEPvPGIdegGRLFVRGPNVMLGYLRAENPGVLEPPADGWYDTGDIVTIDEEGFITIKGRAKrfaKI----AGEMISLAA 1047
|
....*..
gi 1811029393 484 IENLVKE 490
Cdd:PRK06814 1048 VEELAAE 1054
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
58-467 |
1.26e-10 |
|
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: 63.82 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 58 VGILGFNSVEWFIAALGAILAGGLCVGIYATNSADACQYAIAHSKVNILVVENELQLQKIFsipknriQTLKAIiqyrlp 137
Cdd:TIGR01733 28 VAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDSALASRLAG-------LVLPVI------ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 138 vketknydLYSWDDFMELGNSIPDSQLDqiiGSQKANQCAVIIYTSGTTGHPKGAMLSHDNI----TWMAGAaamecnls 213
Cdd:TIGR01733 95 --------LLDPLELAALDDAPAPPPPD---APSGPDDLAYVIYTSGSTGRPKGVVVTHRSLvnllAWLARR-------- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 214 LAPKKQEVVVSYLPLSHIAAqMMDVWIPMKVGASIYFAQPDALKGTLVNT---LQEVKPTAFMGVPRIWEKMHEkikEAA 290
Cdd:TIGR01733 156 YGLDPDDRVLQFASLSFDAS-VEEIFGALLAGATLVVPPEDEERDDAALLaalIAEHPVTVLNLTPSLLALLAA---ALP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 291 SKSSSLRKKVFS-----------WARNVGLK--INTkrmlgahdtpmsYRMAKALVFSkvksslgldHCHIFISGAAPLN 357
Cdd:TIGR01733 232 PALASLRLVILGgealtpalvdrWRARGPGArlINL------------YGPTETTVWS---------TATLVDPDDAPRE 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 358 qetsefflsLDIPIG------EVYGLSESTGPhsmstpenyrilssgkVMTGCknmlyqqnkegIGEVCLWGRHVFMGYL 431
Cdd:TIGR01733 291 ---------SPVPIGrplantRLYVLDDDLRP----------------VPVGV-----------VGELYIGGPGVARGYL 334
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1811029393 432 GSEDATTEAI--------DKEGWLHSGDLGRVDNKGFLYITGRI 467
Cdd:TIGR01733 335 NRPELTAERFvpdpfaggDGARLYRTGDLVRYLPDGNLEFLGRI 378
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
41-502 |
2.41e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 63.22 E-value: 2.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 41 RKAAKAMIKLGLEPFHSVGILGFNSVEWFIAALGAILAGGLCVGIYATNSADACQYAIAHSKVNILVVENELQLQKIFSI 120
Cdd:PRK06164 46 DRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARWLVVWPGFKGIDFAAI 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 121 ----PKNRIQTLKAIIQYRLPVKETKNYDLYSWDDFMELgnsiPDSQLDQIIGSQKA--NQCAVIIYTSGTTGHPKGAMl 194
Cdd:PRK06164 126 laavPPDALPPLRAIAVVDDAADATPAPAPGARVQLFAL----PDPAPPAAAGERAAdpDAGALLFTTSGTTSGPKLVL- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 195 sHDNITWMAGAAAMECNLSLAPkkQEVVVSYLPLShiaaqmmdvwipmkvGASIYfaqpdalkGTLVNTLQEvkptafmG 274
Cdd:PRK06164 201 -HRQATLLRHARAIARAYGYDP--GAVLLAALPFC---------------GVFGF--------STLLGALAG-------G 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 275 VPRIWEKMHEKIKEAASKSSSLRKKVFswARNVGLKintkRMLGAHDTPMSYRMAKALVFSKvksslgldhchiFISGAA 354
Cdd:PRK06164 248 APLVCEPVFDAARTARALRRHRVTHTF--GNDEMLR----RILDTAGERADFPSARLFGFAS------------FAPALG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 355 PLNQETseffLSLDIPIGEVYGLSE-----STGPhsMSTPENYRILSSGKVMTGCKNMLYQQNKEG-------IGEVCLW 422
Cdd:PRK06164 310 ELAALA----RARGVPLTGLYGSSEvqalvALQP--ATDPVSVRIEGGGRPASPEARVRARDPQDGallpdgeSGEIEIR 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 423 GRHVFMGYLGSEDATTEAIDKEGWLHSGDLGR-VDNKGFLYITgRIKEiIITAGGENVAPIPIENLVKEkLPIISNAMLV 501
Cdd:PRK06164 384 APSLMRGYLDNPDATARALTDDGYFRTGDLGYtRGDGQFVYQT-RMGD-SLRLGGFLVNPAEIEHALEA-LPGVAAAQVV 460
|
.
gi 1811029393 502 G 502
Cdd:PRK06164 461 G 461
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
373-502 |
3.22e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 62.87 E-value: 3.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 373 EVYGLSESTGPHSMSTPENYRILSSgkVMTGCKNMLYQQNKEGiGEVCLWGR----HV-----FMGYLGsEDATTEAIDK 443
Cdd:PRK07638 284 EFYGASELSFVTALVDEESERRPNS--VGRPFHNVQVRICNEA-GEEVQKGEigtvYVkspqfFMGYII-GGVLARELNA 359
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1811029393 444 EGWLHSGDLGRVDNKGFLYITGRIKEIIITaGGENVAPIPIENLVKEkLPIISNAMLVG 502
Cdd:PRK07638 360 DGWMTVRDVGYEDEEGFIYIVGREKNMILF-GGINIFPEEIESVLHE-HPAVDEIVVIG 416
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
18-487 |
4.95e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 62.40 E-value: 4.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 18 PALASKKDGkwEILSFNQYYEASRKAAKAMIKLGLEPFHSVGILGFNSVEwFIAALGAILAGGL---CVGIYATnsADAC 94
Cdd:PRK13391 14 PAVIMASTG--EVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLR-YLEVCWAAERSGLyytCVNSHLT--PAEA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 95 QYAIAHSKVNILVVenelqlqkifSIPKNRI--QTLKAIIQYRLPVKETKNYDLYSWDDFMELGNSIPDSQL-DQIIGsq 171
Cdd:PRK13391 89 AYIVDDSGARALIT----------SAAKLDVarALLKQCPGVRHRLVLDGDGELEGFVGYAEAVAGLPATPIaDESLG-- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 172 kanqcAVIIYTSGTTGHPKG--AMLSHDNITWMAGAAAMeCNLSLAPKKQEVVVSYLPLSHIAAQMMdvwipmkVGASIy 249
Cdd:PRK13391 157 -----TDMLYSSGTTGRPKGikRPLPEQPPDTPLPLTAF-LQRLWGFRSDMVYLSPAPLYHSAPQRA-------VMLVI- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 250 faqpdALKGTLVnTLQEVKPTAFMgvpriwekmhEKIKEAASKSSSLRKKVFSwarnvglkintkRMLgahDTPMSYRMA 329
Cdd:PRK13391 223 -----RLGGTVI-VMEHFDAEQYL----------ALIEEYGVTHTQLVPTMFS------------RML---KLPEEVRDK 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 330 KALvfskvkSSLgldhcHIFISGAAPLNQETSEFFLSLDIP-IGEVYGLSESTGPHSMSTPENY-RILSSGKVMTGCKNM 407
Cdd:PRK13391 272 YDL------SSL-----EVAIHAAAPCPPQVKEQMIDWWGPiIHEYYAATEGLGFTACDSEEWLaHPGTVGRAMFGDLHI 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 408 LYQQNKE----GIGEVCLWGRHVFMgYLGSEDATTEAIDKEG-WLHSGDLGRVDNKGFLYITGRIKEIIITaGGENVAPI 482
Cdd:PRK13391 341 LDDDGAElppgEPGTIWFEGGRPFE-YLNDPAKTAEARHPDGtWSTVGDIGYVDEDGYLYLTDRAAFMIIS-GGVNIYPQ 418
|
....*
gi 1811029393 483 PIENL 487
Cdd:PRK13391 419 EAENL 423
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
29-200 |
7.49e-10 |
|
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: 61.72 E-value: 7.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 29 EILSFNQYYEASRKAAKAMIKLGLEPFHSVGILGFNSVEWFIAALGAILAGGLCVGIYATNSADACQYAIAHSKVNILVV 108
Cdd:cd17656 12 QKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRVVLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 109 ENELqlqkifsipknriqtlkaiiqyRLPVKETKNYDLYSWDDFMELGNSipdsqldQIIGSQKANQCAVIIYTSGTTGH 188
Cdd:cd17656 92 QRHL----------------------KSKLSFNKSTILLEDPSISQEDTS-------NIDYINNSDDLLYIIYTSGTTGK 142
|
170
....*....|..
gi 1811029393 189 PKGAMLSHDNIT 200
Cdd:cd17656 143 PKGVQLEHKNMV 154
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
415-507 |
7.80e-10 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 61.56 E-value: 7.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 415 GIGEVCLWGRHVFMGYLGSEDaTTEAIDKEGWLHSGDLGRVDNkGFLYITGRIKEIIITaGGENVAPIPIENLVkEKLPI 494
Cdd:PRK09192 410 VVGHICVRGPSLMSGYFRDEE-SQDVLAADGWLDTGDLGYLLD-GYLYITGRAKDLIII-NGRNIWPQDIEWIA-EQEPE 485
|
90
....*....|...
gi 1811029393 495 ISNamlvGDKAKF 507
Cdd:PRK09192 486 LRS----GDAAAF 494
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
178-502 |
9.99e-10 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 60.39 E-value: 9.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 178 VIIYTSGTTGHPKGAMLSHDNITWMAGAAAMECNLSLAPkkqeVVVSYLPLSHIAAQMMDVWIPMKVGASIYFAQPDALK 257
Cdd:cd17636 4 LAIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGT----VFLNSGPLFHIGTLMFTLATFHAGGTNVFVRRVDAEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 258 gtLVNTLQEVKPTAFMGVPRIWEKMHEKIKEAASKSSSLRKKVFSWARNVglkintkrMLGAHDTPMSYRMA---KALVF 334
Cdd:cd17636 80 --VLELIEAERCTHAFLLPPTIDQIVELNADGLYDLSSLRSSPAAPEWND--------MATVDTSPWGRKPGgygQTEVM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 335 SKVkSSLGLDHCHIFISG-AAPLNQ-----ETSEfflslDIPIGEVyglsestgphsmstpenyrilssgkvmtgcknml 408
Cdd:cd17636 150 GLA-TFAALGGGAIGGAGrPSPLVQvrildEDGR-----EVPDGEV---------------------------------- 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 409 yqqnkegiGEVCLWGRHVFMGYLGSEDATTEAIdKEGWLHSGDLGRVDNKGFLYITGRiKEIIITAGGENVAPIPIENLV 488
Cdd:cd17636 190 --------GEIVARGPTVMAGYWNRPEVNARRT-RGGWHHTNDLGRREPDGSLSFVGP-KTRMIKSGAENIYPAEVERCL 259
|
330
....*....|....
gi 1811029393 489 KEkLPIISNAMLVG 502
Cdd:cd17636 260 RQ-HPAVADAAVIG 272
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
7-253 |
1.01e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 61.90 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 7 FQESVNRFGIYPALASKKdgkwEILSFNQYYEASRKAAKAMIKLGLEPFHSVGILGFNSVEWFIAALGAILAGGLCVGIY 86
Cdd:PRK12316 517 FEEQVERTPEAPALAFGE----ETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLD 592
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 87 ATNSADACQYAIAHSKVNILVVENELqlqkifsipknriqtlkaiiQYRLPV-KETKNYDL---YSWDDFMELGNsiPDS 162
Cdd:PRK12316 593 PEYPAERLAYMLEDSGVQLLLSQSHL--------------------GRKLPLaAGVQVLDLdrpAAWLEGYSEEN--PGT 650
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 163 QLDqiigsqkANQCAVIIYTSGTTGHPKGAMLSHDN----ITWMAGAAAMECNLSLApkkQEVVVSYlPLSHiaaqmMDV 238
Cdd:PRK12316 651 ELN-------PENLAYVIYTSGSTGKPKGAGNRHRAlsnrLCWMQQAYGLGVGDTVL---QKTPFSF-DVSV-----WEF 714
|
250
....*....|....*
gi 1811029393 239 WIPMKVGASIYFAQP 253
Cdd:PRK12316 715 FWPLMSGARLVVAAP 729
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
1-591 |
1.14e-09 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 61.31 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 1 MTIPEFFQESVNRFGIYPALASkkDGKWeiLSFNQYYEASRKAAKAMIKLGLEPFHSVGILGFNSVEWFIAALGAILAGG 80
Cdd:PRK06155 21 RTLPAMLARQAERYPDRPLLVF--GGTR--WTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 81 LCVGIYATNSADACQYAIAHSKVNILVVENELqlqkifsipknrIQTLKAIIQYRLPVKETKNYDLYSWDDFMELGNSIP 160
Cdd:PRK06155 97 IAVPINTALRGPQLEHILRNSGARLLVVEAAL------------LAALEAADPGDLPLPAVWLLDAPASVSVPAGWSTAP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 161 DSQLDQII--GSQKANQCAVIIYTSGTTGHPKGAMLSHDNITWMA--GAAAMECnlslapKKQEVVVSYLPLSHIAAQMM 236
Cdd:PRK06155 165 LPPLDAPApaAAVQPGDTAAILYTSGTTGPSKGVCCPHAQFYWWGrnSAEDLEI------GADDVLYTTLPLFHTNALNA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 237 dvwipmkvgasiyFAQPDALKGTLVNTlqevkptafmgvPRIwekmhekikeAASKssslrkkvFsWARNVGLKINTKRM 316
Cdd:PRK06155 239 -------------FFQALLAGATYVLE------------PRF----------SASG--------F-WPAVRRHGATVTYL 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 317 LGAhdtpmsyrMAKALVfSKVKSSLGLDH-CHIFISGAAPlNQETSEFFLSLDIPIGEVYGLSESTGPHSMSTPENyRIL 395
Cdd:PRK06155 275 LGA--------MVSILL-SQPARESDRAHrVRVALGPGVP-AALHAAFRERFGVDLLDGYGSTETNFVIAVTHGSQ-RPG 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 396 SSGKVMTGCKNMLYQQNKEGI-----GEVCLWGR--HVFM-GYLGSEDATTEAIdKEGWLHSGDLGRVDNKGFLYITGRI 467
Cdd:PRK06155 344 SMGRLAPGFEARVVDEHDQELpdgepGELLLRADepFAFAtGYFGMPEKTVEAW-RNLWFHTGDRVVRDADGWFRFVDRI 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 468 KEiIITAGGENVAPIPIENLVKEKLPIISNAM------LVGDKAKflsVLLTLKcevDKTSGEPLDnltweAIKFCrdvg 541
Cdd:PRK06155 423 KD-AIRRRGENISSFEVEQVLLSHPAVAAAAVfpvpseLGEDEVM---AAVVLR---DGTALEPVA-----LVRHC---- 486
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 1811029393 542 sqastvteivelQDPLVYMAIQKGINAVNQQAISNAQKIQKWVILEKDFS 591
Cdd:PRK06155 487 ------------EPRLAYFAVPRYVEFVAALPKTENGKVQKFVLREQGVT 524
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
31-519 |
1.68e-09 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 60.40 E-value: 1.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 31 LSFNQYYEASRKAAKAMIKLGLEPFHSVGILGFNSVEWFIAALGAILAGGLCVGIYATNSADACQYAIAHSKVNILVVEN 110
Cdd:PRK13383 61 LSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAALRAHHISTVVADN 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 111 ELQLQkifsipknriqtlkaiiqyrlpvketknydLYSWDDFMELGNSIPDSQLDQIIGSQKANQCAVIIYTSGTTGHPK 190
Cdd:PRK13383 141 EFAER------------------------------IAGADDAVAVIDPATAGAEESGGRPAVAAPGRIVLLTSGTTGKPK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 191 GAmlshdnitwmagaaamecnlslaPKKQEVvvsylplshiaAQMMDVWIP------MKVGASIYFAQP--DALK-GTLV 261
Cdd:PRK13383 191 GV-----------------------PRAPQL-----------RSAVGVWVTildrtrLRTGSRISVAMPmfHGLGlGMLM 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 262 NTLqevkptAFMGVprIWEKMHEKIKEAASKSSSLRKKVFSwarnvGLKINTKRMLgahDTPmsyrmakalvfSKVKSSL 341
Cdd:PRK13383 237 LTI------ALGGT--VLTHRHFDAEAALAQASLHRADAFT-----AVPVVLARIL---ELP-----------PRVRARN 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 342 GLDHCHIFISGAAPLNQETSEFFLSL--DIpIGEVYGLSEsTGPHSMSTPENYRIL--SSGKVMTGCKNMLYQQNKEGIG 417
Cdd:PRK13383 290 PLPQLRVVMSSGDRLDPTLGQRFMDTygDI-LYNGYGSTE-VGIGALATPADLRDApeTVGKPVAGCPVRILDRNNRPVG 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 418 EVcLWGRhVFMGYLGSEDATTEAIDK---EGWLHSGDLGRVDNKGFLYITGRIKEIIITaGGENVAPIPIENLVKEKLPI 494
Cdd:PRK13383 368 PR-VTGR-IFVGGELAGTRYTDGGGKavvDGMTSTGDMGYLDNAGRLFIVGREDDMIIS-GGENVYPRAVENALAAHPAV 444
|
490 500 510
....*....|....*....|....*....|..
gi 1811029393 495 ISNAML-VGDK------AKFlsVLLTLKCEVD 519
Cdd:PRK13383 445 ADNAVIgVPDErfghrlAAF--VVLHPGSGVD 474
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
44-297 |
2.09e-09 |
|
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: 60.64 E-value: 2.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 44 AKAMIKLGLEPFHSVGILGFNSVEWFIAALGAILAGGLCVGIYATNSADACQYAIAHSKVNILVVENELQLqkifsipkn 123
Cdd:COG1020 515 AHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYMLEDAGARLVLTQSALAA--------- 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 124 riqtlkaiiqyRLPVKETKNYDLyswdDFMELGNSiPDSQLDQIIGSQkanQCAVIIYTSGTTGHPKGAMLSHDNITWMa 203
Cdd:COG1020 586 -----------RLPELGVPVLAL----DALALAAE-PATNPPVPVTPD---DLAYVIYTSGSTGRPKGVMVEHRALVNL- 645
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 204 gAAAMECNLSLAPkkQEVVVSYLPLSHIAAqMMDVWIPMKVGASIYFAQPDALKGT--LVNTLQEVKPTAFMGVPRIWEK 281
Cdd:COG1020 646 -LAWMQRRYGLGP--GDRVLQFASLSFDAS-VWEIFGALLSGATLVLAPPEARRDPaaLAELLARHRVTVLNLTPSLLRA 721
|
250
....*....|....*.
gi 1811029393 282 MhekIKEAASKSSSLR 297
Cdd:COG1020 722 L---LDAAPEALPSLR 734
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
416-502 |
3.01e-09 |
|
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: 59.65 E-value: 3.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 416 IGEVCLWGRHVFMGYLGSEDATTEAIDKEGWLHSGDLGRVDNKGFLYITGRIKEiIITAGGENVAPIPIENLVKEkLPII 495
Cdd:cd05920 335 EGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKD-QINRGGEKIAAEEVENLLLR-HPAV 412
|
....*..
gi 1811029393 496 SNAMLVG 502
Cdd:cd05920 413 HDAAVVA 419
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
348-488 |
3.77e-09 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 59.24 E-value: 3.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 348 IFISGAAPLNQ--ETSEFflsLDIPIGEVYGLSESTGPHSMSTPENYRI--LSSGKVMTGCKNMLYQQNkegIGEVCLWG 423
Cdd:PRK07445 235 ILLGGAPAWPSllEQARQ---LQLRLAPTYGMTETASQIATLKPDDFLAgnNSSGQVLPHAQITIPANQ---TGNITIQA 308
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1811029393 424 RHVFMGYLgsedatTEAIDKEGWLHSGDLGRVDNKGFLYITGRIKEIIITaGGENVAPIPIENLV 488
Cdd:PRK07445 309 QSLALGYY------PQILDSQGIFETDDLGYLDAQGYLHILGRNSQKIIT-GGENVYPAEVEAAI 366
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
154-502 |
4.40e-09 |
|
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: 59.01 E-value: 4.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 154 ELGNSIPDSQLDQIIGSQKANQCAVIIYTSGTTGHPKGAMLSHDniTWMAGAAAMECNLSLAPKKQEVVvSYLPLSHIAA 233
Cdd:cd05910 65 NLKQCLQEAEPDAFIGIPKADEPAAILFTSGSTGTPKGVVYRHG--TFAAQIDALRQLYGIRPGEVDLA-TFPLFALFGP 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 234 QM-MDVWIPmkvgaSIYFAQP-DALKGTLVNTLQEVKPTAFMGVPRIWEKMHEKIKEAASKSSSLRKkvfswarnvglki 311
Cdd:cd05910 142 ALgLTSVIP-----DMDPTRPaRADPQKLVGAIRQYGVSIVFGSPALLERVARYCAQHGITLPSLRR------------- 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 312 ntkrmlgahdtpmsyrmakalvfskvksslgldhchiFISGAAPLNQETSEFF---LSLDIPIGEVYGLSE-----STGP 383
Cdd:cd05910 204 -------------------------------------VLSAGAPVPIALAARLrkmLSDEAEILTPYGATEalpvsSIGS 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 384 HSMST-----PENYRILSSGKVMTGCKNML----------YQQNKE----GIGEVCLWGRHVFMGYLGSEDATTEA-IDK 443
Cdd:cd05910 247 RELLAtttaaTSGGAGTCVGRPIPGVRVRIieiddepiaeWDDTLElprgEIGEITVTGPTVTPTYVNRPVATALAkIDD 326
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1811029393 444 EG---WLHSGDLGRVDNKGFLYITGRIKEIIITAGGeNVAPIPIENlVKEKLPIISNAMLVG 502
Cdd:cd05910 327 NSegfWHRMGDLGYLDDEGRLWFCGRKAHRVITTGG-TLYTEPVER-VFNTHPGVRRSALVG 386
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
437-502 |
4.73e-09 |
|
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: 58.93 E-value: 4.73e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1811029393 437 TTEAIDKEGWLHSGDLGRVDNKGFLYITGRiKEIIITAGGENVAPIPIENLVKEKlPIISNAMLVG 502
Cdd:cd05929 342 TAAARNEGGWSTLGDVGYLDEDGYLYLTDR-RSDMIISGGVNIYPQEIENALIAH-PKVLDAAVVG 405
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
18-207 |
8.47e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 59.02 E-value: 8.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 18 PALASKKdgkwEILSFNQYYEASRKAAKAMIKLGLEPFHSVGILGFNSVEWFIAALGAILAGGLCVGIYATNSADACQYA 97
Cdd:PRK12467 529 PALVFGE----QVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYM 604
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 98 IAHSKVNILVVENELQLQkifsipknriqtlkaiiqyrLPVKetknydlyswDDFMELGNSIPDSQLDQIIG-----SQK 172
Cdd:PRK12467 605 LDDSGVRLLLTQSHLLAQ--------------------LPVP----------AGLRSLCLDEPADLLCGYSGhnpevALD 654
|
170 180 190
....*....|....*....|....*....|....*
gi 1811029393 173 ANQCAVIIYTSGTTGHPKGAMLSHDNITWMAGAAA 207
Cdd:PRK12467 655 PDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIA 689
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
31-279 |
9.12e-09 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 58.07 E-value: 9.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 31 LSFNQYYEASRKAAKAMIKLGLEPFHSVGILGFNSVEWFIAALGAILAGGLCVGIYATNSADACQYAIAHSKVNILVVEN 110
Cdd:cd12116 13 LSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALVLTDD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 111 ELQlqkifsipknriqtlkaiiqyrlpvketknyDLYSWD-DFMELGNSIPDSQLDQIIGSQKANQCAVIIYTSGTTGHP 189
Cdd:cd12116 93 ALP-------------------------------DRLPAGlPVLLLALAAAAAAPAAPRTPVSPDDLAYVIYTSGSTGRP 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 190 KGAMLSHDNITwmAGAAAMECNLSLAPKKQEVVVSyLPLSHIAAqmMDVWIPMKVGASIYFAQPDALK--GTLVNTLQEV 267
Cdd:cd12116 142 KGVVVSHRNLV--NFLHSMRERLGLGPGDRLLAVT-TYAFDISL--LELLLPLLAGARVVIAPRETQRdpEALARLIEAH 216
|
250
....*....|..
gi 1811029393 268 KPTAFMGVPRIW 279
Cdd:cd12116 217 SITVMQATPATW 228
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
18-538 |
9.43e-09 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 58.10 E-value: 9.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 18 PALASKKDGkwEILSFNQYYEASRKAAKAMIKLGLEPFHSVGILGFNSVEWFIAALGAILAGGLCVGIYATNSADACQYA 97
Cdd:PRK13390 14 PAVIVAETG--EQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 98 IAHSKVNILVVENELQlqkifsipknriqTLKAIIQYRLPVKETKNYDLYSWDDFmelgnsipDSQLDQIiGSQKANQ-C 176
Cdd:PRK13390 92 VGDSGARVLVASAALD-------------GLAAKVGADLPLRLSFGGEIDGFGSF--------EAALAGA-GPRLTEQpC 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 177 -AVIIYTSGTTGHPKGAM---------LSHDNITWMAGAAamecnlsLAPKKQEVVVSYLPLSHIAAQMmdvWIPM--KV 244
Cdd:PRK13390 150 gAVMLYSSGTTGFPKGIQpdlpgrdvdAPGDPIVAIARAF-------YDISESDIYYSSAPIYHAAPLR---WCSMvhAL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 245 GASIYFAQPDALKGTLvNTLQEVKPTAFMGVPRIWEKMhekikeaaskssslrkkvfswarnvgLKINtkrmlgahdtpm 324
Cdd:PRK13390 220 GGTVVLAKRFDAQATL-GHVERYRITVTQMVPTMFVRL--------------------------LKLD------------ 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 325 syrmakalvfSKVKSSLGLDHCHIFISGAAPLNQETSEFFLSLDIPIgeVYGLSESTGPHSMSTPENYRILS-SGKVMTG 403
Cdd:PRK13390 261 ----------ADVRTRYDVSSLRAVIHAAAPCPVDVKHAMIDWLGPI--VYEYYSSTEAHGMTFIDSPDWLAhPGSVGRS 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 404 CKNMLYQQNKEG-------IGEVCLWGRHVFMGYLGSEDATTEAIDKEG--WLHSGDLGRVDNKGFLYITGRiKEIIITA 474
Cdd:PRK13390 329 VLGDLHICDDDGnelpagrIGTVYFERDRLPFRYLNDPEKTAAAQHPAHpfWTTVGDLGSVDEDGYLYLADR-KSFMIIS 407
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1811029393 475 GGENVAPIPIENLVKEKlPIISNAMLVGDKAKFLSVllTLKCEVDKTSG-EPLDNLTWEAIKFCR 538
Cdd:PRK13390 408 GGVNIYPQETENALTMH-PAVHDVAVIGVPDPEMGE--QVKAVIQLVEGiRGSDELARELIDYTR 469
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
25-467 |
9.53e-09 |
|
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: 58.09 E-value: 9.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 25 DGKWEILSFNQYYEASRKAAKAMIKLGLEPFHSVGILGFNSVEWFIAALGAILAGglcvgiyatnsadaCQYaiahskvn 104
Cdd:cd17653 17 ESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAG--------------AAY-------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 105 iLVVENELqlqkifsiPKNRIQTLkaiiqyrlpvketknydlyswddfmeLGNSipDSQLdqIIGSQKANQCAVIIYTSG 184
Cdd:cd17653 75 -VPLDAKL--------PSARIQAI--------------------------LRTS--GATL--LLTTDSPDDLAYIIFTSG 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 185 TTGHPKGAMLSHDNITwmAGAAAMECNLSLAPKKQevvvsylplshiAAQMM----DVWIPMKV-----GASIYFAQPDA 255
Cdd:cd17653 116 STGIPKGVMVPHRGVL--NYVSQPPARLDVGPGSR------------VAQVLsiafDACIGEIFstlcnGGTLVLADPSD 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 256 lkgTLVNTLQEVkpTAFMGVPRIWekmhekikeaasksSSLRKKVFSwarnvglkiNTKRmlgahdtpmsyrmakalvfs 335
Cdd:cd17653 182 ---PFAHVARTV--DALMSTPSIL--------------STLSPQDFP---------NLKT-------------------- 213
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 336 kvksslgldhchIFISGAAP---LNQETSEfflslDIPIGEVYGLSESTGPHSMS--TPENYRILssGKVMTGCKNMLYQ 410
Cdd:cd17653 214 ------------IFLGGEAVppsLLDRWSP-----GRRLYNAYGPTECTISSTMTelLPGQPVTI--GKPIPNSTCYILD 274
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1811029393 411 QNKE-----GIGEVCLWGRHVFMGYLGSEDATTEAI----DKEGWLH--SGDLGRVDNKGFLYITGRI 467
Cdd:cd17653 275 ADLQpvpegVVGEICISGVQVARGYLGNPALTASKFvpdpFWPGSRMyrTGDYGRWTEDGGLEFLGRE 342
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
30-521 |
1.00e-08 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 58.23 E-value: 1.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 30 ILSFNQYYEASRKAAKAMIKLGLEPFHSVGILGFNSvEWFIAALGAilAGGLCVGIYATN---SADACQYAIAHSKVNIL 106
Cdd:PRK13382 68 TLTWRELDERSDALAAALQALPIGEPRVVGIMCRNH-RGFVEALLA--ANRIGADILLLNtsfAGPALAEVVTREGVDTV 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 107 VVENELqlqkIFSIPK---NRIQTLKAIiqyrlpvketknydlySWDDfmelgnsIPDSQLDQIIGSQKANQ-------- 175
Cdd:PRK13382 145 IYDEEF----SATVDRalaDCPQATRIV----------------AWTD-------EDHDLTVEVLIAAHAGQrpeptgrk 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 176 CAVIIYTSGTTGHPKGAMLSHDnitwmAGAAAMECNLSLAP-KKQEVVVsylplshIAAQMMDVWipmkvG-ASIYFAQp 253
Cdd:PRK13382 198 GRVILLTSGTTGTPKGARRSGP-----GGIGTLKAILDRTPwRAEEPTV-------IVAPMFHAW-----GfSQLVLAA- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 254 dALKGTLVN--------TLQEV---KPTAFMGVPRIWEKMHEKIKEAASKSSSlrkkvfswarnvglkintkrmlgahdt 322
Cdd:PRK13382 260 -SLACTIVTrrrfdpeaTLDLIdrhRATGLAVVPVMFDRIMDLPAEVRNRYSG--------------------------- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 323 pMSYRMAKAlvfskvksslgldhchifiSGAAPLNQETSEFFLSLDIPIGEVYGLSEStGPHSMSTPENYR--ILSSGKV 400
Cdd:PRK13382 312 -RSLRFAAA-------------------SGSRMRPDVVIAFMDQFGDVIYNNYNATEA-GMIATATPADLRaaPDTAGRP 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 401 MTGCK-NMLYQQNKE----GIGEVCLWGRHVFMGYlgsedatTEAIDK---EGWLHSGDLGRVDNKGFLYITGRIKEIII 472
Cdd:PRK13382 371 AEGTEiRILDQDFREvptgEVGTIFVRNDTQFDGY-------TSGSTKdfhDGFMASGDVGYLDENGRLFVVGRDDEMIV 443
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1811029393 473 TaGGENVAPIPIENLVKeKLPIISNAMLVG-DKAKF---LSVLLTLKCEVDKT 521
Cdd:PRK13382 444 S-GGENVYPIEVEKTLA-THPDVAEAAVIGvDDEQYgqrLAAFVVLKPGASAT 494
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
38-498 |
1.02e-08 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 58.11 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 38 EASRKAAkAMIKL--GLEPFHsVGILGFNSVEWFIAALGAILAGGLCVGIYATNSADACQYAIAHSKVNILVVENE-LQL 114
Cdd:PRK13388 35 EAAARAA-ALIALadPDRPLH-VGVLLGNTPEMLFWLAAAALGGYVLVGLNTTRRGAALAADIRRADCQLLVTDAEhRPL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 115 QKIFSIPKNRIqtlkaiiqyrLPVketknyDLYSWDDFM-ELGNSIPDSQLDqiigsqkANQCAVIIYTSGTTGHPKGAM 193
Cdd:PRK13388 113 LDGLDLPGVRV----------LDV------DTPAYAELVaAAGALTPHREVD-------AMDPFMLIFTSGTTGAPKAVR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 194 LSHDNITwMAGAAAMEcnlslapkKQEVV---VSYL--PLSHIAAqMMDVWIP-MKVGASIyfAQPDALKgtlvntlqev 267
Cdd:PRK13388 170 CSHGRLA-FAGRALTE--------RFGLTrddVCYVsmPLFHSNA-VMAGWAPaVASGAAV--ALPAKFS---------- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 268 kPTAFMgvPRIwekmhekikeaaskssslrkkvfswarnvglkintkRMLGAhdTPMSYrMAKALVFSKVKSSLGLDH-- 345
Cdd:PRK13388 228 -ASGFL--DDV------------------------------------RRYGA--TYFNY-VGKPLAYILATPERPDDAdn 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 346 --CHIFISGAAPLNQEtsEFFLSLDIPIGEVYGLSESTG---------PHSMSTP-ENYRILSSGKVmTGCKNMLYQQN- 412
Cdd:PRK13388 266 plRVAFGNEASPRDIA--EFSRRFGCQVEDGYGSSEGAVivvrepgtpPGSIGRGaPGVAIYNPETL-TECAVARFDAHg 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 413 -----KEGIGE-VCLWGRHVFMGYLGSEDATTEAIdKEGWLHSGDLGRVDNKGFLYITGRiKEIIITAGGENVAPIPIEN 486
Cdd:PRK13388 343 allnaDEAIGElVNTAGAGFFEGYYNNPEATAERM-RHGMYWSGDLAYRDADGWIYFAGR-TADWMRVDGENLSAAPIER 420
|
490
....*....|..
gi 1811029393 487 LVKeKLPIISNA 498
Cdd:PRK13388 421 ILL-RHPAINRV 431
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
173-481 |
1.05e-08 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 58.10 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 173 ANQCAVIIYTSGTTGHPKGAMLSHDN---------------ITWMAGaaamecnlslapkkqEVVVSYLPLSHIAAQMmd 237
Cdd:PRK05857 168 SEDPLAMIFTSGTTGEPKAVLLANRTffavpdilqkeglnwVTWVVG---------------ETTYSPLPATHIGGLW-- 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 238 vWIP---MKVGASIYFAQPDALKGTLVNTlQEVKPTAFmgVPRIWEKMHEKIKEAASKSSSLRKKVFSWARNVGLKINtk 314
Cdd:PRK05857 231 -WILtclMHGGLCVTGGENTTSLLEILTT-NAVATTCL--VPTLLSKLVSELKSANATVPSLRLVGYGGSRAIAADVR-- 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 315 rmlgahdtpmsyrmakalvfskvksslgldhchiFISGAAplnqetsefflsldIPIGEVYGLSEsTGPHSMSTPENYRI 394
Cdd:PRK05857 305 ----------------------------------FIEATG--------------VRTAQVYGLSE-TGCTALCLPTDDGS 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 395 LSS------GKVMTGCKNMLYQQNKEG-----------IGEVCLWGRHVFMGYLGSEDATTEAIdKEGWLHSGDLGRVDN 457
Cdd:PRK05857 336 IVKieagavGRPYPGVDVYLAATDGIGptapgagpsasFGTLWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLLERRE 414
|
330 340
....*....|....*....|....
gi 1811029393 458 KGFLYITGRIKEIIITaGGENVAP 481
Cdd:PRK05857 415 DGFFYIKGRSSEMIIC-GGVNIAP 437
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
177-500 |
1.12e-08 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 57.87 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 177 AVIIYTSGTTGHPKGAMLSHDNItWMAGAAAMECNlSLAPKKQEVVVSYLPLSH-------IAAQMmdvwipmkVGASIY 249
Cdd:PRK05620 184 AAICYSTGTTGAPKGVVYSHRSL-YLQSLSLRTTD-SLAVTHGESFLCCVPIYHvlswgvpLAAFM--------SGTPLV 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 250 FAQPDALKGTLVNTLQEVKPTAFMGVPRIWEKMHEKIKEAASKSSSLRKkvfswarnvglkintkrmLGAHDTPMSYRMA 329
Cdd:PRK05620 254 FPGPDLSAPTLAKIIATAMPRVAHGVPTLWIQLMVHYLKNPPERMSLQE------------------IYVGGSAVPPILI 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 330 KALvfskvKSSLGLDHCHIFisGAAplnqETSefflsldiPIGEV--------------YGLSESTGPHSMstpeNYRIL 395
Cdd:PRK05620 316 KAW-----EERYGVDVVHVW--GMT----ETS--------PVGTVarppsgvsgearwaYRVSQGRFPASL----EYRIV 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 396 SSGKVMTGcknmlyqqNKEGIGEVCLWGRHVFMGYLGS-----------------EDATTEAIDkEGWLHSGDLGRVDNK 458
Cdd:PRK05620 373 NDGQVMES--------TDRNEGEIQVRGNWVTASYYHSpteegggaastfrgedvEDANDRFTA-DGWLRTGDVGSVTRD 443
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1811029393 459 GFLYITGRIKEiIITAGGENVAPIPIENLVKEKLPIISNAML 500
Cdd:PRK05620 444 GFLTIHDRARD-VIRSGGEWIYSAQLENYIMAAPEVVECAVI 484
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
160-507 |
1.13e-08 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 58.20 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 160 PDSQLDQIigsqkanqcAVIIYTSGTTGHPKGAMLSHDNitwmAGAAAMECNLSLAPKKQEVVVSYLPLSHIAAQMMdVW 239
Cdd:PRK07769 175 PEANEDTI---------AYLQYTSGSTRIPAGVQITHLN----LPTNVLQVIDALEGQEGDRGVSWLPFFHDMGLIT-VL 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 240 IPMKVGASIYFaqpdalkgtlvntlqeVKPTAFMGVPRIWekmhekIKEAASKSSsLRKKVFSWARNVGLKINTKRMLGA 319
Cdd:PRK07769 241 LPALLGHYITF----------------MSPAAFVRRPGRW------IRELARKPG-GTGGTFSAAPNFAFEHAAARGLPK 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 320 HDTPmsyrmakalvfskvksSLGLDHCHIFISGAAPLNQETSEFFLSLDIPIG-------EVYGLSE-----STGPHSMS 387
Cdd:PRK07769 298 DGEP----------------PLDLSNVKGLLNGSEPVSPASMRKFNEAFAPYGlpptaikPSYGMAEatlfvSTTPMDEE 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 388 TPENY---RILSSG---KVMTGCKNMLYQ---------------------QNKEG-IGEVCLWGRHVFMGYLGSEDATTE 439
Cdd:PRK07769 362 PTVIYvdrDELNAGrfvEVPADAPNAVAQvsagkvgvsewavivdpetasELPDGqIGEIWLHGNNIGTGYWGKPEETAA 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 440 -----------------AIDKEGWLHSGDLGrVDNKGFLYITGRIKEIIITaGGENVAPIPIENLVKEKlpiiSNAMLVG 502
Cdd:PRK07769 442 tfqnilksrlseshaegAPDDALWVRTGDYG-VYFDGELYITGRVKDLVII-DGRNHYPQDLEYTAQEA----TKALRTG 515
|
....*
gi 1811029393 503 DKAKF 507
Cdd:PRK07769 516 YVAAF 520
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
5-256 |
1.15e-08 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.
Pssm-ID: 341282 [Multi-domain] Cd Length: 483 Bit Score: 57.60 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 5 EFFQESVNRFGIYPALASKKdgkwEILSFNQYYEASRKAAKAMIKLGLEPFHSVGILGFNSVEwFIAALGAIL-AGGLCV 83
Cdd:cd12117 1 ELFEEQAARTPDAVAVVYGD----RSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPE-LVVALLAVLkAGAAYV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 84 GIYATNSADACQYAIAHSKVNILVVENELQLqkifsipknriqtlkaiiqyRLPVKETKNYDLYSWDDFmELGNsiPDSQ 163
Cdd:cd12117 76 PLDPELPAERLAFMLADAGAKVLLTDRSLAG--------------------RAGGLEVAVVIDEALDAG-PAGN--PAVP 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 164 LDqiigsqkANQCAVIIYTSGTTGHPKGAMLSHDNITwmagAAAMECNLsLAPKKQEVVVSYLPLSHIAAqMMDVWIPMK 243
Cdd:cd12117 133 VS-------PDDLAYVMYTSGSTGRPKGVAVTHRGVV----RLVKNTNY-VTLGPDDRVLQTSPLAFDAS-TFEIWGALL 199
|
250
....*....|...
gi 1811029393 244 VGASIYFAQPDAL 256
Cdd:cd12117 200 NGARLVLAPKGTL 212
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
29-487 |
1.54e-08 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 57.61 E-value: 1.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 29 EILSFNQYYEASRKAAKAMIKLGLEPFHSVGILGFNSVEWFIAALGAILAGGLCVGIYATNSADACQYAIAHSKVNILVV 108
Cdd:PRK08276 10 EVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVLIV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 109 ENELqlqkifsipKNRIQTLKAIIQYRLPVKETKNYDLYSWDDFMELGNSIPDSQL-DQIIGsqkanqcAVIIYTSGTTG 187
Cdd:PRK08276 90 SAAL---------ADTAAELAAELPAGVPLLLVVAGPVPGFRSYEEALAAQPDTPIaDETAG-------ADMLYSSGTTG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 188 HPKGAM--LSHDNITWMAGAAAMECNLSLAPKKQEVVVSYLPLSHIAaqmmdvwiPMKvgasiYFAQPDALKGTLVntlq 265
Cdd:PRK08276 154 RPKGIKrpLPGLDPDEAPGMMLALLGFGMYGGPDSVYLSPAPLYHTA--------PLR-----FGMSALALGGTVV---- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 266 evkptaFMgvPRiWEKmhekikEAAsksssLRKkvfswarnvglkINTKRMLGAHDTP-MSYRMAKalVFSKVKSSLGLD 344
Cdd:PRK08276 217 ------VM--EK-FDA------EEA-----LAL------------IERYRVTHSQLVPtMFVRMLK--LPEEVRARYDVS 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 345 HCHIFISGAAPLNQETSEFFLSLDIPI-GEVYGLSESTGPhSMSTPENY--RILSSGKVMTGCKNMLYQQNKE----GIG 417
Cdd:PRK08276 263 SLRVAIHAAAPCPVEVKRAMIDWWGPIiHEYYASSEGGGV-TVITSEDWlaHPGSVGKAVLGEVRILDEDGNElppgEIG 341
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1811029393 418 EVclwgrHVFMG-----YLGSEDATTEAIDKEGWLHSGDLGRVDNKGFLYITGRIKEIIITaGGENVAPIPIENL 487
Cdd:PRK08276 342 TV-----YFEMDgypfeYHNDPEKTAAARNPHGWVTVGDVGYLDEDGYLYLTDRKSDMIIS-GGVNIYPQEIENL 410
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
2-233 |
2.47e-08 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 56.81 E-value: 2.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 2 TIPEFFQESVNRFGIYPALASKkDGKWEILSFNQyyEASRKAAKAmIKLGLEPFHSVGILGFNSVEWFIAALGAILAGGl 81
Cdd:PRK08279 38 SLGDVFEEAAARHPDRPALLFE-DQSISYAELNA--RANRYAHWA-AARGVGKGDVVALLMENRPEYLAAWLGLAKLGA- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 82 CVGIYATNSADAcqyAIAHS----KVNILVVENELqLQKIFSIpknRIQTLKAIIQYRLPVKETKNYDLysWDDFMELGN 157
Cdd:PRK08279 113 VVALLNTQQRGA---VLAHSlnlvDAKHLIVGEEL-VEAFEEA---RADLARPPRLWVAGGDTLDDPEG--YEDLAAAAA 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1811029393 158 SIPDSQLDQIIGSQkANQCAVIIYTSGTTGHPKGAMLSHdnITWMAGAAAMecNLSLAPKKQEVVVSYLPLSHIAA 233
Cdd:PRK08279 184 GAPTTNPASRSGVT-AKDTAFYIYTSGTTGLPKAAVMSH--MRWLKAMGGF--GGLLRLTPDDVLYCCLPLYHNTG 254
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
177-485 |
2.53e-08 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 56.70 E-value: 2.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 177 AVIIYTSGTTGHPKGAMLSHDNItwMAGAAAMECNLSLAPKkQEVVVSYLPLSHiaaqmmdvwipmKVGASiyFAQPDAL 256
Cdd:PRK05851 155 AVLQGTAGSTGTPRTAILSPGAV--LSNLRGLNARVGLDAA-TDVGCSWLPLYH------------DMGLA--FLLTAAL 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 257 KGTlvnTLQEVKPTAFMGVPRIWekmhekikeaaskssslrkkvFSWarnvgLKINTKRMLGAHDtpMSYRMAKAlvFSK 336
Cdd:PRK05851 218 AGA---PLWLAPTTAFSASPFRW---------------------LSW-----LSDSRATLTAAPN--FAYNLIGK--YAR 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 337 VKSSLGLDHCHIFISGAAPLNQETSEFFLSLDIPIG-------EVYGLSESTGPHSMSTP-----------------ENY 392
Cdd:PRK05851 265 RVSDVDLGALRVALNGGEPVDCDGFERFATAMAPFGfdagaaaPSYGLAESTCAVTVPVPgiglrvdevttddgsgaRRH 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 393 RILSSG----KVMTGCKNMLYQQNKEGIGEVCLWGRHVFMGYLGSEdatteAIDKEGWLHSGDLGRVDNKGfLYITGRIK 468
Cdd:PRK05851 345 AVLGNPipgmEVRISPGDGAAGVAGREIGEIEIRGASMMSGYLGQA-----PIDPDDWFPTGDLGYLVDGG-LVVCGRAK 418
|
330
....*....|....*..
gi 1811029393 469 EIIITAgGENVAPIPIE 485
Cdd:PRK05851 419 ELITVA-GRNIFPTEIE 434
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
29-502 |
4.46e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 56.05 E-value: 4.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 29 EILSFNQYYEASRKAAKAMIKLGLEPFHSVGILGFNSVEWFIAALGAILAGGLCVGIYATNSADACQYAIAHSKVNILVV 108
Cdd:PRK07798 27 RRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLLDDSDAVALVY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 109 ENELqLQKIFSIpKNRIQTLKAIIQYRLPVKETKNYDLYSWDDFMELGNSIPD----SQLDQIIgsqkanqcaviIYTSG 184
Cdd:PRK07798 107 EREF-APRVAEV-LPRLPKLRTLVVVEDGSGNDLLPGAVDYEDALAAGSPERDfgerSPDDLYL-----------LYTGG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 185 TTGHPKGAMLSHDNItWMA--GAAAMECNLSLAPKKQEVVVsylplshIAAQMMDVWI---PMKVGASIYFAQPDALKGT 259
Cdd:PRK07798 174 TTGMPKGVMWRQEDI-FRVllGGRDFATGEPIEDEEELAKR-------AAAGPGMRRFpapPLMHGAGQWAAFAALFSGQ 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 260 LVNTLQEVKptaFMGVpRIWEKMHekikeaaskssslRKKVFS-------WARNvglkintkrMLGAHDTPMSYRMakal 332
Cdd:PRK07798 246 TVVLLPDVR---FDAD-EVWRTIE-------------REKVNVitivgdaMARP---------LLDALEARGPYDL---- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 333 vfskvkSSLGLdhchiFISGAAPLNQETSEFFLSL--DIPIGEVYGLSES-TGPHSMSTP-------ENYRILSSGKVMT 402
Cdd:PRK07798 296 ------SSLFA-----IASGGALFSPSVKEALLELlpNVVLTDSIGSSETgFGGSGTVAKgavhtggPRFTIGPRTVVLD 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 403 GCKNMLyqqnKEGIGEVCLWGR--HVFMGYLGSEDATTEA---IDKEGWLHSGDLGRVDNKGFLYITGRIKEIIITaGGE 477
Cdd:PRK07798 365 EDGNPV----EPGSGEIGWIARrgHIPLGYYKDPEKTAETfptIDGVRYAIPGDRARVEADGTITLLGRGSVCINT-GGE 439
|
490 500
....*....|....*....|....*
gi 1811029393 478 NVAPIPIENLVKEKlPIISNAMLVG 502
Cdd:PRK07798 440 KVFPEEVEEALKAH-PDVADALVVG 463
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
31-198 |
4.95e-08 |
|
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: 55.74 E-value: 4.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 31 LSFNQYYEASRKAAKAMIKLGLEPFHSVGILGFNSVEWFIAALGAILAGGLCVGIYATNSADACQYAIAHSKVNILVVEN 110
Cdd:cd12114 13 LTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARLVLTDG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 111 ElqlqkifsIPKNRIQTLKAIIQYRLPvketknydLYSWDDFmelgnSIPDSQLDQIigsqkanqcAVIIYTSGTTGHPK 190
Cdd:cd12114 93 P--------DAQLDVAVFDVLILDLDA--------LAAPAPP-----PPVDVAPDDL---------AYVIFTSGSTGTPK 142
|
....*...
gi 1811029393 191 GAMLSHDN 198
Cdd:cd12114 143 GVMISHRA 150
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
177-485 |
9.72e-08 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 54.28 E-value: 9.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 177 AVIIYTSGTTGHPKGAMLSHDNITwmAGAAAMECNLS------LApkkqevvvsyLPLSHIAAqmMDVWI--------PM 242
Cdd:PRK07824 38 ALVVATSGTTGTPKGAMLTAAALT--ASADATHDRLGgpgqwlLA----------LPAHHIAG--LQVLVrsviagsePV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 243 KVGASIYFaQPDALKGTlvntlqevkpTAFMGVPRIWekmhekikeaasksSSLrkkvfswarnvglkintkrmlgahdT 322
Cdd:PRK07824 104 ELDVSAGF-DPTALPRA----------VAELGGGRRY--------------TSL-------------------------V 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 323 PMsyRMAKALVFSKVKSSL-GLDHCHIfisGAAPLNQETSEFFLSLDIPIGEVYGLSESTGphsmstpenyrilssgkvm 401
Cdd:PRK07824 134 PM--QLAKALDDPAATAALaELDAVLV---GGGPAPAPVLDAAAAAGINVVRTYGMSETSG------------------- 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 402 tGCknmLYqqnkEGI-----------GEVCLWGRHVFMGYLGSEDAttEAIDKEGWLHSGDLGRVDNkGFLYITGRIKEI 470
Cdd:PRK07824 190 -GC---VY----DGVpldgvrvrvedGRIALGGPTLAKGYRNPVDP--DPFAEPGWFRTDDLGALDD-GVLTVLGRADDA 258
|
330
....*....|....*
gi 1811029393 471 IITaGGENVAPIPIE 485
Cdd:PRK07824 259 IST-GGLTVLPQVVE 272
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
179-502 |
9.74e-08 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 54.31 E-value: 9.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 179 IIYTSGTTGHPKGAMLSHDNITWMA-GAAAMEcnlslapkKQEVVVSYLPLSHIAAQMMDVWI---PMKVGASIYFAQPD 254
Cdd:cd05924 8 ILYTGGTTGMPKGVMWRQEDIFRMLmGGADFG--------TGEFTPSEDAHKAAAAAAGTVMFpapPLMHGTGSWTAFGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 255 ALKGTLVntlqeVKPTAFMGVPRIWEKMHEKikeaaskssslrkkvfswarnvglKINTKRMLGahDTpmsyrMAKALV- 333
Cdd:cd05924 80 LLGGQTV-----VLPDDRFDPEEVWRTIEKH------------------------KVTSMTIVG--DA-----MARPLId 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 334 -FSKVK----SSLgldhcHIFISGAAPLNQETSEFFLSL--DIPIGEVYGLSES--------------TGPHSMSTPENY 392
Cdd:cd05924 124 aLRDAGpydlSSL-----FAISSGGALLSPEVKQGLLELvpNITLVDAFGSSETgftgsghsagsgpeTGPFTRANPDTV 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 393 RILSSGKVMTgcknmlyqqnkEGIGEVCLWGR--HVFMGYLGSEDATTEA---IDKEGWLHSGDLGRVDNKGFLYITGRi 467
Cdd:cd05924 199 VLDDDGRVVP-----------PGSGGVGWIARrgHIPLGYYGDEAKTAETfpeVDGVRYAVPGDRATVEADGTVTLLGR- 266
|
330 340 350
....*....|....*....|....*....|....*
gi 1811029393 468 KEIIITAGGENVAPIPIENLVKeKLPIISNAMLVG 502
Cdd:cd05924 267 GSVCINTGGEKVFPEEVEEALK-SHPAVYDVLVVG 300
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
170-475 |
2.21e-07 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 53.95 E-value: 2.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 170 SQKANQCAVIIYTSGTTGHPKGAMLSHDNItwMAGAAAMECNLSLAPKKQevVVSYLPLSHIAAQMMDVWIPMKVGASIy 249
Cdd:PRK08043 361 KQQPEDAALILFTSGSEGHPKGVVHSHKSL--LANVEQIKTIADFTPNDR--FMSALPLFHSFGLTVGLFTPLLTGAEV- 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 250 FAQPDALKGTLVNTLqevkptafmgvpriwekmhekikeaaskssslrkkvfSWARNVGLKINTKRMLGAHDtpmsyRMA 329
Cdd:PRK08043 436 FLYPSPLHYRIVPEL-------------------------------------VYDRNCTVLFGTSTFLGNYA-----RFA 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 330 KALVFSKVKsslgldhchIFISGAAPLNQETSEFFL-SLDIPIGEVYGLSESTGPHSMSTPENYRILSSGKVMTGCKNML 408
Cdd:PRK08043 474 NPYDFARLR---------YVVAGAEKLQESTKQLWQdKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARL 544
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1811029393 409 YqqNKEGI---GEVCLWGRHVFMGYLGSED---------ATTEAIDKEGWLHSGDLGRVDNKGFLYITGRIKEIIITAG 475
Cdd:PRK08043 545 L--SVPGIeqgGRLQLKGPNIMNGYLRVEKpgvlevptaENARGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAG 621
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
423-501 |
2.80e-07 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 53.46 E-value: 2.80e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1811029393 423 GRHVFMGYLGSEDATTEAIDKEGWLHSGDLGRVDNKGFLYITGRIKEiIITAGGENVAPIPIENLVKeKLPIISNAMLV 501
Cdd:PRK10946 387 GPYTFRGYYKSPQHNASAFDANGFYCSGDLVSIDPDGYITVVGREKD-QINRGGEKIAAEEIENLLL-RHPAVIHAALV 463
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
29-248 |
4.41e-07 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 52.68 E-value: 4.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 29 EILSFNQYYEASRKAAKAMIK-LGLEPFHSVGILGFNSVEWFIAALGaiLAG-GLCVGIYATNS-ADACQYAIAHSKVNI 105
Cdd:cd05938 4 ETYTYRDVDRRSNQAARALLAhAGLRPGDTVALLLGNEPAFLWIWLG--LAKlGCPVAFLNTNIrSKSLLHCFRCCGAKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 106 LVVENELQ--LQKIfsIPKNRIQTLKaiIQYRLPVKETknydlyswDDFMELGNSIPDSQLDQIIGSQKANQC----AVI 179
Cdd:cd05938 82 LVVAPELQeaVEEV--LPALRADGVS--VWYLSHTSNT--------EGVISLLDKVDAASDEPVPASLRAHVTikspALY 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1811029393 180 IYTSGTTGHPKGAMLSHDNItWMAGAAAMECNLslapKKQEVVVSYLPLSHIAAQMMDVWIPMKVGASI 248
Cdd:cd05938 150 IYTSGTTGLPKAARISHLRV-LQCSGFLSLCGV----TADDVIYITLPLYHSSGFLLGIGGCIELGATC 213
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
29-248 |
4.54e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 53.42 E-value: 4.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 29 EILSFNQYYEASRKAAKAMIKLGLEPFHSVGILGFNSVEWFIAALGAILAGGLCVGIYATNSADACQYAIAHSKVNILVV 108
Cdd:PRK12316 2027 QHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLT 2106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 109 ENELQlqkifsipknriqtlkaiiqYRLPV-KETKNYDLYSWDDFMELGNSIPDSQLDqiigsqkANQCAVIIYTSGTTG 187
Cdd:PRK12316 2107 QRHLL--------------------ERLPLpAGVARLPLDRDAEWADYPDTAPAVQLA-------GENLAYVIYTSGSTG 2159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1811029393 188 HPKGAMLSH----DNITWMAGAAAM---ECNLSLAPKKQEVVVS--YLPLSHIAAQMM---DVWIPMKVGASI 248
Cdd:PRK12316 2160 LPKGVAVSHgalvAHCQAAGERYELspaDCELQFMSFSFDGAHEqwFHPLLNGARVLIrddELWDPEQLYDEM 2232
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
181-495 |
4.89e-07 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 52.82 E-value: 4.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 181 YTSGTTGHPKGAMLSHDNitwmAGAAAMECNLSLAPKKQEV-VVSYLPLSHiaaqmmDVWIPMkvgasIYFAqpdALKG- 258
Cdd:PRK12476 200 YTSGSTRPPVGVEITHRA----VGTNLVQMILSIDLLDRNThGVSWLPLYH------DMGLSM-----IGFP---AVYGg 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 259 --TLVNtlqevkPTAFMGVPRIWekmhekIKEAASKSSSLRkkVFSWARNVGLKINTKRMLGAH--------------DT 322
Cdd:PRK12476 262 hsTLMS------PTAFVRRPQRW------IKALSEGSRTGR--VVTAAPNFAYEWAAQRGLPAEgddidlsnvvliigSE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 323 PMSyrMAKALVFSK-----------VKSSLGLDHCHIFISGAAPLNQETSEFFLSLDIPIGEVYGLSESTgPHSMSTpen 391
Cdd:PRK12476 328 PVS--IDAVTTFNKafapyglprtaFKPSYGIAEATLFVATIAPDAEPSVVYLDREQLGAGRAVRVAADA-PNAVAH--- 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 392 yriLSSGKVMTGCKNMLYQQNKE------GIGEVCLWGRHVFMGYLGSEDATTE------------------AIDKEGWL 447
Cdd:PRK12476 402 ---VSCGQVARSQWAVIVDPDTGaelpdgEVGEIWLHGDNIGRGYWGRPEETERtfgaklqsrlaegshadgAADDGTWL 478
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1811029393 448 HSGDLGrVDNKGFLYITGRIKEIIITaGGENVAPIPIENLVKEKLPII 495
Cdd:PRK12476 479 RTGDLG-VYLDGELYITGRIADLIVI-DGRNHYPQDIEATVAEASPMV 524
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
5-278 |
6.11e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 53.04 E-value: 6.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 5 EFFQESVNRFGIYPALASKKdgkwEILSFNQYYEASRKAAKAMIKLGLEPFHSVGILGFNSVEWFIAALGAILAGGLCVG 84
Cdd:PRK12316 3061 RLFEEQVERTPDAVALAFGE----QRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVP 3136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 85 IYATNSADACQYAIAHSKVNILVVENELQLQKifsipknriqtlkaiiqyrlpVKETKNYDLYSWDDfmELGNSIPDSQL 164
Cdd:PRK12316 3137 LDPEYPEERLAYMLEDSGAQLLLSQSHLRLPL---------------------AQGVQVLDLDRGDE--NYAEANPAIRT 3193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 165 DqiigsqkANQCAVIIYTSGTTGHPKGAMLSHDNIT----WMAGAAAM---ECNLSLAPKKQEVVVS--YLPLSHIAA-- 233
Cdd:PRK12316 3194 M-------PENLAYVIYTSGSTGKPKGVGIRHSALSnhlcWMQQAYGLgvgDRVLQFTTFSFDVFVEelFWPLMSGARvv 3266
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1811029393 234 -----QMMDVWIPMKVGASIYFAQPDALKGTLVNTLQEVKPTAFMGVPRI 278
Cdd:PRK12316 3267 lagpeDWRDPALLVELINSEGVDVLHAYPSMLQAFLEEEDAHRCTSLKRI 3316
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
36-202 |
1.11e-06 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 52.09 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 36 YYEASRKA---AKAMIKLGLEPFHSVGILGFNSVEwFIAALGAIL-AGGLCVGIYATNSADACQYAIAHSKVNILVVENE 111
Cdd:PRK12467 1602 YGELNRRAnrlAHRLIALGVGPEVLVGIAVERSLE-MVVGLLAILkAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQSH 1680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 112 LQlQKIFSIPKNRIQTLKAIiqyrlpvketknydlyswDDFMElgnSIPDSQLDQIIGSQkanQCAVIIYTSGTTGHPKG 191
Cdd:PRK12467 1681 LQ-ARLPLPDGLRSLVLDQE------------------DDWLE---GYSDSNPAVNLAPQ---NLAYVIYTSGSTGRPKG 1735
|
170
....*....|....*
gi 1811029393 192 AMLSHDN----ITWM 202
Cdd:PRK12467 1736 AGNRHGAlvnrLCAT 1750
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
31-205 |
1.84e-06 |
|
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: 50.54 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 31 LSFNQYYEASRKAAKAMIKLGLEPFHSVGILGFNSVEWFIAALGAILAGGLCVGIYATNSADACQYAIAHSKVNILVVEN 110
Cdd:cd17650 13 LTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLEDSGAKLLLTQP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 111 ElqlqkifsipknriqtlkaiiqyrlpvketknyDLyswddfmelgnsipdsqldqiigsqkanqcAVIIYTSGTTGHPK 190
Cdd:cd17650 93 E---------------------------------DL------------------------------AYVIYTSGTTGKPK 109
|
170
....*....|....*
gi 1811029393 191 GAMLSHDNITWMAGA 205
Cdd:cd17650 110 GVMVEHRNVAHAAHA 124
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
29-197 |
2.46e-06 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 50.66 E-value: 2.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 29 EILSFNQYYEASRKAAKAMIKLGLEPFHSVGILGFNSVEWFIAALGAILAGGLCVGIYATNSADACQYAIAHSKVNILVV 108
Cdd:PRK04319 72 EKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLIT 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 109 ENELqLQKIfsiPKNRIQTLKAIIQYRLPVKETKNYDlyswdDFMELGNSIPDsqlDQIIGSQKANQCAVIIYTSGTTGH 188
Cdd:PRK04319 152 TPAL-LERK---PADDLPSLKHVLLVGEDVEEGPGTL-----DFNALMEQASD---EFDIEWTDREDGAILHYTSGSTGK 219
|
....*....
gi 1811029393 189 PKGAMLSHD 197
Cdd:PRK04319 220 PKGVLHVHN 228
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
3-211 |
2.47e-06 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 50.93 E-value: 2.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 3 IPEFFQESVNRFGIYPALASKKdgkwEILSFNQYYEASRKAAKAMIKLGLEPFHSVGILGFNSVEWFIAALGAILAGGLC 82
Cdd:PRK12467 3097 VHQLIEAQVARTPEAPALVFGD----QQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAY 3172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 83 VGIYATNSADACQYAIAHSKVNILVVENELqLQKIFSIPKNRIQTLkaiiqyrlpvketknyDLYSWddfmelgNSIPDS 162
Cdd:PRK12467 3173 VPLDPEYPRERLAYMIEDSGVKLLLTQAHL-LEQLPAPAGDTALTL----------------DRLDL-------NGYSEN 3228
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1811029393 163 QLDQIIGSQkanQCAVIIYTSGTTGHPKGAMLSHDNIT----WMAGAAAMECN 211
Cdd:PRK12467 3229 NPSTRVMGE---NLAYVIYTSGSTGKPKGVGVRHGALAnhlcWIAEAYELDAN 3278
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
161-200 |
2.70e-06 |
|
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: 50.00 E-value: 2.70e-06
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1811029393 161 DSQLDQIIGsqKANQCAVIIYTSGTTGHPKGAMLSHDNIT 200
Cdd:cd17643 82 DSGPSLLLT--DPDDLAYVIYTSGSTGRPKGVVVSHANVL 119
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
36-209 |
4.67e-06 |
|
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341306 [Multi-domain] Cd Length: 491 Bit Score: 49.65 E-value: 4.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 36 YYEASRKA---AKAMIKLGLEPFHSVGILGFNSVEWFIAALGAILAGGLCVGIYATNSADACQYAIAHSKVNILVVENEL 112
Cdd:cd17651 23 YAELDRRAnrlAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFMLADAGPVLVLTHPAL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 113 QLqkifsipknriqtlkaiiqyRLPVKEtknyDLYSWDDfMELGNSIPDSQLDqiIGSQKANQcAVIIYTSGTTGHPKGA 192
Cdd:cd17651 103 AG--------------------ELAVEL----VAVTLLD-QPGAAAGADAEPD--PALDADDL-AYVIYTSGSTGRPKGV 154
|
170 180
....*....|....*....|.
gi 1811029393 193 MLSHDNIT----WMAGAAAME 209
Cdd:cd17651 155 VMPHRSLAnlvaWQARASSLG 175
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
36-302 |
4.70e-06 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 49.96 E-value: 4.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 36 YYEASRKA---AKAMIKLGLEPFHSVGILGFNSVEWFIAALGAILAGGLCVGIYATNSADACQYAIAHSKVNILVVENEL 112
Cdd:PRK12316 4579 YAELNRRAnrlAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALLLTQSHL 4658
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 113 QLQkiFSIPKNrIQTLkAIIQYRlpvketknydlySWDDFmelGNSIPDSQLDqiigsqkANQCAVIIYTSGTTGHPKGA 192
Cdd:PRK12316 4659 LQR--LPIPDG-LASL-ALDRDE------------DWEGF---PAHDPAVRLH-------PDNLAYVIYTSGSTGRPKGV 4712
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 193 MLSHDNITWMAGAAAMECNLSLApkkqEVVVSYLPLSHIAAQMMDVWiPMKVGASIYFAQPDA-LKGTLVNTLQEVKPTA 271
Cdd:PRK12316 4713 AVSHGSLVNHLHATGERYELTPD----DRVLQFMSFSFDGSHEGLYH-PLINGASVVIRDDSLwDPERLYAEIHEHRVTV 4787
|
250 260 270
....*....|....*....|....*....|.
gi 1811029393 272 FMGVPRIWEKMHEKiKEAASKSSSLRKKVFS 302
Cdd:PRK12316 4788 LVFPPVYLQQLAEH-AERDGEPPSLRVYCFG 4817
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
180-238 |
6.48e-06 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 48.96 E-value: 6.48e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1811029393 180 IYTSGTTGHPKGAMLSHDNITWMAGAAAMecnlSLAPKKQEVVVSYLPLSHIAAQMMDV 238
Cdd:cd05939 110 IYTSGTTGLPKAAVIVHSRYYRIAAGAYY----AFGMRPEDVVYDCLPLYHSAGGIMGV 164
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
177-276 |
7.92e-06 |
|
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: 48.81 E-value: 7.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 177 AVIIYTSGTTGHPKGAMLSHDNI----TWMAGAaamecnLSLAPKkqEVVVSYLPLShiaaqmMDV-----WIPMKVGAS 247
Cdd:cd17646 141 AYVIYTSGSTGRPKGVMVTHAGIvnrlLWMQDE------YPLGPG--DRVLQKTPLS------FDVsvwelFWPLVAGAR 206
|
90 100 110
....*....|....*....|....*....|.
gi 1811029393 248 IYFAQPDALK--GTLVNTLQEVKPTAFMGVP 276
Cdd:cd17646 207 LVVARPGGHRdpAYLAALIREHGVTTCHFVP 237
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
177-248 |
9.46e-06 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 48.50 E-value: 9.46e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1811029393 177 AVIIYTSGTTGHPKGAMLSHDNITWMAGAAAMecnlSLAPKKQEVVVSYLPLSHIAAQMMDVWIPMKVGASI 248
Cdd:cd05940 84 ALYIYTSGTTGLPKAAIISHRRAWRGGAFFAG----SGGALPSDVLYTCLPLYHSTALIVGWSACLASGATL 151
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
24-488 |
1.04e-05 |
|
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: 48.64 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 24 KDGKWEILSFNQYYEASRKAAKAMIKLGLEPFHSVGILGFNSVEWFIAALGAILAGGLCVGIYATNSADACQYAIAHSKV 103
Cdd:cd05968 85 EDGTSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEA 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 104 NILVVEN-------ELQLQKIFSIPKNRIQTLKAIIQYR---LPVKETkNYDLYSWDDFMElgnsipdSQLDQIIGSQKA 173
Cdd:cd05968 165 KALITADgftrrgrEVNLKEEADKACAQCPTVEKVVVVRhlgNDFTPA-KGRDLSYDEEKE-------TAGDGAERTESE 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 174 NQCaVIIYTSGTTGHPKGAMLSHDNITwMAGAAAMECNLSLAPKKQEVVVSYLplshiaAQMMDVWI---PMKVGASI-- 248
Cdd:cd05968 237 DPL-MIIYTSGTTGKPKGTVHVHAGFP-LKAAQDMYFQFDLKPGDLLTWFTDL------GWMMGPWLifgGLILGATMvl 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 249 YFAQPDalkgtlvntlqevkptaFMGVPRIWEkMHEKIKeaaskssslrkkvfswARNVGLKINTKRMLGAHDTpmsyrm 328
Cdd:cd05968 309 YDGAPD-----------------HPKADRLWR-MVEDHE----------------ITHLGLSPTLIRALKPRGD------ 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 329 akALVFSKVKSSLgldhcHIFISGAAPLNQETSEFFLSL----DIPIGEVYGLSESTG------------PHSMSTPeny 392
Cdd:cd05968 349 --APVNAHDLSSL-----RVLGSTGEPWNPEPWNWLFETvgkgRNPIINYSGGTEISGgilgnvlikpikPSSFNGP--- 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 393 rilssgkvMTGCKNMLYQQN----KEGIGEVCLWGRHVFM--GYLGSEDATTEAI-DK-EG-WLHsGDLGRVDNKGFLYI 463
Cdd:cd05968 419 --------VPGMKADVLDESgkpaRPEVGELVLLAPWPGMtrGFWRDEDRYLETYwSRfDNvWVH-GDFAYYDEEGYFYI 489
|
490 500
....*....|....*....|....*
gi 1811029393 464 TGRIKEIIITAgGENVAPIPIENLV 488
Cdd:cd05968 490 LGRSDDTINVA-GKRVGPAEIESVL 513
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
177-255 |
1.22e-05 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 48.50 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 177 AVIIYTSGTTGHPKGAMLSHDNIT----WMA---GAAAmecnlslapkkQEVVVSYLPLShiaaqmMDV-----WIPMKV 244
Cdd:PRK10252 601 AYIIFTSGSTGRPKGVMVGQTAIVnrllWMQnhyPLTA-----------DDVVLQKTPCS------FDVsvwefFWPFIA 663
|
90
....*....|.
gi 1811029393 245 GASIYFAQPDA 255
Cdd:PRK10252 664 GAKLVMAEPEA 674
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
118-202 |
2.10e-05 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 47.58 E-value: 2.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 118 FSIPKNRIQTLKAIIQYRLpvketknydLYSWDDFMELGNSIPDSQLDQIIGSQ------------KANQCAVIIYTSGT 185
Cdd:PRK04813 84 VSSPAERIEMIIEVAKPSL---------IIATEELPLEILGIPVITLDELKDIFatgnpydfdhavKGDDNYYIIFTSGT 154
|
90 100
....*....|....*....|.
gi 1811029393 186 TGHPKGAMLSHDNI----TWM 202
Cdd:PRK04813 155 TGKPKGVQISHDNLvsftNWM 175
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
152-200 |
2.67e-05 |
|
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: 47.15 E-value: 2.67e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1811029393 152 FMELGNSIPDSQLDQIIGSQKA--------NQCAVIIYTSGTTGHPKGAMLSHDNIT 200
Cdd:cd05918 76 FVPLDPSHPLQRLQEILQDTGAkvvltsspSDAAYVIFTSGSTGKPKGVVIEHRALS 132
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
322-502 |
4.03e-05 |
|
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: 46.36 E-value: 4.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 322 TPMSYRM---AKALVFSKVKSSLgldhcHIFISGAAPLNQETSEFF-LSLDIPIGEVYGLSESTGP----HSMSTPenYR 393
Cdd:cd05973 185 SPTAYRLlmaAGAEVPARPKGRL-----RRVSSAGEPLTPEVIRWFdAALGVPIHDHYGQTELGMVlanhHALEHP--VH 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 394 ILSSGKVMTGCKNMLYQQNKEGIGE-------------VCLWgrhvFMGYLGSEDATTEAidkeGWLHSGDLGRVDNKGF 460
Cdd:cd05973 258 AGSAGRAMPGWRVAVLDDDGDELGPgepgrlaidiansPLMW----FRGYQLPDTPAIDG----GYYLTGDTVEFDPDGS 329
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1811029393 461 LYITGRIKEIIITAgGENVAPIPIENLVKEKlPIISNAMLVG 502
Cdd:cd05973 330 FSFIGRADDVITMS-GYRIGPFDVESALIEH-PAVAEAAVIG 369
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
2-210 |
4.67e-05 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 46.70 E-value: 4.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 2 TIPEFFQESVNRFGIYPALASkkDGkwEILSFNQYYEASRKAAKAMIKLGLEPFHSVGILGFNSVEWFIAALGAILAGGL 81
Cdd:PRK05691 2189 TLHGLFAAQAARTPQAPALTF--AG--QTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGA 2264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 82 CVGIYATNSADACQYAIAHSKVNILVVENELqlqkifsipknriqtLKAIIQyrLPVKETKnydlysW---DDFMELGnS 158
Cdd:PRK05691 2265 YVPLDPEYPLERLHYMIEDSGIGLLLSDRAL---------------FEALGE--LPAGVAR------WcleDDAAALA-A 2320
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1811029393 159 IPDSQLDQIIGSQkaNQcAVIIYTSGTTGHPKGAMLSHdnitwmaGAAAMEC 210
Cdd:PRK05691 2321 YSDAPLPFLSLPQ--HQ-AYLIYTSGSTGKPKGVVVSH-------GEIAMHC 2362
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
170-259 |
5.06e-05 |
|
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: 46.21 E-value: 5.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 170 SQKANQCAVIIYTSGTTGHPKGAMLSHDNITwMAGAAAMECnLSLAPkkQEVVVSYLPLSHIAA--QMMDVWIpmkVGAS 247
Cdd:cd17649 90 THHPRQLAYVIYTSGSTGTPKGVAVSHGPLA-AHCQATAER-YGLTP--GDRELQFASFNFDGAheQLLPPLI---CGAC 162
|
90
....*....|..
gi 1811029393 248 IYFAQPDALKGT 259
Cdd:cd17649 163 VVLRPDELWASA 174
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
416-502 |
7.97e-05 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 45.66 E-value: 7.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 416 IGEVCLWGRHVFMGYLGSEDATTEA--IDKEG--WLHSGDLGRVDNKGFLYITGRIKEIIITAGGeNVAPIPIENLVKEk 491
Cdd:PRK09274 387 IGEIVVAGPMVTRSYYNRPEATRLAkiPDGQGdvWHRMGDLGYLDAQGRLWFCGRKAHRVETAGG-TLYTIPCERIFNT- 464
|
90
....*....|.
gi 1811029393 492 LPIISNAMLVG 502
Cdd:PRK09274 465 HPGVKRSALVG 475
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
177-212 |
8.58e-05 |
|
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: 45.32 E-value: 8.58e-05
10 20 30
....*....|....*....|....*....|....*.
gi 1811029393 177 AVIIYTSGTTGHPKGAMLSHDNITWMAGAAAMECNL 212
Cdd:cd17652 96 AYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAAFDV 131
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|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
350-501 |
8.14e-04 |
|
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: 42.17 E-value: 8.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 350 ISGAA-PLNQETSEFFLSL-DIPIGEVYGLSESTGPHSMSTPENYRILSSGKVMTGCKNMLYQQ--NKEGIGEVCL---W 422
Cdd:cd05974 205 VVGAGePLNPEVIEQVRRAwGLTIRDGYGQTETTALVGNSPGQPVKAGSMGRPLPGYRVALLDPdgAPATEGEVALdlgD 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811029393 423 GRHV--FMGYLGSEDATTEAIdKEGWLHSGDLGRVDNKGFLYITGRIKEiIITAGGENVAPIPIENLVKEKlPIISNAML 500
Cdd:cd05974 285 TRPVglMKGYAGDPDKTAHAM-RGGYYRTGDIAMRDEDGYLTYVGRADD-VFKSSDYRISPFELESVLIEH-PAVAEAAV 361
|
.
gi 1811029393 501 V 501
Cdd:cd05974 362 V 362
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
161-201 |
1.21e-03 |
|
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: 41.65 E-value: 1.21e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1811029393 161 DSQLdQIIGSQKANqCAVIIYTSGTTGHPKGAMLSHD---NITW 201
Cdd:cd17644 95 DAQI-SVLLTQPEN-LAYVIYTSGSTGKPKGVMIEHQslvNLSH 136
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
161-199 |
1.43e-03 |
|
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: 41.62 E-value: 1.43e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1811029393 161 DSQLDQIIGSQKanQCAVIIYTSGTTGHPKGAMLSHDNI 199
Cdd:cd17648 83 DTGARVVITNST--DLAYAIYTSGTTGKPKGVLVEHGSV 119
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
173-210 |
2.72e-03 |
|
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: 40.38 E-value: 2.72e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1811029393 173 ANQCAVIIYTSGTTGHPKGAMLSHDNITWMAGAAAMEC 210
Cdd:cd12115 104 PDDLAYVIYTSGSTGRPKGVAIEHRNAAAFLQWAAAAF 141
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
442-485 |
3.10e-03 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 40.24 E-value: 3.10e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1811029393 442 DKEGWLHSGDLGRVDNkGFLYITGRIKEIIITaGGENVAPIPIE 485
Cdd:PRK09029 329 NDEGWFATRDRGEWQN-GELTILGRLDNLFFS-GGEGIQPEEIE 370
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
444-502 |
3.83e-03 |
|
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: 40.25 E-value: 3.83e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1811029393 444 EGWLHSGDLGRVDNKGFLYITGRIKEIIITAgGENVAPIPIENLVKEKlPIISNAMLVG 502
Cdd:cd17634 469 KGMYFSGDGARRDEDGYYWITGRSDDVINVA-GHRLGTAEIESVLVAH-PKVAEAAVVG 525
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
445-475 |
9.36e-03 |
|
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: 38.84 E-value: 9.36e-03
10 20 30
....*....|....*....|....*....|.
gi 1811029393 445 GWLHSGDLGRVDNKGFLYITGRIKEIIITAG 475
Cdd:cd05967 471 GYYDTGDAGYKDEDGYLFIMGRTDDVINVAG 501
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