|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
1-580 |
0e+00 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 1271.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 1 MDDLALCEANNVPLTPMTFLKRASECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEM 80
Cdd:PLN03102 1 MDNLALCEANNVPLTPITFLKRASECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 81 HFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFLDRSFEALARESLHLLSSEDSNLNLPVIFIHENDFPKRASFEEL 160
Cdd:PLN03102 81 HFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFVDRSFEPLAREVLHLLSSEDSNLNLPVIFIHEIDFPKRPSSEEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 161 DYECLIQRGEPTPSMVARMFRIQDEHDPISLNYTSGTTADPKGVVISHRGAYLCTLSAIIGWEMGTCPVYLWTLPMFHCN 240
Cdd:PLN03102 161 DYECLIQRGEPTPSLVARMFRIQDEHDPISLNYTSGTTADPKGVVISHRGAYLSTLSAIIGWEMGTCPVYLWTLPMFHCN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 241 GWTFTWGTAARGGTSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSPRSGPVHVLTGGSPPPAALVKKV 320
Cdd:PLN03102 241 GWTFTWGTAARGGTSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSPRSGPVHVLTGGSPPPAALVKKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 321 QRLGFQVMHAYGQTEATGPILFCEWQDEWNRLPENQQMELKARQGISILGLADVDVKNKETQKSAPRDGKTMGEILIKGS 400
Cdd:PLN03102 321 QRLGFQVMHAYGLTEATGPVLFCEWQDEWNRLPENQQMELKARQGVSILGLADVDVKNKETQESVPRDGKTMGEIVIKGS 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 401 SIMKGYLKNPKATFEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPT 480
Cdd:PLN03102 401 SIMKGYLKNPKATSEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPT 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 481 WGETPCAFVVLEKSETTIkEDRVDKFQTRERNLIEYCRENLPHFMCPRKVVFLEELPKNGNGKILKPKLRDIAKGLVVED 560
Cdd:PLN03102 481 WGETPCAFVVLEKGETTK-EDRVDKLVTRERDLIEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKLRDIAKGLVVED 559
|
570 580
....*....|....*....|
gi 15218839 561 EINVIAKEVKRPVGHFISRL 580
Cdd:PLN03102 560 EDNVIKKVHQRPVEHFSSRL 579
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
11-551 |
0e+00 |
|
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: 841.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 11 NVPLTPMTFLKRASECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAV 90
Cdd:cd12118 1 YVPLTPLSFLERAAAVYPDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 91 LNPINTRLDATSIAAILRHAKPKILFLDRSFEalareslhllssedsnlnlpvifihendfpkrasfeeldYECLIQRGE 170
Cdd:cd12118 81 LNALNTRLDAEEIAFILRHSEAKVLFVDREFE---------------------------------------YEDLLAEGD 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 171 PTPSMVarmfRIQDEHDPISLNYTSGTTADPKGVVISHRGAYLCTLSAIIGWEMGTCPVYLWTLPMFHCNGWTFTWGTAA 250
Cdd:cd12118 122 PDFEWI----PPADEWDPIALNYTSGTTGRPKGVVYHHRGAYLNALANILEWEMKQHPVYLWTLPMFHCNGWCFPWTVAA 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 251 RGGTSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSPRSGPVHVLTGGSPPPAALVKKVQRLGFQVMHA 330
Cdd:cd12118 198 VGGTNVCLRKVDAKAIYDLIEKHKVTHFCGAPTVLNMLANAPPSDARPLPHRVHVMTAGAPPPAAVLAKMEELGFDVTHV 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 331 YGQTEATGPILFCEWQDEWNRLPENQQMELKARQGISILGLADVDVKNKETQKSAPRDGKTMGEILIKGSSIMKGYLKNP 410
Cdd:cd12118 278 YGLTETYGPATVCAWKPEWDELPTEERARLKARQGVRYVGLEEVDVLDPETMKPVPRDGKTIGEIVFRGNIVMKGYLKNP 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 411 KATFEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVV 490
Cdd:cd12118 358 EATAEAFRGGWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVE 437
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15218839 491 LEKSETTIKEDrvdkfqtrernLIEYCRENLPHFMCPRKVVFlEELPKNGNGKILKPKLRD 551
Cdd:cd12118 438 LKEGAKVTEEE-----------IIAFCREHLAGFMVPKTVVF-GELPKTSTGKIQKFVLRD 486
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
2-556 |
0e+00 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 738.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 2 DDLALCEANNVPLTPMTFLKRASECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMH 81
Cdd:PRK08162 6 QGLDRNAANYVPLTPLSFLERAAEVYPDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 82 FAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFLDRSFEALARESLHLLSsedsNLNLPVIFIHENDFPKRASFEELD 161
Cdd:PRK08162 86 FGVPMAGAVLNTLNTRLDAASIAFMLRHGEAKVLIVDTEFAEVAREALALLP----GPKPLVIDVDDPEYPGGRFIGALD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 162 YECLIQRGEPtpSMVARMfrIQDEHDPISLNYTSGTTADPKGVVISHRGAYLCTLSAIIGWEMGTCPVYLWTLPMFHCNG 241
Cdd:PRK08162 162 YEAFLASGDP--DFAWTL--PADEWDAIALNYTSGTTGNPKGVVYHHRGAYLNALSNILAWGMPKHPVYLWTLPMFHCNG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 242 WTFTWGTAARGGTSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSPRSGPVHVLTGGSPPPAALVKKVQ 321
Cdd:PRK08162 238 WCFPWTVAARAGTNVCLRKVDPKLIFDLIREHGVTHYCGAPIVLSALINAPAEWRAGIDHPVHAMVAGAAPPAAVIAKME 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 322 RLGFQVMHAYGQTEATGPILFCEWQDEWNRLPENQQMELKARQGISILGLADVDVKNKETQKSAPRDGKTMGEILIKGSS 401
Cdd:PRK08162 318 EIGFDLTHVYGLTETYGPATVCAWQPEWDALPLDERAQLKARQGVRYPLQEGVTVLDPDTMQPVPADGETIGEIMFRGNI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 402 IMKGYLKNPKATFEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTW 481
Cdd:PRK08162 398 VMKGYLKNPKATEEAFAGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKW 477
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15218839 482 GETPCAFVVLeKSETTIKEDrvdkfqtrerNLIEYCRENLPHFMCPRKVVFlEELPKNGNGKILKPKLRDIAKGL 556
Cdd:PRK08162 478 GEVPCAFVEL-KDGASATEE----------EIIAHCREHLAGFKVPKAVVF-GELPKTSTGKIQKFVLREQAKSL 540
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
1-556 |
0e+00 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 623.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 1 MDDLALCEANNVPLTPMTFLKRASECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEM 80
Cdd:PLN02479 7 IDDLPKNAANYTALTPLWFLERAAVVHPTRKSVVHGSVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 81 HFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFLDRSFEALARESLHLLSSED-SNLNLPVIFIHENDFPKRASFEE 159
Cdd:PLN02479 87 HFGVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEVVMVDQEFFTLAEEALKILAEKKkSSFKPPLLIVIGDPTCDPKSLQY 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 160 ------LDYECLIQRGEP----TPSmvarmfriQDEHDPISLNYTSGTTADPKGVVISHRGAYLCTLSAIIGWEMGTCPV 229
Cdd:PLN02479 167 algkgaIEYEKFLETGDPefawKPP--------ADEWQSIALGYTSGTTASPKGVVLHHRGAYLMALSNALIWGMNEGAV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 230 YLWTLPMFHCNGWTFTWGTAARGGTSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLD-LSPRSGPVHVLTG 308
Cdd:PLN02479 239 YLWTLPMFHCNGWCFTWTLAALCGTNICLRQVTAKAIYSAIANYGVTHFCAAPVVLNTIVNAPKSEtILPLPRVVHVMTA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 309 GSPPPAALVKKVQRLGFQVMHAYGQTEATGPILFCEWQDEWNRLPENQQMELKARQGISILGLADVDVKNKETQKSAPRD 388
Cdd:PLN02479 319 GAAPPPSVLFAMSEKGFRVTHTYGLSETYGPSTVCAWKPEWDSLPPEEQARLNARQGVRYIGLEGLDVVDTKTMKPVPAD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 389 GKTMGEILIKGSSIMKGYLKNPKATFEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKV 468
Cdd:PLN02479 399 GKTMGEIVMRGNMVMKGYLKNPKANEEAFANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAV 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 469 LETAVVAMPHPTWGETPCAFVVLEKsettiKEDRVDKFQTrERNLIEYCRENLPHFMCPRKVVFlEELPKNGNGKILKPK 548
Cdd:PLN02479 479 LEASVVARPDERWGESPCAFVTLKP-----GVDKSDEAAL-AEDIMKFCRERLPAYWVPKSVVF-GPLPKTATGKIQKHV 551
|
....*...
gi 15218839 549 LRDIAKGL 556
Cdd:PLN02479 552 LRAKAKEM 559
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
19-559 |
7.04e-152 |
|
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: 443.87 E-value: 7.04e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 19 FLKRASECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRL 98
Cdd:COG0318 4 LLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 99 DATSIAAILRHAKPKILFLdrsfealareslhllssedsnlnlpvifihendfpkrasfeeldyeCLIQrgeptpsmvar 178
Cdd:COG0318 84 TAEELAYILEDSGARALVT----------------------------------------------ALIL----------- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 179 mfriqdehdpislnYTSGTTADPKGVVISHRGAYLCTLSAIIGWEMGTCPVYLWTLPMFHCNGWTFTWGTA-ARGGTSVC 257
Cdd:COG0318 107 --------------YTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPlLAGATLVL 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 258 MRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLK---GNSLDLSP-RsgpvHVLTGGSPPPAALVKKVQ-RLGFQVMHAYG 332
Cdd:COG0318 173 LPRFDPERVLELIERERVTVLFGVPTMLARLLRhpeFARYDLSSlR----LVVSGGAPLPPELLERFEeRFGVRIVEGYG 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 333 QTEaTGPILFCEWQDEWNRLPenqqmelkARQGISILGlADVDVKNKETQKSAPRdgkTMGEILIKGSSIMKGYLKNPKA 412
Cdd:COG0318 249 LTE-TSPVVTVNPEDPGERRP--------GSVGRPLPG-VEVRIVDEDGRELPPG---EVGEIVVRGPNVMKGYWNDPEA 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 413 TFEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLE 492
Cdd:COG0318 316 TAEAFRDGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLR 395
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15218839 493 KSETTIKEDrvdkfqtrernLIEYCRENLPHFMCPRKVVFLEELPKNGNGKILKPKLRDIAKGLVVE 559
Cdd:COG0318 396 PGAELDAEE-----------LRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRERYAAGALE 451
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
9-551 |
1.44e-146 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 432.69 E-value: 1.44e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 9 ANNVPLTPMTFLKRASECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAG 88
Cdd:PRK06187 1 MQDYPLTIGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 89 AVLNPINTRLDATSIAAILRHAKPKILFLDRSFEALARESLHLLSSEDSnlnlpVIFIHENDfPKRASFEELDYECLIQR 168
Cdd:PRK06187 81 AVLHPINIRLKPEEIAYILNDAEDRVVLVDSEFVPLLAAILPQLPTVRT-----VIVEGDGP-AAPLAPEVGEYEELLAA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 169 GEPTPSMVARmfriqDEHDPISLNYTSGTTADPKGVVISHRGAYLCTLSAIIGWEMGTCPVYLWTLPMFHCNGWTftWGT 248
Cdd:PRK06187 155 ASDTFDFPDI-----DENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPMFHVHAWG--LPY 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 249 AA--RGGTSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKgnsldlSPRSGPV------HVLTGGSPPPAALVKK- 319
Cdd:PRK06187 228 LAlmAGAKQVIPRRFDPENLLDLIETERVTFFFAVPTIWQMLLK------APRAYFVdfsslrLVIYGGAALPPALLREf 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 320 VQRLGFQVMHAYGQTEaTGPILFCewqdewNRLPENQQMELKAR--QGISILGladVDVK-NKETQKSAPRDGKTMGEIL 396
Cdd:PRK06187 302 KEKFGIDLVQGYGMTE-TSPVVSV------LPPEDQLPGQWTKRrsAGRPLPG---VEARiVDDDGDELPPDGGEVGEII 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 397 IKGSSIMKGYLKNPKATFEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAM 476
Cdd:PRK06187 372 VRGPWLMQGYWNRPEATAETIDGGWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGV 451
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15218839 477 PHPTWGETPCAFVVLEKSETtikedrVDkfqtrERNLIEYCRENLPHFMCPRKVVFLEELPKNGNGKILKPKLRD 551
Cdd:PRK06187 452 PDEKWGERPVAVVVLKPGAT------LD-----AKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLRE 515
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
13-550 |
4.04e-139 |
|
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: 413.37 E-value: 4.04e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 13 PLTPMTFLKRASECYPNRTsiiYGKTRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLN 92
Cdd:cd05915 1 LERAAALFGRKEVVSRLHT---GEVHRTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 93 PINTRLDATSIAAILRHAKPKILFLDRSFEALARESLHLLSSedsnlnlpvifIHENDfPKRASFEEldYECLIQRGEPT 172
Cdd:cd05915 78 TANPRLSPKEIAYILNHAEDKVLLFDPNLLPLVEAIRGELKT-----------VQHFV-VMDEKAPE--GYLAYEEALGE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 173 psmvARMFRIQDEHDPISLNYTSGTTADPKGVVISHRGAYLCTLSAIIGWEMGT--CPVYLWTLPMFHCNGWTFTWGTAA 250
Cdd:cd05915 144 ----EADPVRVPERAACGMAYTTGTTGLPKGVVYSHRALVLHSLAASLVDGTALseKDVVLPVVPMFHVNAWCLPYAATL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 251 RGGTSVCMRHVTAPE-IYKNIEMHNVTHMCCVPTVFNILlkGNSLDLSPRSGP--VHVLTGGSPPPAALVkKVQRLG-FQ 326
Cdd:cd05915 220 VGAKQVLPGPRLDPAsLVELFDGEGVTFTAGVPTVWLAL--ADYLESTGHRLKtlRRLVVGGSAAPRSLI-ARFERMgVE 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 327 VMHAYGQTEATGPILFCEWQDEWNRLPENQQMELKARQGISILGLAdVDVKNKETQkSAPRDGKTMGEILIKGSSIMKGY 406
Cdd:cd05915 297 VRQGYGLTETSPVVVQNFVKSHLESLSEEEKLTLKAKTGLPIPLVR-LRVADEEGR-PVPKDGKALGEVQLKGPWITGGY 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 407 LKNPKAT-FEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETP 485
Cdd:cd05915 375 YGNEEATrSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERP 454
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15218839 486 CAFVVLEKSEttikedrvdkfqTRERNLIEYCRENLPHF-MCPRKVVFLEELPKNGNGKILKPKLR 550
Cdd:cd05915 455 LAVVVPRGEK------------PTPEELNEHLLKAGFAKwQLPDAYVFAEEIPRTSAGKFLKRALR 508
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
19-551 |
1.50e-136 |
|
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: 407.02 E-value: 1.50e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 19 FLKRASECYPNRTsIIY-----GKTRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNP 93
Cdd:cd12119 1 LLEHAARLHGDRE-IVSrthegEVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 94 INTRLDATSIAAILRHAKPKILFLDRSFEALARESLhllsSEDSNLNLPVIFIHENDFPKRASFEELDYECLIQRGEPTP 173
Cdd:cd12119 80 INPRLFPEQIAYIINHAEDRVVFVDRDFLPLLEAIA----PRLPTVEHVVVMTDDAAMPEPAGVGVLAYEELLAAESPEY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 174 SmvarmFRIQDEHDPISLNYTSGTTADPKGVVISHRGAYLCTLSAIIGWEMGTCP--VYLWTLPMFHCNGWTFTWgTAAR 251
Cdd:cd12119 156 D-----WPDFDENTAAAICYTSGTTGNPKGVVYSHRSLVLHAMAALLTDGLGLSEsdVVLPVVPMFHVNAWGLPY-AAAM 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 252 GGTSVCM--RHVTAPEIYKNIEMHNVTHMCCVPTVFNILL---KGNSLDLSPRsgpVHVLTGGSPPPAALVKKVQRLGFQ 326
Cdd:cd12119 230 VGAKLVLpgPYLDPASLAELIEREGVTFAAGVPTVWQGLLdhlEANGRDLSSL---RRVVIGGSAVPRSLIEAFEERGVR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 327 VMHAYGQTEaTGPILFCEW-QDEWNRLPENQQMELKARQGISILGLaDVDVKNKETQKsAPRDGKTMGEILIKGSSIMKG 405
Cdd:cd12119 307 VIHAWGMTE-TSPLGTVARpPSEHSNLSEDEQLALRAKQGRPVPGV-ELRIVDDDGRE-LPWDGKAVGELQVRGPWVTKS 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 406 YLKNPKATFEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETP 485
Cdd:cd12119 384 YYKNDEESEALTEDGWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERP 463
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15218839 486 CAFVVLEKSETTIKEDrvdkfqtrernLIEYCRENLPHFMCPRKVVFLEELPKNGNGKILKPKLRD 551
Cdd:cd12119 464 LAVVVLKEGATVTAEE-----------LLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
20-546 |
2.73e-129 |
|
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: 385.42 E-value: 2.73e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 20 LKRASECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRLD 99
Cdd:cd17631 1 LRRRARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 100 ATSIAAILRHAKPKILFldrsfealareslhllssedsnlnlpvifihendfpkrasfeeldyecliqrgeptpsmvarm 179
Cdd:cd17631 81 PPEVAYILADSGAKVLF--------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 180 friqdeHDPISLNYTSGTTADPKGVVISHRGAYLCTLSAIIGWEMGTCPVYLWTLPMFHCNGW-TFTWGTAARGGTSVCM 258
Cdd:cd17631 98 ------DDLALLMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDLGPDDVLLVVAPLFHIGGLgVFTLPTLLRGGTVVIL 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 259 RHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSPRSGPVHVLTGGSPPPAALVKKVQRLGFQVMHAYGQTEATG 338
Cdd:cd17631 172 RKFDPETVLDLIERHRVTSFFLVPTMIQALLQHPRFATTDLSSLRAVIYGGAPMPERLLRALQARGVKFVQGYGMTETSP 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 339 PILFcewqdewnrLPENQQMELKARQGISILGlADVDVKNKETQKSAPRdgkTMGEILIKGSSIMKGYLKNPKATFEAFK 418
Cdd:cd17631 252 GVTF---------LSPEDHRRKLGSAGRPVFF-VEVRIVDPDGREVPPG---EVGEIVVRGPHVMAGYWNRPEATAAAFR 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 419 HGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLeKSETTI 498
Cdd:cd17631 319 DGWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVP-RPGAEL 397
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 15218839 499 KEDrvdkfqtrerNLIEYCRENLPHFMCPRKVVFLEELPKNGNGKILK 546
Cdd:cd17631 398 DED----------ELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
20-449 |
2.15e-111 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 338.90 E-value: 2.15e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 20 LKRASECYPNRTSI-IYGKTRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRL 98
Cdd:pfam00501 1 LERQAARTPDKTALeVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 99 DATSIAAILRHAKPKILFLDRSFEALA-RESLHLLSSEDSnlnlpVIFIHENDFPKrasfeeldYECLIQRGEPtPSMVA 177
Cdd:pfam00501 81 PAEELAYILEDSGAKVLITDDALKLEElLEALGKLEVVKL-----VLVLDRDPVLK--------EEPLPEEAKP-ADVPP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 178 RMFRIQDEHDPISLNYTSGTTADPKGVVISHRG----AYLCTLSAIIGWEMGTCPVYLWTLPMFHCNGWT-FTWGTAARG 252
Cdd:pfam00501 147 PPPPPPDPDDLAYIIYTSGTTGKPKGVMLTHRNlvanVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSlGLLGPLLAG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 253 GTSVCMRHVTAP---EIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSPRSGPVHVLTGGSPPPAALVKKV-QRLGFQVM 328
Cdd:pfam00501 227 ATVVLPPGFPALdpaALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLPPELARRFrELFGGALV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 329 HAYGQTEATGPIlfcewqdeWNRLPENQQMELKARQGISILGlADVDVKNKETQKSAPRDGKtmGEILIKGSSIMKGYLK 408
Cdd:pfam00501 307 NGYGLTETTGVV--------TTPLPLDEDLRSLGSVGRPLPG-TEVKIVDDETGEPVPPGEP--GELCVRGPGVMKGYLN 375
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 15218839 409 NPKATFEAFKH-GWLNTGDVGVIHPDGHVEIKDRSKDIIISG 449
Cdd:pfam00501 376 DPELTAEAFDEdGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
187-545 |
1.23e-99 |
|
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: 305.75 E-value: 1.23e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 187 DPISLNYTSGTTADPKGVVISHRG--AYLCTLSAIIGWEMGTcpVYLWTLPMFHCNGWTFTWGTAARGGTSVCMRHVTAP 264
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNllAAAAALAASGGLTEGD--VFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKFDPE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 265 EIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSPRSGPVHVLTGGSPPPAALVKKV-QRLGFQVMHAYGQTEATGPILFC 343
Cdd:cd04433 79 AALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPPELLERFeEAPGIKLVNGYGLTETGGTVATG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 344 eWQDEWNRLPENQqmelkarqGISILGLaDVDVKNKETQKSAPRdgkTMGEILIKGSSIMKGYLKNPKATFEAFKHGWLN 423
Cdd:cd04433 159 -PPDDDARKPGSV--------GRPVPGV-EVRIVDPDGGELPPG---EIGELVVRGPSVMKGYWNNPEATAAVDEDGWYR 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 424 TGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKSETTIKEDrv 503
Cdd:cd04433 226 TGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDAEE-- 303
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 15218839 504 dkfqtrernLIEYCRENLPHFMCPRKVVFLEELPKNGNGKIL 545
Cdd:cd04433 304 ---------LRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
10-551 |
3.07e-99 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 310.68 E-value: 3.07e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 10 NNVPLTPMTFLKRASECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGA 89
Cdd:PRK07656 1 DNEWMTLPELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 90 VLNPINTRLDATSIAAILRHAKPKILFLDRSFEALARESLHLLssedsnLNLPVIFIHENDFPKRASFEELDYECLIQRG 169
Cdd:PRK07656 81 VVVPLNTRYTADEAAYILARGDAKALFVLGLFLGVDYSATTRL------PALEHVVICETEEDDPHTEKMKTFTDFLAAG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 170 EPtpsmvARMFRIQDEHDPISLNYTSGTTADPKGVVISHRGaylcTLSAIIGW----EMGTCPVYLWTLPMFHCNGWTFT 245
Cdd:PRK07656 155 DP-----AERAPEVDPDDVADILFTSGTTGRPKGAMLTHRQ----LLSNAADWaeylGLTEGDRYLAANPFFHVFGYKAG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 246 WGTA-ARGGTSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILL---KGNSLDLSP-RSGpvhvLTGGSPPPAALVKKV 320
Cdd:PRK07656 226 VNAPlMRGATILPLPVFDPDEVFRLIETERITVLPGPPTMYNSLLqhpDRSAEDLSSlRLA----VTGAASMPVALLERF 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 321 Q-RLGFQ-VMHAYGQTEATGPILFCEWQDEWNRLPenqqmelkarqgiSILGLADVDVKNK--ETQKSAPRDGKTmGEIL 396
Cdd:PRK07656 302 EsELGVDiVLTGYGLSEASGVTTFNRLDDDRKTVA-------------GTIGTAIAGVENKivNELGEEVPVGEV-GELL 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 397 IKGSSIMKGYLKNPKATFEAFKH-GWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVA 475
Cdd:PRK07656 368 VRGPNVMKGYYDDPEATAAAIDAdGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIG 447
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15218839 476 MPHPTWGETPCAFVVLeKSETTIKEDrvdkfqtrerNLIEYCRENLPHFMCPRKVVFLEELPKNGNGKILKPKLRD 551
Cdd:PRK07656 448 VPDERLGEVGKAYVVL-KPGAELTEE----------ELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRALRE 512
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
19-556 |
1.57e-98 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 309.17 E-value: 1.57e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 19 FLKRASECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRL 98
Cdd:PRK08316 16 ILRRSARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFML 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 99 DATSIAAILRHAKPKILFLDRSFEALARESLHLLSSEDSNLNLPVIfihendfPKRASFEELDYECLIQRGEPTPSMVar 178
Cdd:PRK08316 96 TGEELAYILDHSGARAFLVDPALAPTAEAALALLPVDTLILSLVLG-------GREAPGGWLDFADWAEAGSVAEPDV-- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 179 mfRIQDEhDPISLNYTSGTTADPKGVVISHRGAYLCTLSAIIGWEMGTCPVYLWTLPMFHCNGW-TFTWGTAARGGTSVC 257
Cdd:PRK08316 167 --ELADD-DLAQILYTSGTESLPKGAMLTHRALIAEYVSCIVAGDMSADDIPLHALPLYHCAQLdVFLGPYLYVGATNVI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 258 MRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLkgNSLDLSPR--SGPVHVLTGGSPPPAALVKKVQ-RL-GFQVMHAYGQ 333
Cdd:PRK08316 244 LDAPDPELILRTIEAERITSFFAPPTVWISLL--RHPDFDTRdlSSLRKGYYGASIMPVEVLKELReRLpGLRFYNCYGQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 334 TEaTGPIlfcewqdewnrlpenqQMELKARQGISILGLADVDVKNKETQ------KSAPRDgkTMGEILIKGSSIMKGYL 407
Cdd:PRK08316 322 TE-IAPL----------------ATVLGPEEHLRRPGSAGRPVLNVETRvvdddgNDVAPG--EVGEIVHRSPQLMLGYW 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 408 KNPKATFEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCA 487
Cdd:PRK08316 383 DDPEKTAEAFRGGWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTA 462
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15218839 488 FVVLeKSETTIKEDrvdkfqtrerNLIEYCRENLPHFMCPRKVVFLEELPKNGNGKILKPKLRDIAKGL 556
Cdd:PRK08316 463 VVVP-KAGATVTED----------ELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKRELRERYAGA 520
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
20-550 |
7.93e-95 |
|
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: 297.94 E-value: 7.93e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 20 LKRASECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRLD 99
Cdd:cd05936 5 LEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 100 ATSIAAILRHAKPKILFLDRSFEalareslHLLSSedsnlnlpvifihendfpkrasfeeldyecliqrGEPTPSMVARm 179
Cdd:cd05936 85 PRELEHILNDSGAKALIVAVSFT-------DLLAA----------------------------------GAPLGERVAL- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 180 friqDEHDPISLNYTSGTTADPKGVVISHRgAYLCTLSAIIGWE---MGTCPVYLWTLPMFHcngwTFTWGTA-----AR 251
Cdd:cd05936 123 ----TPEDVAVLQYTSGTTGVPKGAMLTHR-NLVANALQIKAWLedlLEGDDVVLAALPLFH----VFGLTVAlllplAL 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 252 GGTSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSPRSGPVHVLTGGSPPPAALVKKVQRL-GFQVMHA 330
Cdd:cd05936 194 GATIVLIPRFRPIGVLKEIRKHRVTIFPGVPTMYIALLNAPEFKKRDFSSLRLCISGGAPLPVEVAERFEELtGVPIVEG 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 331 YGQTEaTGPILFCewqdewNRLPENQqmelkaRQGiSI-LGLADVDVK--NKETQKSAPrdGKTmGEILIKGSSIMKGYL 407
Cdd:cd05936 274 YGLTE-TSPVVAV------NPLDGPR------KPG-SIgIPLPGTEVKivDDDGEELPP--GEV-GELWVRGPQVMKGYW 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 408 KNPKATFEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCA 487
Cdd:cd05936 337 NRPEETAEAFVDGWLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKA 416
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15218839 488 FVVLEKSETTIKEDrvdkfqtrernLIEYCRENLPHFMCPRKVVFLEELPKNGNGKILKPKLR 550
Cdd:cd05936 417 FVVLKEGASLTEEE-----------IIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
38-550 |
9.29e-85 |
|
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: 270.32 E-value: 9.29e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 38 TRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFL 117
Cdd:cd05934 2 RRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 118 DrsfealareslhllssedsnlnlpvifihendfpkrasfeeldyecliqrgeptpsmvarmfriqdehdPISLNYTSGT 197
Cdd:cd05934 82 D---------------------------------------------------------------------PASILYTSGT 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 198 TADPKGVVISHrgAYLCTLSAIIGWEMGTCP--VYLWTLPMFHCNGWTFTW-GTAARGGTSVCMRHVTAPEIYKNIEMHN 274
Cdd:cd05934 93 TGPPKGVVITH--ANLTFAGYYSARRFGLGEddVYLTVLPLFHINAQAVSVlAALSVGATLVLLPRFSASRFWSDVRRYG 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 275 VTHMCCVPTVFNILLKGNSLDlSPRSGPVHVlTGGSPPPAALVKKV-QRLGFQVMHAYGQTEATGPIlfcewqdeWNRLP 353
Cdd:cd05934 171 ATVTNYLGAMLSYLLAQPPSP-DDRAHRLRA-AYGAPNPPELHEEFeERFGVRLLEGYGMTETIVGV--------IGPRD 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 354 EnqqmelKARQGiSIlGLA----DVDVKNKETQkSAPRDgkTMGEILIK---GSSIMKGYLKNPKATFEAFKHGWLNTGD 426
Cdd:cd05934 241 E------PRRPG-SI-GRPapgyEVRIVDDDGQ-ELPAG--EPGELVIRglrGWGFFKGYYNMPEATAEAMRNGWFHTGD 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 427 VGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKSETTIKEDrvdkf 506
Cdd:cd05934 310 LGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDPEE----- 384
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 15218839 507 qtrernLIEYCRENLPHFMCPRKVVFLEELPKNGNGKILKPKLR 550
Cdd:cd05934 385 ------LFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
13-551 |
6.18e-83 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 269.31 E-value: 6.18e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 13 PLTPMTFLKRASECYPNR---TSIIYGK-TRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAG 88
Cdd:PRK06018 9 PLLCHRIIDHAARIHGNRevvTRSVEGPiVRTTYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 89 AVLNPINTRLDATSIAAILRHAKPKILFLDRSF----EALAReslHLLSSEdsnlnLPVIFIHENDFPKRASFEELDYEC 164
Cdd:PRK06018 89 AICHTVNPRLFPEQIAWIINHAEDRVVITDLTFvpilEKIAD---KLPSVE-----RYVVLTDAAHMPQTTLKNAVAYEE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 165 LIqrGEPTPSMVARMFriqDEHDPISLNYTSGTTADPKGVVISHRGAYLCTLSAIIGWEMGTCP--VYLWTLPMFHCNGW 242
Cdd:PRK06018 161 WI--AEADGDFAWKTF---DENTAAGMCYTSGTTGDPKGVLYSHRSNVLHALMANNGDALGTSAadTMLPVVPLFHANSW 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 243 TFTWgTAARGGTSVCM--RHVTAPEIYKNIEMHNVTHMCCVPTVFNILLK---GNSLDLSPRSgpvHVLTGGSPPPAALV 317
Cdd:PRK06018 236 GIAF-SAPSMGTKLVMpgAKLDGASVYELLDTEKVTFTAGVPTVWLMLLQymeKEGLKLPHLK---MVVCGGSAMPRSMI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 318 KKVQRLGFQVMHAYGQTEaTGPI-LFCEWQDEWNRLPENQQMELKARQGISILGLaDVDVKNKETqKSAPRDGKTMGEIL 396
Cdd:PRK06018 312 KAFEDMGVEVRHAWGMTE-MSPLgTLAALKPPFSKLPGDARLDVLQKQGYPPFGV-EMKITDDAG-KELPWDGKTFGRLK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 397 IKGSSIMKGYLKNPKATFEAfkHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAM 476
Cdd:PRK06018 389 VRGPAVAAAYYRVDGEILDD--DGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGV 466
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15218839 477 PHPTWGETPCAFVVLEKSETTIKEDrvdkfqtrernLIEYCRENLPHFMCPRKVVFLEELPKNGNGKILKPKLRD 551
Cdd:PRK06018 467 YHPKWDERPLLIVQLKPGETATREE-----------ILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALRE 530
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
39-557 |
2.48e-82 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 267.73 E-value: 2.48e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 39 RFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFLD 118
Cdd:PRK07008 39 RYTYRDCERRAKQLAQALAALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRLFPEQIAYIVNHAEDRYVLFD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 119 RSFEALArESLHllsSEDSNLNLPVIFIHENDFPKrASFEELDYECLI--QRGEPT-PSMvarmfriqDEHDPISLNYTS 195
Cdd:PRK07008 119 LTFLPLV-DALA---PQCPNVKGWVAMTDAAHLPA-GSTPLLCYETLVgaQDGDYDwPRF--------DENQASSLCYTS 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 196 GTTADPKGVVISHRGAYLCTLSAIIGWEMGTCP--VYLWTLPMFHCNGWTFTWGTAARGGTSVCM-RHVTAPEIYKNIEM 272
Cdd:PRK07008 186 GTTGNPKGALYSHRSTVLHAYGAALPDAMGLSArdAVLPVVPMFHVNAWGLPYSAPLTGAKLVLPgPDLDGKSLYELIEA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 273 HNVTHMCCVPTVFNILL---KGNSLDLSPRSGPVhvlTGGSPPPAALVKKVQR-LGFQVMHAYGQTEATGPILFCEWQDE 348
Cdd:PRK07008 266 ERVTFSAGVPTVWLGLLnhmREAGLRFSTLRRTV---IGGSACPPAMIRTFEDeYGVEVIHAWGMTEMSPLGTLCKLKWK 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 349 WNRLPENQQMELKARQGISILGladVDVK-NKETQKSAPRDGKTMGEILIKGSSIMKGYLKNpkaTFEAFKHGWLNTGDV 427
Cdd:PRK07008 343 HSQLPLDEQRKLLEKQGRVIYG---VDMKiVGDDGRELPWDGKAFGDLQVRGPWVIDRYFRG---DASPLVDGWFPTGDV 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 428 GVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKSETTikedrvdkfq 507
Cdd:PRK07008 417 ATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRPGAEV---------- 486
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 15218839 508 TRERnLIEYCRENLPHFMCPRKVVFLEELPKNGNGKILKPKLRDIAKGLV 557
Cdd:PRK07008 487 TREE-LLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLREQFRDYV 535
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
19-560 |
2.34e-81 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 265.82 E-value: 2.34e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 19 FLKRASECYPNRTSIIY-----GKTRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNP 93
Cdd:COG0365 14 CLDRHAEGRGDKVALIWegedgEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 94 INTRLDATSIAAILRHAKPKILFLD---------RSFEALARESLHLLSSedsnlnLPVIFIHENDFPKRASFEELDYEC 164
Cdd:COG0365 94 VFPGFGAEALADRIEDAEAKVLITAdgglrggkvIDLKEKVDEALEELPS------LEHVIVVGRTGADVPMEGDLDWDE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 165 LIQRGEPTPSMVARMFriqdeHDPISLNYTSGTTADPKGVVISHRG---AYLCTLSAIIGWEMGTcpVYLWTLPMfhcnG 241
Cdd:COG0365 168 LLAAASAEFEPEPTDA-----DDPLFILYTSGTTGKPKGVVHTHGGylvHAATTAKYVLDLKPGD--VFWCTADI----G 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 242 W-TFTWGTA----ARGGTSVCMR----HVTAPEIYKNIEMHNVTHMCCVPTVFNILLK-----GNSLDLSP-RsgpvHVL 306
Cdd:COG0365 237 WaTGHSYIVygplLNGATVVLYEgrpdFPDPGRLWELIEKYGVTVFFTAPTAIRALMKagdepLKKYDLSSlR----LLG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 307 TGGSPPPAALVKKVQR-LGFQVMHAYGQTEATGPILFCewqdewnrLPEnqqMELKARQ-GISILGlADVDVKNkETQKS 384
Cdd:COG0365 313 SAGEPLNPEVWEWWYEaVGVPIVDGWGQTETGGIFISN--------LPG---LPVKPGSmGKPVPG-YDVAVVD-EDGNP 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 385 APRDgkTMGEILIKGS--SIMKGYLKNPKATFEAFKH---GWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVE 459
Cdd:COG0365 380 VPPG--EEGELVIKGPwpGMFRGYWNDPERYRETYFGrfpGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIE 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 460 NVLYKYPKVLETAVVAMPHPTWGETPCAFVVL----EKSETTIKEdrvdkfqtrernLIEYCRENLPHFMCPRKVVFLEE 535
Cdd:COG0365 458 SALVSHPAVAEAAVVGVPDEIRGQVVKAFVVLkpgvEPSDELAKE------------LQAHVREELGPYAYPREIEFVDE 525
|
570 580
....*....|....*....|....*
gi 15218839 536 LPKNGNGKILKPKLRDIAKGLVVED 560
Cdd:COG0365 526 LPKTRSGKIMRRLLRKIAEGRPLGD 550
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
10-549 |
3.19e-81 |
|
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: 263.71 E-value: 3.19e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 10 NNVPLTPMTFLkrASECYPNRTSIIYGKT--RFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMA 87
Cdd:cd05904 3 TDLPLDSVSFL--FASAHPSRPALIDAATgrALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 88 GAVL---NPINTrldATSIAAILRHAKPKILFLDRS-FEALAReslhllssedsnLNLPVIFIHENDFpkrasfEELDYE 163
Cdd:cd05904 81 GAVVttaNPLST---PAEIAKQVKDSGAKLAFTTAElAEKLAS------------LALPVVLLDSAEF------DSLSFS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 164 CLIQRGEPTPSMVARMfriqDEHDPISLNYTSGTTADPKGVVISHRG--AYLCTLSAIIGWEMGTCPVYLWTLPMFHCNG 241
Cdd:cd05904 140 DLLFEADEAEPPVVVI----KQDDVAALLYSSGTTGRSKGVMLTHRNliAMVAQFVAGEGSNSDSEDVFLCVLPMFHIYG 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 242 WT-FTWGTAARGGTSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSPRSGPVHVLTGGSPPPAALVKKV 320
Cdd:cd05904 216 LSsFALGLLRLGATVVVMPRFDLEELLAAIERYKVTHLPVVPPIVLALVKSPIVDKYDLSSLRQIMSGAAPLGKELIEAF 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 321 -QRL-GFQVMHAYGQTEATGPILFCEwqdewnrlpenQQMELKARQGISILGLADVDVK--NKETQKSAPRdGKTmGEIL 396
Cdd:cd05904 296 rAKFpNVDLGQGYGMTESTGVVAMCF-----------APEKDRAKYGSVGRLVPNVEAKivDPETGESLPP-NQT-GELW 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 397 IKGSSIMKGYLKNPKATFEAF-KHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVA 475
Cdd:cd05904 363 IRGPSIMKGYLNNPEATAATIdKEGWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIP 442
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15218839 476 MPHPTWGETPCAFVVLeKSETTIKEDRVdkfqtrernlIEYCRENLPHFMCPRKVVFLEELPKNGNGKILKPKL 549
Cdd:cd05904 443 YPDEEAGEVPMAFVVR-KPGSSLTEDEI----------MDFVAKQVAPYKKVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
38-545 |
3.65e-81 |
|
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: 262.92 E-value: 3.65e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 38 TRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFL 117
Cdd:cd05911 9 KELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 118 DRSFEALARESLHLLSSED-----SNLNLPVIFIHENDFPKRASFEELDYECLIQRGEptpsmvarmfriqdehDPISLN 192
Cdd:cd05911 89 DPDGLEKVKEAAKELGPKDkiivlDDKPDGVLSIEDLLSPTLGEEDEDLPPPLKDGKD----------------DTAAIL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 193 YTSGTTADPKGVVISHRGAYLCTLSA--IIGWEMGTCPVYLWTLPMFHCNGWTFTWGTAARGGTSVCMRHVTAPEIYKNI 270
Cdd:cd05911 153 YSSGTTGLPKGVCLSHRNLIANLSQVqtFLYGNDGSNDVILGFLPLYHIYGLFTTLASLLNGATVIIMPKFDSELFLDLI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 271 EMHNVTHMCCVPTVFNILLKGNSLDLSPRSGPVHVLTGGSPPPAALVKKVQRLGFQ--VMHAYGQTEATGPILFCEWQDE 348
Cdd:cd05911 233 EKYKITFLYLVPPIAAALAKSPLLDKYDLSSLRVILSGGAPLSKELQELLAKRFPNatIKQGYGMTETGGILTVNPDGDD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 349 WN----RLPENqqMELKarqgisilgladvdVKNKETQKSAPRDgkTMGEILIKGSSIMKGYLKNPKATFEAF-KHGWLN 423
Cdd:cd05911 313 KPgsvgRLLPN--VEAK--------------IVDDDGKDSLGPN--EPGEICVRGPQVMKGYYNNPEATKETFdEDGWLH 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 424 TGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKSETTIKEDrv 503
Cdd:cd05911 375 TGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEKLTEKE-- 452
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 15218839 504 dkfqtrernLIEYCRENLPHFmcprK-----VVFLEELPKNGNGKIL 545
Cdd:cd05911 453 ---------VKDYVAKKVASY----KqlrggVVFVDEIPKSASGKIL 486
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
17-556 |
1.73e-76 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 250.65 E-value: 1.73e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 17 MTFLKRASECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINT 96
Cdd:PRK03640 5 PNWLKQRAFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 97 RLDATSIAAILRHAKPKILFLDRSFEALARESLHLLSSEDSNLNLPVIFIhENDFPkrasfeeLDyecliqrgeptpsmv 176
Cdd:PRK03640 85 RLSREELLWQLDDAEVKCLITDDDFEAKLIPGISVKFAELMNGPKEEAEI-QEEFD-------LD--------------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 177 armfriqdehDPISLNYTSGTTADPKGVVISHRGAYLctlSAI-----IGWEMGTCpvYLWTLPMFHCNGWTFTWGTAAR 251
Cdd:PRK03640 142 ----------EVATIMYTSGTTGKPKGVIQTYGNHWW---SAVgsalnLGLTEDDC--WLAAVPIFHISGLSILMRSVIY 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 252 GGTSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKgnslDLSPRSGPVH---VLTGGSPPPAALVKKVQRLGFQVM 328
Cdd:PRK03640 207 GMRVVLVEKFDAEKINKLLQTGGVTIISVVSTMLQRLLE----RLGEGTYPSSfrcMLLGGGPAPKPLLEQCKEKGIPVY 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 329 HAYGQTEATgpilfcewqdewnrlpeNQQMELKARQGISILG-----LADVDVK-NKETQKSAPRDgktMGEILIKGSSI 402
Cdd:PRK03640 283 QSYGMTETA-----------------SQIVTLSPEDALTKLGsagkpLFPCELKiEKDGVVVPPFE---EGEIVVKGPNV 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 403 MKGYLKNPKATFEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWG 482
Cdd:PRK03640 343 TKGYLNREDATRETFQDGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWG 422
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15218839 483 ETPCAFVVlekSETTIKEDRvdkfqtrernLIEYCRENLPHFMCPRKVVFLEELPKNGNGKILKPKLRDIAKGL 556
Cdd:PRK03640 423 QVPVAFVV---KSGEVTEEE----------LRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQLVEEM 483
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
51-551 |
1.50e-75 |
|
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: 248.38 E-value: 1.50e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 51 RLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFLDRSFEALARESLH 130
Cdd:cd05926 26 DLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVLTPKGELGPASRAAS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 131 LLSSEDSNLNLPVIFIHENDFPKRASFEELDYECLIQRGEPTPSmvarmfriqdehDPISLNYTSGTTADPKGVVISHRG 210
Cdd:cd05926 106 KLGLAILELALDVGVLIRAPSAESLSNLLADKKNAKSEGVPLPD------------DLALILHTSGTTGRPKGVPLTHRN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 211 ayLCTLSAII--GWEMGTCPVYLWTLPMFHCNGWTFT-WGTAARGGTSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNI 287
Cdd:cd05926 174 --LAASATNItnTYKLTPDDRTLVVMPLFHVHGLVASlLSTLAAGGSVVLPPRFSASTFWPDVRDYNATWYTAVPTIHQI 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 288 LLKgnsldlSPRSGPVHVL-------TGGSP-PPAALVKKVQRLGFQVMHAYGQTEATGPIlFCewqdewNRLPEnqqme 359
Cdd:cd05926 252 LLN------RPEPNPESPPpklrfirSCSASlPPAVLEALEATFGAPVLEAYGMTEAAHQM-TS------NPLPP----- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 360 lkARQGISILGLAD-VDVK----NKETQKsaprDGKTmGEILIKGSSIMKGYLKNPKATFE-AFKHGWLNTGDVGVIHPD 433
Cdd:cd05926 314 --GPRKPGSVGKPVgVEVRildeDGEILP----PGVV-GEICLRGPNVTRGYLNNPEANAEaAFKDGWFRTGDLGYLDAD 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 434 GHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKSETTIKEDrvdkfqtrernL 513
Cdd:cd05926 387 GYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGASVTEEE-----------L 455
|
490 500 510
....*....|....*....|....*....|....*...
gi 15218839 514 IEYCRENLPHFMCPRKVVFLEELPKNGNGKILKPKLRD 551
Cdd:cd05926 456 RAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
41-551 |
4.52e-74 |
|
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: 241.87 E-value: 4.52e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 41 TWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKilfldrs 120
Cdd:cd05912 3 TFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVK------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 121 FEALAreslhllssedsnlnlpvifihendfpkrasfeeldyecliqrgeptpsmvarmfriqdehdpiSLNYTSGTTAD 200
Cdd:cd05912 76 LDDIA----------------------------------------------------------------TIMYTSGTTGK 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 201 PKGVVISHRGAYLctlSAI-----IGWEMGTCpvYLWTLPMFHCNGWTFTWGTAARGGTSVCMRHVTAPEIYKNIEMHNV 275
Cdd:cd05912 92 PKGVQQTFGNHWW---SAIgsalnLGLTEDDN--WLCALPLFHISGLSILMRSVIYGMTVYLVDKFDAEQVLHLINSGKV 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 276 THMCCVPTVFNILLKgnsldLSPRSGPVH---VLTGGSPPPAALVKKVQRLGFQVMHAYGQTEATGPILFCEWQDEWNRL 352
Cdd:cd05912 167 TIISVVPTMLQRLLE-----ILGEGYPNNlrcILLGGGPAPKPLLEQCKEKGIPVYQSYGMTETCSQIVTLSPEDALNKI 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 353 penqqmelkarqGISILGLADVDVKNKETQKSAprdgKTMGEILIKGSSIMKGYLKNPKATFEAFKHGWLNTGDVGVIHP 432
Cdd:cd05912 242 ------------GSAGKPLFPVELKIEDDGQPP----YEVGEILLKGPNVTKGYLNRPDATEESFENGWFKTGDIGYLDE 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 433 DGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKSETtikedrvdkfqtrERN 512
Cdd:cd05912 306 EGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSERPIS-------------EEE 372
|
490 500 510
....*....|....*....|....*....|....*....
gi 15218839 513 LIEYCRENLPHFMCPRKVVFLEELPKNGNGKILKPKLRD 551
Cdd:cd05912 373 LIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHELKQ 411
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
28-554 |
7.29e-73 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 241.30 E-value: 7.29e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 28 PNRTSIIYGKTRFTWPQTYDRCCRLAASLI-SLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRLDATSIAAI 106
Cdd:PRK06839 16 PDRIAIITEEEEMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 107 LRHAKPKILFLDRSFEALARESLHLLSSEdsnlnlPVIFIH---ENDFPKRASFEEldyecliqrgeptpsmvarmfriQ 183
Cdd:PRK06839 96 LKDSGTTVLFVEKTFQNMALSMQKVSYVQ------RVISITslkEIEDRKIDNFVE-----------------------K 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 184 DEHDPISLNYTSGTTADPKGVVISHRGAYLCTLSAIIGWEMGTCPVYLWTLPMFHCNGWT-FTWGTAARGGTSVCMRHVT 262
Cdd:PRK06839 147 NESASFIICYTSGTTGKPKGAVLTQENMFWNALNNTFAIDLTMHDRSIVLLPLFHIGGIGlFAFPTLFAGGVIIVPRKFE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 263 APEIYKNIEMHNVTHMCCVPTVFNILLKGnSLDLSPRSGPVHVL-TGGSPPPAALVKKVQRLGFQVMHAYGQTEaTGPIL 341
Cdd:PRK06839 227 PTKALSMIEKHKVTVVMGVPTIHQALINC-SKFETTNLQSVRWFyNGGAPCPEELMREFIDRGFLFGQGFGMTE-TSPTV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 342 FCEWQDEWNRLPenqqmelkARQGISILgLADVDVKNKETQKSAPRDgktMGEILIKGSSIMKGYLKNPKATFEAFKHGW 421
Cdd:PRK06839 305 FMLSEEDARRKV--------GSIGKPVL-FCDYELIDENKNKVEVGE---VGELLIRGPNVMKEYWNRPDATEETIQDGW 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 422 LNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKSETTIKED 501
Cdd:PRK06839 373 LCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIEKD 452
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 15218839 502 rvdkfqtrernLIEYCRENLPHFMCPRKVVFLEELPKNGNGKILKPKLRDIAK 554
Cdd:PRK06839 453 -----------VIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVNQLK 494
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
9-554 |
2.84e-72 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 241.64 E-value: 2.84e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 9 ANNVPLTPMT---FLKRASECYPNRTSIIY--GKTRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFA 83
Cdd:PRK08315 8 PTDVPLLEQTigqLLDRTAARYPDREALVYrdQGLRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 84 VPMAGAVLNPINTRLDATSIAAILRHAKPKILFLDRSF---------EALAREslhLLSSEDSNLN---LP----VIFIH 147
Cdd:PRK08315 88 TAKIGAILVTINPAYRLSELEYALNQSGCKALIAADGFkdsdyvamlYELAPE---LATCEPGQLQsarLPelrrVIFLG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 148 ENDFPKRASFEELdyeclIQRGEPTPsmVARMFRIQDE---HDPISLNYTSGTTADPKGVVISHRG----AYLctlsaiI 220
Cdd:PRK08315 165 DEKHPGMLNFDEL-----LALGRAVD--DAELAARQATldpDDPINIQYTSGTTGFPKGATLTHRNilnnGYF------I 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 221 GWEMG-------TCPVylwtlPMFHCNGWTFtwGTAA---RGGTSVCMRHVTAPE-IYKNIEMHNVTHMCCVPTVFNILL 289
Cdd:PRK08315 232 GEAMKlteedrlCIPV-----PLYHCFGMVL--GNLAcvtHGATMVYPGEGFDPLaTLAAVEEERCTALYGVPTMFIAEL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 290 KG---NSLDLSP-RSGpvhvLTGGSPPPAALVKKVQRLgfqvMH------AYGQTEaTGPILFCEWQDEwnrlpenqqmE 359
Cdd:PRK08315 305 DHpdfARFDLSSlRTG----IMAGSPCPIEVMKRVIDK----MHmsevtiAYGMTE-TSPVSTQTRTDD----------P 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 360 LKARqgISILGLA--DVDVK--NKETQKSAPRdGKTmGEILIKGSSIMKGYLKNPKATFEAFKH-GWLNTGDVGVIHPDG 434
Cdd:PRK08315 366 LEKR--VTTVGRAlpHLEVKivDPETGETVPR-GEQ-GELCTRGYSVMKGYWNDPEKTAEAIDAdGWMHTGDLAVMDEEG 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 435 HVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKSETTIKEDrvdkfqtrernLI 514
Cdd:PRK08315 442 YVNIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGATLTEED-----------VR 510
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 15218839 515 EYCRENLPHFMCPRKVVFLEELPKNGNGKILKPKLRDIAK 554
Cdd:PRK08315 511 DFCRGKIAHYKIPRYIRFVDEFPMTVTGKIQKFKMREMMI 550
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
28-551 |
1.51e-71 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 237.86 E-value: 1.51e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 28 PNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRLDATSIAAIL 107
Cdd:PRK06145 16 PDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYIL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 108 RHAKPKILFLDRSFEALAreslhllssedsNLNLPVIFIHENdfpkrasfEELDYECLIQRGEPTPSMVARMfriqdEHD 187
Cdd:PRK06145 96 GDAGAKLLLVDEEFDAIV------------ALETPKIVIDAA--------AQADSRRLAQGGLEIPPQAAVA-----PTD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 188 PISLNYTSGTTADPKGVVISHRGAYLCTLSAIIGWEMGTCPVYLWTLPMFHCNGWTFTwGTA--ARGGTSVCMRHVTAPE 265
Cdd:PRK06145 151 LVRLMYTSGTTDRPKGVMHSYGNLHWKSIDHVIALGLTASERLLVVGPLYHVGAFDLP-GIAvlWVGGTLRIHREFDPEA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 266 IYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSPRSGPVHVLTGGSPPPAALVKKVQRL--GFQVMHAYGQTEATGPILFC 343
Cdd:PRK06145 230 VLAAIERHRLTCAWMAPVMLSRVLTVPDRDRFDLDSLAWCIGGGEKTPESRIRDFTRVftRARYIDAYGLTETCSGDTLM 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 344 EWQDEWNRLpenqqmelkarqGISILGLADVDVKnketqkSAPRDGKTM-----GEILIKGSSIMKGYLKNPKATFEAFK 418
Cdd:PRK06145 310 EAGREIEKI------------GSTGRALAHVEIR------IADGAGRWLppnmkGEICMRGPKVTKGYWKDPEKTAEAFY 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 419 HGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKSETTI 498
Cdd:PRK06145 372 GDWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGATLT 451
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 15218839 499 KEDrvdkfqtrernLIEYCRENLPHFMCPRKVVFLEELPKNGNGKILKPKLRD 551
Cdd:PRK06145 452 LEA-----------LDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLRD 493
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
186-550 |
5.88e-67 |
|
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: 221.38 E-value: 5.88e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 186 HDPISLNYTSGTTADPKGVVISHRGayLCTLSAIIGWEMGT-------CPVylwtlPMFHCNGWTF-TWGTAARGGTSVC 257
Cdd:cd05917 2 DDVINIQFTSGTTGSPKGATLTHHN--IVNNGYFIGERLGLteqdrlcIPV-----PLFHCFGSVLgVLACLTHGATMVF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 258 M-RHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDL----SPRSGpvhvLTGGSPPPAALVKKV-QRLGFQVMH-A 330
Cdd:cd05917 75 PsPSFDPLAVLEAIEKEKCTALHGVPTMFIAELEHPDFDKfdlsSLRTG----IMAGAPCPPELMKRViEVMNMKDVTiA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 331 YGQTEATgPILFCEWQDEwnrlpenqQMELKARQGISILGLADVDVKNKETQKSAPRDGKtmGEILIKGSSIMKGYLKNP 410
Cdd:cd05917 151 YGMTETS-PVSTQTRTDD--------SIEKRVNTVGRIMPHTEAKIVDPEGGIVPPVGVP--GELCIRGYSVMKGYWNDP 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 411 KATFEAFKH-GWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFV 489
Cdd:cd05917 220 EKTAEAIDGdGWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWI 299
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15218839 490 VLEKSETTIKEDrvdkfqtrernLIEYCRENLPHFMCPRKVVFLEELPKNGNGKILKPKLR 550
Cdd:cd05917 300 RLKEGAELTEED-----------IKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
41-549 |
7.65e-67 |
|
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 162605 [Multi-domain] Cd Length: 436 Bit Score: 223.86 E-value: 7.65e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 41 TWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFLDRS 120
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 121 FEAlareslhllssEDsnlnLPVIFIHENDFPKRASFEELDYecliqrgeptpsmvarmfrIQDEhDPISLNYTSGTTAD 200
Cdd:TIGR01923 81 LEE-----------KD----FQADSLDRIEAAGRYETSLSAS-------------------FNMD-QIATLMFTSGTTGK 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 201 PKGVVISHRGAYLctlSAI-----IGWEMGTCpvYLWTLPMFHCNGWTFTWGTAARGGTSVCmrHVTAPEIYKNIEMHNV 275
Cdd:TIGR01923 126 PKAVPHTFRNHYA---SAVgskenLGFTEDDN--WLLSLPLYHISGLSILFRWLIEGATLRI--VDKFNQLLEMIANERV 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 276 THMCCVPTVFNILLKGNSLDLSPRSgpvhVLTGGSPPPAALVKKVQRLGFQVMHAYGQTEATGPILFCEWQDewnrlpen 355
Cdd:TIGR01923 199 THISLVPTQLNRLLDEGGHNENLRK----ILLGGSAIPAPLIEEAQQYGLPIYLSYGMTETCSQVTTATPEM-------- 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 356 qqmeLKARQGISILgLADVDVKNKetqksapRDGKT-MGEILIKGSSIMKGYLKNPKATFEAFKHGWLNTGDVGVIHPDG 434
Cdd:TIGR01923 267 ----LHARPDVGRP-LAGREIKIK-------VDNKEgHGEIMVKGANLMKGYLYQGELTPAFEQQGWFNTGDIGELDGEG 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 435 HVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKSETTIKedrvdkfqtrernLI 514
Cdd:TIGR01923 335 FLYVLGRRDDLIISGGENIYPEEIETVLYQHPGIQEAVVVPKPDAEWGQVPVAYIVSESDISQAK-------------LI 401
|
490 500 510
....*....|....*....|....*....|....*
gi 15218839 515 EYCRENLPHFMCPRKVVFLEELPKNGNGKILKPKL 549
Cdd:TIGR01923 402 AYLTEKLAKYKVPIAFEKLDELPYNASGKILRNQL 436
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
20-553 |
1.17e-66 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 226.58 E-value: 1.17e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 20 LKRASECYPNRTSIIYGK--TRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTR 97
Cdd:PRK12583 24 FDATVARFPDREALVVRHqaLRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 98 LDATSIAAILRHAKPKILFLDRSFEA---------LARESLHLLSSEDSNLNLP----VIFIHENDFPKRASFEELdyec 164
Cdd:PRK12583 104 YRASELEYALGQSGVRWVICADAFKTsdyhamlqeLLPGLAEGQPGALACERLPelrgVVSLAPAPPPGFLAWHEL---- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 165 lIQRGEpTPSMvARMFRIQ---DEHDPISLNYTSGTTADPKGVVISH----RGAYLCTLSAIIGWEMGTC-PVylwtlPM 236
Cdd:PRK12583 180 -QARGE-TVSR-EALAERQaslDRDDPINIQYTSGTTGFPKGATLSHhnilNNGYFVAESLGLTEHDRLCvPV-----PL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 237 FHCNGWTFTwgtaarggTSVCMRH---VTAPEIY-------KNIEMHNVTHMCCVPTVFNILL---KGNSLDLSP-RSGp 302
Cdd:PRK12583 252 YHCFGMVLA--------NLGCMTVgacLVYPNEAfdplatlQAVEEERCTALYGVPTMFIAELdhpQRGNFDLSSlRTG- 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 303 vhvLTGGSPPPAALVKKVqrlgFQVMH------AYGQTEATGPILFCEWQDEWNRLPE----NQ-QMELKarqgisilgL 371
Cdd:PRK12583 323 ---IMAGAPCPIEVMRRV----MDEMHmaevqiAYGMTETSPVSLQTTAADDLERRVEtvgrTQpHLEVK---------V 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 372 ADVDvknketQKSAPRDgkTMGEILIKGSSIMKGYLKNPKATFEAF-KHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGG 450
Cdd:PRK12583 387 VDPD------GATVPRG--EIGELCTRGYSVMKGYWNNPEATAESIdEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGG 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 451 ENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKSEttikedrvdkfQTRERNLIEYCRENLPHFMCPRKV 530
Cdd:PRK12583 459 ENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHPGH-----------AASEEELREFCKARIAHFKVPRYF 527
|
570 580
....*....|....*....|...
gi 15218839 531 VFLEELPKNGNGKILKPKLRDIA 553
Cdd:PRK12583 528 RFVDEFPMTVTGKVQKFRMREIS 550
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
39-550 |
1.53e-65 |
|
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: 220.33 E-value: 1.53e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 39 RFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFLD 118
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 119 RSFealareslhllssedsnlnlpvifihendfpkrasfeeldyecliqrgeptpsmvaRMFRIQDEHDPIS-LNYTSGT 197
Cdd:cd05903 81 ERF--------------------------------------------------------RQFDPAAMPDAVAlLLFTSGT 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 198 TADPKGVVISHRgAYLCTLSAIIG-WEMGTCPVYLWTLPMFHCNGwtFTWGTAA---RGGTSVCMRHVTAPEIYKNIEMH 273
Cdd:cd05903 105 TGEPKGVMHSHN-TLSASIRQYAErLGLGPGDVFLVASPMAHQTG--FVYGFTLpllLGAPVVLQDIWDPDKALALMREH 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 274 NVTHMCCVPTVFNILLkgNSLDLSPRSGP--VHVLTGGSPPPAALVKKVQ-RLGFQVMHAYGQTEATGPILFCEWQDEWN 350
Cdd:cd05903 182 GVTFMMGATPFLTDLL--NAVEEAGEPLSrlRTFVCGGATVPRSLARRAAeLLGAKVCSAYGSTECPGAVTSITPAPEDR 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 351 RLPENQqmelKARQGISIlgladvdvknketqKSAPRDGKTM-----GEILIKGSSIMKGYLKNPKATFEAFKHGWLNTG 425
Cdd:cd05903 260 RLYTDG----RPLPGVEI--------------KVVDDTGATLapgveGELLSRGPSVFLGYLDRPDLTADAAPEGWFRTG 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 426 DVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLeKSETTIKEDRVDK 505
Cdd:cd05903 322 DLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVT-KSGALLTFDELVA 400
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 15218839 506 FQTRERnlieycrenLPHFMCPRKVVFLEELPKNGNGKILKPKLR 550
Cdd:cd05903 401 YLDRQG---------VAKQYWPERLVHVDDLPRTPSGKVQKFRLR 436
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
22-550 |
5.62e-64 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 218.70 E-value: 5.62e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 22 RASECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALyemhFAVPMAGAV-------LNPI 94
Cdd:PRK06188 20 SALKRYPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEV----LMAIGAAQLaglrrtaLHPL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 95 NTRLDAtsiAAILRHAKPKIL------FLDRSFEALARES--LHLLSSEDSNlnlpvifihendfpkrasfEELDYECLI 166
Cdd:PRK06188 96 GSLDDH---AYVLEDAGISTLivdpapFVERALALLARVPslKHVLTLGPVP-------------------DGVDLLAAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 167 QRGEPTPSMVArmfriQDEHDPISLNYTSGTTADPKGVVISHRGayLCTLSAII--GWEMGTCPVYLWTLPMFHCNGWTF 244
Cdd:PRK06188 154 AKFGPAPLVAA-----ALPPDIAGLAYTGGTTGKPKGVMGTHRS--IATMAQIQlaEWEWPADPRFLMCTPLSHAGGAFF 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 245 TwGTAARGGTSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSPRSGPVHVLTGGSP-PPAALVKKVQRL 323
Cdd:PRK06188 227 L-PTLLRGGTVIVLAKFDPAEVLRAIEEQRITATFLVPTMIYALLDHPDLRTRDLSSLETVYYGASPmSPVRLAEAIERF 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 324 GFQVMHAYGQTEATGPILFCEWQDEWNRLPEnqqmeLKARQGISILGLaDVDVKNKETQKSAPrdgKTMGEILIKGSSIM 403
Cdd:PRK06188 306 GPIFAQYYGQTEAPMVITYLRKRDHDPDDPK-----RLTSCGRPTPGL-RVALLDEDGREVAQ---GEVGEICVRGPLVM 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 404 KGYLKNPKATFEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGE 483
Cdd:PRK06188 377 DGYWNRPEETAEAFRDGWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGE 456
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15218839 484 TPCAFVVLeKSETTIKEDRvdkfqtrernLIEYCRENLPHFMCPRKVVFLEELPKNGNGKILKPKLR 550
Cdd:PRK06188 457 AVTAVVVL-RPGAAVDAAE----------LQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALR 512
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
18-562 |
1.02e-63 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 217.99 E-value: 1.02e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 18 TFLKRASECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTR 97
Cdd:PRK07470 11 HFLRQAARRFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 98 LDATSIAAILRHAKPKILFLDRSF----EALARESLHLLSsedsnlnlpVIFIHENDFpkrasfeELDYECLIQRGEPTP 173
Cdd:PRK07470 91 QTPDEVAYLAEASGARAMICHADFpehaAAVRAASPDLTH---------VVAIGGARA-------GLDYEALVARHLGAR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 174 SMVARMfriqDEHDPISLNYTSGTTADPKGVVISH-RGAY-----LCTLSAiigwemGTCP--VYLWTLPMFHCNGwTFT 245
Cdd:PRK07470 155 VANAAV----DHDDPCWFFFTSGTTGRPKAAVLTHgQMAFvitnhLADLMP------GTTEqdASLVVAPLSHGAG-IHQ 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 246 WGTAARGGTSVCM--RHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSPRSGPVHVLTGGSPPPAALVKK-VQR 322
Cdd:PRK07470 224 LCQVARGAATVLLpsERFDPAEVWALVERHRVTNLFTVPTILKMLVEHPAVDRYDHSSLRYVIYAGAPMYRADQKRaLAK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 323 LGFQVMHAYGQTEATGPILFCEwqdewnrlPENQQMELKARQGISILGLA----DVDVKNKETQKSAPrdGKTmGEILIK 398
Cdd:PRK07470 304 LGKVLVQYFGLGEVTGNITVLP--------PALHDAEDGPDARIGTCGFErtgmEVQIQDDEGRELPP--GET-GEICVI 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 399 GSSIMKGYLKNPKATFEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPH 478
Cdd:PRK07470 373 GPAVFAGYYNNPEANAKAFRDGWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPD 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 479 PTWGETPCAFVVLEKSETtikedrVDkfqtrERNLIEYCRENLPHFMCPRKVVFLEELPKNGNGKILKPKLRD--IAKGL 556
Cdd:PRK07470 453 PVWGEVGVAVCVARDGAP------VD-----EAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVREelEERGL 521
|
....*.
gi 15218839 557 VVEDEI 562
Cdd:PRK07470 522 LDLERA 527
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
30-551 |
2.02e-61 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 211.30 E-value: 2.02e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 30 RTSIIYGK-TRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRLDATSIAAILR 108
Cdd:PRK08276 1 PAVIMAPSgEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 109 HAKPKILFLDRSFEALARESLHLLSsedsnLNLPVIFIHENDFPKRASFEELdyeclIQRGEPTPsmvarmfrIQDEHDP 188
Cdd:PRK08276 81 DSGAKVLIVSAALADTAAELAAELP-----AGVPLLLVVAGPVPGFRSYEEA-----LAAQPDTP--------IADETAG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 189 ISLNYTSGTTADPKGVVISHRG----AYLCTLSAIIGWEMGTCP--VYLWTLPMFHCNGWTFTWGTAARGGTSVCMRHVT 262
Cdd:PRK08276 143 ADMLYSSGTTGRPKGIKRPLPGldpdEAPGMMLALLGFGMYGGPdsVYLSPAPLYHTAPLRFGMSALALGGTVVVMEKFD 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 263 APEIYKNIEMHNVTHMCCVPTVFNILLK-----GNSLDLSPRSGPVHvltGGSPPPAAlVKK--VQRLGFQVMHAYGQTE 335
Cdd:PRK08276 223 AEEALALIERYRVTHSQLVPTMFVRMLKlpeevRARYDVSSLRVAIH---AAAPCPVE-VKRamIDWWGPIIHEYYASSE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 336 ATGpILFCEWQDeWNRLPENQQmelKARQG-ISILGLADVDVknketqksAPRdgkTMGEILIKGSSIMKGYLKNPKATF 414
Cdd:PRK08276 299 GGG-VTVITSED-WLAHPGSVG---KAVLGeVRILDEDGNEL--------PPG---EIGTVYFEMDGYPFEYHNDPEKTA 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 415 EAF-KHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAfVVLEK 493
Cdd:PRK08276 363 AARnPHGWVTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKA-VVQPA 441
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 15218839 494 SETTIKEDRVDKfqtrernLIEYCRENLPHFMCPRKVVFLEELPKNGNGKILKPKLRD 551
Cdd:PRK08276 442 DGADAGDALAAE-------LIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLRD 492
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
20-552 |
2.15e-60 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 209.61 E-value: 2.15e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 20 LKRASECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRLD 99
Cdd:PRK06155 27 LARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 100 ATSIAAILRHAKPKILFLDRSFEAlareslHLLSSEDSNLNLPVIFIHENDfPKRASFEELDYECLIQRGEPTPSMVARm 179
Cdd:PRK06155 107 GPQLEHILRNSGARLLVVEAALLA------ALEAADPGDLPLPAVWLLDAP-ASVSVPAGWSTAPLPPLDAPAPAAAVQ- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 180 friqdEHDPISLNYTSGTTADPKGVVISHRGAYLCTLSAIIGWEMGTCPVYLWTLPMFHCNGWTFTWGTAARGGTSVCMR 259
Cdd:PRK06155 179 -----PGDTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTLPLFHTNALNAFFQALLAGATYVLEP 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 260 HVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDlSPRSGPVHVLTGGSPPPAALVKKVQRLGFQVMHAYGQTEATGP 339
Cdd:PRK06155 254 RFSASGFWPAVRRHGATVTYLLGAMVSILLSQPARE-SDRAHRVRVALGPGVPAALHAAFRERFGVDLLDGYGSTETNFV 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 340 IlfcewqdeWNRLPENQQMEL-KARQGISILgLADvdvknkETQKSAPrDGkTMGEILIKGS---SIMKGYLKNPKATFE 415
Cdd:PRK06155 333 I--------AVTHGSQRPGSMgRLAPGFEAR-VVD------EHDQELP-DG-EPGELLLRADepfAFATGYFGMPEKTVE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 416 AFKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPhPTWGETPCAFVVLEKSE 495
Cdd:PRK06155 396 AWRNLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVP-SELGEDEVMAAVVLRDG 474
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 15218839 496 TTIkeDRVDkfqtrernLIEYCRENLPHFMCPRKVVFLEELPKNGNGKILKPKLRDI 552
Cdd:PRK06155 475 TAL--EPVA--------LVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLREQ 521
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
29-551 |
3.00e-60 |
|
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: 206.37 E-value: 3.00e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 29 NRTSIIYGKTRFTWPQTYDRCCRLAASLI-SLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTrldatsiaail 107
Cdd:cd05941 1 DRIAIVDDGDSITYADLVARAARLANRLLaLGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNP----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 108 rhakpkilfldrSFEAlaRESLHLLSseDSnlnlpvifihendfpkrasfeeldyecliqrgepTPSMVARMFRIQdehd 187
Cdd:cd05941 70 ------------SYPL--AELEYVIT--DS----------------------------------EPSLVLDPALIL---- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 188 pislnYTSGTTADPKGVVISHRGAYLCTLSAIIGWEMGTCPVYLWTLPMFHCNGWTFT-WGTAARGGTSVCMRHVTAPEI 266
Cdd:cd05941 96 -----YTSGTTGRPKGVVLTHANLAANVRALVDAWRWTEDDVLLHVLPLHHVHGLVNAlLCPLFAGASVEFLPKFDPKEV 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 267 YKNIEMHNVTHMCCVPTVFNILLKGNSLDLSPRSG-------PVHVLTGGSP--PPAALVKKVQRLGFQVMHAYGQTEaT 337
Cdd:cd05941 171 AISRLMPSITVFMGVPTIYTRLLQYYEAHFTDPQFaraaaaeRLRLMVSGSAalPVPTLEEWEAITGHTLLERYGMTE-I 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 338 GPILFcewqdewNRLpenqqmELKARQGISILGLADVDVKNKETQKSAPRDGKTMGEILIKGSSIMKGYLKNPKATFEAF 417
Cdd:cd05941 250 GMALS-------NPL------DGERRPGTVGMPLPGVQARIVDEETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEF 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 418 KH-GWLNTGDVGVIHPDGHVEIKDRSK-DIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKSE 495
Cdd:cd05941 317 TDdGWFKTGDLGVVDEDGYYWILGRSSvDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGA 396
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 15218839 496 TTIKEDrvdkfqtrerNLIEYCRENLPHFMCPRKVVFLEELPKNGNGKILKPKLRD 551
Cdd:cd05941 397 AALSLE----------ELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
20-550 |
1.42e-59 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 207.32 E-value: 1.42e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 20 LKRASECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRLD 99
Cdd:PRK07786 23 LARHALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 100 ATSIAAILRHAKPKILFLDRSFEALAREslhlLSSEDSNLNLPVIFIHENDFpkrasfEELDYECLIQRGEPTPSMVarm 179
Cdd:PRK07786 103 PPEIAFLVSDCGAHVVVTEAALAPVATA----VRDIVPLLSTVVVAGGSSDD------SVLGYEDLLAEAGPAHAPV--- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 180 friqD--EHDPISLNYTSGTTADPKGVVISHRGAYLCTLSAIIGWEMGT-CPVYLWTLPMFHCNGWTFTWGTAARGGTSV 256
Cdd:PRK07786 170 ----DipNDSPALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGADInSDVGFVGVPLFHIAGIGSMLPGLLLGAPTV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 257 C--MRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDlsPRSGPVHVLT-GGSPPPAALVKKVQRL--GFQVMHAY 331
Cdd:PRK07786 246 IypLGAFDPGQLLDVLEAEKVTGIFLVPAQWQAVCAEQQAR--PRDLALRVLSwGAAPASDTLLRQMAATfpEAQILAAF 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 332 GQTEATGPILFCEWQDEWNRLpenqqmelkARQGISILGLAdVDVKNKETQKSAPrdgKTMGEILIKGSSIMKGYLKNPK 411
Cdd:PRK07786 324 GQTEMSPVTCMLLGEDAIRKL---------GSVGKVIPTVA-ARVVDENMNDVPV---GEVGEIVYRAPTLMSGYWNNPE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 412 ATFEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVL 491
Cdd:PRK07786 391 ATAEAFAGGWFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAV 470
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 15218839 492 EKSETTIKEDRVDKFQTrernlieycrENLPHFMCPRKVVFLEELPKNGNGKILKPKLR 550
Cdd:PRK07786 471 RNDDAALTLEDLAEFLT----------DRLARYKHPKALEIVDALPRNPAGKVLKTELR 519
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
16-549 |
1.81e-59 |
|
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: 205.82 E-value: 1.81e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 16 PMTF--LKRASECYPNRTSIIY--GKTRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVL 91
Cdd:cd05923 1 QTVFemLRRAASRAPDACAIADpaRGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 92 NPINTRLDATSIAAILRHAKpkilfLDRSFEALAREslhllssedsnlnlpvifihendfPKRASF----EELDYECLIQ 167
Cdd:cd05923 81 ALINPRLKAAELAELIERGE-----MTAAVIAVDAQ------------------------VMDAIFqsgvRVLALSDLVG 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 168 RGEPTPSMVARMFRIQDEHDPISLNYTSGTTADPKGVVISHRGA--YLCTLSAIIGWEMGTCPVYLWTLPMFHCNG-WTF 244
Cdd:cd05923 132 LGEPESAGPLIEDPPREPEQPAFVFYTSGTTGLPKGAVIPQRAAesRVLFMSTQAGLRHGRHNVVLGLMPLYHVIGfFAV 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 245 TWGTAARGGTSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILL---KGNSLDLSPRSgpvHVLTGGSPPPAALVKKVQ 321
Cdd:cd05923 212 LVAALALDGTYVVVEEFDPADALKLIEQERVTSLFATPTHLDALAaaaEFAGLKLSSLR---HVTFAGATMPDAVLERVN 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 322 RL--GFQVMHaYGQTEATGPiLFCEWQDEWNRLPENQQMELKArqgISILGLADVDVKNKETqksaprdgktmGEILIK- 398
Cdd:cd05923 289 QHlpGEKVNI-YGTTEAMNS-LYMRDARTGTEMRPGFFSEVRI---VRIGGSPDEALANGEE-----------GELIVAa 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 399 -GSSIMKGYLKNPKATFEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMP 477
Cdd:cd05923 353 aADAAFTGYLNQPEATAKKLQDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVA 432
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15218839 478 HPTWGETPCAFVVLekSETTIKEDRVDKFqtrernlieyCREN-LPHFMCPRKVVFLEELPKNGNGKILKPKL 549
Cdd:cd05923 433 DERWGQSVTACVVP--REGTLSADELDQF----------CRASeLADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
12-555 |
2.87e-59 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 206.35 E-value: 2.87e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 12 VPLTP-MTFLKRASECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLIS-LNISKNDVVSVMAPNTPALYEMHFAVPMAGA 89
Cdd:PRK08314 7 LPETSlFHNLEVSARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQQeCGVRKGDRVLLYMQNSPQFVIAYYAILRANA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 90 VLNPINTRLDATSIAAILRHAKPKILF-----LDRSFEALARESL-HLLS-------SEDSNLNLPVIFIHENDFPKRAS 156
Cdd:PRK08314 87 VVVPVNPMNREEELAHYVTDSGARVAIvgselAPKVAPAVGNLRLrHVIVaqysdylPAEPEIAVPAWLRAEPPLQALAP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 157 FEELDYECLIQRGEPTPSMVARmfriqdeHDPIS-LNYTSGTTADPKGVVISHRGAYLCTLSAIIgWEMGTC-PVYLWTL 234
Cdd:PRK08314 167 GGVVAWKEALAAGLAPPPHTAG-------PDDLAvLPYTSGTTGVPKGCMHTHRTVMANAVGSVL-WSNSTPeSVVLAVL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 235 PMFHCNGWTFTWGTA-ARGGTSVCM----RHvTAPEIyknIEMHNVTHMCCVPTVFNILLKGNSLDLSPRSGPVHVLTGG 309
Cdd:PRK08314 239 PLFHVTGMVHSMNAPiYAGATVVLMprwdRE-AAARL---IERYRVTHWTNIPTMVVDFLASPGLAERDLSSLRYIGGGG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 310 SPPPAALVKKVQRL-GFQVMHAYGQTEATGPILFcewqdewNrlPenqqmelKARQGISILGLA--DVD--VKNKETQKS 384
Cdd:PRK08314 315 AAMPEAVAERLKELtGLDYVEGYGLTETMAQTHS-------N--P-------PDRPKLQCLGIPtfGVDarVIDPETLEE 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 385 APrDGKTmGEILIKGSSIMKGYLKNPKATFEAF-----KHgWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVE 459
Cdd:PRK08314 379 LP-PGEV-GEIVVHGPQVFKGYWNRPEATAEAFieidgKR-FFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVE 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 460 NVLYKYPKVLETAVVAMPHPTWGETPCAFVVLeksettiKEDRVDKfqTRERNLIEYCRENLPHFMCPRKVVFLEELPKN 539
Cdd:PRK08314 456 NLLYKHPAIQEACVIATPDPRRGETVKAVVVL-------RPEARGK--TTEEEIIAWAREHMAAYKYPRIVEFVDSLPKS 526
|
570
....*....|....*.
gi 15218839 540 GNGKILKPKLRDIAKG 555
Cdd:PRK08314 527 GSGKILWRQLQEQEKA 542
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
8-550 |
3.47e-58 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 205.57 E-value: 3.47e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 8 EANNVPLTPMTFLKRASECYPNRTSIIYGKT--------RFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPalyE 79
Cdd:PRK07529 19 AARDLPASTYELLSRAAARHPDAPALSFLLDadpldrpeTWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLP---E 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 80 MHFAV--PMAGAVLNPINTRLDATSIAAILRHAKPKILFLDRSF----------EALAR--ESLHLLSSEDSN-LNLPVI 144
Cdd:PRK07529 96 THFALwgGEAAGIANPINPLLEPEQIAELLRAAGAKVLVTLGPFpgtdiwqkvaEVLAAlpELRTVVEVDLARyLPGPKR 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 145 FIHENDFPKrASFEELDYECLIQRgEPTPSMVArmFRIQDEHDPISLNYTSGTTADPKGVVISHRG----AYLctLSAII 220
Cdd:PRK07529 176 LAVPLIRRK-AHARILDFDAELAR-QPGDRLFS--GRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNevanAWL--GALLL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 221 GWEMGTcpVYLWTLPMFHCNGwTFTWGTA--ARGG-----TSVCMRHvtaPEIYKN----IEMHNVTHMCCVPTVFNILL 289
Cdd:PRK07529 250 GLGPGD--TVFCGLPLFHVNA-LLVTGLAplARGAhvvlaTPQGYRG---PGVIANfwkiVERYRINFLSGVPTVYAALL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 290 K--GNSLDLSPRSGpvhVLTGGSPPPAALVKKVQ-RLGFQVMHAYGQTEAT---------GPIlfcewqdewnrlpenqq 357
Cdd:PRK07529 324 QvpVDGHDISSLRY---ALCGAAPLPVEVFRRFEaATGVRIVEGYGLTEATcvssvnppdGER----------------- 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 358 melkaRQGiSIlGL----ADVDVKNKETQKSAPRDGKT--MGEILIKGSSIMKGYLKNPKATFEAFKHGWLNTGDVGVIH 431
Cdd:PRK07529 384 -----RIG-SV-GLrlpyQRVRVVILDDAGRYLRDCAVdeVGVLCIAGPNVFSGYLEAAHNKGLWLEDGWLNTGDLGRID 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 432 PDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLeKSETTIKEDRvdkfqtrer 511
Cdd:PRK07529 457 ADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYVQL-KPGASATEAE--------- 526
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 15218839 512 nLIEYCRENLPHFMC-PRKVVFLEELPKNGNGKILKPKLR 550
Cdd:PRK07529 527 -LLAFARDHIAERAAvPKHVRILDALPKTAVGKIFKPALR 565
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
193-546 |
7.62e-58 |
|
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: 196.57 E-value: 7.62e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 193 YTSGTTADPKGVVISHRGaylcTLSAIIGW----EMGTCPVYLWTLPMFHCNGWTFTWGTA-ARGGTSVCMRHVTAPEIY 267
Cdd:cd17638 7 FTSGTTGRSKGVMCAHRQ----TLRAAAAWadcaDLTEDDRYLIINPFFHTFGYKAGIVAClLTGATVVPVAVFDVDAIL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 268 KNIEMHNVTHMCCVPTVFNILL---KGNSLDLSP-RSGpvhvLTGGSPPPAALVKKVQ-RLGFQ-VMHAYGQTEAtGPIL 341
Cdd:cd17638 83 EAIERERITVLPGPPTLFQSLLdhpGRKKFDLSSlRAA----VTGAATVPVELVRRMRsELGFEtVLTAYGLTEA-GVAT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 342 FCEwqdewnrlPENQQMELKARQGISIlglADVDVKNKETqksaprdgktmGEILIKGSSIMKGYLKNPKATFEAF-KHG 420
Cdd:cd17638 158 MCR--------PGDDAETVATTCGRAC---PGFEVRIADD-----------GEVLVRGYNVMQGYLDDPEATAEAIdADG 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 421 WLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKSETTIKE 500
Cdd:cd17638 216 WLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGVTLTEE 295
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 15218839 501 DrvdkfqtrernLIEYCRENLPHFMCPRKVVFLEELPKNGNGKILK 546
Cdd:cd17638 296 D-----------VIAWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
20-551 |
4.89e-57 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 201.00 E-value: 4.89e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 20 LKRASECYPNRTSI-IYGKTRfTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVL---NPIN 95
Cdd:PRK05605 38 YDNAVARFGDRPALdFFGATT-TYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVvehNPLY 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 96 TrldatsiAAILRH------AKPKIlFLDRS---FEALARE-------SLHLLSS----EDSNLNLPVifihendfPK-R 154
Cdd:PRK05605 117 T-------AHELEHpfedhgARVAI-VWDKVaptVERLRRTtpletivSVNMIAAmpllQRLALRLPI--------PAlR 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 155 ASFEEL--------DYECLIQRGEPTPSMVARMFRIqDEHDPISLNYTSGTTADPKGVVISHRGayLCTlSAIIG--W-- 222
Cdd:PRK05605 181 KARAALtgpapgtvPWETLVDAAIGGDGSDVSHPRP-TPDDVALILYTSGTTGKPKGAQLTHRN--LFA-NAAQGkaWvp 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 223 EMGTCP-VYLWTLPMFHCNGWTFTwGTAAR--GGTSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKG---NSLDL 296
Cdd:PRK05605 257 GLGDGPeRVLAALPMFHAYGLTLC-LTLAVsiGGELVLLPAPDIDLILDAMKKHPPTWLPGVPPLYEKIAEAaeeRGVDL 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 297 SprsGPVHVLTGGSPPPAALVKKVQRL-GFQVMHAYGQTEaTGPILFCewqdewNRLPENQqmelkaRQG-ISI-LGLAD 373
Cdd:PRK05605 336 S---GVRNAFSGAMALPVSTVELWEKLtGGLLVEGYGLTE-TSPIIVG------NPMSDDR------RPGyVGVpFPDTE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 374 VDVKNKETQKSAPRDGkTMGEILIKGSSIMKGYLKNPKATFEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENI 453
Cdd:PRK05605 400 VRIVDPEDPDETMPDG-EEGELLVRGPQVFKGYWNRPEETAKSFLDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNV 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 454 SSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKSETTIKEDrvdkfqtrernLIEYCRENLPHFMCPRKVVFL 533
Cdd:PRK05605 479 YPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPGAALDPEG-----------LRAYCREHLTRYKVPRRFYHV 547
|
570
....*....|....*...
gi 15218839 534 EELPKNGNGKILKPKLRD 551
Cdd:PRK05605 548 DELPRDQLGKVRRREVRE 565
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
58-566 |
6.67e-56 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 198.08 E-value: 6.67e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 58 SLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFLDrsfEALARESLHLLSSEDS 137
Cdd:PRK05620 58 ELGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIVAD---PRLAEQLGEILKECPC 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 138 NLNlpVIFIHENDFPKRAS-----FEELDYECLIQrGEPT----PsmvarmfrIQDEHDPISLNYTSGTTADPKGVVISH 208
Cdd:PRK05620 135 VRA--VVFIGPSDADSAAAhmpegIKVYSYEALLD-GRSTvydwP--------ELDETTAAAICYSTGTTGAPKGVVYSH 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 209 RGAYLCTLSAI----IGWEMGTcpVYLWTLPMFHcngwTFTWG---TAARGGTSVCM--RHVTAPEIYKNIE--MHNVTH 277
Cdd:PRK05620 204 RSLYLQSLSLRttdsLAVTHGE--SFLCCVPIYH----VLSWGvplAAFMSGTPLVFpgPDLSAPTLAKIIAtaMPRVAH 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 278 mcCVPTVFnILLKGNSLDLSP-RSGPVHVLTGGSPPPAALVKK-VQRLGFQVMHAYGQTEaTGPIlfcewqDEWNRLPEN 355
Cdd:PRK05620 278 --GVPTLW-IQLMVHYLKNPPeRMSLQEIYVGGSAVPPILIKAwEERYGVDVVHVWGMTE-TSPV------GTVARPPSG 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 356 QQMELKAR----QGISILGLADVDVKNKETQKSAPRDgktMGEILIKGSSIMKGYLKNPKATFEAFKH------------ 419
Cdd:PRK05620 348 VSGEARWAyrvsQGRFPASLEYRIVNDGQVMESTDRN---EGEIQVRGNWVTASYYHSPTEEGGGAAStfrgedvedand 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 420 -----GWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVL-EK 493
Cdd:PRK05620 425 rftadGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLaPG 504
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15218839 494 SETTIkedrvdkfQTRERnLIEYCRENLPHFMCPRKVVFLEELPKNGNGKILKPKLRDiakgLVVEDEINVIA 566
Cdd:PRK05620 505 IEPTR--------ETAER-LRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLRQ----HLADGDFEIIK 564
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
39-545 |
7.87e-56 |
|
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: 194.23 E-value: 7.87e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 39 RFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFLD 118
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 119 RSFEALAreslhllssedsnlnlpVIFihendfpkrasfeeldyecliqrgeptpsmvarmfriqdehdpislnYTSGTT 198
Cdd:cd05935 81 SELDDLA-----------------LIP-----------------------------------------------YTSGTT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 199 ADPKGVVISHRGAyLCTLSAIIGWEMGTCP-VYLWTLPMFHCNGWTFTWGTA-ARGGTSVCMRHVTAPEIYKNIEMHNVT 276
Cdd:cd05935 97 GLPKGCMHTHFSA-AANALQSAVWTGLTPSdVILACLPLFHVTGFVGSLNTAvYVGGTYVLMARWDRETALELIEKYKVT 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 277 HMCCVPTVFNILLkgNSLDLSPR--SGPVHVLTGGSPPPAALVKKV-QRLGFQVMHAYGQTEATGPIlfcewqdewnrlp 353
Cdd:cd05935 176 FWTNIPTMLVDLL--ATPEFKTRdlSSLKVLTGGGAPMPPAVAEKLlKLTGLRFVEGYGLTETMSQT------------- 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 354 enqQMELKARQGISILGLA--DVDVKNKETQKSAPRDGKTMGEILIKGSSIMKGYLKNPKATFEAFKH----GWLNTGDV 427
Cdd:cd05935 241 ---HTNPPLRPKLQCLGIP*fGVDARVIDIETGRELPPNEVGEIVVRGPQIFKGYWNRPEETEESFIEikgrRFFRTGDL 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 428 GVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLeKSETTIKEDrvdkfq 507
Cdd:cd05935 318 GYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVL-RPEYRGKVT------ 390
|
490 500 510
....*....|....*....|....*....|....*...
gi 15218839 508 trERNLIEYCRENLPHFMCPRKVVFLEELPKNGNGKIL 545
Cdd:cd05935 391 --EEDIIEWAREQMAAYKYPREVEFVDELPRSASGKIL 426
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
19-554 |
3.19e-55 |
|
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: 194.98 E-value: 3.19e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 19 FLKRASECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVlnPINT-- 96
Cdd:COG1021 30 LLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAI--PVFAlp 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 97 --RldATSIAAILRHAKPKILFLDRSFE-----ALARESLHLLSSedsnlnLPVIFIHeNDFPKRASFEELdYECLIQRG 169
Cdd:COG1021 108 ahR--RAEISHFAEQSEAVAYIIPDRHRgfdyrALARELQAEVPS------LRHVLVV-GDAGEFTSLDAL-LAAPADLS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 170 EPTPsmvarmfriqDEHDPISLNYTSGTTADPKGVVISHRgAYLCTL--SAII-GWEMGTcpVYLWTLPMFH-----CNG 241
Cdd:COG1021 178 EPRP----------DPDDVAFFQLSGGTTGLPKLIPRTHD-DYLYSVraSAEIcGLDADT--VYLAALPAAHnfplsSPG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 242 WTftwGTAARGGTSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILL---KGNSLDLSprSGPVhVLTGGSPPPAALVK 318
Cdd:COG1021 245 VL---GVLYAGGTVVLAPDPSPDTAFPLIERERVTVTALVPPLALLWLdaaERSRYDLS--SLRV-LQVGGAKLSPELAR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 319 KV-QRLGFQVMHAYGQTEatGPILFCEWQDewnrlPEnqqmELKAR-QG--IS------ILGLADVDVKNKETqksaprd 388
Cdd:COG1021 319 RVrPALGCTLQQVFGMAE--GLVNYTRLDD-----PE----EVILTtQGrpISpddevrIVDEDGNPVPPGEV------- 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 389 gktmGEILIKGSSIMKGYLKNPKATFEAF-KHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPK 467
Cdd:COG1021 381 ----GELLTRGPYTIRGYYRAPEHNARAFtPDGFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPA 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 468 VLETAVVAMPHPTWGETPCAFVVLEKSETTIKEdrvdkfqtrernLIEYCRE-NLPHFMCPRKVVFLEELPKNGNGKILK 546
Cdd:COG1021 457 VHDAAVVAMPDEYLGERSCAFVVPRGEPLTLAE------------LRRFLRErGLAAFKLPDRLEFVDALPLTAVGKIDK 524
|
....*...
gi 15218839 547 PKLRDIAK 554
Cdd:COG1021 525 KALRAALA 532
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
19-491 |
4.73e-55 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 196.09 E-value: 4.73e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 19 FLKRASEcYPNRTSIIY----GKTRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPI 94
Cdd:COG1022 17 LRRRAAR-FPDRVALREkedgIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVPI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 95 NTRLDATSIAAILRHAKPKILFLDrSFEALAReslhLLSSEDSNLNLPVIFIHENDfPKRASFEELDYECLIQRGEP--T 172
Cdd:COG1022 96 YPTSSAEEVAYILNDSGAKVLFVE-DQEQLDK----LLEVRDELPSLRHIVVLDPR-GLRDDPRLLSLDELLALGREvaD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 173 PSMVARMFRIQDEHDPISLNYTSGTTADPKGVVISHRgAYLCTLSAIIG-WEMGTCPVYLWTLPMFHCNGWTFTWGTAAR 251
Cdd:COG1022 170 PAELEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHR-NLLSNARALLErLPLGPGDRTLSFLPLAHVFERTVSYYALAA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 252 GGTsvcmrhVTAPEIYKNIeMHNV-----THMCCVPTVF-----NILLKGNS------------LDLSPRSGPvHVLTGG 309
Cdd:COG1022 249 GAT------VAFAESPDTL-AEDLrevkpTFMLAVPRVWekvyaGIQAKAEEagglkrklfrwaLAVGRRYAR-ARLAGK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 310 SPPP--------------------------------AALVKKVQR----LGFQVMHAYGQTEATGPILFcewqdewNRLP 353
Cdd:COG1022 321 SPSLllrlkhaladklvfsklrealggrlrfavsggAALGPELARffraLGIPVLEGYGLTETSPVITV-------NRPG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 354 ENQqmelkarqgisiLG-----LADVDVKNKETqksaprdgktmGEILIKGSSIMKGYLKNPKATFEAF-KHGWLNTGDV 427
Cdd:COG1022 394 DNR------------IGtvgppLPGVEVKIAED-----------GEILVRGPNVMKGYYKNPEATAEAFdADGWLHTGDI 450
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15218839 428 GVIHPDGHVEIKDRSKDIII-SGGENISSVEVENVLYKYPKVLETAVVA--MPHPTwgetpcAFVVL 491
Cdd:COG1022 451 GELDEDGFLRITGRKKDLIVtSGGKNVAPQPIENALKASPLIEQAVVVGdgRPFLA------ALIVP 511
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
38-555 |
1.96e-54 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 193.35 E-value: 1.96e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 38 TRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFL 117
Cdd:PRK13295 54 RRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAESKVLVV 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 118 DRSF-----EALAREslhlLSSEdsnlnLP----VIFIH---ENDFPKRASFEELDYE----CLIQRGEPTPSMVARmfr 181
Cdd:PRK13295 134 PKTFrgfdhAAMARR----LRPE-----LPalrhVVVVGgdgADSFEALLITPAWEQEpdapAILARLRPGPDDVTQ--- 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 182 iqdehdpisLNYTSGTTADPKGVVISHRGAYlctlSAIIGW----EMGTCPVYLWTLPMFHCNGWTFTWGTAARGGTSVC 257
Cdd:PRK13295 202 ---------LIYTSGTTGEPKGVMHTANTLM----ANIVPYaerlGLGADDVILMASPMAHQTGFMYGLMMPVMLGATAV 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 258 MRHVTAP-EIYKNIEMHNVTH-MCCVPTVFNILlkgNSLDLSPRsgPVHVLT----GGSPPPAALVKKVQR-LGFQVMHA 330
Cdd:PRK13295 269 LQDIWDPaRAAELIRTEGVTFtMASTPFLTDLT---RAVKESGR--PVSSLRtflcAGAPIPGALVERARAaLGAKIVSA 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 331 YGQTEaTGPILFCEWQDEWNRLPENQQ-----MELKArqgisilgladVDVKNketqksAPRDGKTMGEILIKGSSIMKG 405
Cdd:PRK13295 344 WGMTE-NGAVTLTKLDDPDERASTTDGcplpgVEVRV-----------VDADG------APLPAGQIGRLQVRGCSNFGG 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 406 YLKNPKATFEAFKhGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETP 485
Cdd:PRK13295 406 YLKRPQLNGTDAD-GWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERA 484
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 486 CAFVVLEKSETTIKEDRVDkFQTRERNLIEYcrenlphfmCPRKVVFLEELPKNGNGKILKPKLRDIAKG 555
Cdd:PRK13295 485 CAFVVPRPGQSLDFEEMVE-FLKAQKVAKQY---------IPERLVVRDALPRTPSGKIQKFRLREMLRG 544
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
51-551 |
3.65e-53 |
|
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: 187.16 E-value: 3.65e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 51 RLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILfldrsfealareslh 130
Cdd:cd05972 12 KAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAI--------------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 131 llssedsnlnlpvifihendfpkrasfeeldyecliqrgeptpsmvarmfrIQDEHDPISLNYTSGTTADPKGVVISHRG 210
Cdd:cd05972 77 ---------------------------------------------------VTDAEDPALIYFTSGTTGLPKGVLHTHSY 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 211 AY--LCTLSAIIGWEMGTCpvyLWTL--PmfhcnGW-TFTWGT----AARGGTSVC--MRHVTAPEIYKNIEMHNVTHMC 279
Cdd:cd05972 106 PLghIPTAAYWLGLRPDDI---HWNIadP-----GWaKGAWSSffgpWLLGATVFVyeGPRFDAERILELLERYGVTSFC 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 280 CVPTVFNILLKgnsLDLSPR--SGPVHVLTGGSP-PPAALVKKVQRLGFQVMHAYGQTEATGPILFCEWQDewnrlpenq 356
Cdd:cd05972 178 GPPTAYRMLIK---QDLSSYkfSHLRLVVSAGEPlNPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMP--------- 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 357 qmelkARQGiSI---LGLADVDVKNKETQKSAPrdgKTMGEILIKGS--SIMKGYLKNPKATFEAFKHGWLNTGDVGVIH 431
Cdd:cd05972 246 -----VKPG-SMgrpTPGYDVAIIDDDGRELPP---GEEGDIAIKLPppGLFLGYVGDPEKTEASIRGDYYLTGDRAYRD 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 432 PDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKSETTIKEDrvdkfqTREr 511
Cdd:cd05972 317 EDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPSEEL------AEE- 389
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 15218839 512 nLIEYCRENLPHFMCPRKVVFLEELPKNGNGKILKPKLRD 551
Cdd:cd05972 390 -LQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRVELRD 428
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
28-551 |
1.43e-52 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 187.59 E-value: 1.43e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 28 PNRTSIIYGKTR--FTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRLDATSIAA 105
Cdd:PRK13391 11 PDKPAVIMASTGevVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 106 ILRHAKPKILFLDRSFEALAREslhlLSSEDSNLNLPVIFIHENDFPKRASFEELdyeclIQRGEPTPsmvarmfrIQDE 185
Cdd:PRK13391 91 IVDDSGARALITSAAKLDVARA----LLKQCPGVRHRLVLDGDGELEGFVGYAEA-----VAGLPATP--------IADE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 186 HDPISLNYTSGTTADPKGVV-------ISHRGAYLCTLSAIIGWEMGTcpVYLWTLPMFHCNGWTFTWGTAARGGTSVCM 258
Cdd:PRK13391 154 SLGTDMLYSSGTTGRPKGIKrplpeqpPDTPLPLTAFLQRLWGFRSDM--VYLSPAPLYHSAPQRAVMLVIRLGGTVIVM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 259 RHVTAPEIYKNIEMHNVTHMCCVPTVFNILLK-----GNSLDLSPRSGPVHvltGGSPPPAaLVKK--VQRLGFQVMHAY 331
Cdd:PRK13391 232 EHFDAEQYLALIEEYGVTHTQLVPTMFSRMLKlpeevRDKYDLSSLEVAIH---AAAPCPP-QVKEqmIDWWGPIIHEYY 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 332 GQTEATGpILFCEWQdEWnrlpenqqMELKARQGISILGlaDVDVKNKETQKSAPrdgKTMGEILIKGSSIMKgYLKNPK 411
Cdd:PRK13391 308 AATEGLG-FTACDSE-EW--------LAHPGTVGRAMFG--DLHILDDDGAELPP---GEPGTIWFEGGRPFE-YLNDPA 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 412 ATFEAfKH---GWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAF 488
Cdd:PRK13391 372 KTAEA-RHpdgTWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAV 450
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15218839 489 VVLeksettikEDRVDKFQTRERNLIEYCRENLPHFMCPRKVVFLEELPKNGNGKILKPKLRD 551
Cdd:PRK13391 451 VQP--------VDGVDPGPALAAELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLRD 505
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
18-549 |
1.60e-52 |
|
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: 186.76 E-value: 1.60e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 18 TFLKRASECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVlnPINT- 96
Cdd:cd05920 19 DLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAV--PVLAl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 97 -RLDATSIAAILRHAKPKILFLDRSFEalareslhllssedsnlnlpvifihenDFPKRASFEELDYECliqrgePTPSM 175
Cdd:cd05920 97 pSHRRSELSAFCAHAEAVAYIVPDRHA---------------------------GFDHRALARELAESI------PEVAL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 176 varmfriqdehdpisLNYTSGTTADPKGVVISHRG-AYLCTLSAIIGWeMGTCPVYLWTLPMFH-----CNGwtfTWGTA 249
Cdd:cd05920 144 ---------------FLLSGGTTGTPKLIPRTHNDyAYNVRASAEVCG-LDQDTVYLAVLPAAHnfplaCPG---VLGTL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 250 ARGGTSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILL-KGNSLDLSPRSgpVHVLTGG----SPPPAALVKKVqrLG 324
Cdd:cd05920 205 LAGGRVVLAPDPSPDAAFPLIEREGVTVTALVPALVSLWLdAAASRRADLSS--LRLLQVGgarlSPALARRVPPV--LG 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 325 FQVMHAYGQTEAtgpiLFCewqdeWNRL--PENQQMElkaRQGISILGLADVDVKNKETQKSAPrdgKTMGEILIKGSSI 402
Cdd:cd05920 281 CTLQQVFGMAEG----LLN-----YTRLddPDEVIIH---TQGRPMSPDDEIRVVDEEGNPVPP---GEEGELLTRGPYT 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 403 MKGYLKNPKATFEAF-KHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTW 481
Cdd:cd05920 346 IRGYYRAPEHNARAFtPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELL 425
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15218839 482 GETPCAFVVLEKSETTIKEDRVdkfQTRERNLIEYCRenlphfmcPRKVVFLEELPKNGNGKILKPKL 549
Cdd:cd05920 426 GERSCAFVVLRDPPPSAAQLRR---FLRERGLAAYKL--------PDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
20-550 |
2.76e-52 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 187.70 E-value: 2.76e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 20 LKRASECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRLD 99
Cdd:PLN02860 13 LTRLATLRGNAVVTISGNRRRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 100 ATSIAAILRHAKPKILFLDRSFEALAresLHLLSSEDSNLNLPVI--FIHENDFPKRASFeeLDYECLIQRGEPTPSMva 177
Cdd:PLN02860 93 FEEAKSAMLLVRPVMLVTDETCSSWY---EELQNDRLPSLMWQVFleSPSSSVFIFLNSF--LTTEMLKQRALGTTEL-- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 178 rMFRIQDEhDPISLNYTSGTTADPKGVVISHRGAYLCTLS--AIIGWemGTCPVYLWTLPMFHCNGWTFTWGTAARGGTS 255
Cdd:PLN02860 166 -DYAWAPD-DAVLICFTSGTTGRPKGVTISHSALIVQSLAkiAIVGY--GEDDVYLHTAPLCHIGGLSSALAMLMVGACH 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 256 VCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSPRSGPV--HVLTGGSPPPAALVKKVQRL--GFQVMHAY 331
Cdd:PLN02860 242 VLLPKFDAKAALQAIKQHNVTSMITVPAMMADLISLTRKSMTWKVFPSvrKILNGGGSLSSRLLPDAKKLfpNAKLFSAY 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 332 GQTEATGPILFCEWQDEWNRLPENQQMELKARQGISILGLADVDVKnketqKSAPR--------DGKTMGEILIKGSSIM 403
Cdd:PLN02860 322 GMTEACSSLTFMTLHDPTLESPKQTLQTVNQTKSSSVHQPQGVCVG-----KPAPHvelkigldESSRVGRILTRGPHVM 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 404 KGYLKNPKATFEAF-KHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWG 482
Cdd:PLN02860 397 LGYWGQNSETASVLsNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLT 476
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15218839 483 ETPCAFVVLEKS---ETTIKEDRVDKFQTRERNLIEYCRE-NLPHFMCPRKVVFLEE-LPKNGNGKILKPKLR 550
Cdd:PLN02860 477 EMVVACVRLRDGwiwSDNEKENAKKNLTLSSETLRHHCREkNLSRFKIPKLFVQWRKpFPLTTTGKIRRDEVR 549
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
65-551 |
1.14e-51 |
|
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: 184.12 E-value: 1.14e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 65 DVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFLDRSFEALARESLHLLSSedsnLNLPVI 144
Cdd:cd05929 21 DVYSIALNRNARAAAAEGVWIADGVYIYLINSILTVFAAAAAWKCGACPAYKSSRAPRAEACAIIEIKAA----ALVCGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 145 FIHENDFPKRASFEEldyeclIQRGEPTPSmvarmfrIQDEHDPISLNYTSGTTADPKGVVISHRGAYLCTLsAIIGWEM 224
Cdd:cd05929 97 FTGGGALDGLEDYEA------AEGGSPETP-------IEDEAAGWKMLYSGGTTGRPKGIKRGLPGGPPDND-TLMAAAL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 225 GTCP----VYLWTLPMFHCNGWTFTWGTAARGGTSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLK-----GNSLD 295
Cdd:cd05929 163 GFGPgadsVYLSPAPLYHAAPFRWSMTALFMGGTLVLMEKFDPEEFLRLIERYRVTFAQFVPTMFVRLLKlpeavRNAYD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 296 LSPRSGPVHVltgGSPPPAALVKKVQRLGFQVMHA-YGQTEATGpiLFCEWQDEWnrlpenqqmeLKARQGISILGLADV 374
Cdd:cd05929 243 LSSLKRVIHA---AAPCPPWVKEQWIDWGGPIIWEyYGGTEGQG--LTIINGEEW----------LTHPGSVGRAVLGKV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 375 DVKNKETQKSAPRdgkTMGEILIKGSSiMKGYLKNPKATFEAF-KHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENI 453
Cdd:cd05929 308 HILDEDGNEVPPG---EIGEVYFANGP-GFEYTNDPEKTAAARnEGGWSTLGDVGYLDEDGYLYLTDRRSDMIISGGVNI 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 454 SSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVvleksETtikEDRVDKFQTRERNLIEYCRENLPHFMCPRKVVFL 533
Cdd:cd05929 384 YPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVV-----QP---APGADAGTALAEELIAFLRDRLSRYKCPRSIEFV 455
|
490
....*....|....*...
gi 15218839 534 EELPKNGNGKILKPKLRD 551
Cdd:cd05929 456 AELPRDDTGKLYRRLLRD 473
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
40-548 |
4.16e-51 |
|
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: 182.02 E-value: 4.16e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 40 FTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFLDr 119
Cdd:cd05907 6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFVE- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 120 sfealareslhllssedsnlnlpvifihendfpkrasfeeldyecliqrgepTPSmvarmfriqdehDPISLNYTSGTTA 199
Cdd:cd05907 85 ----------------------------------------------------DPD------------DLATIIYTSGTTG 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 200 DPKGVVISHRGAYLCTLSAIIGWEMGTCPVYLWTLPMFHCNGWTF-TWGTAARGgtsVCMRHVTAPE-IYKNIEMHNVTH 277
Cdd:cd05907 101 RPKGVMLSHRNILSNALALAERLPATEGDRHLSFLPLAHVFERRAgLYVPLLAG---ARIYFASSAEtLLDDLSEVRPTV 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 278 MCCVPTVFNILLKGNSLDLSPR---------SGP--VHVLTGGSPPPAALVKKVQRLGFQVMHAYGQTEATGPILFCEWQ 346
Cdd:cd05907 178 FLAVPRVWEKVYAAIKVKAVPGlkrklfdlaVGGrlRFAASGGAPLPAELLHFFRALGIPVYEGYGLTETSAVVTLNPPG 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 347 DewNRLpenqqmelkARQGISILGladVDVKNKETqksaprdgktmGEILIKGSSIMKGYLKNPKATFEAFKH-GWLNTG 425
Cdd:cd05907 258 D--NRI---------GTVGKPLPG---VEVRIADD-----------GEILVRGPNVMLGYYKNPEATAEALDAdGWLHTG 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 426 DVGVIHPDGHVEIKDRSKDIII-SGGENISSVEVENVLYKYPKVLETAVVA--MPHPTwgetpcAFVVLE-------KSE 495
Cdd:cd05907 313 DLGEIDEDGFLHITGRKKDLIItSGGKNISPEPIENALKASPLISQAVVIGdgRPFLV------ALIVPDpealeawAEE 386
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15218839 496 TTIKEDRVDKFQTRE--RNLIE--YCREN--LPHFMCPRKVVFLEELPKNGNGKI---LKPK 548
Cdd:cd05907 387 HGIAYTDVAELAANPavRAEIEaaVEAANarLSRYEQIKKFLLLPEPFTIENGELtptLKLK 448
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
59-552 |
2.92e-50 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 182.35 E-value: 2.92e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 59 LNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFLdrsfealARESLHLLSSedsn 138
Cdd:PLN02574 87 MGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFT-------SPENVEKLSP---- 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 139 LNLPVIFIHEN-DFPKRASFEELDYECLIQRGEPTPSMVARmfriqdEHDPISLNYTSGTTADPKGVVISHRGaYLCTLS 217
Cdd:PLN02574 156 LGVPVIGVPENyDFDSKRIEFPKFYELIKEDFDFVPKPVIK------QDDVAAIMYSSGTTGASKGVVLTHRN-LIAMVE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 218 AIIGWEM------GTCPVYLWTLPMFHCNGWT-FTWGTAARGGTSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLK 290
Cdd:PLN02574 229 LFVRFEAsqyeypGSDNVYLAALPMFHIYGLSlFVVGLLSLGSTIVVMRRFDASDMVKVIDRFKVTHFPVVPPILMALTK 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 291 ------GNSLDlsprsGPVHVLTGGSPPPAALVKK-VQRLG-FQVMHAYGQTEATGPilfcewqdewnrlpENQQMELKA 362
Cdd:PLN02574 309 kakgvcGEVLK-----SLKQVSCGAAPLSGKFIQDfVQTLPhVDFIQGYGMTESTAV--------------GTRGFNTEK 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 363 RQGISILGLADVDVKNK----ETQKSAPRDGKtmGEILIKGSSIMKGYLKNPKAT-FEAFKHGWLNTGDVGVIHPDGHVE 437
Cdd:PLN02574 370 LSKYSSVGLLAPNMQAKvvdwSTGCLLPPGNC--GELWIQGPGVMKGYLNNPKATqSTIDKDGWLRTGDIAYFDEDGYLY 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 438 IKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVlEKSETTIKEDRVdkfqtrernlIEYC 517
Cdd:PLN02574 448 IVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVV-RRQGSTLSQEAV----------INYV 516
|
490 500 510
....*....|....*....|....*....|....*
gi 15218839 518 RENLPHFMCPRKVVFLEELPKNGNGKILKPKLRDI 552
Cdd:PLN02574 517 AKQVAPYKKVRKVVFVQSIPKSPAGKILRRELKRS 551
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
19-549 |
2.10e-49 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 179.84 E-value: 2.10e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 19 FLKRASECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRL 98
Cdd:PRK06710 29 YVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLY 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 99 DATSIAAILRHAKPK-ILFLDRSFEALAR-----ESLHLLSSEDSNL-----NLPVIFIHENDFPKRASFEELDYECLIQ 167
Cdd:PRK06710 109 TERELEYQLHDSGAKvILCLDLVFPRVTNvqsatKIEHVIVTRIADFlpfpkNLLYPFVQKKQSNLVVKVSESETIHLWN 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 168 RGEPTPSMVARMFrIQDEHDPISLNYTSGTTADPKGVVISHRGAYLCTLSAIiGWeMGTC----PVYLWTLPMFHCNGWT 243
Cdd:PRK06710 189 SVEKEVNTGVEVP-CDPENDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGV-QW-LYNCkegeEVVLGVLPFFHVYGMT 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 244 FTWG-TAARGGTSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSPRSGPVHVLTGGSPPPAALVKKVQR 322
Cdd:PRK06710 266 AVMNlSIMQGYKMVLIPKFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIRACISGSAPLPVEVQEKFET 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 323 L-GFQVMHAYGQTEATgPILFCEWQDEwNRLPENqqmelkarqgisiLGL----ADVDVKNKETQKSAPRDgkTMGEILI 397
Cdd:PRK06710 346 VtGGKLVEGYGLTESS-PVTHSNFLWE-KRVPGS-------------IGVpwpdTEAMIMSLETGEALPPG--EIGEIVV 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 398 KGSSIMKGYLKNPKATFEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMP 477
Cdd:PRK06710 409 KGPQIMKGYWNKPEETAAVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVP 488
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15218839 478 HPTWGETPCAFVVLeKSETTIKEDRVDKFqtrernlieyCRENLPHFMCPRKVVFLEELPKNGNGKILKPKL 549
Cdd:PRK06710 489 DPYRGETVKAFVVL-KEGTECSEEELNQF----------ARKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
39-551 |
2.36e-49 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 178.08 E-value: 2.36e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 39 RFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFLD 118
Cdd:PRK09088 22 RWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLLLGD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 119 RSFEALARESLHLlssedsnlnlpvifiheNDFPKRASFEELDyecliqrgePTPSMvarmfriqDEHDPISLNYTSGTT 198
Cdd:PRK09088 102 DAVAAGRTDVEDL-----------------AAFIASADALEPA---------DTPSI--------PPERVSLILFTSGTS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 199 ADPKGVVISHRGAYLCTLSAIIGWEMGTCPVYLWTLPMFHCNGW-TFTWGTAARGGT---------SVCMRHVTAPEIyk 268
Cdd:PRK09088 148 GQPKGVMLSERNLQQTAHNFGVLGRVDAHSSFLCDAPMFHIIGLiTSVRPVLAVGGSilvsngfepKRTLGRLGDPAL-- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 269 niemhNVTHMCCVPTVFNILLKGNSLDLSPRSGPVHVLTGGSPPPAALVKKVQRLGFQVMHAYGQTEAtGPILfcewqde 348
Cdd:PRK09088 226 -----GITHYFCVPQMAQAFRAQPGFDAAALRHLTALFTGGAPHAAEDILGWLDDGIPMVDGFGMSEA-GTVF------- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 349 wnRLPENQQMeLKARQGISIL-----GLADVDVKNKETQKSAPrdgktmGEILIKGSSIMKGYLKNPKATFEAF-KHGWL 422
Cdd:PRK09088 293 --GMSVDCDV-IRAKAGAAGIptptvQTRVVDDQGNDCPAGVP------GELLLRGPNLSPGYWRRPQATARAFtGDGWF 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 423 NTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKSETTIKEDr 502
Cdd:PRK09088 364 RTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAPLDLER- 442
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 15218839 503 vdkfqtrernLIEYCRENLPHFMCPRKVVFLEELPKNGNGKILKPKLRD 551
Cdd:PRK09088 443 ----------IRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLRD 481
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
9-550 |
2.48e-48 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 176.32 E-value: 2.48e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 9 ANNVPLTPMTFlKRASEcYPNRTSIIYGKT--RFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPM 86
Cdd:PLN02246 20 PNHLPLHDYCF-ERLSE-FSDRPCLIDGATgrVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 87 AGAVL---NPINTrldATSIAAILRHAKPKILFLdrsfEALARESLHLLSSEDsnlNLPVIFIHEnDFPKRASFEELdye 163
Cdd:PLN02246 98 RGAVTttaNPFYT---PAEIAKQAKASGAKLIIT----QSCYVDKLKGLAEDD---GVTVVTIDD-PPEGCLHFSEL--- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 164 clIQRGEPTPSMVArmfrIQDEhDPISLNYTSGTTADPKGVVISHRGAYLCTLSAIIG----WEMGTCPVYLWTLPMFHC 239
Cdd:PLN02246 164 --TQADENELPEVE----ISPD-DVVALPYSSGTTGLPKGVMLTHKGLVTSVAQQVDGenpnLYFHSDDVILCVLPMFHI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 240 NGWTFTWGTAAR-GGTSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKG---NSLDLSP-RSgpvhVLTGGSPppa 314
Cdd:PLN02246 237 YSLNSVLLCGLRvGAAILIMPKFEIGALLELIQRHKVTIAPFVPPIVLAIAKSpvvEKYDLSSiRM----VLSGAAP--- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 315 aLVKKVQR----------LGfqvmHAYGQTEAtGPIL-----FCEwqdewnrlpenQQMELKARQGISILGLADVDVKNK 379
Cdd:PLN02246 310 -LGKELEDafraklpnavLG----QGYGMTEA-GPVLamclaFAK-----------EPFPVKSGSCGTVVRNAELKIVDP 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 380 ETQKSAPRDgkTMGEILIKGSSIMKGYLKNPKATFEAF-KHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEV 458
Cdd:PLN02246 373 ETGASLPRN--QPGEICIRGPQIMKGYLNDPEATANTIdKDGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAEL 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 459 ENVLYKYPKVLETAVVAMPHPTWGETPCAFVVleKSE-TTIKEDRVDKFQTRErnLIEYCRENlphfmcprKVVFLEELP 537
Cdd:PLN02246 451 EALLISHPSIADAAVVPMKDEVAGEVPVAFVV--RSNgSEITEDEIKQFVAKQ--VVFYKRIH--------KVFFVDSIP 518
|
570
....*....|...
gi 15218839 538 KNGNGKILKPKLR 550
Cdd:PLN02246 519 KAPSGKILRKDLR 531
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
25-550 |
4.19e-48 |
|
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: 175.25 E-value: 4.19e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 25 ECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRLDATSIA 104
Cdd:cd05959 15 EGRGDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 105 AILRHAKPKILFLDRSFEALARESLHLLSSEDSNLNLPVifihendfPKRASFEELDYECLIQRGEPTPSMVArmfriQD 184
Cdd:cd05959 95 YYLEDSRARVVVVSGELAPVLAAALTKSEHTLVVLIVSG--------GAGPEAGALLLAELVAAEAEQLKPAA-----TH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 185 EHDPISLNYTSGTTADPKGVVISHRG-AYLCTLSA--IIGWEMGTcpVYLWTLPMFHC----NGWTFTWGTaarGGTSVC 257
Cdd:cd05959 162 ADDPAFWLYSSGSTGRPKGVVHLHADiYWTAELYArnVLGIREDD--VCFSAAKLFFAyglgNSLTFPLSV---GATTVL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 258 M-RHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGnslDLSPRSGPVHV---LTGGSPPPAALVKKVQ-RLGFQVMHAYG 332
Cdd:cd05959 237 MpERPTPAAVFKRIRRYRPTVFFGVPTLYAAMLAA---PNLPSRDLSSLrlcVSAGEALPAEVGERWKaRFGLDILDGIG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 333 QTEATGpiLFCEwqdewNRlPEnqqmelKARQGISILGLADVDVKNKETQKSAPRDGKTmGEILIKGSSIMKGYLKNPKA 412
Cdd:cd05959 314 STEMLH--IFLS-----NR-PG------RVRYGTTGKPVPGYEVELRDEDGGDVADGEP-GELYVRGPSSATMYWNNRDK 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 413 TFEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLe 492
Cdd:cd05959 379 TRDTFQGEWTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVL- 457
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 15218839 493 KSETTIKEdrvdkfqTRERNLIEYCRENLPHFMCPRKVVFLEELPKNGNGKILKPKLR 550
Cdd:cd05959 458 RPGYEDSE-------ALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
28-544 |
9.30e-48 |
|
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: 172.71 E-value: 9.30e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 28 PNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRLDATSIAAIL 107
Cdd:cd05930 1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 108 RHAKPKILFLDRSfealareslhllssedsnlNLPVIFihendfpkrasfeeldyecliqrgeptpsmvarmfriqdehd 187
Cdd:cd05930 81 EDSGAKLVLTDPD-------------------DLAYVI------------------------------------------ 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 188 pislnYTSGTTADPKGVVISHRG--AYLCTLSAIIGweMGTCPVYL-WTLPMFHCNGWTFtWGTAARGGTSVCMR---HV 261
Cdd:cd05930 100 -----YTSGSTGKPKGVMVEHRGlvNLLLWMQEAYP--LTPGDRVLqFTSFSFDVSVWEI-FGALLAGATLVVLPeevRK 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 262 TAPEIYKNIEMHNVTHMCCVPTVFNILLkgNSLDLSPRSGPVHVLTGGSPPPAALVKKVQRLGF--QVMHAYGQTEATGP 339
Cdd:cd05930 172 DPEALADLLAEEGITVLHLTPSLLRLLL--QELELAALPSLRLVLVGGEALPPDLVRRWRELLPgaRLVNLYGPTEATVD 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 340 ILFCewqdewnRLPEnqqmELKARQGISIlG--LADVDV----KNKETQKsaprDGKtMGEILIKGSSIMKGYLKNPKAT 413
Cdd:cd05930 250 ATYY-------RVPP----DDEEDGRVPI-GrpIPNTRVyvldENLRPVP----PGV-PGELYIGGAGLARGYLNRPELT 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 414 FEAFKHGWLN-------TGDVGVIHPDGHVEIKDRSKDII-ISG-----GEnissveVENVLYKYPKVLETAVVAMPHPT 480
Cdd:cd05930 313 AERFVPNPFGpgermyrTGDLVRWLPDGNLEFLGRIDDQVkIRGyrielGE------IEAALLAHPGVREAAVVAREDGD 386
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15218839 481 WGETPCAFVVLEKSETTIKEDrvdkfqtrernLIEYCRENLPHFMCPRKVVFLEELPKNGNGKI 544
Cdd:cd05930 387 GEKRLVAYVVPDEGGELDEEE-----------LRAHLAERLPDYMVPSAFVVLDALPLTPNGKV 439
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
22-561 |
1.20e-47 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 174.94 E-value: 1.20e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 22 RASECYPNRTSIIYGK-TRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRLDA 100
Cdd:PRK06087 31 QTARAMPDKIAVVDNHgASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWRE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 101 TSIAAILRHAKPKILFLDRSFEALARESLHLLSSEDSNLNLPVIFIHENdfpkRASFEELDYECLIQRGEP--TPSMVar 178
Cdd:PRK06087 111 AELVWVLNKCQAKMFFAPTLFKQTRPVDLILPLQNQLPQLQQIVGVDKL----APATSSLSLSQIIADYEPltTAITT-- 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 179 mfriqDEHDPISLNYTSGTTADPKGVVISHRG------AYLCTLSaiIGWEmgtcPVYLWTLPMFHCNGwtFTWGTAAR- 251
Cdd:PRK06087 185 -----HGDELAAVLFTSGTEGLPKGVMLTHNNilaserAYCARLN--LTWQ----DVFMMPAPLGHATG--FLHGVTAPf 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 252 --GGTSVCMRHVTAPEIYKNIEMHNVT-HMCCVPTVFNILlkgNSLDlsprSGPVHV------LTGGSPPPAALVKKVQR 322
Cdd:PRK06087 252 liGARSVLLDIFTPDACLALLEQQRCTcMLGATPFIYDLL---NLLE----KQPADLsalrffLCGGTTIPKKVARECQQ 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 323 LGFQVMHAYGQTEATgPILFCEWQD--EWNrlpenqqmelKARQGISILGLaDVDVKNKETQKSAPrdgKTMGEILIKGS 400
Cdd:PRK06087 325 RGIKLLSVYGSTESS-PHAVVNLDDplSRF----------MHTDGYAAAGV-EIKVVDEARKTLPP---GCEGEEASRGP 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 401 SIMKGYLKNPKATFEAF-KHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHP 479
Cdd:PRK06087 390 NVFMGYLDEPELTARALdEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDE 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 480 TWGETPCAFVVLEKSETTIKEDRVDKFqtrernlieYCRENLPHFMCPRKVVFLEELPKNGNGKILKPKLR-DIAKGLVV 558
Cdd:PRK06087 470 RLGERSCAYVVLKAPHHSLTLEEVVAF---------FSRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRkDIMRRLTQ 540
|
...
gi 15218839 559 EDE 561
Cdd:PRK06087 541 DVC 543
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
23-551 |
6.03e-47 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 172.64 E-value: 6.03e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 23 ASECyPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRLDATS 102
Cdd:PRK13382 53 AQRC-PDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 103 IAAILRHAKPKILFLDRSFEALARESL----HLLSSEDSNlnlpvifihenDFPKRASFEELDYECLIQRGEPTPsmvaR 178
Cdd:PRK13382 132 LAEVVTREGVDTVIYDEEFSATVDRALadcpQATRIVAWT-----------DEDHDLTVEVLIAAHAGQRPEPTG----R 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 179 MFRIqdehdpISLnyTSGTTADPKGVVISHRGAYLcTLSAI---IGWEMGTcPVYLwTLPMFHcngwtfTWG-----TAA 250
Cdd:PRK13382 197 KGRV------ILL--TSGTTGTPKGARRSGPGGIG-TLKAIldrTPWRAEE-PTVI-VAPMFH------AWGfsqlvLAA 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 251 RGGTSVCMRHVTAPE-IYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSPRSGPV--HVLTGGSP-PPAALVKKVQRLGFQ 326
Cdd:PRK13382 260 SLACTIVTRRRFDPEaTLDLIDRHRATGLAVVPVMFDRIMDLPAEVRNRYSGRSlrFAAASGSRmRPDVVIAFMDQFGDV 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 327 VMHAYGQTEAtGPILFCEwQDEWNRLPENQQmelKARQG--ISILGLADVDVKNKETqksaprdgktmGEILIKGSSIMK 404
Cdd:PRK13382 340 IYNNYNATEA-GMIATAT-PADLRAAPDTAG---RPAEGteIRILDQDFREVPTGEV-----------GTIFVRNDTQFD 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 405 GYlkNPKATFEaFKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGET 484
Cdd:PRK13382 404 GY--TSGSTKD-FHDGFMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQR 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15218839 485 PCAFVVLEksettikedrvDKFQTRERNLIEYCRENLPHFMCPRKVVFLEELPKNGNGKILKPKLRD 551
Cdd:PRK13382 481 LAAFVVLK-----------PGASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQA 536
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
27-550 |
1.59e-46 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 171.02 E-value: 1.59e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 27 YPNRTSIIY----GKTR-FTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRLDAT 101
Cdd:PRK08008 20 YGHKTALIFessgGVVRrYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLRE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 102 SIAAILRHAKPKILFLDRSFEALARESLHllsSEDSNLN-LPVIFIHENDFPKRASFEELdyecliqRGEPTPSMvarmf 180
Cdd:PRK08008 100 ESAWILQNSQASLLVTSAQFYPMYRQIQQ---EDATPLRhICLTRVALPADDGVSSFTQL-------KAQQPATL----- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 181 riqDEHDPISLN------YTSGTTADPKGVVISH--------RGAYLCTLSAiigwemgtCPVYLWTLPMFH----CNGW 242
Cdd:PRK08008 165 ---CYAPPLSTDdtaeilFTSGTTSRPKGVVITHynlrfagyYSAWQCALRD--------DDVYLTVMPAFHidcqCTAA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 243 --TFTwgtaaRGGTSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLkgnsldlsprsgpvhvltggSPPPAALVKK- 319
Cdd:PRK08008 234 maAFS-----AGATFVLLEKYSARAFWGQVCKYRATITECIPMMIRTLM--------------------VQPPSANDRQh 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 320 -------------------VQRLGFQVMHAYGQTEATGPILFCEWQDEwNRLPEnqqmelKARQGISIlglaDVDVKNKE 380
Cdd:PRK08008 289 clrevmfylnlsdqekdafEERFGVRLLTSYGMTETIVGIIGDRPGDK-RRWPS------IGRPGFCY----EAEIRDDH 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 381 TQKSAPrdgKTMGEILIKG---SSIMKGYLKNPKATFEAFK-HGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSV 456
Cdd:PRK08008 358 NRPLPA---GEIGEICIKGvpgKTIFKEYYLDPKATAKVLEaDGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCV 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 457 EVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKSETTIKEDrvdkfqtrernLIEYCRENLPHFMCPRKVVFLEEL 536
Cdd:PRK08008 435 ELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEE-----------FFAFCEQNMAKFKVPSYLEIRKDL 503
|
570
....*....|....
gi 15218839 537 PKNGNGKILKPKLR 550
Cdd:PRK08008 504 PRNCSGKIIKKNLK 517
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
23-552 |
1.92e-46 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 171.26 E-value: 1.92e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 23 ASECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRLDATS 102
Cdd:PRK07788 58 AARRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQ 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 103 IAAILRHAKPKILFLDRSFEALAReslhllSSEDSNLNLPVIFIH-ENDFPKRASFEELDYecLIQRGEPTPSMVARmfr 181
Cdd:PRK07788 138 LAEVAAREGVKALVYDDEFTDLLS------ALPPDLGRLRAWGGNpDDDEPSGSTDETLDD--LIAGSSTAPLPKPP--- 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 182 iqdEHDPISLnYTSGTTADPKGVVISHRGAyLCTLSAI---IGWEMGTcpVYLWTLPMFHCNGW-TFTWGTAArGGTSVC 257
Cdd:PRK07788 207 ---KPGGIVI-LTSGTTGTPKGAPRPEPSP-LAPLAGLlsrVPFRAGE--TTLLPAPMFHATGWaHLTLAMAL-GSTVVL 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 258 MRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLK-----GNSLDLSprSGPVhVLTGGSPPPAALVKKVQ-RLGFQVMHAY 331
Cdd:PRK07788 279 RRRFDPEATLEDIAKHKATALVVVPVMLSRILDlgpevLAKYDTS--SLKI-IFVSGSALSPELATRALeAFGPVLYNLY 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 332 GQTE---AT--GPilfcewqDEWNRLPenqqmelkarqgiSILGLADVDVKNK---ETQKSAPRDgkTMGEILIKGSSIM 403
Cdd:PRK07788 356 GSTEvafATiaTP-------EDLAEAP-------------GTVGRPPKGVTVKildENGNEVPRG--VVGRIFVGNGFPF 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 404 KGYL--KNPKAtfeafKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTW 481
Cdd:PRK07788 414 EGYTdgRDKQI-----IDGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEF 488
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15218839 482 GETPCAFVVLEKSETtikedrVDKFQTRernliEYCRENLPHFMCPRKVVFLEELPKNGNGKILKPKLRDI 552
Cdd:PRK07788 489 GQRLRAFVVKAPGAA------LDEDAIK-----DYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELREM 548
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
193-550 |
4.07e-46 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 169.01 E-value: 4.07e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 193 YTSGTTADPKGVVIShRGAYLCTLSAII-GWEmgtcpvylWT--------LPMFHCNGWTF-TWGTAARGGTsvcMRHVT 262
Cdd:PRK07787 135 YTSGTTGPPKGVVLS-RRAIAADLDALAeAWQ--------WTaddvlvhgLPLFHVHGLVLgVLGPLRIGNR---FVHTG 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 263 --APEIYKNIEMHNVTHMCCVPTVFNILlkGNSLDLSPRSGPVHVLTGGSPP-PAALVKKVQRL-GFQVMHAYGQTE--- 335
Cdd:PRK07787 203 rpTPEAYAQALSEGGTLYFGVPTVWSRI--AADPEAARALRGARLLVSGSAAlPVPVFDRLAALtGHRPVERYGMTEtli 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 336 -----ATGPilfcewqdewnrlpenqqmelkARQGISILGLADVDVK-NKETQKSAPRDGKTMGEILIKGSSIMKGYLKN 409
Cdd:PRK07787 281 tlstrADGE----------------------RRPGWVGLPLAGVETRlVDEDGGPVPHDGETVGELQVRGPTLFDGYLNR 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 410 PKATFEAF-KHGWLNTGDVGVIHPDGHVEIKDR-SKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCA 487
Cdd:PRK07787 339 PDATAAAFtADGWFRTGDVAVVDPDGMHRIVGReSTDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVA 418
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15218839 488 FVVleksettiKEDRVDkfqtrERNLIEYCRENLPHFMCPRKVVFLEELPKNGNGKILKPKLR 550
Cdd:PRK07787 419 YVV--------GADDVA-----ADELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLL 468
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
30-550 |
1.68e-45 |
|
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: 166.48 E-value: 1.68e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 30 RTSIIYGKTRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRLDATSIAAILRH 109
Cdd:cd05919 1 KTAFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 110 AKPKILFldRSFEALAreslhllssedsnlnlpvifihendfpkrasfeeldyecliqrgeptpsmvarmfriqdehdpi 189
Cdd:cd05919 81 CEARLVV--TSADDIA---------------------------------------------------------------- 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 190 SLNYTSGTTADPKGVVISHRGAYL-------------------CTLSAIIGWEMGtcpvylwtlpmfhcNGWTFTWGTaa 250
Cdd:cd05919 95 YLLYSSGTTGPPKGVMHAHRDPLLfadamarealgltpgdrvfSSAKMFFGYGLG--------------NSLWFPLAV-- 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 251 rGGTSVCMRH-VTAPEIYKNIEMHNVTHMCCVPTVFNILLKgnSLDLSPR--SGPVHVLTGGSPPPAALVKK-VQRLGFQ 326
Cdd:cd05919 159 -GASAVLNPGwPTAERVLATLARFRPTVLYGVPTFYANLLD--SCAGSPDalRSLRLCVSAGEALPRGLGERwMEHFGGP 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 327 VMHAYGQTEaTGPILFCEWQDEWN------RLPeNQQMELKARQGisilgladvdvknketqKSAPRDgkTMGEILIKGS 400
Cdd:cd05919 236 ILDGIGATE-VGHIFLSNRPGAWRlgstgrPVP-GYEIRLVDEEG-----------------HTIPPG--EEGDLLVRGP 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 401 SIMKGYLKNPKATFEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPT 480
Cdd:cd05919 295 SAAVGYWNNPEKSRATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPEST 374
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 481 WGETPCAFVVLeKSETTIKEDRVdkfqtreRNLIEYCRENLPHFMCPRKVVFLEELPKNGNGKILKPKLR 550
Cdd:cd05919 375 GLSRLTAFVVL-KSPAAPQESLA-------RDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
187-544 |
2.71e-45 |
|
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: 163.21 E-value: 2.71e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 187 DPISLNYTSGTTADPKGVVISHRGAYLCTLSAIIGWEMGTCPVYLWTLPMFHCNGWTFTWGTAARGGTSVCMRHVTAPEI 266
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAGLNLALATFHAGGANVVMEKFDPAEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 267 YKNIEMHNVTHMCCVPTV-FNIL--LKGNSLDLSPRSgpvHVLTGGSPPPAALVKKVQRLGFQVMhaYGQTEATGPILFC 343
Cdd:cd17637 81 LELIEEEKVTLMGSFPPIlSNLLdaAEKSGVDLSSLR---HVLGLDAPETIQRFEETTGATFWSL--YGQTETSGLVTLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 344 EWQDewnrlpenqqmelkaRQGIS--ILGLADVDVKNkETQKSAPRdGKTmGEILIKGSSIMKGYLKNPKATFEAFKHGW 421
Cdd:cd17637 156 PYRE---------------RPGSAgrPGPLVRVRIVD-DNDRPVPA-GET-GEIVVRGPLVFQGYWNLPELTAYTFRNGW 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 422 LNTGDVGVIHPDGHVEIKDRS--KDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLeKSETTIK 499
Cdd:cd17637 218 HHTGDLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVL-KPGATLT 296
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 15218839 500 EDrvdkfqtrerNLIEYCRENLPHFMCPRKVVFLEELPKNGNGKI 544
Cdd:cd17637 297 AD----------ELIEFVGSRIARYKKPRYVVFVEALPKTADGSI 331
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
33-551 |
3.74e-43 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 161.40 E-value: 3.74e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 33 IIYGKTRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKP 112
Cdd:PRK12406 5 IISGDRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 113 KILF----LDRSFEALARESLHLLSSEDSNLNLPVIFIHENDFPKRASfeELDYECLIQRGEPTPSMVARmfriqdehDP 188
Cdd:PRK12406 85 RVLIahadLLHGLASALPAGVTVLSVPTPPEIAAAYRISPALLTPPAG--AIDWEGWLAQQEPYDGPPVP--------QP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 189 ISLNYTSGTTADPKGV-----VISHRGAYLCTLSAIIGWEMGTcpVYLWTLPMFHCNGWTFTWGTAARGGTSVCMRHVTA 263
Cdd:PRK12406 155 QSMIYTSGTTGHPKGVrraapTPEQAAAAEQMRALIYGLKPGI--RALLTGPLYHSAPNAYGLRAGRLGGVLVLQPRFDP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 264 PEIYKNIEMHNVTHMCCVPTVFNILLK-----GNSLDLSPRSgpvHVLTGGSPPPAAlVKK--VQRLGFQVMHAYGQTEa 336
Cdd:PRK12406 233 EELLQLIERHRITHMHMVPTMFIRLLKlpeevRAKYDVSSLR---HVIHAAAPCPAD-VKRamIEWWGPVIYEYYGSTE- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 337 TGPILFCEWQDeWNRLPENQQmelKARQGISilgLADVDVKNKETQKSAPrdgktmGEILIKGSSIMK-GYLKNPKATFE 415
Cdd:PRK12406 308 SGAVTFATSED-ALSHPGTVG---KAAPGAE---LRFVDEDGRPLPQGEI------GEIYSRIAGNPDfTYHNKPEKRAE 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 416 AFKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEK-- 493
Cdd:PRK12406 375 IDRGGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPga 454
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 494 --SETTIKedrvdkfqtrernliEYCRENLPHFMCPRKVVFLEELPKNGNGKILKPKLRD 551
Cdd:PRK12406 455 tlDEADIR---------------AQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLRD 499
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
25-549 |
2.40e-42 |
|
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: 157.79 E-value: 2.40e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 25 ECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRLDATSIA 104
Cdd:cd05945 2 AANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 105 AILRHAKPKILfldrsfealareslhllssedsnlnlpvifihendfpkrasfeeldyecliqrgeptpsmvarmfrIQD 184
Cdd:cd05945 82 EILDAAKPALL------------------------------------------------------------------IAD 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 185 EHDPISLNYTSGTTADPKGVVISHRGaylctLSAIIGWE-----MGTCPVYLWTLPmFHCNGWTFTW-GTAARGGTSVCM 258
Cdd:cd05945 96 GDDNAYIIFTSGSTGRPKGVQISHDN-----LVSFTNWMlsdfpLGPGDVFLNQAP-FSFDLSVMDLyPALASGATLVPV 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 259 RHvtapEIYKN-------IEMHNVTHMCCVPTVFNILLKgnSLDLSPRSGP--VHVLTGGSPPPAALVKKVQRL--GFQV 327
Cdd:cd05945 170 PR----DATADpkqlfrfLAEHGITVWVSTPSFAAMCLL--SPTFTPESLPslRHFLFCGEVLPHKTARALQQRfpDARI 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 328 MHAYGQTEATGPILFCEWQDE----WNRLPenqqmelkarqgisiLGLADVDVKNK-ETQKSAPRDGKTMGEILIKGSSI 402
Cdd:cd05945 244 YNTYGPTEATVAVTYIEVTPEvldgYDRLP---------------IGYAKPGAKLViLDEDGRPVPPGEKGELVISGPSV 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 403 MKGYLKNPKATFEAF----KHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPH 478
Cdd:cd05945 309 SKGYLNNPEKTAAAFfpdeGQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYK 388
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15218839 479 PTWGETPCAFVVLEKSettikedrVDKFQTRErnLIEYCRENLPHFMCPRKVVFLEELPKNGNGKILKPKL 549
Cdd:cd05945 389 GEKVTELIAFVVPKPG--------AEAGLTKA--IKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
39-556 |
2.80e-42 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 158.89 E-value: 2.80e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 39 RFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTP---ALYemhFAVPMAGAVLNPINTRLDATSIAAILRHAKPKIL 115
Cdd:PRK07514 28 RYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPealALY---LATLRAGAVFLPLNTAYTLAELDYFIGDAEPALV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 116 FLD-RSFEALARESlhllssedSNLNLPVIFIHENDfpKRASFEELdyecliQRGEPTP-SMVARmfriqDEHDPISLNY 193
Cdd:PRK07514 105 VCDpANFAWLSKIA--------AAAGAPHVETLDAD--GTGSLLEA------AAAAPDDfETVPR-----GADDLAAILY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 194 TSGTTADPKGVVISHR--GAYLCTLSAIIGWEMGTcpVYLWTLPMFHCNGwTF--TWGTAARGGTSVCMRHVTAPEIYKn 269
Cdd:PRK07514 164 TSGTTGRSKGAMLSHGnlLSNALTLVDYWRFTPDD--VLIHALPIFHTHG-LFvaTNVALLAGASMIFLPKFDPDAVLA- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 270 iEMHNVTHMCCVPTVFNILLKGNSLDlspRSGPVHV--LTGGSPPPAALVKKV--QRLGFQVMHAYGQTEaTGPILFCEW 345
Cdd:PRK07514 240 -LMPRATVMMGVPTFYTRLLQEPRLT---REAAAHMrlFISGSAPLLAETHREfqERTGHAILERYGMTE-TNMNTSNPY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 346 QDEwnRLPenqqmelkarqGISILGLADVDVK--NKETQKSAPRDGktMGEILIKGSSIMKGYLKNPKATFEAFKH-GWL 422
Cdd:PRK07514 315 DGE--RRA-----------GTVGFPLPGVSLRvtDPETGAELPPGE--IGMIEVKGPNVFKGYWRMPEKTAEEFRAdGFF 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 423 NTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKSETtikedr 502
Cdd:PRK07514 380 ITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPGAA------ 453
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 15218839 503 VDkfqtrERNLIEYCRENLPHFMCPRKVVFLEELPKNGNGKILKPKLRDIAKGL 556
Cdd:PRK07514 454 LD-----EAAILAALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLLREQYADL 502
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
37-552 |
2.98e-42 |
|
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: 159.23 E-value: 2.98e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 37 KTRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTpalyeMHFAVPM-----AGAVLNPINTRLDATSIAAILRHAK 111
Cdd:cd17642 42 GVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENS-----LQFFLPViaglfIGVGVAPTNDIYNERELDHSLNISK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 112 PKILF-----LDRSFEALAR----ESLHLLSSEDSNLNLPVI--FIHENDFPkraSFEELDYecliqrgepTPSMVARmf 180
Cdd:cd17642 117 PTIVFcskkgLQKVLNVQKKlkiiKTIIILDSKEDYKGYQCLytFITQNLPP---GFNEYDF---------KPPSFDR-- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 181 riqDEHDPISLNyTSGTTADPKGVVISHRGAyLCTLSAIIGWEMGTCPV----YLWTLPMFHCNGWTFTWGTAARGGTSV 256
Cdd:cd17642 183 ---DEQVALIMN-SSGSTGLPKGVQLTHKNI-VARFSHARDPIFGNQIIpdtaILTVIPFHHGFGMFTTLGYLICGFRVV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 257 CMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSPRSGPVHVLTGGSP---PPAALVKKVQRLGFqVMHAYGQ 333
Cdd:cd17642 258 LMYKFEEELFLRSLQDYKVQSALLVPTLFAFFAKSTLVDKYDLSNLHEIASGGAPlskEVGEAVAKRFKLPG-IRQGYGL 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 334 TEATGPILFcewQDEWNRLPenqqmelkarqgisilGLADVDVKNKETQKSAPRDGKTMG-----EILIKGSSIMKGYLK 408
Cdd:cd17642 337 TETTSAILI---TPEGDDKP----------------GAVGKVVPFFYAKVVDLDTGKTLGpnergELCVKGPMIMKGYVN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 409 NPKATFEAF-KHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCA 487
Cdd:cd17642 398 NPEATKALIdKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAA 477
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 488 FVVLEKSEttikedrvdkfQTRERNLIEYCRENlphfMCPRK-----VVFLEELPKNGNGKILKPKLRDI 552
Cdd:cd17642 478 VVVLEAGK-----------TMTEKEVMDYVASQ----VSTAKrlrggVKFVDEVPKGLTGKIDRRKIREI 532
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
14-551 |
3.59e-42 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 159.37 E-value: 3.59e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 14 LTPMTFLKRASECYPNRTSII---YGKTrFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAV 90
Cdd:PLN02330 28 LTLPDFVLQDAELYADKVAFVeavTGKA-VTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 91 LNPINTRLDATSIAAILRHAKPKILFLDrsfeALARESLhllssedSNLNLPVIFIHENDFPKRASFEELdyeclIQRGE 170
Cdd:PLN02330 107 FSGANPTALESEIKKQAEAAGAKLIVTN----DTNYGKV-------KGLGLPVIVLGEEKIEGAVNWKEL-----LEAAD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 171 PTPSMVARMFRIQDehDPISLNYTSGTTADPKGVVISHRG--AYLCTLSAIIGWEMGTCPVYLWTLPMFHCNGWT-FTWG 247
Cdd:PLN02330 171 RAGDTSDNEEILQT--DLCALPFSSGTTGISKGVMLTHRNlvANLCSSLFSVGPEMIGQVVTLGLIPFFHIYGITgICCA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 248 TAARGGTSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKG---NSLDLSpRSGPVHVLTGGSPPPAALVKKVQRL- 323
Cdd:PLN02330 249 TLRNKGKVVVMSRFELRTFLNALITQEVSFAPIVPPIILNLVKNpivEEFDLS-KLKLQAIMTAAAPLAPELLTAFEAKf 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 324 -GFQVMHAYGQTEATGPILFcewqdewNRLPENQQmELKARQGISILgLADVDVK--NKETQKSAPRDgkTMGEILIKGS 400
Cdd:PLN02330 328 pGVQVQEAYGLTEHSCITLT-------HGDPEKGH-GIAKKNSVGFI-LPNLEVKfiDPDTGRSLPKN--TPGELCVRSQ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 401 SIMKGYLKNPKATFEAF-KHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHP 479
Cdd:PLN02330 397 CVMQGYYNNKEETDRTIdEDGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDE 476
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15218839 480 TWGETPCAFVVLEKSETTIKEDrvdkfqtrernLIEYCRENLPHFMCPRKVVFLEELPKNGNGKILKPKLRD 551
Cdd:PLN02330 477 EAGEIPAACVVINPKAKESEED-----------ILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKE 537
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
28-557 |
6.90e-42 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 159.05 E-value: 6.90e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 28 PNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRLDATSIAAIL 107
Cdd:PRK06178 47 PQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYEL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 108 RHAKPK-ILFLDR------------SFEALARESLH-LLSSEDSnlnLPVIFIHenDFPKRASFEELDYECLIqRGEPTP 173
Cdd:PRK06178 127 NDAGAEvLLALDQlapvveqvraetSLRHVIVTSLAdVLPAEPT---LPLPDSL--RAPRLAAAGAIDLLPAL-RACTAP 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 174 SMVARMfriqDEHDPISLNYTSGTTADPKGVVISHRG-AYLCTLSAIIGWEMGTCPVYLWTLPMFHCNGWTFtwGT---A 249
Cdd:PRK06178 201 VPLPPP----ALDALAALNYTGGTTGMPKGCEHTQRDmVYTAAAAYAVAVVGGEDSVFLSFLPEFWIAGENF--GLlfpL 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 250 ARGGTSVCMRHVTAPEIYKNIEMHNVTHMccvptvfnILLKGNSLDL--SPRSGPVHVLTGGSPPPAALVKKV-----QR 322
Cdd:PRK06178 275 FSGATLVLLARWDAVAFMAAVERYRVTRT--------VMLVDNAVELmdHPRFAEYDLSSLRQVRVVSFVKKLnpdyrQR 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 323 ---LGFQVMH--AYGQTEA-TGPILFCEWQDEwnrlpenqQMELKARQ---GISILGlADVDVKNKETQKSAPRDGKtmG 393
Cdd:PRK06178 347 wraLTGSVLAeaAWGMTEThTCDTFTAGFQDD--------DFDLLSQPvfvGLPVPG-TEFKICDFETGELLPLGAE--G 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 394 EILIKGSSIMKGYLKNPKATFEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAV 473
Cdd:PRK06178 416 EIVVRTPSLLKGYWNKPEATAEALRDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAV 495
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 474 VAMPHPTWGETPCAFVVLeKSETTIKEDrvdkfqtrerNLIEYCRENLPHFMCPrKVVFLEELPKNGNGKILKPKLRDIA 553
Cdd:PRK06178 496 VGRPDPDKGQVPVAFVQL-KPGADLTAA----------ALQAWCRENMAVYKVP-EIRIVDALPMTATGKVRKQDLQALA 563
|
....
gi 15218839 554 KGLV 557
Cdd:PRK06178 564 EELK 567
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
28-545 |
9.73e-42 |
|
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: 158.89 E-value: 9.73e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 28 PNRTSIIY------GKTRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRLDAT 101
Cdd:cd17634 67 GDRTAIIYegddtsQSRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 102 SIAAILRHAKPKILFLDRSFEALAReSLHLLSSEDSNLNLPVIFIHENDFPKRASFE-------ELDYECLIQRGEPTPS 174
Cdd:cd17634 147 AVAGRIIDSSSRLLITADGGVRAGR-SVPLKKNVDDALNPNVTSVEHVIVLKRTGSDidwqegrDLWWRDLIAKASPEHQ 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 175 MVArmfriQDEHDPISLNYTSGTTADPKGVVISHrGAYLCTLSaiigWEMGTC------PVYLWTLPMfhcnGWT----- 243
Cdd:cd17634 226 PEA-----MNAEDPLFILYTSGTTGKPKGVLHTT-GGYLVYAA----TTMKYVfdygpgDIYWCTADV----GWVtghsy 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 244 FTWGTAARGGTSVCMR----HVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNS-----LDLSPrsgpVHVLTG-GSP-- 311
Cdd:cd17634 292 LLYGPLACGATTLLYEgvpnWPTPARMWQVVDKHGVNILYTAPTAIRALMAAGDdaiegTDRSS----LRILGSvGEPin 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 312 --PPAALVKKVQRLGFQVMHAYGQTEATGPILfcewqdewnrLPENQQMELKARQG-ISILGLAdVDVKNKETQksaPRD 388
Cdd:cd17634 368 peAYEWYWKKIGKEKCPVVDTWWQTETGGFMI----------TPLPGAIELKAGSAtRPVFGVQ-PAVVDNEGH---PQP 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 389 GKTMGEILIKGS--SIMKGYLKNPK-------ATFEAFkhgWLnTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVE 459
Cdd:cd17634 434 GGTEGNLVITDPwpGQTRTLFGDHErfeqtyfSTFKGM---YF-SGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIE 509
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 460 NVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKSETTIKEDRVDkfqtrernLIEYCRENLPHFMCPRKVVFLEELPKN 539
Cdd:cd17634 510 SVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNHGVEPSPELYAE--------LRNWVRKEIGPLATPDVVHWVDSLPKT 581
|
....*.
gi 15218839 540 GNGKIL 545
Cdd:cd17634 582 RSGKIM 587
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
191-551 |
1.09e-41 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 158.29 E-value: 1.09e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 191 LNYTSGTTADPKGVVISHR----------GAYLCTLSAiiGWEMGTCPvylwtLPMFH-----CNGWTFTwgtaARGGTS 255
Cdd:PRK08974 211 LQYTGGTTGVAKGAMLTHRnmlanleqakAAYGPLLHP--GKELVVTA-----LPLYHifaltVNCLLFI----ELGGQN 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 256 VCM---RHVtaPEIYKNIEMHNVTHMCCVPTVFNILLKG---NSLDLSPRSGPVhvlTGGSPPPAALVKKVQRL-GFQVM 328
Cdd:PRK08974 280 LLItnpRDI--PGFVKELKKYPFTAITGVNTLFNALLNNeefQELDFSSLKLSV---GGGMAVQQAVAERWVKLtGQYLL 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 329 HAYGQTEATgPILFCEwqdewnrlPENqqmeLKARQGiSI-LGLADVDVK-NKETQKSAPRdGKTmGEILIKGSSIMKGY 406
Cdd:PRK08974 355 EGYGLTECS-PLVSVN--------PYD----LDYYSG-SIgLPVPSTEIKlVDDDGNEVPP-GEP-GELWVKGPQVMLGY 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 407 LKNPKATFEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPC 486
Cdd:PRK08974 419 WQRPEATDEVIKDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVK 498
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15218839 487 AFVVleksettikedRVDKFQTRErNLIEYCRENLPHFMCPRKVVFLEELPKNGNGKILKPKLRD 551
Cdd:PRK08974 499 IFVV-----------KKDPSLTEE-ELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRD 551
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
50-550 |
2.02e-41 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 155.68 E-value: 2.02e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 50 CRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRLDATSIAAILRH----AKPKILFLDRSFEALA 125
Cdd:cd05922 4 SAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRLGLVFVPLNPTLKESVLRYlvadAGGRIVLADAGAADRL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 126 RESLHLLSSEDsnlnlpvifihendfpkrasfEELDYECLIQRGEPTPSmvarmFRIQDEhDPISLNYTSGTTADPKGVV 205
Cdd:cd05922 84 RDALPASPDPG---------------------TVLDADGIRAARASAPA-----HEVSHE-DLALLLYTSGSTGSPKLVR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 206 ISHRGayLCTLSAIIGWEMGTCP--VYLWTLPMFHCNGWTFTWGTAARGGTSVC-MRHVTAPEIYKNIEMHNVTHMCCVP 282
Cdd:cd05922 137 LSHQN--LLANARSIAEYLGITAddRALTVLPLSYDYGLSVLNTHLLRGATLVLtNDGVLDDAFWEDLREHGATGLAGVP 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 283 TVFNILLkgnSLDLSPRSGPV--HVLTGGSPPPAALVKKVQRL--GFQVMHAYGQTEATGPILFcewqdewnrLPENQQM 358
Cdd:cd05922 215 STYAMLT---RLGFDPAKLPSlrYLTQAGGRLPQETIARLRELlpGAQVYVMYGQTEATRRMTY---------LPPERIL 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 359 ELKARQGISILGlADVDVKNKETQKSAPrdgKTMGEILIKGSSIMKGYLKNPKA-TFEAFKHGWLNTGDVGVIHPDGHVE 437
Cdd:cd05922 283 EKPGSIGLAIPG-GEFEILDDDGTPTPP---GEPGEIVHRGPNVMKGYWNDPPYrRKEGRGGGVLHTGDLARRDEDGFLF 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 438 IKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPhPTWGETPCAFVVLeKSETTIKEdrvdkfqtrernLIEYC 517
Cdd:cd05922 359 IVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLP-DPLGEKLALFVTA-PDKIDPKD------------VLRSL 424
|
490 500 510
....*....|....*....|....*....|...
gi 15218839 518 RENLPHFMCPRKVVFLEELPKNGNGKILKPKLR 550
Cdd:cd05922 425 AERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
20-544 |
1.49e-40 |
|
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: 154.17 E-value: 1.49e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 20 LKRASECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRLD 99
Cdd:TIGR03098 6 LEDAAARLPDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 100 ATSIAAILRHAKPKILFldRSFEALAreSLHLLSSEDSNLNLPVIF-IHENDFPKRASFEELDYECLIQRGEPTPSMVar 178
Cdd:TIGR03098 86 AEQVAHILADCNVRLLV--TSSERLD--LLHPALPGCHDLRTLIIVgDPAHASEGHPGEEPASWPKLLALGDADPPHP-- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 179 mfRIQDehDPISLNYTSGTTADPKGVVISHRGAYLCTLSAIIGWEMGTCPVYLWTLPMfhcngwTFTWG-----TA-ARG 252
Cdd:TIGR03098 160 --VIDS--DMAAILYTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPL------SFDYGfnqltTAfYVG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 253 GTSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFnilLKGNSLDLSPRSGPvHVL----TGGSPPPAALVKKVQRLGFQVM 328
Cdd:TIGR03098 230 ATVVLHDYLLPRDVLKALEKHGITGLAAVPPLW---AQLAQLDWPESAAP-SLRyltnSGGAMPRATLSRLRSFLPNARL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 329 H-AYGQTEA----TGPilfcewqdewnrlPEnqqmELKARQGiSI---LGLADVDVKNKETQKSAPRDgktMGEILIKGS 400
Cdd:TIGR03098 306 FlMYGLTEAfrstYLP-------------PE----EVDRRPD-SIgkaIPNAEVLVLREDGSECAPGE---EGELVHRGA 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 401 SIMKGYLKNPKATFEAFK-----HGWLN-------TGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKV 468
Cdd:TIGR03098 365 LVAMGYWNDPEKTAERFRplppfPGELHlpelavwSGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLV 444
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15218839 469 LETAVVAMPHPTWGEtpcAFVVLEKSETTIKEDRVDkfqtrernLIEYCRENLPHFMCPRKVVFLEELPKNGNGKI 544
Cdd:TIGR03098 445 AEAVAFGVPDPTLGQ---AIVLVVTPPGGEELDRAA--------LLAECRARLPNYMVPALIHVRQALPRNANGKI 509
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
193-553 |
2.81e-40 |
|
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: 149.94 E-value: 2.81e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 193 YTSGTTADPKGVVISHRGaylctlSAIIGWEMGTCPVY------LWTLPMFHCNGWTFTWGTAARGGTSVCM------RH 260
Cdd:cd05944 9 HTGGTTGTPKLAQHTHSN------EVYNAWMLALNSLFdpddvlLCGLPLFHVNGSVVTLLTPLASGAHVVLagpagyRN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 261 VTA-PEIYKNIEMHNVTHMCCVPTVFNILLK--GNSlDLSPRSGpvhVLTGGSPPPAALVKKVQ-RLGFQVMHAYGQTEA 336
Cdd:cd05944 83 PGLfDNFWKLVERYRITSLSTVPTVYAALLQvpVNA-DISSLRF---AMSGAAPLPVELRARFEdATGLPVVEGYGLTEA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 337 TGpILFCEWQDEWNRLPENQQMELKARQGISILgladvdvkNKETQKSAPRDGKTMGEILIKGSSIMKGYLKNPKATFEA 416
Cdd:cd05944 159 TC-LVAVNPPDGPKRPGSVGLRLPYARVRIKVL--------DGVGRLLRDCAPDEVGEICVAGPGVFGGYLYTEGNKNAF 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 417 FKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLeKSET 496
Cdd:cd05944 230 VADGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQL-KPGA 308
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 15218839 497 TIKEDRvdkfqtrernLIEYCRENLPH-FMCPRKVVFLEELPKNGNGKILKPKLRDIA 553
Cdd:cd05944 309 VVEEEE----------LLAWARDHVPErAAVPKHIEVLEELPVTAVGKVFKPALRADA 356
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
40-553 |
4.59e-40 |
|
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: 151.50 E-value: 4.59e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 40 FTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPIntrldatsiaailrhakpkilfldr 119
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPL------------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 120 sFEALAREslhllssedsnlnlpvifihendfPKRASFEELDYECLIQrgepTPSMVARMfriqDEHDPISLNYTSGTTA 199
Cdd:cd05969 56 -FSAFGPE------------------------AIRDRLENSEAKVLIT----TEELYERT----DPEDPTLLHYTSGTTG 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 200 DPKGVVISHRGAYLCTLSAiiGWEMGTCPVylwtlPMFHCN---GW---TF--TWGTAARGGTSVCMRHVTAPE-IYKNI 270
Cdd:cd05969 103 TPKGVLHVHDAMIFYYFTG--KYVLDLHPD-----DIYWCTadpGWvtgTVygIWAPWLNGVTNVVYEGRFDAEsWYGII 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 271 EMHNVTHMCCVPTVFNILLK-----GNSLDLSPRSgpvHVLTGGSP-PPAALVKKVQRLGFQVMHAYGQTEaTGPILFCE 344
Cdd:cd05969 176 ERVKVTVWYTAPTAIRMLMKegdelARKYDLSSLR---FIHSVGEPlNPEAIRWGMEVFGVPIHDTWWQTE-TGSIMIAN 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 345 WqdewnrlpenQQMELKA-RQGISILGLADVDVKNketQKSAPRDGKtMGEILIKGS--SIMKGYLKNPKATFEAFKHGW 421
Cdd:cd05969 252 Y----------PCMPIKPgSMGKPLPGVKAAVVDE---NGNELPPGT-KGILALKPGwpSMFRGIWNDEERYKNSFIDGW 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 422 LNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKSETTIKED 501
Cdd:cd05969 318 YLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSDEL 397
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 15218839 502 RVDkfqtrernLIEYCRENLPHFMCPRKVVFLEELPKNGNGKILKPKLRDIA 553
Cdd:cd05969 398 KEE--------IINFVRQKLGAHVAPREIEFVDNLPKTRSGKIMRRVLKAKE 441
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
47-553 |
3.63e-39 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 150.66 E-value: 3.63e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 47 DRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFLDRSFEALAR 126
Cdd:PRK06164 43 ALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARWLVVWPGFKGIDF 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 127 ESLHLLSSEDSNLNLPVIFIHEN---DFPKRASFEELDyeclIQRGEPTPSMVARMFRIQDEHDPISLNYTSGTTADPKG 203
Cdd:PRK06164 123 AAILAAVPPDALPPLRAIAVVDDaadATPAPAPGARVQ----LFALPDPAPPAAAGERAADPDAGALLFTTSGTTSGPKL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 204 VVisHRGAYLCTLSAIIGWEMGTCP--VYLWTLPMFHCNGWTFTWGTAARGGTSVCMRHVTAPEIYKNIEMHNVTHmccv 281
Cdd:PRK06164 199 VL--HRQATLLRHARAIARAYGYDPgaVLLAALPFCGVFGFSTLLGALAGGAPLVCEPVFDAARTARALRRHRVTH---- 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 282 pTVFNILLKGNSLDLSPRSGP---VHVLTGGSPPPAA--LVKKVQRLGFQVMHAYGQTEATGpiLFCEWQDEwnrLPENQ 356
Cdd:PRK06164 273 -TFGNDEMLRRILDTAGERADfpsARLFGFASFAPALgeLAALARARGVPLTGLYGSSEVQA--LVALQPAT---DPVSV 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 357 QMElkaRQGISILGLADVDVKNKETQKSAPrDGKTmGEILIKGSSIMKGYLKNPKATFEAFK-HGWLNTGDVGVIHPDGH 435
Cdd:PRK06164 347 RIE---GGGRPASPEARVRARDPQDGALLP-DGES-GEIEIRAPSLMRGYLDNPDATARALTdDGYFRTGDLGYTRGDGQ 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 436 VEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPtwGET-PCAFVVLEksettikedrvDKFQTRERNLI 514
Cdd:PRK06164 422 FVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGATRD--GKTvPVAFVIPT-----------DGASPDEAGLM 488
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 15218839 515 EYCRENLPHFMCPRKVVFLEELP--KNGNG-KILKPKLRDIA 553
Cdd:PRK06164 489 AACREALAGFKVPARVQVVEAFPvtESANGaKIQKHRLREMA 530
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
28-555 |
4.73e-39 |
|
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: 151.31 E-value: 4.73e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 28 PNRTSIIY------GKTRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTP-ALYEMhFAVPMAGAVLNPINTRLDA 100
Cdd:cd05967 65 GDQIALIYdspvtgTERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPeAAIAM-LACARIGAIHSVVFGGFAA 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 101 TSIAAILRHAKPKiLFLDRSFEALARESLHLLSSEDSNLNLP------VIFIHENDFPKRA--SFEELDYECLIQRGEPT 172
Cdd:cd05967 144 KELASRIDDAKPK-LIVTASCGIEPGKVVPYKPLLDKALELSghkphhVLVLNRPQVPADLtkPGRDLDWSELLAKAEPV 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 173 PSMVArmfriqDEHDPISLNYTSGTTADPKGVVishR--GAYLCTLSaiigWEMGTC------PVYLWTLPMfhcnGWT- 243
Cdd:cd05967 223 DCVPV------AATDPLYILYTSGTTGKPKGVV---RdnGGHAVALN----WSMRNIygikpgDVWWAASDV----GWVv 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 244 ----FTWGTAARGGTSVC-----MRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLK----GNSLDLSPRSGPVHVLTGGS 310
Cdd:cd05967 286 ghsyIVYGPLLHGATTVLyegkpVGTPDPGAFWRVIEKYQVNALFTAPTAIRAIRKedpdGKYIKKYDLSSLRTLFLAGE 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 311 ---PPPAALVKKVqrLGFQVMHAYGQTEaTGPILFCEwqdewnrlPEN-QQMELKARQ-GISILGLaDVDVKNKETQKSA 385
Cdd:cd05967 366 rldPPTLEWAENT--LGVPVIDHWWQTE-TGWPITAN--------PVGlEPLPIKAGSpGKPVPGY-QVQVLDEDGEPVG 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 386 PRdgkTMGEILIKGS---SIMKGYLKNPkatfEAFKHGWLN-------TGDVGVIHPDGHVEIKDRSKDIIISGGENISS 455
Cdd:cd05967 434 PN---ELGNIVIKLPlppGCLLTLWKND----ERFKKLYLSkfpgyydTGDAGYKDEDGYLFIMGRTDDVINVAGHRLST 506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 456 VEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLeKSETTIKEDRVdkfqtrERNLIEYCRENLPHFMCPRKVVFLEE 535
Cdd:cd05967 507 GEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVVL-KEGVKITAEEL------EKELVALVREQIGPVAAFRLVIFVKR 579
|
570 580
....*....|....*....|
gi 15218839 536 LPKNGNGKILKPKLRDIAKG 555
Cdd:cd05967 580 LPKTRSGKILRRTLRKIADG 599
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
52-544 |
5.24e-39 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 150.42 E-value: 5.24e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 52 LAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFLDRSFEALARESLHL 131
Cdd:PRK05852 56 LAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLIDADGPHDRAEPTTR 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 132 LssedsnlnLPVIFIHENDFPKRASFEELDyecLIQRGEPTPSMVARM-FRiqdeHDPISLNYTSGTTADPKGVVISHRG 210
Cdd:PRK05852 136 W--------WPLTVNVGGDSGPSGGTLSVH---LDAATEPTPATSTPEgLR----PDDAMIMFTGGTTGLPKMVPWTHAN 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 211 AYLCTLSAIIGWEMGTCPVYLWTLPMFHCNGWTFTW-GTAARGGTSVCMRH--VTAPEIYKNIEMHNVTHMCCVPTVFNI 287
Cdd:PRK05852 201 IASSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALlATLASGGAVLLPARgrFSAHTFWDDIKAVGATWYTAVPTIHQI 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 288 LLKGNSLDLSPRS-GPVHVLTGGSPP--PAALVKKVQRLGFQVMHAYGQTEATGPIlfCEWQDEWNRLPENQQME--LKA 362
Cdd:PRK05852 281 LLERAATEPSGRKpAALRFIRSCSAPltAETAQALQTEFAAPVVCAFGMTEATHQV--TTTQIEGIGQTENPVVStgLVG 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 363 RQGIsilglADVDVKNKETQKSAPrdgKTMGEILIKGSSIMKGYLKNPKATFEAFKHGWLNTGDVGVIHPDGHVEIKDRS 442
Cdd:PRK05852 359 RSTG-----AQIRIVGSDGLPLPA---GAVGEVWLRGTTVVRGYLGDPTITAANFTDGWLRTGDLGSLSAAGDLSIRGRI 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 443 KDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKSETTIKEDrvdkfqtrernLIEYCRENLP 522
Cdd:PRK05852 431 KELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPRESAPPTAEE-----------LVQFCRERLA 499
|
490 500
....*....|....*....|..
gi 15218839 523 HFMCPRKVVFLEELPKNGNGKI 544
Cdd:PRK05852 500 AFEIPASFQEASGLPHTAKGSL 521
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
194-553 |
7.33e-39 |
|
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: 145.17 E-value: 7.33e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 194 TSGTTADPKGVVISHRgAYLCTLSAIIGWEMGTCP-VYLWTLPMFHCNGWTFTWGTAARGGTSVCMRHvtAPEIYKNIEM 272
Cdd:cd17630 8 TSGSTGTPKAVVHTAA-NLLASAAGLHSRLGFGGGdSWLLSLPLYHVGGLAILVRSLLAGAELVLLER--NQALAEDLAP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 273 HNVTHMCCVPTVFNILLKgNSLDLSPRSGPVHVLTGGSPPPAALVKKVQRLGFQVMHAYGQTEATGPIlfCEWqdewnRL 352
Cdd:cd17630 85 PGVTHVSLVPTQLQRLLD-SGQGPAALKSLRAVLLGGAPIPPELLERAADRGIPLYTTYGMTETASQV--ATK-----RP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 353 PENQQMELKarqgiSILGLADVDVKNKetqksaprdgktmGEILIKGSSIMKGYLKNPKaTFEAFKHGWLNTGDVGVIHP 432
Cdd:cd17630 157 DGFGRGGVG-----VLLPGRELRIVED-------------GEIWVGGASLAMGYLRGQL-VPEFNEDGWFTTKDLGELHA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 433 DGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKSettikedrvdkfqTRERN 512
Cdd:cd17630 218 DGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGP-------------ADPAE 284
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 15218839 513 LIEYCRENLPHFMCPRKVVFLEELPKNGNGKILKPKLRDIA 553
Cdd:cd17630 285 LRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRAWL 325
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
34-544 |
4.97e-38 |
|
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: 146.05 E-value: 4.97e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 34 IYGKTRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPK 113
Cdd:cd05914 2 YYGGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 114 ILFldrsfealareslhllssedsnlnlpvifihendfpkrasfeeldyecliqrgeptpsmvarmfrIQDEHDPISLNY 193
Cdd:cd05914 82 AIF-----------------------------------------------------------------VSDEDDVALINY 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 194 TSGTTADPKGVVISHRGaylctlsaiIGWEMGTCPVY---------LWTLPMFHCNGWTFTWGTAARGGTSVCMRHVTAP 264
Cdd:cd05914 97 TSGTTGNSKGVMLTYRN---------IVSNVDGVKEVvllgkgdkiLSILPLHHIYPLTFTLLLPLLNGAHVVFLDKIPS 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 265 EIYKNIEMHNVTHMCCVPTVFnILLKGNSLDLSPRSG----------PVHVL----------------------TGGSPP 312
Cdd:cd05914 168 AKIIALAFAQVTPTLGVPVPL-VIEKIFKMDIIPKLTlkkfkfklakKINNRkirklafkkvheafggnikefvIGGAKI 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 313 PAALVKKVQRLGFQVMHAYGQTEaTGPILFcewQDEWNRLpenqqmelkarqgisILGLADVDVKNKETQKSAPRDGKTM 392
Cdd:cd05914 247 NPDVEEFLRTIGFPYTIGYGMTE-TAPIIS---YSPPNRI---------------RLGSAGKVIDGVEVRIDSPDPATGE 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 393 GEILIKGSSIMKGYLKNPKATFEAF-KHGWLNTGDVGVIHPDGHVEIKDRSKDIIISG-GENISSVEVENVLYKYPKVLE 470
Cdd:cd05914 308 GEIIVRGPNVMKGYYKNPEATAEAFdKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSsGKNIYPEEIEAKINNMPFVLE 387
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 471 TAVV---------AMPHPTWgETPCAFVVLEKSEtTIKEDRVDKFQTrernlieycreNLPHFMCPRKV-VFLEELPKNG 540
Cdd:cd05914 388 SLVVvqekklvalAYIDPDF-LDVKALKQRNIID-AIKWEVRDKVNQ-----------KVPNYKKISKVkIVKEEFEKTP 454
|
....
gi 15218839 541 NGKI 544
Cdd:cd05914 455 KGKI 458
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
38-551 |
5.34e-38 |
|
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: 145.65 E-value: 5.34e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 38 TRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFL 117
Cdd:cd05971 5 EKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 118 DRSfealareslhllssedsnlnlpvifihendfpkrasfeeldyecliqrgeptpsmvarmfriqdeHDPISLNYTSGT 197
Cdd:cd05971 85 DGS-----------------------------------------------------------------DDPALIIYTSGT 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 198 TADPKGVVISHRgaYLctlsaiigweMGTCPVYLWTLPMFHCNGWTFtWGTAARG---------------GTSVC---MR 259
Cdd:cd05971 100 TGPPKGALHAHR--VL----------LGHLPGVQFPFNLFPRDGDLY-WTPADWAwigglldvllpslyfGVPVLahrMT 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 260 HVTAPEIYKNIEMHNVTHMCCVPTVFNIL-LKGNSLDLSPRSgPVHVLTGGSPPPAALVKKVQR-LGFQVMHAYGQTEA- 336
Cdd:cd05971 167 KFDPKAALDLMSRYGVTTAFLPPTALKMMrQQGEQLKHAQVK-LRAIATGGESLGEELLGWAREqFGVEVNEFYGQTECn 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 337 ----TGPILFCewqdewnrlPENQQMelkarqGISILGlADVDVKNKETQKSAPRDgktMGEILIK--GSSIMKGYLKNP 410
Cdd:cd05971 246 lvigNCSALFP---------IKPGSM------GKPIPG-HRVAIVDDNGTPLPPGE---VGEIAVElpDPVAFLGYWNNP 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 411 KATFEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVV 490
Cdd:cd05971 307 SATEKKMAGDWLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVV 386
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15218839 491 LEKSETTIKEdrvdkfqtRERNLIEYCRENLPHFMCPRKVVFLEELPKNGNGKILKPKLRD 551
Cdd:cd05971 387 LNPGETPSDA--------LAREIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRRELRA 439
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
187-542 |
7.02e-38 |
|
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: 142.83 E-value: 7.02e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 187 DPISLNYTSGTTADPKGVVISHRGAYLCTLSAIIGWEMGTCPVYLWTLPMFHCNGWTFTWGTAARGGTSVCMRHVTAPEI 266
Cdd:cd17636 1 DPVLAIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLNSGPLFHIGTLMFTLATFHAGGTNVFVRRVDAEEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 267 YKNIEMHNVTH-MCCVPTVFNI--LLKGNSLDLS-PRSGPvhvltgGSPPPAALVKKVQRLGFQVMHAYGQTEATGPILF 342
Cdd:cd17636 81 LELIEAERCTHaFLLPPTIDQIveLNADGLYDLSsLRSSP------AAPEWNDMATVDTSPWGRKPGGYGQTEVMGLATF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 343 cEWQdewnrlpenqqmelkARQGISILG----LADVDVKNKETQKSAprDGKTmGEILIKGSSIMKGYLKNPKATFEAFK 418
Cdd:cd17636 155 -AAL---------------GGGAIGGAGrpspLVQVRILDEDGREVP--DGEV-GEIVARGPTVMAGYWNRPEVNARRTR 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 419 HGWLNTGDVGVIHPDGHVEI---KDRskdIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKSE 495
Cdd:cd17636 216 GGWHHTNDLGRREPDGSLSFvgpKTR---MIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGA 292
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 15218839 496 TTIKEDrvdkfqtrernLIEYCRENLPHFMCPRKVVFLEELPKNGNG 542
Cdd:cd17636 293 SVTEAE-----------LIEHCRARIASYKKPKSVEFADALPRTAGG 328
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
191-551 |
2.09e-37 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 146.06 E-value: 2.09e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 191 LNYTSGTTADPKGVVISHRG--AYLCTLSAIIGWEMGT-CPVYLWTLPMFHCNGWTFTWG-TAARGGTSVCM---RHVta 263
Cdd:PRK05677 212 LQYTGGTTGVAKGAMLTHRNlvANMLQCRALMGSNLNEgCEILIAPLPLYHIYAFTFHCMaMMLIGNHNILIsnpRDL-- 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 264 PEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSPRSGPVHVLTGGSPPPAALVKKVQRL-GFQVMHAYGQTEaTGPIlf 342
Cdd:PRK05677 290 PAMVKELGKWKFSGFVGLNTLFVALCNNEAFRKLDFSALKLTLSGGMALQLATAERWKEVtGCAICEGYGMTE-TSPV-- 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 343 cewqdewnrlpenqqMELKARQGISIlGLADVDVKNKETqKSAPRDGKTM-----GEILIKGSSIMKGYLKNPKATFEAF 417
Cdd:PRK05677 367 ---------------VSVNPSQAIQV-GTIGIPVPSTLC-KVIDDDGNELplgevGELCVKGPQVMKGYWQRPEATDEIL 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 418 -KHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKSET 496
Cdd:PRK05677 430 dSDGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKPGET 509
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 15218839 497 TIKEdrvdkfqtrerNLIEYCRENLPHFMCPRKVVFLEELPKNGNGKILKPKLRD 551
Cdd:PRK05677 510 LTKE-----------QVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRRELRD 553
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
28-550 |
2.16e-37 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 145.15 E-value: 2.16e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 28 PNRTSIIYGKT--RFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRLDATSIAA 105
Cdd:PRK13390 11 PDRPAVIVAETgeQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 106 ILRHAKPKILFLDRSFEALARESlhllssedsnlnlpvifihENDFPKRASFE-ELD----YECLIQRGEPtpsmvarmf 180
Cdd:PRK13390 91 IVGDSGARVLVASAALDGLAAKV-------------------GADLPLRLSFGgEIDgfgsFEAALAGAGP--------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 181 RIQDEHDPISLNYTSGTTADPKGVVISHRGAYLCT----LSAIIG--WEMGTCPVYLWTLPMFHCNGWTFTWGTAARGGT 254
Cdd:PRK13390 143 RLTEQPCGAVMLYSSGTTGFPKGIQPDLPGRDVDApgdpIVAIARafYDISESDIYYSSAPIYHAAPLRWCSMVHALGGT 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 255 SVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNS-----LDLSPRSGPVHvltGGSPPPAAlVKK--VQRLGFQV 327
Cdd:PRK13390 223 VVLAKRFDAQATLGHVERYRITVTQMVPTMFVRLLKLDAdvrtrYDVSSLRAVIH---AAAPCPVD-VKHamIDWLGPIV 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 328 MHAYGQTEATGPILfcewqdewnrLPENQQMELKARQGISILGlaDVDVKNKETQK-SAPRdgktMGEILIKGSSIMKGY 406
Cdd:PRK13390 299 YEYYSSTEAHGMTF----------IDSPDWLAHPGSVGRSVLG--DLHICDDDGNElPAGR----IGTVYFERDRLPFRY 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 407 LKNPKATFEAfKHG----WLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWG 482
Cdd:PRK13390 363 LNDPEKTAAA-QHPahpfWTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMG 441
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15218839 483 ETPCAFVVLEKSettikedrVDKFQTRERNLIEYCRENLPHFMCPRKVVFLEELPKNGNGKILKPKLR 550
Cdd:PRK13390 442 EQVKAVIQLVEG--------IRGSDELARELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
187-544 |
5.87e-37 |
|
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: 140.47 E-value: 5.87e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 187 DPISLNYTSGTTADPKGVVISHRGAYLCTLSAII-GWEMGTCPVYLWTLPMFHCNG-WTFTWGTAARGGTSVCMRHVTAP 264
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKeGLNWVVGDVTYLPLPATHIGGlWWILTCLIHGGLCVTGGENTTYK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 265 EIYKNIEMHNVTHMCCVPTVFN--ILLKGNSLDLSPRSGPVHVltGGSPPPAALVKKVQRLGF-QVMHAYGQTEaTGPIL 341
Cdd:cd17635 82 SLFKILTTNAVTTTCLVPTLLSklVSELKSANATVPSLRLIGY--GGSRAIAADVRFIEATGLtNTAQVYGLSE-TGTAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 342 FCEWQDEwnrlpenqqmelkaRQGISILG--LADVDVKNKETQKSAPRDGKTmGEILIKGSSIMKGYLKNPKATFEAFKH 419
Cdd:cd17635 159 CLPTDDD--------------SIEINAVGrpYPGVDVYLAATDGIAGPSASF-GTIWIKSPANMLGYWNNPERTAEVLID 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 420 GWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVleKSEttik 499
Cdd:cd17635 224 GWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVV--ASA---- 297
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 15218839 500 edrvDKFQTRERNLIEYCRENLPHFMCPRKVVFLEELPKNGNGKI 544
Cdd:cd17635 298 ----ELDENAIRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKV 338
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
18-554 |
1.58e-36 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 142.23 E-value: 1.58e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 18 TFLKRASEcYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNiSKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTR 97
Cdd:PRK07638 6 EYKKHASL-QPNKIAIKENDRVLTYKDWFESVCKVANWLNEKE-SKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 98 LDATSIAAILRHAKPKILFLDRSFealaresLHLLSSEDSnlnlPVIFIHEndfpkrasfeeldYECLIQRGEPTPSMVa 177
Cdd:PRK07638 84 WKQDELKERLAISNADMIVTERYK-------LNDLPDEEG----RVIEIDE-------------WKRMIEKYLPTYAPI- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 178 rmfrIQDEHDPISLNYTSGTTADPKGVVISHRG---AYLCTLSAiigWEMGTCPVYLWTLPMFHCNgwtFTWG---TAAR 251
Cdd:PRK07638 139 ----ENVQNAPFYMGFTSGSTGKPKAFLRAQQSwlhSFDCNVHD---FHMKREDSVLIAGTLVHSL---FLYGaisTLYV 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 252 GGTSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLdlspRSGPVHVLTGGSPPPAALVKKVQRlgfQVMHA- 330
Cdd:PRK07638 209 GQTVHLMRKFIPNQVLDKLETENISVMYTVPTMLESLYKENRV----IENKMKIISSGAKWEAEAKEKIKN---IFPYAk 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 331 ----YGQTEATgpilFCEW--QDEWNRLP-------ENQQMELKARQGisilgladvdvknKETQKsaprdGKTmGEILI 397
Cdd:PRK07638 282 lyefYGASELS----FVTAlvDEESERRPnsvgrpfHNVQVRICNEAG-------------EEVQK-----GEI-GTVYV 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 398 KGSSIMKGYLKNPKATFEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMP 477
Cdd:PRK07638 339 KSPQFFMGYIIGGVLARELNADGWMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVP 418
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15218839 478 HPTWGETPCAFVvleksettikedrvdKFQTRERNLIEYCRENLPHFMCPRKVVFLEELPKNGNGKILKPKLRDIAK 554
Cdd:PRK07638 419 DSYWGEKPVAII---------------KGSATKQQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAKSWIE 480
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
178-554 |
3.68e-36 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 142.32 E-value: 3.68e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 178 RMFRIQDEHDPIS-LNYTSGTTADPKGVVISHRGaYLCTLSAIIGWEMGT------CPVYLWTLPMFH-----CNGWTFT 245
Cdd:PRK08751 199 SMPTLQIEPDDIAfLQYTGGTTGVAKGAMLTHRN-LVANMQQAHQWLAGTgkleegCEVVITALPLYHifaltANGLVFM 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 246 wgtaARGGtsvCMRHVTAPE----IYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSPRSGPVHVLTGGSPPPAALVKKVQ 321
Cdd:PRK08751 278 ----KIGG---CNHLISNPRdmpgFVKELKKTRFTAFTGVNTLFNGLLNTPGFDQIDFSSLKMTLGGGMAVQRSVAERWK 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 322 RL-GFQVMHAYGQTEATgpilfcewqdewnrlPEN--QQMELKARQGISILGLADVDVKNKETQKSAPRDGKtMGEILIK 398
Cdd:PRK08751 351 QVtGLTLVEAYGLTETS---------------PAAciNPLTLKEYNGSIGLPIPSTDACIKDDAGTVLAIGE-IGELCIK 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 399 GSSIMKGYLKNPKATFEAFK-HGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMP 477
Cdd:PRK08751 415 GPQVMKGYWKRPEETAKVMDaDGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVP 494
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15218839 478 HPTWGETpcAFVVLEKSETTIKEDRVDkfqtrernliEYCRENLPHFMCPRKVVFLEELPKNGNGKILKPKLRDIAK 554
Cdd:PRK08751 495 DEKSGEI--VKVVIVKKDPALTAEDVK----------AHARANLTGYKQPRIIEFRKELPKTNVGKILRRELRDAAK 559
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
51-551 |
3.29e-35 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 139.14 E-value: 3.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 51 RLAASLIS--LNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFLDrsfEALAREs 128
Cdd:cd05928 52 RKAANVLSgaCGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTS---DELAPE- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 129 LHLLSSEDSNLNLPVIfIHENDFPKRASFEELdyecliqrgeptpsmvarMFRIQDEH--------DPISLNYTSGTTAD 200
Cdd:cd05928 128 VDSVASECPSLKTKLL-VSEKSRDGWLNFKEL------------------LNEASTEHhcvetgsqEPMAIYFTSGTTGS 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 201 PKGVVISHrGAYLCTLSAIIGWEMGTCPV-YLWTLPMfhcNGWT-FTWGTA----ARGGTSVC--MRHVTAPEIYKNIEM 272
Cdd:cd05928 189 PKMAEHSH-SSLGLGLKVNGRYWLDLTASdIMWNTSD---TGWIkSAWSSLfepwIQGACVFVhhLPRFDPLVILKTLSS 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 273 HNVTHMCCVPTVFNILLKGnslDLSPRSGPV--HVLTGGSP-PPAALVKKVQRLGFQVMHAYGQTEaTGPILFCEWQdew 349
Cdd:cd05928 265 YPITTFCGAPTVYRMLVQQ---DLSSYKFPSlqHCVTGGEPlNPEVLEKWKAQTGLDIYEGYGQTE-TGLICANFKG--- 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 350 nrlpenqqMELKArqGISILGLADVDVKNKETQKSAPRDGKTmGEILIKGS-----SIMKGYLKNPKATFEAFKHGWLNT 424
Cdd:cd05928 338 --------MKIKP--GSMGKASPPYDVQIIDDNGNVLPPGTE-GDIGIRVKpirpfGLFSGYVDNPEKTAATIRGDFYLT 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 425 GDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKSETTIKEDRVd 504
Cdd:cd05928 407 GDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAPQFLSHDPEQL- 485
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 15218839 505 kfqTRErnLIEYCRENLPHFMCPRKVVFLEELPKNGNGKILKPKLRD 551
Cdd:cd05928 486 ---TKE--LQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRD 527
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
178-553 |
3.27e-34 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 136.88 E-value: 3.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 178 RMFRIQDEHDPIS-LNYTSGTTADPKGVVISHRG--AYLCTLSAIIG---------WEMGTcPVYLWTLPMFHCngWTFT 245
Cdd:PRK12492 198 SLKPVPVGLDDIAvLQYTGGTTGLAKGAMLTHGNlvANMLQVRACLSqlgpdgqplMKEGQ-EVMIAPLPLYHI--YAFT 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 246 wgtaargGTSVCM----RH---VTAPE----IYKNIEMHNVTHMCCVPTVFNILLKG---NSLDLSPRSGpvhVLTGGSp 311
Cdd:PRK12492 275 -------ANCMCMmvsgNHnvlITNPRdipgFIKELGKWRFSALLGLNTLFVALMDHpgfKDLDFSALKL---TNSGGT- 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 312 ppaALVKKV-----QRLGFQVMHAYGQTEaTGPILFCEWQDEWNRLpenqqmelkARQGISILGLAdvdvknketQKSAP 386
Cdd:PRK12492 344 ---ALVKATaerweQLTGCTIVEGYGLTE-TSPVASTNPYGELARL---------GTVGIPVPGTA---------LKVID 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 387 RDGKTM-----GEILIKGSSIMKGYLKNPKATFEAF-KHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVEN 460
Cdd:PRK12492 402 DDGNELplgerGELCIKGPQVMKGYWQQPEATAEALdAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIED 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 461 VLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKSETTIKEdrvdkfqtrernLIEYCRENLPHFMCPRKVVFLEELPKNG 540
Cdd:PRK12492 482 VVMAHPKVANCAAIGVPDERSGEAVKLFVVARDPGLSVEE------------LKAYCKENFTGYKVPKHIVLRDSLPMTP 549
|
410
....*....|...
gi 15218839 541 NGKILKPKLRDIA 553
Cdd:PRK12492 550 VGKILRRELRDIA 562
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
161-550 |
2.26e-33 |
|
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: 132.60 E-value: 2.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 161 DYECLIQRGEPTPSMVARMFRIQDehDPISLNYTSGTTADPKGVVISHRGaylcTLSAIIGWE---MGTCP--VYLWTLP 235
Cdd:cd05958 74 ELAYILDKARITVALCAHALTASD--DICILAFTSGTTGAPKATMHFHRD----PLASADRYAvnvLRLREddRFVGSPP 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 236 MFhcngwtFTWGtaaRGGTSVCMRHV----------TAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSPRSGPVHV 305
Cdd:cd05958 148 LA------FTFG---LGGVLLFPFGVgasgvlleeaTPDLLLSAIARYKPTVLFTAPTAYRAMLAHPDAAGPDLSSLRKC 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 306 LTGGSPPPAALVKKVQR-LGFQVMHAYGQTEATGpILFCEWQDEwnrlpenqqmelkARQGIS---ILG--LADVDvknk 379
Cdd:cd05958 219 VSAGEALPAALHRAWKEaTGIPIIDGIGSTEMFH-IFISARPGD-------------ARPGATgkpVPGyeAKVVD---- 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 380 ETQKSAPrDGkTMGEILIKGSSIMKGYLKNPKATFeaFKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVE 459
Cdd:cd05958 281 DEGNPVP-DG-TIGRLAVRGPTGCRYLADKRQRTY--VQGGWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVE 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 460 NVLYKYPKVLETAVVAMPHPTWGETPCAFVVLeKSETTIKEDRVdkfqtreRNLIEYCRENLPHFMCPRKVVFLEELPKN 539
Cdd:cd05958 357 DVLLQHPAVAECAVVGHPDESRGVVVKAFVVL-RPGVIPGPVLA-------RELQDHAKAHIAPYKYPRAIEFVTELPRT 428
|
410
....*....|.
gi 15218839 540 GNGKILKPKLR 550
Cdd:cd05958 429 ATGKLQRFALR 439
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
38-474 |
5.75e-33 |
|
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: 131.71 E-value: 5.75e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 38 TRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFL 117
Cdd:cd17640 4 KRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 118 DRSFEALAreslhllssedsnlnlpvifihendfpkrasfeeldyecliqrgeptpsmvarmfriqdehdpiSLNYTSGT 197
Cdd:cd17640 84 ENDSDDLA----------------------------------------------------------------TIIYTSGT 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 198 TADPKGVVISHRGAY--LCTLSAIIGWEMGTcpVYLWTLPMFHCNGWTFTWGTAARGGTSVCMRHVTAPEIYKNIemhNV 275
Cdd:cd17640 100 TGNPKGVMLTHANLLhqIRSLSDIVPPQPGD--RFLSILPIWHSYERSAEYFIFACGCSQAYTSIRTLKDDLKRV---KP 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 276 THMCCVPTVFNILLKGnsLDLSPRSGP----------------VHVLTGGSPPPAALVKKVQRLGFQVMHAYGQTEaTGP 339
Cdd:cd17640 175 HYIVSVPRLWESLYSG--IQKQVSKSSpikqflflfflsggifKFGISGGGALPPHVDTFFEAIGIEVLNGYGLTE-TSP 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 340 ILFCewqdewNRLPENqqmelkarqgisILG-----LADVDVK--NKETQKSAPRDGKtmGEILIKGSSIMKGYLKNPKA 412
Cdd:cd17640 252 VVSA------RRLKCN------------VRGsvgrpLPGTEIKivDPEGNVVLPPGEK--GIVWVRGPQVMKGYYKNPEA 311
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15218839 413 TFEAF-KHGWLNTGDVGVIHPDGHVEIKDRSKD-IIISGGENISSVEVENVLYKYPkVLETAVV 474
Cdd:cd17640 312 TSKVLdSDGWFNTGDLGWLTCGGELVLTGRAKDtIVLSNGENVEPQPIEEALMRSP-FIEQIMV 374
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
28-543 |
1.97e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 131.16 E-value: 1.97e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 28 PNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRLDATSIAAIL 107
Cdd:PRK07798 17 PDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 108 RHAKPKILFLDRSF-----EALARESL--HLLSSEDSNlnlpvifihENDFPKRAsfeeLDYECLIQRGEPTPSMVARmf 180
Cdd:PRK07798 97 DDSDAVALVYEREFaprvaEVLPRLPKlrTLVVVEDGS---------GNDLLPGA----VDYEDALAAGSPERDFGER-- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 181 riqdEHDPISLNYTSGTTADPKGVVISHRGAYLCTLSAI---IG------WEM------GTCPVYLWTLPMFHCNG-WTf 244
Cdd:PRK07798 162 ----SPDDLYLLYTGGTTGMPKGVMWRQEDIFRVLLGGRdfaTGepiedeEELakraaaGPGMRRFPAPPLMHGAGqWA- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 245 TWGTAARGGTSVCMRHVT--APEIYKNIEMHNVTHMCCVPTVF-----NILLKGNSLDLSprsGPVHVLTGGspppAALV 317
Cdd:PRK07798 237 AFAALFSGQTVVLLPDVRfdADEVWRTIEREKVNVITIVGDAMarpllDALEARGPYDLS---SLFAIASGG----ALFS 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 318 KKVQRlGFQ-------VMHAYGQTEaTGpilfcewqdewnrlpeNQQMELKARQGISILGL-----ADVDVKNKETQKSA 385
Cdd:PRK07798 310 PSVKE-ALLellpnvvLTDSIGSSE-TG----------------FGGSGTVAKGAVHTGGPrftigPRTVVLDEDGNPVE 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 386 PRDGKtMGeILIKGSSIMKGYLKNPKATFEAFK----HGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENV 461
Cdd:PRK07798 372 PGSGE-IG-WIARRGHIPLGYYKDPEKTAETFPtidgVRYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEA 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 462 LYKYPKVLETAVVAMPHPTWGETPCAfvVLEKSETTikedRVDkfqtrERNLIEYCRENLPHFMCPRKVVFLEELPKNGN 541
Cdd:PRK07798 450 LKAHPDVADALVVGVPDERWGQEVVA--VVQLREGA----RPD-----LAELRAHCRSSLAGYKVPRAIWFVDEVQRSPA 518
|
..
gi 15218839 542 GK 543
Cdd:PRK07798 519 GK 520
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
41-479 |
3.00e-32 |
|
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: 130.80 E-value: 3.00e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 41 TWPQTYDRCCRLAASLISLNI--SKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFLD 118
Cdd:cd05927 7 SYKEVAERADNIGSALRSLGGkpAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVFCD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 119 RSFEalareslhLLSSEDsnlnlpvifihendfpkrasFEELDYECLIQRGEPTPSMVArmfriqdehdpiSLNYTSGTT 198
Cdd:cd05927 87 AGVK--------VYSLEE--------------------FEKLGKKNKVPPPPPKPEDLA------------TICYTSGTT 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 199 ADPKGVVISHRGayLCTLSAIIGWEMGTCP------VYLWTLPMFHCNGWTFTWGTAARGGtSVCMRHVTAPEIYKNIEM 272
Cdd:cd05927 127 GNPKGVMLTHGN--IVSNVAGVFKILEILNkinptdVYISYLPLAHIFERVVEALFLYHGA-KIGFYSGDIRLLLDDIKA 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 273 HNVTHMCCVPTVFNIL---LKGNSLDLSPRS---------------------------------------GPVHVLTGGS 310
Cdd:cd05927 204 LKPTVFPGVPRVLNRIydkIFNKVQAKGPLKrklfnfalnyklaelrsgvvraspfwdklvfnkikqalgGNVRLMLTGS 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 311 PPPAALVKKVQR--LGFQVMHAYGQTEATGPIlFCEWQDEWNR------LPENqqmELKarqgisilgLADVDVKNKETQ 382
Cdd:cd05927 284 APLSPEVLEFLRvaLGCPVLEGYGQTECTAGA-TLTLPGDTSVghvggpLPCA---EVK---------LVDVPEMNYDAK 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 383 KSAPRdgktmGEILIKGSSIMKGYLKNPKATFEAF-KHGWLNTGDVGVIHPDGHVEIKDRSKDII-ISGGENISSVEVEN 460
Cdd:cd05927 351 DPNPR-----GEVCIRGPNVFSGYYKDPEKTAEALdEDGWLHTGDIGEWLPNGTLKIIDRKKNIFkLSQGEYVAPEKIEN 425
|
490 500
....*....|....*....|....*...
gi 15218839 461 VL---------YKYPKVLETAVVAMPHP 479
Cdd:cd05927 426 IYarspfvaqiFVYGDSLKSFLVAIVVP 453
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
191-554 |
3.58e-32 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 130.53 E-value: 3.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 191 LNYTSGTTADPKGVVISHRG--AYLCTLSAIIGWEMGTCP-----VYLWTLPMFHCNGWTFTWGTAAR-GGTSVCM---R 259
Cdd:PRK07059 209 LQYTGGTTGVSKGATLLHRNivANVLQMEAWLQPAFEKKPrpdqlNFVCALPLYHIFALTVCGLLGMRtGGRNILIpnpR 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 260 HVtaPEIYKNIEMHNVTHMCCVPTVFNILLKG---NSLDLSPRsgpVHVLTGGSPPPAALVKK-VQRLGFQVMHAYGQTE 335
Cdd:PRK07059 289 DI--PGFIKELKKYQVHIFPAVNTLYNALLNNpdfDKLDFSKL---IVANGGGMAVQRPVAERwLEMTGCPITEGYGLSE 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 336 aTGPILFCewqdewNRLPENqqmELKARQGISILGlADVDVKNKetqksaprDGKTM-----GEILIKGSSIMKGYLKNP 410
Cdd:PRK07059 364 -TSPVATC------NPVDAT---EFSGTIGLPLPS-TEVSIRDD--------DGNDLplgepGEICIRGPQVMAGYWNRP 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 411 KATFEA-FKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFV 489
Cdd:PRK07059 425 DETAKVmTADGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFV 504
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15218839 490 VleKSETTIKEDRVdkfqtrernlIEYCRENLPHFMCPRKVVFLEELPKNGNGKILKPKLRDIAK 554
Cdd:PRK07059 505 V--KKDPALTEEDV----------KAFCKERLTNYKRPKFVEFRTELPKTNVGKILRRELRDGKA 557
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
28-544 |
3.77e-32 |
|
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: 129.33 E-value: 3.77e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 28 PNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRLDATSIAAIL 107
Cdd:cd12116 1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 108 RHAKPKILFLDRsfEALARESLHLLSSEDSNLNLPVifihendfpkrasfeeldyecliQRGEPTPSMvarmfriqDEHD 187
Cdd:cd12116 81 EDAEPALVLTDD--ALPDRLPAGLPVLLLALAAAAA-----------------------APAAPRTPV--------SPDD 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 188 PISLNYTSGTTADPKGVVISHRGAyLCTLSAIIGwEMGTCPVYLW---TLPMFHCNGWTFTWGTAARGGTSVCMR-HVTA 263
Cdd:cd12116 128 LAYVIYTSGSTGRPKGVVVSHRNL-VNFLHSMRE-RLGLGPGDRLlavTTYAFDISLLELLLPLLAGARVVIAPReTQRD 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 264 PEIYKN-IEMHNVTHMCCVPTVFNILLKGnslDLSPRSGpVHVLTGGSPPPAALVKKVQRLGFQVMHAYGQTEATGPILF 342
Cdd:cd12116 206 PEALARlIEAHSITVMQATPATWRMLLDA---GWQGRAG-LTALCGGEALPPDLAARLLSRVGSLWNLYGPTETTIWSTA 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 343 CEWQDEWNRLPenqqmelkarQGISILG----LADVDvknketQKSAPRDgkTMGEILIKGSSIMKGYLKNPKATFEAFK 418
Cdd:cd12116 282 ARVTAAAGPIP----------IGRPLANtqvyVLDAA------LRPVPPG--VPGELYIGGDGVAQGYLGRPALTAERFV 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 419 HG--------WLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAmpHPTWGETPCAFVV 490
Cdd:cd12116 344 PDpfagpgsrLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVV--REDGGDRRLVAYV 421
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 15218839 491 LEKSETTIKEDRvdkfqtrernLIEYCRENLPHFMCPRKVVFLEELPKNGNGKI 544
Cdd:cd12116 422 VLKAGAAPDAAA----------LRAHLRATLPAYMVPSAFVRLDALPLTANGKL 465
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
28-550 |
5.15e-32 |
|
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: 130.69 E-value: 5.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 28 PNRTSIIY----GKTR-FTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRLDATS 102
Cdd:cd05968 75 RTRPALRWegedGTSRtLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEA 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 103 IAAILRHAKPKILFLDRSFEALARESLHLLSSEDSNLNLPV---IFIHE---NDFPKrASFEELDYEcliQRGEPTPSMV 176
Cdd:cd05968 155 AATRLQDAEAKALITADGFTRRGREVNLKEEADKACAQCPTvekVVVVRhlgNDFTP-AKGRDLSYD---EEKETAGDGA 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 177 ARMfriqDEHDPISLNYTSGTTADPKGVVISHRGAYL-CTLSAIIGWEMGTCPVYLWTLPMfhcnGWT----FTWGTAAR 251
Cdd:cd05968 231 ERT----ESEDPLMIIYTSGTTGKPKGTVHVHAGFPLkAAQDMYFQFDLKPGDLLTWFTDL----GWMmgpwLIFGGLIL 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 252 GGTSVCMR----HVTAPEIYKNIEMHNVTHMCCVPTVFNILlKGNSLDLSPRSG--PVHVLTG-GSP----PPAALVKKV 320
Cdd:cd05968 303 GATMVLYDgapdHPKADRLWRMVEDHEITHLGLSPTLIRAL-KPRGDAPVNAHDlsSLRVLGStGEPwnpePWNWLFETV 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 321 QRLGFQVMHAYGQTEATGPILFCewqdewNRLPENQQMELKArqgiSILGLAdVDVKNKETQKSAPrdgkTMGEILIKGS 400
Cdd:cd05968 382 GKGRNPIINYSGGTEISGGILGN------VLIKPIKPSSFNG----PVPGMK-ADVLDESGKPARP----EVGELVLLAP 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 401 --SIMKGYLKNPKATFEAFKHGWLNT---GDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVA 475
Cdd:cd05968 447 wpGMTRGFWRDEDRYLETYWSRFDNVwvhGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIG 526
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15218839 476 MPHPTWGETPCAFVVLeksettikEDRVDKFQTRERNLIEYCRENLPHFMCPRKVVFLEELPKNGNGKILKPKLR 550
Cdd:cd05968 527 VPHPVKGEAIVCFVVL--------KPGVTPTEALAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIR 593
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
28-544 |
1.08e-31 |
|
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: 128.47 E-value: 1.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 28 PNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRLDATSIAAIL 107
Cdd:cd12117 11 PDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAERLAFML 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 108 RHAKPKILFLDRSFEALARESLhllssedsnlnLPVIFIHENDfpkrasfeeldyecliQRGEPTPSMVArmfriqDEHD 187
Cdd:cd12117 91 ADAGAKVLLTDRSLAGRAGGLE-----------VAVVIDEALD----------------AGPAGNPAVPV------SPDD 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 188 PISLNYTSGTTADPKGVVISHRG-AYLCTLSAIIGWEMGTcpVYLWTLPM-FhcNGWTF-TWGTAARGGTSVCMRH---V 261
Cdd:cd12117 138 LAYVMYTSGSTGRPKGVAVTHRGvVRLVKNTNYVTLGPDD--RVLQTSPLaF--DASTFeIWGALLNGARLVLAPKgtlL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 262 TAPEIYKNIEMHNVTHMCCVPTVFNILLkgnslDLSPR--SGPVHVLTGGSPPPAALVKKVQRL--GFQVMHAYGQTEAT 337
Cdd:cd12117 214 DPDALGALIAEEGVTVLWLTAALFNQLA-----DEDPEcfAGLRELLTGGEVVSPPHVRRVLAAcpGLRLVNGYGPTENT 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 338 gpiLFCEWQdewnRLPEnqqMELKARQgISI---LGLADVDVKNkETQKSAPRDgkTMGEILIKGSSIMKGYLKNPKATF 414
Cdd:cd12117 289 ---TFTTSH----VVTE---LDEVAGS-IPIgrpIANTRVYVLD-EDGRPVPPG--VPGELYVGGDGLALGYLNRPALTA 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 415 EAF-KHGWLN------TGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCA 487
Cdd:cd12117 355 ERFvADPFGPgerlyrTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVA 434
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 15218839 488 FVVleksettiKEDRVDKFQTRErnlieYCRENLPHFMCPRKVVFLEELPKNGNGKI 544
Cdd:cd12117 435 YVV--------AEGALDAAELRA-----FLRERLPAYMVPAAFVVLDELPLTANGKV 478
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
28-544 |
1.08e-31 |
|
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: 128.55 E-value: 1.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 28 PNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRLDATSIAAIL 107
Cdd:cd17646 12 PDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAYML 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 108 RHAKPKILFLDRSFEALARESLhllsseDSNLNLPVIFIHENDFPKRAsfeeldyecliqrgEPTPsmvarmfriqdeHD 187
Cdd:cd17646 92 ADAGPAVVLTTADLAARLPAGG------DVALLGDEALAAPPATPPLV--------------PPRP------------DN 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 188 PISLNYTSGTTADPKGVVISHRGaylctLSAIIGWEMGTCP------VYLWTLPMFHCNGWTFTWGTAArGGTSVCMR-- 259
Cdd:cd17646 140 LAYVIYTSGSTGRPKGVMVTHAG-----IVNRLLWMQDEYPlgpgdrVLQKTPLSFDVSVWELFWPLVA-GARLVVARpg 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 260 -HVTAPEIYKNIEMHNVTHMCCVPTVFNILLkgNSLDLSPRSGPVHVLTGGSPPPAALVKKV-QRLGFQVMHAYGQTEAT 337
Cdd:cd17646 214 gHRDPAYLAALIREHGVTTCHFVPSMLRVFL--AEPAAGSCASLRRVFCSGEALPPELAARFlALPGAELHNLYGPTEAA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 338 GPILFCEWQDEWNRLPenqqmelkarqgISI------LGLADVDvknketQKSAPRDGKTMGEILIKGSSIMKGYLKNPK 411
Cdd:cd17646 292 IDVTHWPVRGPAETPS------------VPIgrpvpnTRLYVLD------DALRPVPVGVPGELYLGGVQLARGYLGRPA 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 412 ATFEAFKHGWLN-------TGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGET 484
Cdd:cd17646 354 LTAERFVPDPFGpgsrmyrTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAAR 433
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 485 PCAFVVLEKSETTIKEDRvdkfqtrernLIEYCRENLPHFMCPRKVVFLEELPKNGNGKI 544
Cdd:cd17646 434 LVGYVVPAAGAAGPDTAA----------LRAHLAERLPEYMVPAAFVVLDALPLTANGKL 483
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
30-551 |
4.02e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 127.10 E-value: 4.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 30 RTSIIYGKTRFTWPQTYDRCCRLAASLIS-LNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRLDATSIAAILR 108
Cdd:PRK07867 19 DRGLYFEDSFTSWREHIRGSAARAAALRArLDPTRPPHVGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDIA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 109 HAKPKILFLDRsfealarESLHLLSSEDSNLnlPVIfihenDFPKRASFEELDYEcliQRGEPTPSMVARMfriqdehDP 188
Cdd:PRK07867 99 HADCQLVLTES-------AHAELLDGLDPGV--RVI-----NVDSPAWADELAAH---RDAEPPFRVADPD-------DL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 189 ISLNYTSGTTADPKGVVISHR-----GAYLCTlsaiigwEMGTCP---VYLwTLPMFHCNGWTFTWGTAARGGTSVCMR- 259
Cdd:PRK07867 155 FMLIFTSGTSGDPKAVRCTHRkvasaGVMLAQ-------RFGLGPddvCYV-SMPLFHSNAVMAGWAVALAAGASIALRr 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 260 HVTAPEIYKNIEMHNVTHMCCVPTVFNILLkgnSLDLSP--RSGPVHVLTGGSPPPAALVKKVQRLGFQVMHAYGQTEat 337
Cdd:PRK07867 227 KFSASGFLPDVRRYGATYANYVGKPLSYVL---ATPERPddADNPLRIVYGNEGAPGDIARFARRFGCVVVDGFGSTE-- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 338 GPILFcewqdewNRLPENQQMEL-KARQGISILgladvdvkNKETQKSAPR-----DGKT-----MGEIL-IKGSSIMKG 405
Cdd:PRK07867 302 GGVAI-------TRTPDTPPGALgPLPPGVAIV--------DPDTGTECPPaedadGRLLnadeaIGELVnTAGPGGFEG 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 406 YLKNPKATFEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETP 485
Cdd:PRK07867 367 YYNDPEADAERMRGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQV 446
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15218839 486 CAFVVLeKSETTIKEDRVDKFqtrernLIEycRENLPHFMCPRKVVFLEELPKNGNGKILKPKLRD 551
Cdd:PRK07867 447 MAALVL-APGAKFDPDAFAEF------LAA--QPDLGPKQWPSYVRVCAELPRTATFKVLKRQLSA 503
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
30-551 |
6.57e-31 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 126.68 E-value: 6.57e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 30 RTSIIYGKTRFTWPQTYDRCCRLAASLISLNISKNDV-VSVMAPNTPalyEMHF---AVPMAGAVLNPINTRLDATSIAA 105
Cdd:PRK13388 17 TIAVRYGDRTWTWREVLAEAAARAAALIALADPDRPLhVGVLLGNTP---EMLFwlaAAALGGYVLVGLNTTRRGAALAA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 106 ILRHAKPKILFLDRsfealarESLHLLSSedsnLNLPVIFIHENDFPKRAsfeeldyECLIQRGEPTPsmvarmFRIQDE 185
Cdd:PRK13388 94 DIRRADCQLLVTDA-------EHRPLLDG----LDLPGVRVLDVDTPAYA-------ELVAAAGALTP------HREVDA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 186 HDPISLNYTSGTTADPKGVVISHRGAYLCTLSAIIGWEMGTCPVYLWTLPMFHCNGWTFTWGTAARGGTSVCMR-HVTAP 264
Cdd:PRK13388 150 MDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDDVCYVSMPLFHSNAVMAGWAPAVASGAAVALPaKFSAS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 265 EIYKNIEMHNVTHMCCVPTVFNILLKGNSLDlSPRSGPVHVLTGGSPPPAALVKKVQRLGFQVMHAYGQTEATGPILfce 344
Cdd:PRK13388 230 GFLDDVRRYGATYFNYVGKPLAYILATPERP-DDADNPLRVAFGNEASPRDIAEFSRRFGCQVEDGYGSSEGAVIVV--- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 345 wqdewnRLPENQQMEL-KARQGISILgladvdvkNKETQKSAPR-----DGK------TMGEILIK-GSSIMKGYLKNPK 411
Cdd:PRK13388 306 ------REPGTPPGSIgRGAPGVAIY--------NPETLTECAVarfdaHGAllnadeAIGELVNTaGAGFFEGYYNNPE 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 412 ATFEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVL 491
Cdd:PRK13388 372 ATAERMRHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVMAALVL 451
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 492 eKSETTIKEDRVDKFQTRErnlieycrENLPHFMCPRKVVFLEELPKNGNGKILKPKLRD 551
Cdd:PRK13388 452 -RDGATFDPDAFAAFLAAQ--------PDLGTKAWPRYVRIAADLPSTATNKVLKRELIA 502
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
40-550 |
1.83e-30 |
|
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: 124.17 E-value: 1.83e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 40 FTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFLDR 119
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 120 SfealareSLHLLSSedsnlnlpvifihendfpkrasfeeldyecliqrgeptpsmvarmfriqdehDPISLNYTSGTTA 199
Cdd:cd05973 81 A-------NRHKLDS----------------------------------------------------DPFVMMFTSGTTG 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 200 DPKGVVIShrgaylctLSAIIGWE------MGTCP--VYlWTL--PmfhcnGWTFTWGTAARG----GTSVCMRH--VTA 263
Cdd:cd05973 102 LPKGVPVP--------LRALAAFGaylrdaVDLRPedSF-WNAadP-----GWAYGLYYAITGplalGHPTILLEggFSV 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 264 PEIYKNIEMHNVTHMCCVPTVFNILLK-GNSLDLSPRSGPVHVLTGGSP-PPAALVKKVQRLGFQVMHAYGQTEaTGPIL 341
Cdd:cd05973 168 ESTWRVIERLGVTNLAGSPTAYRLLMAaGAEVPARPKGRLRRVSSAGEPlTPEVIRWFDAALGVPIHDHYGQTE-LGMVL 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 342 FCEWQDEwnrlpenqqMELKA-RQGISILGLAdVDVKNKETQKSAPRDgktMGEILI--KGSSIM--KGYLKNPKATFEA 416
Cdd:cd05973 247 ANHHALE---------HPVHAgSAGRAMPGWR-VAVLDDDGDELGPGE---PGRLAIdiANSPLMwfRGYQLPDTPAIDG 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 417 fkhGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVL-EKSE 495
Cdd:cd05973 314 ---GYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLrGGHE 390
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 15218839 496 TTikEDRVDKFQTrernlieYCRENLPHFMCPRKVVFLEELPKNGNGKILKPKLR 550
Cdd:cd05973 391 GT--PALADELQL-------HVKKRLSAHAYPRTIHFVDELPKTPSGKIQRFLLR 436
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
40-500 |
1.94e-30 |
|
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: 124.89 E-value: 1.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 40 FTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFLDR 119
Cdd:cd05932 7 FTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFVGK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 120 -----SFEALARESLHLLSSEdsnlnlpvifihendFPKRASFEElDYECLIQRGEPTPSMVARmfriqDEHDPISLNYT 194
Cdd:cd05932 87 lddwkAMAPGVPEGLISISLP---------------PPSAANCQY-QWDDLIAQHPPLEERPTR-----FPEQLATLIYT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 195 SGTTADPKGVVISHrGAYLCTLSAIIGwEMGTCP--VYLWTLPMFHCNGWTFTWGTAARGGTSVCMRHV--TAPEiykNI 270
Cdd:cd05932 146 SGTTGQPKGVMLTF-GSFAWAAQAGIE-HIGTEEndRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAESldTFVE---DV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 271 EMHNVTHMCCVP---TVF-------------NILLK--------------GNSLDlsprsgPVHVLTGGSPP-PAALVKK 319
Cdd:cd05932 221 QRARPTLFFSVPrlwTKFqqgvqdkipqqklNLLLKipvvnslvkrkvlkGLGLD------QCRLAGCGSAPvPPALLEW 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 320 VQRLGFQVMHAYGQTEATGpilfcewqdewnrlpeNQQMELKARQGISILGLA--DVDVKNKETqksaprdgktmGEILI 397
Cdd:cd05932 295 YRSLGLNILEAYGMTENFA----------------YSHLNYPGRDKIGTVGNAgpGVEVRISED-----------GEILV 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 398 KGSSIMKGYLKNPKATFEAF-KHGWLNTGDVGVIHPDGHVEIKDRSKDII-ISGGENISSVEVENVLYKYPKVLETAVVA 475
Cdd:cd05932 348 RSPALMMGYYKDPEATAEAFtADGFLRTGDKGELDADGNLTITGRVKDIFkTSKGKYVAPAPIENKLAEHDRVEMVCVIG 427
|
490 500
....*....|....*....|....*..
gi 15218839 476 --MPHPTWGETPCAFVVLEKSETTIKE 500
Cdd:cd05932 428 sgLPAPLALVVLSEEARLRADAFARAE 454
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
41-544 |
4.21e-30 |
|
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: 124.27 E-value: 4.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 41 TWPQTYDRCCRLAASLISLNiSKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPI----NTRLDATsIAAILRHAKPKILF 116
Cdd:cd05931 26 TYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLppptPGRHAER-LAAILADAGPRVVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 117 LDRSFEALARESLHLLSSedsNLNLPVIFIHENDFPKRASFEEldyecliqrgePTPsmvarmfriqDEHDPISLNYTSG 196
Cdd:cd05931 104 TTAAALAAVRAFAASRPA---AGTPRLLVVDLLPDTSAADWPP-----------PSP----------DPDDIAYLQYTSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 197 TTADPKGVVISHRGAyLCTLSAII-GWEMG-TCPVYLWtLPMFHCNGWTFTWGTAA-RGGTSVCM---RHVTAPEIY-KN 269
Cdd:cd05931 160 STGTPKGVVVTHRNL-LANVRQIRrAYGLDpGDVVVSW-LPLYHDMGLIGGLLTPLySGGPSVLMspaAFLRRPLRWlRL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 270 IEMHNVTHMCcVPT-VFNILLK------GNSLDLSPrsgpVHVLTGGSPP--PAAL---VKKVQRLGF--QVMH-AYGQT 334
Cdd:cd05931 238 ISRYRATISA-APNfAYDLCVRrvrdedLEGLDLSS----WRVALNGAEPvrPATLrrfAEAFAPFGFrpEAFRpSYGLA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 335 EAT----------GPILfcewqDEWNRLPENQQMELKA---RQGISILG----LADVDVKNKETQKSAPRDGKTMGEILI 397
Cdd:cd05931 313 EATlfvsggppgtGPVV-----LRVDRDALAGRAVAVAaddPAARELVScgrpLPDQEVRIVDPETGRELPDGEVGEIWV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 398 KGSSIMKGYLKNPKATFEAFK-------HGWLNTGDVGVIHpDGHVEIKDRSKDIIISGGENIssvevenvlykYPKVLE 470
Cdd:cd05931 388 RGPSVASGYWGRPEATAETFGalaatdeGGWLRTGDLGFLH-DGELYITGRLKDLIIVRGRNH-----------YPQDIE 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 471 TAVVAMPHPTWGETPCAFVVLEKSETT---IKEDRVDKFQTRERNLIEYCRENLP--HFMCPRKVVFLE--ELPKNGNGK 543
Cdd:cd05931 456 ATAEEAHPALRPGCVAAFSVPDDGEERlvvVAEVERGADPADLAAIAAAIRAAVAreHGVAPADVVLVRpgSIPRTSSGK 535
|
.
gi 15218839 544 I 544
Cdd:cd05931 536 I 536
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
54-557 |
6.21e-30 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 125.81 E-value: 6.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 54 ASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFLDRSF-EALAreslhlL 132
Cdd:PRK08633 655 ARLLKRELKDEENVGILLPPSVAGALANLALLLAGKVPVNLNYTASEAALKSAIEQAQIKTVITSRKFlEKLK------N 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 133 SSEDSNLNLPVIFIHENDFPKRASFEELDYECLIQRGEPTPSMVARMFRIQDEHDPISLNYTSGTTADPKGVVISHR--G 210
Cdd:PRK08633 729 KGFDLELPENVKVIYLEDLKAKISKVDKLTALLAARLLPARLLKRLYGPTFKPDDTATIIFSSGSEGEPKGVMLSHHniL 808
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 211 AYLCTLSAIIGWEMGTcpVYLWTLPMFHCNGWTFT-WGTAARGGTSVCmrHVT---APEIYKNIEMHNVTHMCCVPTVFN 286
Cdd:PRK08633 809 SNIEQISDVFNLRNDD--VILSSLPFFHSFGLTVTlWLPLLEGIKVVY--HPDptdALGIAKLVAKHRATILLGTPTFLR 884
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 287 ILLKGN--------SLDLsprsgpvhVLTGGSPPPAALVKKVQ-RLGFQVMHAYGQTEaTGPILFCEwqdewnrLP---E 354
Cdd:PRK08633 885 LYLRNKklhplmfaSLRL--------VVAGAEKLKPEVADAFEeKFGIRILEGYGATE-TSPVASVN-------LPdvlA 948
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 355 NQQMELKA-RQGISILGLADVDVK--NKETQKSAPrdGKTMGEILIKGSSIMKGYLKNPKATFEAFKH----GWLNTGDV 427
Cdd:PRK08633 949 ADFKRQTGsKEGSVGMPLPGVAVRivDPETFEELP--PGEDGLILIGGPQVMKGYLGDPEKTAEVIKDidgiGWYVTGDK 1026
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 428 GVIHPDGHVEIKDR----SKdIiisGGENISSVEVENVLYK--YPKVLETAVVAMPHPTWGEtpcAFVVLEKSETTiked 501
Cdd:PRK08633 1027 GHLDEDGFLTITDRysrfAK-I---GGEMVPLGAVEEELAKalGGEEVVFAVTAVPDEKKGE---KLVVLHTCGAE---- 1095
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 15218839 502 rvdKFQTRERNLIEycrENLPHFMCPRKVVFLEELPKNGNGKI-LKpKLRDIAKGLV 557
Cdd:PRK08633 1096 ---DVEELKRAIKE---SGLPNLWKPSRYFKVEALPLLGSGKLdLK-GLKELALALL 1145
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
29-546 |
1.22e-29 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 123.08 E-value: 1.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 29 NRTSIIY----GKTRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRLDATSIA 104
Cdd:PRK04319 59 DKVALRYldasRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVR 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 105 AILRHAKPKILFL-DRSFEALARESL----H-LLSSEDSNLNLPVIfihenDFPKRASFEELDYECliqrgEPTpsmvar 178
Cdd:PRK04319 139 DRLEDSEAKVLITtPALLERKPADDLpslkHvLLVGEDVEEGPGTL-----DFNALMEQASDEFDI-----EWT------ 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 179 mfriqDEHDPISLNYTSGTTADPKGVVISHRGA------------------YLCTlsAIIGWEMGTcpVYLWTLPMFHcn 240
Cdd:PRK04319 203 -----DREDGAILHYTSGSTGKPKGVLHVHNAMlqhyqtgkyvldlheddvYWCT--ADPGWVTGT--SYGIFAPWLN-- 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 241 gwtftwgtaarGGTSVCMRHVTAPEI-YKNIEMHNVTHMCCVPTVFNILLKGNS-----LDLSP-RsgpvHVLTGGSP-P 312
Cdd:PRK04319 272 -----------GATNVIDGGRFSPERwYRILEDYKVTVWYTAPTAIRMLMGAGDdlvkkYDLSSlR----HILSVGEPlN 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 313 PAALV--KKVqrLGFQVMHAYGQTEaTGPILFCEWQdewnrlpenqQMELK-ARQGISILGLADVDVKNKETQKSAPRdg 389
Cdd:PRK04319 337 PEVVRwgMKV--FGLPIHDNWWMTE-TGGIMIANYP----------AMDIKpGSMGKPLPGIEAAIVDDQGNELPPNR-- 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 390 ktMGEILIKGS--SIMKGYLKNPKATFEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPK 467
Cdd:PRK04319 402 --MGNLAIKKGwpSMMRGIWNNPEKYESYFAGDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPA 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 468 VLETAVVAMPHPTWGETPCAFVVL----EKSEtTIKEDrvdkfqtrernLIEYCRENLPHFMCPRKVVFLEELPKNGNGK 543
Cdd:PRK04319 480 VAEAGVIGKPDPVRGEIIKAFVALrpgyEPSE-ELKEE-----------IRGFVKKGLGAHAAPREIEFKDKLPKTRSGK 547
|
...
gi 15218839 544 ILK 546
Cdd:PRK04319 548 IMR 550
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
16-549 |
1.48e-29 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 122.41 E-value: 1.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 16 PMTFLKRASECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPIN 95
Cdd:PRK13383 37 PYTLLAVTAARWPGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPIS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 96 TRLDATSIAAILRHAKPKILFLDRSF-EALAreslhllSSEDSnlnlpVIFIHendfPKRASFEEldyecliQRGEPTPS 174
Cdd:PRK13383 117 TEFRSDALAAALRAHHISTVVADNEFaERIA-------GADDA-----VAVID----PATAGAEE-------SGGRPAVA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 175 MVARMFRIqdehdpislnyTSGTTADPKGV-----VISHRGAYLCTLSAI---IGWEMGTcpvylwTLPMFHCNGWTFTW 246
Cdd:PRK13383 174 APGRIVLL-----------TSGTTGKPKGVprapqLRSAVGVWVTILDRTrlrTGSRISV------AMPMFHGLGLGMLM 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 247 GTAARGGTSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFnillkGNSLDLSPR---SGPVHVL-----TGGSPPPAALVK 318
Cdd:PRK13383 237 LTIALGGTVLTHRHFDAEAALAQASLHRADAFTAVPVVL-----ARILELPPRvraRNPLPQLrvvmsSGDRLDPTLGQR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 319 KVQRLGFQVMHAYGQTE------ATgPILFCEWqdewnrlPENQqmelkarqGISILGlADVDVKNKETQKSAPRdgkTM 392
Cdd:PRK13383 312 FMDTYGDILYNGYGSTEvgigalAT-PADLRDA-------PETV--------GKPVAG-CPVRILDRNNRPVGPR---VT 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 393 GEILIKGSSIMKGYlknPKATFEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETA 472
Cdd:PRK13383 372 GRIFVGGELAGTRY---TDGGGKAVVDGMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNA 448
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15218839 473 VVAMPHPTWGETPCAFVVLEKSETtikedrVDKFQTRernliEYCRENLPHFMCPRKVVFLEELPKNGNGKILKPKL 549
Cdd:PRK13383 449 VIGVPDERFGHRLAAFVVLHPGSG------VDAAQLR-----DYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
16-555 |
7.09e-29 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 120.88 E-value: 7.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 16 PMTFLKRASECYPNRTSIIY-----GKTRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAV 90
Cdd:PRK05857 13 PSTVLDRVFEQARQQPEAIAlrrcdGTSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 91 LNPINTRLDATSIAAILRHAKPKILFLDRSFEALARESLHLLSSedsnlnLPVIFIH-ENDFPKRASFEELDYecliQRG 169
Cdd:PRK05857 93 AVMADGNLPIAAIERFCQITDPAAALVAPGSKMASSAVPEALHS------IPVIAVDiAAVTRESEHSLDAAS----LAG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 170 EPTPSMvarmfriqdeHDPISLNYTSGTTADPKGVVISHRgaylcTLSAI-----------IGWEMGTCPVYlwTLPMFH 238
Cdd:PRK05857 163 NADQGS----------EDPLAMIFTSGTTGEPKAVLLANR-----TFFAVpdilqkeglnwVTWVVGETTYS--PLPATH 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 239 CNGWTFTWGTAARGGTSVCMRHVTApEIYKNIEMHNVTHMCCVPTVFNIL---LKGNSLDLSPRSGPVHvltGGSPPPAA 315
Cdd:PRK05857 226 IGGLWWILTCLMHGGLCVTGGENTT-SLLEILTTNAVATTCLVPTLLSKLvseLKSANATVPSLRLVGY---GGSRAIAA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 316 LVKKVQRLGFQVMHAYGQTEaTGPILFCewqdewnrLPENQQMELKARQGIsiLG---------LADVDVKNKETQKSAP 386
Cdd:PRK05857 302 DVRFIEATGVRTAQVYGLSE-TGCTALC--------LPTDDGSIVKIEAGA--VGrpypgvdvyLAATDGIGPTAPGAGP 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 387 rdGKTMGEILIKGSSIMKGYLKNPKATFEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYP 466
Cdd:PRK05857 371 --SASFGTLWIKSPANMLGYWNNPERTAEVLIDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVS 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 467 KVLETAVVAMPHPTWGetpcAFVVLEKSETTiKEDRVDKFQTRERNLIEYCRENlPHFMCPRKVVFLEELPKNGNGKILK 546
Cdd:PRK05857 449 GVREAACYEIPDEEFG----ALVGLAVVASA-ELDESAARALKHTIAARFRRES-EPMARPSTIVIVTDIPRTQSGKVMR 522
|
....*....
gi 15218839 547 PKLRDIAKG 555
Cdd:PRK05857 523 ASLAAAATA 531
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
20-551 |
7.70e-29 |
|
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.
Pssm-ID: 341274 [Multi-domain] Cd Length: 537 Bit Score: 120.68 E-value: 7.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 20 LKRASECYPNRTSII----YGKTR-FTWPQTYDRCCRLAASLISLNISKNDVVSVMapnTPALYEMHFAVP---MAGAVL 91
Cdd:cd05970 23 VDAMAKEYPDKLALVwcddAGEERiFTFAELADYSDKTANFFKAMGIGKGDTVMLT---LKRRYEFWYSLLalhKLGAIA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 92 NPINTRLDATSIAAILRHAKPKILFLDRsfEALARESLHLLSSEDSNLNLPViFIHEndfPKRASFEELDYECLiqrgEP 171
Cdd:cd05970 100 IPATHQLTAKDIVYRIESADIKMIVAIA--EDNIPEEIEKAAPECPSKPKLV-WVGD---PVPEGWIDFRKLIK----NA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 172 TPSMVARMFRIQDEHDPISLNY-TSGTTADPKgvVISHRGAYlcTLSAIIgwemgtcpvylwTLPMFHC---NGWTFT-- 245
Cdd:cd05970 170 SPDFERPTANSYPCGEDILLVYfSSGTTGMPK--MVEHDFTY--PLGHIV------------TAKYWQNvreGGLHLTva 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 246 ---WGTAARG---GTSVC--------MRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGnslDLSPR--SGPVHVLTGG 309
Cdd:cd05970 234 dtgWGKAVWGkiyGQWIAgaavfvydYDKFDPKALLEKLSKYGVTTFCAPPTIYRFLIRE---DLSRYdlSSLRYCTTAG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 310 SP-PPAALVKKVQRLGFQVMHAYGQTEATGPILFCEWQDewnrlPENQQMELKARQ-GISILglaDVDVKNKETQKSapr 387
Cdd:cd05970 311 EAlNPEVFNTFKEKTGIKLMEGFGQTETTLTIATFPWME-----PKPGSMGKPAPGyEIDLI---DREGRSCEAGEE--- 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 388 dgktmGEILIKGSS-----IMKGYLKNPKATFEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVL 462
Cdd:cd05970 380 -----GEIVIRTSKgkpvgLFGGYYKDAEKTAEVWHDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESAL 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 463 YKYPKVLETAVVAMPHPTWGETPCAFVVLEK----SETTIKEdrvdkfqtrernLIEYCRENLPHFMCPRKVVFLEELPK 538
Cdd:cd05970 455 IQHPAVLECAVTGVPDPIRGQVVKATIVLAKgyepSEELKKE------------LQDHVKKVTAPYKYPRIVEFVDELPK 522
|
570
....*....|...
gi 15218839 539 NGNGKILKPKLRD 551
Cdd:cd05970 523 TISGKIRRVEIRE 535
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
29-553 |
1.05e-28 |
|
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: 119.74 E-value: 1.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 29 NRTSIIYGKTRFtwpqtydrccrlAASLISLNISKN----DVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRLDATSIA 104
Cdd:cd05909 4 LGTSLTYRKLLT------------GAIALARKLAKMtkegENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 105 AILRHAKPKILFLDRSFEalarESLHLLSSEDSNLNLPVIFIheNDFPKRASFEEldyECL--IQRGEPTPSMVARMFRI 182
Cdd:cd05909 72 ACIKLAGIKTVLTSKQFI----EKLKLHHLFDVEYDARIVYL--EDLRAKISKAD---KCKafLAGKFPPKWLLRIFGVA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 183 -QDEHDPISLNYTSGTTADPKGVVISHRG----AYLCTlsAIIgwEMGTCPVYLWTLPMFHCNGWTFT-WGTAARGGTSV 256
Cdd:cd05909 143 pVQPDDPAVILFTSGSEGLPKGVVLSHKNllanVEQIT--AIF--DPNPEDVVFGALPFFHSFGLTGClWLPLLSGIKVV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 257 CMRHVTAPE-IYKNIEMHNVTHMCCVPTVFNILLK-GNSLDLSprsGPVHVLTGGSPPPAALVKKVQ-RLGFQVMHAYGQ 333
Cdd:cd05909 219 FHPNPLDYKkIPELIYDKKATILLGTPTFLRGYARaAHPEDFS---SLRLVVAGAEKLKDTLRQEFQeKFGIRILEGYGT 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 334 TEATgPILFCewqdewNRlpenQQMElkARQGISILGLADVDVKNKETQKSAPRDGKTMGEILIKGSSIMKGYLKNPKAT 413
Cdd:cd05909 296 TECS-PVISV------NT----PQSP--NKEGTVGRPLPGMEVKIVSVETHEEVPIGEGGLLLVRGPNVMLGYLNEPELT 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 414 FEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYK-YPKVLETAVVAMPHPTWGETPCAFVVLE 492
Cdd:cd05909 363 SFAFGDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEiLPEDNEVAVVSVPDGRKGEKIVLLTTTT 442
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15218839 493 ksettikedrvdkFQTRErNLIEYCRE-NLPHFMCPRKVVFLEELPKNGNGKILKPKLRDIA 553
Cdd:cd05909 443 -------------DTDPS-SLNDILKNaGISNLAKPSYIHQVEEIPLLGTGKPDYVTLKALA 490
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
186-551 |
1.08e-28 |
|
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: 118.95 E-value: 1.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 186 HDPISLNYTSGTTADPKGVVISHRGaylctLSAIIGWE---MGTCP---VYLWTLPMFHCNGWTFtWGTAARGGTsVCMR 259
Cdd:cd17653 105 DDLAYIIFTSGSTGIPKGVMVPHRG-----VLNYVSQPparLDVGPgsrVAQVLSIAFDACIGEI-FSTLCNGGT-LVLA 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 260 HVTAPEIYKnIEMHNVTHmcCVPTVFNILlkgnsldlSPRSGP-VH-VLTGGSPPPAALVKKvQRLGFQVMHAYGQTEAT 337
Cdd:cd17653 178 DPSDPFAHV-ARTVDALM--STPSILSTL--------SPQDFPnLKtIFLGGEAVPPSLLDR-WSPGRRLYNAYGPTECT 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 338 GPILFCEWQDEwNRLPENQQMelkARQGISILgladvdvknkETQKSAPRDGKTmGEILIKGSSIMKGYLKNPKATFEAF 417
Cdd:cd17653 246 ISSTMTELLPG-QPVTIGKPI---PNSTCYIL----------DADLQPVPEGVV-GEICISGVQVARGYLGNPALTASKF 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 418 K-----HGWL--NTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPhptwGETPCAFVV 490
Cdd:cd17653 311 VpdpfwPGSRmyRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQSQPEVTQAAAIVV----NGRLVAFVT 386
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15218839 491 LEksetTIKEDRvdkfqtrernLIEYCRENLPHFMCPRKVVFLEELPKNGNGKILKPKLRD 551
Cdd:cd17653 387 PE----TVDVDG----------LRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
28-546 |
1.22e-28 |
|
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: 119.30 E-value: 1.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 28 PNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRLDATSIAAIL 107
Cdd:cd12114 1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 108 rhakpkilfldrsfeALARESLHLLSSEDSnlnlpvifiHENDFPKRASFEELDyeclIQRGEPTPSMVARmfriqDEHD 187
Cdd:cd12114 81 ---------------ADAGARLVLTDGPDA---------QLDVAVFDVLILDLD----ALAAPAPPPPVDV-----APDD 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 188 PISLNYTSGTTADPKGVVISHRGAyLCTLSAIIG-WEMGTCPVYLwTLPMFHCNGWTF-TWGTAARGGTSVCMRHVTAPE 265
Cdd:cd12114 128 LAYVIFTSGSTGTPKGVMISHRAA-LNTILDINRrFAVGPDDRVL-ALSSLSFDLSVYdIFGALSAGATLVLPDEARRRD 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 266 IY---KNIEMHNVTHMCCVPTVFNILL----KGNSLDLSPRSgpvhVLTGGSPPPAALVKKVQRL--GFQVMHAYGQTEA 336
Cdd:cd12114 206 PAhwaELIERHGVTLWNSVPALLEMLLdvleAAQALLPSLRL----VLLSGDWIPLDLPARLRALapDARLISLGGATEA 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 337 TGPILFCEWQD---EWNRLP-----ENQQMELKARQGisilglADVdvknketqksaPrDGkTMGEILIKGSSIMKGYLK 408
Cdd:cd12114 282 SIWSIYHPIDEvppDWRSIPygrplANQRYRVLDPRG------RDC-----------P-DW-VPGELWIGGRGVALGYLG 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 409 NPKATFEAFKH-----GWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTwGE 483
Cdd:cd12114 343 DPELTAARFVThpdgeRLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDPG-GK 421
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15218839 484 TPCAFVVLEKSETTIKEDRVDKFQTrernlieycrENLPHFMCPRKVVFLEELPKNGNGKILK 546
Cdd:cd12114 422 RLAAFVVPDNDGTPIAPDALRAFLA----------QTLPAYMIPSRVIALEALPLTANGKVDR 474
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
19-561 |
2.31e-28 |
|
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: 120.73 E-value: 2.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 19 FLKRAsECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRL 98
Cdd:COG1020 482 FEAQA-ARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAY 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 99 DATSIAAILRHAKPKILFLDRSFealaRESLhllssedSNLNLPVIfihendfpkrasfeELDYECLIQRGEPTPSmvar 178
Cdd:COG1020 561 PAERLAYMLEDAGARLVLTQSAL----AARL-------PELGVPVL--------------ALDALALAAEPATNPP---- 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 179 mfRIQDEHDPISLNYTSGTTADPKGVVISHRGAyLCTLSAIIGW-EMGTCPVYLWTLPMfhcngwTF------TWGTAAR 251
Cdd:COG1020 612 --VPVTPDDLAYVIYTSGSTGRPKGVMVEHRAL-VNLLAWMQRRyGLGPGDRVLQFASL------SFdasvweIFGALLS 682
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 252 GGTSVCMR---HVTAPEIYKNIEMHNVTHMCCVPTVFNILLkgnSLDLSPRSGPVHVLTGGSPPPAALVKKVQRL--GFQ 326
Cdd:COG1020 683 GATLVLAPpeaRRDPAALAELLARHRVTVLNLTPSLLRALL---DAAPEALPSLRLVLVGGEALPPELVRRWRARlpGAR 759
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 327 VMHAYGQTEATGPILFCEWQDE---WNRLP-----ENQQMELkarqgisilgladVDvknkETQKSAPrDGkTMGEILIK 398
Cdd:COG1020 760 LVNLYGPTETTVDSTYYEVTPPdadGGSVPigrpiANTRVYV-------------LD----AHLQPVP-VG-VPGELYIG 820
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 399 GSSIMKGYLKNPKATFEAF------KHG--WLNTGDVGVIHPDGHVEIKDRS----KdiiISG-----GenissvEVENV 461
Cdd:COG1020 821 GAGLARGYLNRPELTAERFvadpfgFPGarLYRTGDLARWLPDGNLEFLGRAddqvK---IRGfrielG------EIEAA 891
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 462 LYKYPKVLETAVVAMPHPTWGETPCAFVVLEKSETTIKEDRVDKFQTRernlieycrenLPHFMCPRKVVFLEELPKNGN 541
Cdd:COG1020 892 LLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLALALL-----------LPPYMVPAAVVLLLPLPLTGN 960
|
570 580
....*....|....*....|
gi 15218839 542 GKILKPKLRDIAKGLVVEDE 561
Cdd:COG1020 961 GKLDRLALPAPAAAAAAAAA 980
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
193-540 |
4.21e-28 |
|
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: 118.09 E-value: 4.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 193 YTSGTTADPKGVVISHRG--AYLCTLSAIIGWEMGTCPVYLWTLPMFHCNGWTFTWGTAARGGT----SVcmRHVTaPEI 266
Cdd:cd17639 95 YTSGSTGNPKGVMLTHGNlvAGIAGLGDRVPELLGPDDRYLAYLPLAHIFELAAENVCLYRGGTigygSP--RTLT-DKS 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 267 YKN----IEMHNVTHMCCVPTVFNILLKGNSLDLSPRSG-----------------------PV---------------- 303
Cdd:cd17639 172 KRGckgdLTEFKPTLMVGVPAIWDTIRKGVLAKLNPMGGlkrtlfwtayqsklkalkegpgtPLldelvfkkvraalggr 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 304 --HVLTGGSPppaaLVKKVQR----LGFQVMHAYGQTE--ATGPILfcEWQD-EWNRL--PENQQmELKarqgisilgLA 372
Cdd:cd17639 252 lrYMLSGGAP----LSADTQEflniVLCPVIQGYGLTEtcAGGTVQ--DPGDlETGRVgpPLPCC-EIK---------LV 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 373 DVDVKNKETQKSAPRdgktmGEILIKGSSIMKGYLKNPKATFEAFK-HGWLNTGDVGVIHPDGHVEIKDRSKDII-ISGG 450
Cdd:cd17639 316 DWEEGGYSTDKPPPR-----GEILIRGPNVFKGYYKNPEKTKEAFDgDGWFHTGDIGEFHPDGTLKIIDRKKDLVkLQNG 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 451 ENISSVEVENVLYKYPKVLETAVVAMPHPTWgetPCAFVV-----LEKS-----------ETTIKEDRVDKFQTRErnLI 514
Cdd:cd17639 391 EYIALEKLESIYRSNPLVNNICVYADPDKSY---PVAIVVpnekhLTKLaekhgvinsewEELCEDKKLQKAVLKS--LA 465
|
410 420
....*....|....*....|....*....
gi 15218839 515 EYCRE-NLPHFMCPRKVVFLEEL--PKNG 540
Cdd:cd17639 466 ETARAaGLEKFEIPQGVVLLDEEwtPENG 494
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
22-544 |
6.56e-28 |
|
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: 117.44 E-value: 6.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 22 RASECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRLDAT 101
Cdd:cd17651 3 RQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 102 SIAAILRHAKPKILfldrsfealareslhLLSSEDSNlnlpvifihendfpkRASFEELDYECLIQRGEPTPSMVARMFR 181
Cdd:cd17651 83 RLAFMLADAGPVLV---------------LTHPALAG---------------ELAVELVAVTLLDQPGAAAGADAEPDPA 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 182 IqDEHDPISLNYTSGTTADPKGVVISHRgaylcTLSAIIGW---EMGTCP---VYLWTLPMFHCNGWTfTWGTAARGGTs 255
Cdd:cd17651 133 L-DADDLAYVIYTSGSTGRPKGVVMPHR-----SLANLVAWqarASSLGPgarTLQFAGLGFDVSVQE-IFSTLCAGAT- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 256 vcmRHVTAPEIYKN-------IEMHNVTHmCCVPTVFnillkGNSLDLSPRSGPV------HVLTGGSPPP--AALVKKV 320
Cdd:cd17651 205 ---LVLPPEEVRTDppalaawLDEQRISR-VFLPTVA-----LRALAEHGRPLGVrlaalrYLLTGGEQLVltEDLREFC 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 321 QRLGFQVMH-AYGQTEATgpILFCEW----QDEWNRLPenqqmelkarqgiSI---LGLADVDVKNkETQKSAPrDGKTm 392
Cdd:cd17651 276 AGLPGLRLHnHYGPTETH--VVTALSlpgdPAAWPAPP-------------PIgrpIDNTRVYVLD-AALRPVP-PGVP- 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 393 GEILIKGSSIMKGYLKNPKATFEAF-KHGWLN------TGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKY 465
Cdd:cd17651 338 GELYIGGAGLARGYLNRPELTAERFvPDPFVPgarmyrTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARH 417
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15218839 466 PKVLETAVVAMPHPTWGETPCAFVVLEksettiKEDRVDKFQTRERnlieyCRENLPHFMCPRKVVFLEELPKNGNGKI 544
Cdd:cd17651 418 PGVREAVVLAREDRPGEKRLVAYVVGD------PEAPVDAAELRAA-----LATHLPEYMVPSAFVLLDALPLTPNGKL 485
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
12-554 |
2.63e-27 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 115.86 E-value: 2.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 12 VPLTPMtfLKRasECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVl 91
Cdd:PRK10946 25 LPLTDI--LTR--HAASDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGVA- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 92 nPINT-----RLDATSIAailRHAKPKILFLDRSFEALARES-LHLLSSEDSNLNLpVIFIHENdfpkrasfEELDYECL 165
Cdd:PRK10946 100 -PVNAlfshqRSELNAYA---SQIEPALLIADRQHALFSDDDfLNTLVAEHSSLRV-VLLLNDD--------GEHSLDDA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 166 IQRGE------PTPSMVARMFRIqdehdpislnyTSGTTADPKGVVISH-------RGA-----------YLCTLSAIIG 221
Cdd:PRK10946 167 INHPAedftatPSPADEVAFFQL-----------SGGSTGTPKLIPRTHndyyysvRRSveicgftpqtrYLCALPAAHN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 222 WEMGTcPvylWTLPMFHCngwtftwgtaarGGTSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKG---------- 291
Cdd:PRK10946 236 YPMSS-P---GALGVFLA------------GGTVVLAPDPSATLCFPLIEKHQVNVTALVPPAVSLWLQAiaeggsraql 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 292 NSLDLsprsgpvhVLTGGSPPPAALVKKV-QRLGFQVMHAYGQTEAtgpiLFCewqdeWNRLPENQQMELKArQGISILG 370
Cdd:PRK10946 300 ASLKL--------LQVGGARLSETLARRIpAELGCQLQQVFGMAEG----LVN-----YTRLDDSDERIFTT-QGRPMSP 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 371 LADVDVKNKETQKSAPrdGKTmGEILIKGSSIMKGYLKNPKATFEAF-KHGWLNTGDVGVIHPDGHVEIKDRSKDIIISG 449
Cdd:PRK10946 362 DDEVWVADADGNPLPQ--GEV-GRLMTRGPYTFRGYYKSPQHNASAFdANGFYCSGDLVSIDPDGYITVVGREKDQINRG 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 450 GENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVlekSETTIKEDRVDKFqTRERNLIEYcrenlphfMCPRK 529
Cdd:PRK10946 439 GEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLV---VKEPLKAVQLRRF-LREQGIAEF--------KLPDR 506
|
570 580
....*....|....*....|....*
gi 15218839 530 VVFLEELPKNGNGKILKPKLRDIAK 554
Cdd:PRK10946 507 VECVDSLPLTAVGKVDKKQLRQWLA 531
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
18-544 |
3.88e-27 |
|
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: 114.34 E-value: 3.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 18 TFLKRASECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTR 97
Cdd:cd12115 3 DLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 98 LDATSIAAILRHAKPKILfldrsfealareslhllssedsnlnlpvifihendfpkrasfeeldyecliqrgeptpsmva 177
Cdd:cd12115 83 YPPERLRFILEDAQARLV-------------------------------------------------------------- 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 178 rmfrIQDEHDPISLNYTSGTTADPKGVVISHRGAylctlSAIIGWEMGTCPVYLWT-----------LPMFHcngwtfTW 246
Cdd:cd12115 101 ----LTDPDDLAYVIYTSGSTGRPKGVAIEHRNA-----AAFLQWAAAAFSAEELAgvlastsicfdLSVFE------LF 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 247 GTAARGGTSVCMRHVTAPEIYKNIEmhNVTHMCCVPTVFNILLKGNSLdlsPRSgpVHVLT-GGSPPPAALVKKVQRL-- 323
Cdd:cd12115 166 GPLATGGKVVLADNVLALPDLPAAA--EVTLINTVPSAAAELLRHDAL---PAS--VRVVNlAGEPLPRDLVQRLYARlq 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 324 GFQVMHAYGQTEATGPILFCEwqdewnrlpenqqMELKARQGISI---LGLADVDVKNKETQksaPRDGKTMGEILIKGS 400
Cdd:cd12115 239 VERVVNLYGPSEDTTYSTVAP-------------VPPGASGEVSIgrpLANTQAYVLDRALQ---PVPLGVPGELYIGGA 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 401 SIMKGYLKNPKATFEAF----KHGWL---NTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAV 473
Cdd:cd12115 303 GVARGYLGRPGLTAERFlpdpFGPGArlyRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVV 382
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15218839 474 VAMPHPTWGETPCAFVVLEKSETTIKEDRVDKFQTRernlieycrenLPHFMCPRKVVFLEELPKNGNGKI 544
Cdd:cd12115 383 VAIGDAAGERRLVAYIVAEPGAAGLVEDLRRHLGTR-----------LPAYMVPSRFVRLDALPLTPNGKI 442
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
28-555 |
1.02e-26 |
|
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.
Pssm-ID: 341270 [Multi-domain] Cd Length: 608 Bit Score: 114.58 E-value: 1.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 28 PNRTSIIY-----GKTR-FTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRLDAT 101
Cdd:cd05966 67 GDKVAIIWegdepDQSRtITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFAGFSAE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 102 SIAAILRHAKPKILF-LDRSF--------EALARESLHLLSSEDS-----NLNLPVIFIHENDFPkrasFEELdyecliQ 167
Cdd:cd05966 147 SLADRINDAQCKLVItADGGYrggkviplKEIVDEALEKCPSVEKvlvvkRTGGEVPMTEGRDLW----WHDL------M 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 168 RGEPTPSMVARMfriqDEHDPISLNYTSGTTADPKGVVISHrGAYL--------------------CTlsAIIGWEMG-T 226
Cdd:cd05966 217 AKQSPECEPEWM----DSEDPLFILYTSGSTGKPKGVVHTT-GGYLlyaattfkyvfdyhpddiywCT--ADIGWITGhS 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 227 CPVYLwtlPMfhCNGWTftwgTAARGGTsvcMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLK-GNS-LDLSPRSGPVH 304
Cdd:cd05966 290 YIVYG---PL--ANGAT----TVMFEGT---PTYPDPGRYWDIVEKHKVTIFYTAPTAIRALMKfGDEwVKKHDLSSLRV 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 305 VLTGGSP-PPAA---LVKKVQRLGFQVMHAYGQTEaTGPILFCEwqdewnrLPenQQMELKArqgisilGLA-------D 373
Cdd:cd05966 358 LGSVGEPiNPEAwmwYYEVIGKERCPIVDTWWQTE-TGGIMITP-------LP--GATPLKP-------GSAtrpffgiE 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 374 VDVKNKETQKSAPRDGktmGEILIKGS--SIMKGYLKNP----KATFEAFKhGWLNTGDVGVIHPDGHVEIKDRSKDIII 447
Cdd:cd05966 421 PAILDEEGNEVEGEVE---GYLVIKRPwpGMARTIYGDHeryeDTYFSKFP-GYYFTGDGARRDEDGYYWITGRVDDVIN 496
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 448 SGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKSETTIKEDRVDkfqtrernLIEYCRENLPHFMCP 527
Cdd:cd05966 497 VSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSDELRKE--------LRKHVRKEIGPIATP 568
|
570 580
....*....|....*....|....*...
gi 15218839 528 RKVVFLEELPKNGNGKILKPKLRDIAKG 555
Cdd:cd05966 569 DKIQFVPGLPKTRSGKIMRRILRKIAAG 596
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
19-549 |
1.39e-26 |
|
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: 113.19 E-value: 1.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 19 FLKRASECyPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRL 98
Cdd:cd17655 3 FEEQAEKT-PDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 99 DATSIAAILRHAKPKILFLDRSFEALARESLHLLSSEDSNLnlpvifihendfpkrASFEELDYECLIQrgeptPSMVAR 178
Cdd:cd17655 82 PEERIQYILEDSGADILLTQSHLQPPIAFIGLIDLLDEDTI---------------YHEESENLEPVSK-----SDDLAY 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 179 MFriqdehdpislnYTSGTTADPKGVVISHRGaylctLSAIIGW--------EMGTCPVY------LWTLPMFHcngwtf 244
Cdd:cd17655 142 VI------------YTSGSTGKPKGVMIEHRG-----VVNLVEWankviyqgEHLRVALFasisfdASVTEIFA------ 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 245 twgTAARGGTSVCMRHVT---APEIYKNIEMHNVTHMCCVPTVFNILlkgNSLDLSPRSGPVHVLTGGSPPPAALVKKV- 320
Cdd:cd17655 199 ---SLLSGNTLYIVRKETvldGQALTQYIRQNRITIIDLTPAHLKLL---DAADDSEGLSLKHLIVGGEALSTELAKKIi 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 321 --QRLGFQVMHAYGQTEAT-GPILFcewqdewnrlpenqQMELKARQGISI-LGLADVDVKN---KETQKSAPRDgkTMG 393
Cdd:cd17655 273 elFGTNPTITNAYGPTETTvDASIY--------------QYEPETDQQVSVpIGKPLGNTRIyilDQYGRPQPVG--VAG 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 394 EILIKGSSIMKGYLKNPKATFEAF-KHGWL------NTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYP 466
Cdd:cd17655 337 ELYIGGEGVARGYLNRPELTAEKFvDDPFVpgermyRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHP 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 467 KVLETAVVAMPHPTWGETPCAFVVLEKSettIKEDRVDKFQTRErnlieycrenLPHFMCPRKVVFLEELPKNGNGKILK 546
Cdd:cd17655 417 DIKEAVVIARKDEQGQNYLCAYIVSEKE---LPVAQLREFLARE----------LPDYMIPSYFIKLDEIPLTPNGKVDR 483
|
...
gi 15218839 547 PKL 549
Cdd:cd17655 484 KAL 486
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
45-474 |
1.45e-26 |
|
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: 111.97 E-value: 1.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 45 TY----DRCCRLAASLISL-NISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFLDR 119
Cdd:TIGR01733 1 TYreldERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 120 SFEALAREslhllssedsnLNLPVIFIhendfpkrasfeELDYECLIQRGEPTPSmvarmfrIQDEHDPISLNY---TSG 196
Cdd:TIGR01733 81 ALASRLAG-----------LVLPVILL------------DPLELAALDDAPAPPP-------PDAPSGPDDLAYviyTSG 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 197 TTADPKGVVISHRGaylctLSAIIGWeMGTCPVYLWTLPMFHCNGWTF------TWGTAARGGTSVC----MRHVTAPEI 266
Cdd:TIGR01733 131 STGRPKGVVVTHRS-----LVNLLAW-LARRYGLDPDDRVLQFASLSFdasveeIFGALLAGATLVVppedEERDDAALL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 267 YKNIEMHNVTHMCCVPTVFNILLkgnSLDLSPRSGPVHVLTGGSPPPAALVKKVQRL--GFQVMHAYGQTEATGPILFCE 344
Cdd:TIGR01733 205 AALIAEHPVTVLNLTPSLLALLA---AALPPALASLRLVILGGEALTPALVDRWRARgpGARLINLYGPTETTVWSTATL 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 345 WQDEWNRLPENqqmelkarqgISI---LGLADVDVKNKETQKSAPrdGKTmGEILIKGSSIMKGYLKNPKATFEAF---- 417
Cdd:TIGR01733 282 VDPDDAPRESP----------VPIgrpLANTRLYVLDDDLRPVPV--GVV-GELYIGGPGVARGYLNRPELTAERFvpdp 348
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15218839 418 -----KHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVlETAVV 474
Cdd:TIGR01733 349 faggdGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGV-REAVV 409
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
27-507 |
2.28e-26 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 112.27 E-value: 2.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 27 YPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRLDATSIAAI 106
Cdd:PRK09029 16 RPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLLEEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 107 LRHAKPK-ILFLDRSFEALARESLHLLSSEDSNlnlpvifihendfpkrasfeELDYECliQRgeptpsmvarmfriqde 185
Cdd:PRK09029 96 LPSLTLDfALVLEGENTFSALTSLHLQLVEGAH--------------------AVAWQP--QR----------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 186 hdPISLNYTSGTTADPKGVVISHRgAYLCtlSAIigwemGTCPV--------YLWTLPMFHCNGWTFTWGTAARGGTSVc 257
Cdd:PRK09029 137 --LATMTLTSGSTGLPKAAVHTAQ-AHLA--SAE-----GVLSLmpftaqdsWLLSLPLFHVSGQGIVWRWLYAGATLV- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 258 mrhVTAPE-IYKNIEMhnVTHMCCVPTVFNILLKGNSLDLSPRsgpvHVLTGGSPPPAALVKKVQRLGFQVMHAYGQTEA 336
Cdd:PRK09029 206 ---VRDKQpLEQALAG--CTHASLVPTQLWRLLDNRSEPLSLK----AVLLGGAAIPVELTEQAEQQGIRCWCGYGLTEM 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 337 TGPIlfCewqdewnrlpenqqmelkARQgisILGLADVDV--KNKETQKSAprdgktmGEILIKGSSIMKGYLKNPKATF 414
Cdd:PRK09029 277 ASTV--C------------------AKR---ADGLAGVGSplPGREVKLVD-------GEIWLRGASLALGYWRQGQLVP 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 415 EAFKHGWLNTGDVGVIHpDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEkS 494
Cdd:PRK09029 327 LVNDEGWFATRDRGEWQ-NGELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVADAEFGQRPVAVVESD-S 404
|
490
....*....|....*....
gi 15218839 495 ETTIKE------DRVDKFQ 507
Cdd:PRK09029 405 EAAVVNlaewlqDKLARFQ 423
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
187-544 |
3.89e-26 |
|
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: 109.03 E-value: 3.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 187 DPISLNYTSGTTADPKGVVISHR---GAYLCT--LSAIIGWEMGTCPVYL-WTLPMFHCNGWTFTwgtaarGGTSVCMRH 260
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERswiESFVCNedLFNISGEDAILAPGPLsHSLFLYGAISALYL------GGTFIGQRK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 261 VTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSPRSgpvhVLTGGSPPPAALVKKVQRlgfQVMHA-----YGQTE 335
Cdd:cd17633 75 FNPKSWIRKINQYNATVIYLVPTMLQALARTLEPESKIKS----IFSSGQKLFESTKKKLKN---IFPKAnliefYGTSE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 336 ATgpilFCEWqdewnRLPEnqqmELKARQGISILgLADVDVKNKEtqksapRDGKTMGEILIKGSSIMKGYLKNPKATfe 415
Cdd:cd17633 148 LS----FITY-----NFNQ----ESRPPNSVGRP-FPNVEIEIRN------ADGGEIGKIFVKSEMVFSGYVRGGFSN-- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 416 afKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKse 495
Cdd:cd17633 206 --PDGWMSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYSGDK-- 281
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 15218839 496 ttikedrVDKfqtreRNLIEYCRENLPHFMCPRKVVFLEELPKNGNGKI 544
Cdd:cd17633 282 -------LTY-----KQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKI 318
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
457-543 |
1.56e-25 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 99.93 E-value: 1.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 457 EVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKSETTIKEDrvdkfqtrernLIEYCRENLPHFMCPRKVVFLEEL 536
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLEEE-----------LVAHVREELGPYAVPKEVVFVDEL 69
|
....*..
gi 15218839 537 PKNGNGK 543
Cdd:pfam13193 70 PKTRSGK 76
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
166-550 |
2.24e-25 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 108.81 E-value: 2.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 166 IQRGEPTpsmVARMFRIQDEHDPISLNYTSGTTADPKGVVISHRGAYLCTLSAI--IGWEMGTCPvylWTL--PMFHCNG 241
Cdd:cd05974 68 VDRGGAV---YAAVDENTHADDPMLLYFTSGTTSKPKLVEHTHRSYPVGHLSTMywIGLKPGDVH---WNIssPGWAKHA 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 242 WTFTWGTAARGGTSVCMRHV--TAPEIYKNIEMHNVTHMCCVPTVFNILLKGN--SLDLSPRsgpvHVLTGGSPPPAALV 317
Cdd:cd05974 142 WSCFFAPWNAGATVFLFNYArfDAKRVLAALVRYGVTTLCAPPTVWRMLIQQDlaSFDVKLR----EVVGAGEPLNPEVI 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 318 KKVQRL-GFQVMHAYGQTEATGPIlfcewqdeWNRLPENQQMELKARQ--GISILGLADVDVKNKETQKSAP-RDGKTMG 393
Cdd:cd05974 218 EQVRRAwGLTIRDGYGQTETTALV--------GNSPGQPVKAGSMGRPlpGYRVALLDPDGAPATEGEVALDlGDTRPVG 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 394 eilikgssIMKGYLKNPKATFEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAV 473
Cdd:cd05974 290 --------LMKGYAGDPDKTAHAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAV 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 474 VAMPHPTWGETPCAFVVL----EKSETTIKEdrvdkfqtrernLIEYCRENLPHFMCPRKVVFLeELPKNGNGKILKPKL 549
Cdd:cd05974 362 VPSPDPVRLSVPKAFIVLragyEPSPETALE------------IFRFSRERLAPYKRIRRLEFA-ELPKTISGKIRRVEL 428
|
.
gi 15218839 550 R 550
Cdd:cd05974 429 R 429
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
28-544 |
2.57e-25 |
|
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: 108.99 E-value: 2.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 28 PNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPintrLDATSIAAIL 107
Cdd:cd17649 1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVP----LDPEYPAERL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 108 RHakpkILfldrsfealareslhllssEDSNLNLpvifihendfpkrasfeeldyeCLIQRGEpTPSMVArmfriqdehd 187
Cdd:cd17649 77 RY----ML-------------------EDSGAGL----------------------LLTHHPR-QLAYVI---------- 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 188 pislnYTSGTTADPKGVVISHrgAYLCTLSAIIG--WEMGTCPVYLWTLPmFHCNGWTFTWGTAARGGTSVCMRH----V 261
Cdd:cd17649 101 -----YTSGSTGTPKGVAVSH--GPLAAHCQATAerYGLTPGDRELQFAS-FNFDGAHEQLLPPLICGACVVLRPdelwA 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 262 TAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSPRSGPVHVL-TGGSPPPAALVKKVQRLGFQVMHAYGQTEAT-GP 339
Cdd:cd17649 173 SADELAEMVRELGVTVLDLPPAYLQQLAEEADRTGDGRPPSLRLYiFGGEALSPELLRRWLKAPVRLFNAYGPTEATvTP 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 340 ILF-CEWQDE--WNRLPENQQMELKArqgISILGladvdvknkeTQKSAPRDGKTmGEILIKGSSIMKGYLKNPKATFEA 416
Cdd:cd17649 253 LVWkCEAGAAraGASMPIGRPLGGRS---AYILD----------ADLNPVPVGVT-GELYIGGEGLARGYLGRPELTAER 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 417 F------KHG--WLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTwGETPCAF 488
Cdd:cd17649 319 FvpdpfgAPGsrLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAG-GKQLVAY 397
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 15218839 489 VVLEKSETtikedrvdKFQTRERnLIEYCRENLPHFMCPRKVVFLEELPKNGNGKI 544
Cdd:cd17649 398 VVLRAAAA--------QPELRAQ-LRTALRASLPDYMVPAHLVFLARLPLTPNGKL 444
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
28-544 |
4.76e-25 |
|
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: 108.16 E-value: 4.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 28 PNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRLDATSIAAIL 107
Cdd:cd17643 1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 108 RHAKPKILfldrsfealareslhllssedsnlnlpvifihendfpkrasfeeldyecliqrgeptpsmvarmfrIQDEHD 187
Cdd:cd17643 81 ADSGPSLL------------------------------------------------------------------LTDPDD 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 188 PISLNYTSGTTADPKGVVISHRGayLCTLSAIIGWEMGTCPVYLWTlpMFHCNGWTFT----WGTAARGGTSVCMRHVTA 263
Cdd:cd17643 95 LAYVIYTSGSTGRPKGVVVSHAN--VLALFAATQRWFGFNEDDVWT--LFHSYAFDFSvweiWGALLHGGRLVVVPYEVA 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 264 --PEIYKN-IEMHNVTHMCCVPTVFNILLKGNSLDLSPRSGPVHVLTGGSPPPAALVKK-VQRLGF---QVMHAYGQTEA 336
Cdd:cd17643 171 rsPEDFARlLRDEGVTVLNQTPSAFYQLVEAADRDGRDPLALRYVIFGGEALEAAMLRPwAGRFGLdrpQLVNMYGITET 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 337 TGPILFcewqdewnRLPENQQMELKARQ----GISILGLADVDvknkETQKSAPRDGktMGEILIKGSSIMKGYLKNPKA 412
Cdd:cd17643 251 TVHVTF--------RPLDAADLPAAAASpigrPLPGLRVYVLD----ADGRPVPPGV--VGELYVSGAGVARGYLGRPEL 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 413 TFEAFKHGWLN--------TGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGET 484
Cdd:cd17643 317 TAERFVANPFGgpgsrmyrTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTR 396
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15218839 485 PCAFVVL-EKSETTIKEDRvdkfqtrernliEYCRENLPHFMCPRKVVFLEELPKNGNGKI 544
Cdd:cd17643 397 LVAYVVAdDGAAADIAELR------------ALLKELLPDYMVPARYVPLDALPLTVNGKL 445
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
13-544 |
7.87e-24 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 106.97 E-value: 7.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 13 PLTPMT---FLKRASEcYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGA 89
Cdd:PRK12316 4548 PATRCVhqlVAERARM-TPDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGG 4626
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 90 VLNPINTRLDATSIAAILRHAKPKILFLDRsfealareslHLLSsedsnlNLPVifihendfPKRASFEELDYECLIQ-R 168
Cdd:PRK12316 4627 AYVPLDPEYPRERLAYMMEDSGAALLLTQS----------HLLQ------RLPI--------PDGLASLALDRDEDWEgF 4682
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 169 GEPTPsmvarmfriQDEHDPISLNY---TSGTTADPKGVVISHRG--AYLCTLSAIIGWEMGTCPVYLWTLPmFHCNGWT 243
Cdd:PRK12316 4683 PAHDP---------AVRLHPDNLAYviyTSGSTGRPKGVAVSHGSlvNHLHATGERYELTPDDRVLQFMSFS-FDGSHEG 4752
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 244 FTWGTAArgGTSVCMRHVTA--PE-IYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSPRSGPVHVLTGGSPPPAALVKKV 320
Cdd:PRK12316 4753 LYHPLIN--GASVVIRDDSLwdPErLYAEIHEHRVTVLVFPPVYLQQLAEHAERDGEPPSLRVYCFGGEAVAQASYDLAW 4830
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 321 QRLGFQVMH-AYGQTEATgpilfcEWQDEWNRLPENQQMELKARQGISILGLADVDVKNKetqkSAPRDGKTMGEILIKG 399
Cdd:PRK12316 4831 RALKPVYLFnGYGPTETT------VTVLLWKARDGDACGAAYMPIGTPLGNRSGYVLDGQ----LNPLPVGVAGELYLGG 4900
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 400 SSIMKGYLKNPKATFEAF------KHG--WLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLET 471
Cdd:PRK12316 4901 EGVARGYLERPALTAERFvpdpfgAPGgrLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREA 4980
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15218839 472 AVVAMPHPTwGETPCAFVVLEKSETTIKEDRVDKFQTRERNLIeycRENLPHFMCPRKVVFLEELPKNGNGKI 544
Cdd:PRK12316 4981 VVIAQEGAV-GKQLVGYVVPQDPALADADEAQAELRDELKAAL---RERLPEYMVPAHLVFLARMPLTPNGKL 5049
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
40-474 |
3.34e-23 |
|
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: 103.66 E-value: 3.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 40 FTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILF--- 116
Cdd:cd17641 12 FTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIaed 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 117 ---LDRSFEALAResLHLLssedsnlnLPVIFIHEN-----DFPKRASFEELdYECLIQRGEPTPSMVARMFRIQDEHDP 188
Cdd:cd17641 92 eeqVDKLLEIADR--IPSV--------RYVIYCDPRgmrkyDDPRLISFEDV-VALGRALDRRDPGLYEREVAAGKGEDV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 189 ISLNYTSGTTADPKGVVISHRgaylctlsAIIGWEMGTCPV--------YLWTLPMFHCNGWTFTWGTAARGGTSVC--- 257
Cdd:cd17641 161 AVLCTTSGTTGKPKLAMLSHG--------NFLGHCAAYLAAdplgpgdeYVSVLPLPWIGEQMYSVGQALVCGFIVNfpe 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 258 --------MRHV------TAPEIYKNIEMHNVTHMCCVP----TVFNILLK-------------GNSLDLSPRSGPVHVL 306
Cdd:cd17641 233 epetmmedLREIgptfvlLPPRVWEGIAADVRARMMDATpfkrFMFELGMKlglraldrgkrgrPVSLWLRLASWLADAL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 307 ------------------TGGSPPPAALVKKVQRLGFQVMHAYGQTEATGPILfcewqdewnrlpenQQMELKARQGISI 368
Cdd:cd17641 313 lfrplrdrlgfsrlrsaaTGGAALGPDTFRFFHAIGVPLKQLYGQTELAGAYT--------------VHRDGDVDPDTVG 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 369 LGLADVDVKNKETqksaprdgktmGEILIKGSSIMKGYLKNPKATFEAF-KHGWLNTGDVGVIHPDGHVEIKDRSKDI-I 446
Cdd:cd17641 379 VPFPGTEVRIDEV-----------GEILVRSPGVFVGYYKNPEATAEDFdEDGWLHTGDAGYFKENGHLVVIDRAKDVgT 447
|
490 500
....*....|....*....|....*...
gi 15218839 447 ISGGENISSVEVENVLYKYPKVLEtAVV 474
Cdd:cd17641 448 TSDGTRFSPQFIENKLKFSPYIAE-AVV 474
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
193-556 |
6.62e-23 |
|
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: 102.24 E-value: 6.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 193 YTSGTTADPKGVVISHRGAYLCTLSAIIGWEMGTCPVYLWtlpmFhcNGWTF------TWGTAARGGTsVCmrhVTAPEI 266
Cdd:cd05918 113 FTSGSTGKPKGVVIEHRALSTSALAHGRALGLTSESRVLQ----F--ASYTFdvsileIFTTLAAGGC-LC---IPSEED 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 267 YKN-----IEMHNVTHMCCVPTVFNILlkgnsldlSPRSGP--VHVLTGGSPPPAALVKK-VQRLgfQVMHAYGQTEATg 338
Cdd:cd05918 183 RLNdlagfINRLRVTWAFLTPSVARLL--------DPEDVPslRTLVLGGEALTQSDVDTwADRV--RLINAYGPAECT- 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 339 pILFCewqdewnrlpeNQQMELKARqgISILGLA--------DVDVKNKETQKSAPrdgktmGEILIKGSSIMKGYLKNP 410
Cdd:cd05918 252 -IAAT-----------VSPVVPSTD--PRNIGRPlgatcwvvDPDNHDRLVPIGAV------GELLIEGPILARGYLNDP 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 411 KATFEAFKHG--WL------------NTGDVGVIHPDGHVEIKDRsKD--IIISG-----GEnissveVENVLYKYPKVL 469
Cdd:cd05918 312 EKTAAAFIEDpaWLkqegsgrgrrlyRTGDLVRYNPDGSLEYVGR-KDtqVKIRGqrvelGE------IEHHLRQSLPGA 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 470 ETAVVAMPHPTWGETP---CAFVVLEKSETTIKEDRV------DKFQTRERNLIEYCRENLPHFMCPRKVVFLEELPKNG 540
Cdd:cd05918 385 KEVVVEVVKPKDGSSSpqlVAFVVLDGSSSGSGDGDSlflepsDEFRALVAELRSKLRQRLPSYMVPSVFLPLSHLPLTA 464
|
410
....*....|....*.
gi 15218839 541 NGKILKPKLRDIAKGL 556
Cdd:cd05918 465 SGKIDRRALRELAESL 480
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
28-549 |
1.20e-22 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 103.50 E-value: 1.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 28 PNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRLDATSIAAIL 107
Cdd:PRK12316 2017 PEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYML 2096
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 108 RHAKPKILFLDRSFEA--LARESLHLLSSEDSnLNLPvifihenDFPKRASFEELDYECLiqrgeptpsmvarMFRIqde 185
Cdd:PRK12316 2097 EDSGAALLLTQRHLLErlPLPAGVARLPLDRD-AEWA-------DYPDTAPAVQLAGENL-------------AYVI--- 2152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 186 hdpislnYTSGTTADPKGVVISHrGAylctLSAIIGW-----EMGTCPVYLWTLPmFHCNGWTFTWGTAARGGTSVCMR- 259
Cdd:PRK12316 2153 -------YTSGSTGLPKGVAVSH-GA----LVAHCQAageryELSPADCELQFMS-FSFDGAHEQWFHPLLNGARVLIRd 2219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 260 --HVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSPRSGPVHVLTGGSPPPAALVKKVQRLGFQ-VMHAYGQTEA 336
Cdd:PRK12316 2220 deLWDPEQLYDEMERHGVTILDFPPVYLQQLAEHAERDGRPPAVRVYCFGGEAVPAASLRLAWEALRPVyLFNGYGPTEA 2299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 337 T-GPILF-CEWQDEWNRLPENQQMELKARQGiSILGlADVDVknketqkSAPRdgkTMGEILIKGSSIMKGYLKNPKATF 414
Cdd:PRK12316 2300 VvTPLLWkCRPQDPCGAAYVPIGRALGNRRA-YILD-ADLNL-------LAPG---MAGELYLGGEGLARGYLNRPGLTA 2367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 415 EAF-------KHGWL-NTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTwGETPC 486
Cdd:PRK12316 2368 ERFvpdpfsaSGERLyRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQDGAS-GKQLV 2446
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15218839 487 AFVVLEKSETTIKEDrvdkfqtrernLIEYCRENLPHFMCPRKVVFLEELPKNGNGKILKPKL 549
Cdd:PRK12316 2447 AYVVPDDAAEDLLAE-----------LRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKAL 2498
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
27-474 |
1.78e-22 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 101.49 E-value: 1.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 27 YPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRLDATSIAAI 106
Cdd:PRK08279 50 HPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQRGAVLAHS 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 107 LRHAKPKILFLDrsfealaRESLHLLSSEDSNLNLPVIFIHENDFPKRASFEELDYECLIQRGEPTPSMVARmfRIQDEh 186
Cdd:PRK08279 130 LNLVDAKHLIVG-------EELVEAFEEARADLARPPRLWVAGGDTLDDPEGYEDLAAAAAGAPTTNPASRS--GVTAK- 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 187 DPISLNYTSGTTADPKGVVISHRgAYLCTLSAIIG-WEMGTCPVYLWTLPMFHCNGWTFTWGTA-ARGGTSVCMRHVTAP 264
Cdd:PRK08279 200 DTAFYIYTSGTTGLPKAAVMSHM-RWLKAMGGFGGlLRLTPDDVLYCCLPLYHNTGGTVAWSSVlAAGATLALRRKFSAS 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 265 EIYKNIEMHNVTHMCCVPTVFNILLkgNSlDLSP--RSGPVHVLTGGSPPPAALVKKVQRLG-FQVMHAYGQTEatGPIL 341
Cdd:PRK08279 279 RFWDDVRRYRATAFQYIGELCRYLL--NQ-PPKPtdRDHRLRLMIGNGLRPDIWDEFQQRFGiPRILEFYAASE--GNVG 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 342 FCewqdewN---------RLPenqqmeLKARQGISILGLaDVD----VKNKE--TQKSAPrdGKTmGEIL--IKGSSIMK 404
Cdd:PRK08279 354 FI------NvfnfdgtvgRVP------LWLAHPYAIVKY-DVDtgepVRDADgrCIKVKP--GEV-GLLIgrITDRGPFD 417
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15218839 405 GYLkNPKATfE------AFKHG--WLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLEtAVV 474
Cdd:PRK08279 418 GYT-DPEAS-EkkilrdVFKKGdaWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENALSGFPGVEE-AVV 492
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
39-550 |
1.82e-22 |
|
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: 100.51 E-value: 1.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 39 RFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFLD 118
Cdd:cd05940 3 ALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLVVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 119 RSFealareslhllssedsnlnlpvifihendfpkrasfeeldyecLIqrgeptpsmvarmfriqdehdpislnYTSGTT 198
Cdd:cd05940 83 AAL-------------------------------------------YI--------------------------YTSGTT 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 199 ADPKGVVISHRGAYLCT-LSAIIGWEMGTCPVYLwTLPMFHCNGWTFTWGTAARGGTSVCMRH-VTAPEIYKNIEMHNVT 276
Cdd:cd05940 94 GLPKAAIISHRRAWRGGaFFAGSGGALPSDVLYT-CLPLYHSTALIVGWSACLASGATLVIRKkFSASNFWDDIRKYQAT 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 277 hmcCVPTVFNI---LLKGNSLDLSpRSGPVHVLTGGSPPPAALVKKVQRLGF-QVMHAYGQTEatGPILFcewqdeWNRl 352
Cdd:cd05940 173 ---IFQYIGELcryLLNQPPKPTE-RKHKVRMIFGNGLRPDIWEEFKERFGVpRIAEFYAATE--GNSGF------INF- 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 353 pENQQMELKARQGISILGLADVDVK-NKETQ----------KSAPRdGKTmGEIL--IKGSSIMKGYLKNPKAT----FE 415
Cdd:cd05940 240 -FGKPGAIGRNPSLLRKVAPLALVKyDLESGepirdaegrcIKVPR-GEP-GLLIsrINPLEPFDGYTDPAATEkkilRD 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 416 AFKHG--WLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHP-TWGETPCAFVVLE 492
Cdd:cd05940 317 VFKKGdaWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQVPgTDGRAGMAAIVLQ 396
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 15218839 493 KSETTIKEdrvdkfqtrerNLIEYCRENLPHFMCPRKVVFLEELPKNGNGKILKPKLR 550
Cdd:cd05940 397 PNEEFDLS-----------ALAAHLEKNLPGYARPLFLRLQPEMEITGTFKQQKVDLR 443
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
41-460 |
1.91e-22 |
|
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: 101.28 E-value: 1.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 41 TWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFLDRs 120
Cdd:cd05933 10 TYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEANILVVEN- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 121 fealARESLHLLSSEDSnlnLP----VIFIHENDFPKRAS------FEELDyecliqRGEPTPSMVARMFRiQDEHDPIS 190
Cdd:cd05933 89 ----QKQLQKILQIQDK---LPhlkaIIQYKEPLKEKEPNlyswdeFMELG------RSIPDEQLDAIISS-QKPNQCCT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 191 LNYTSGTTADPKGVVISHRGAYLCTLSAIIGWEMGTCPV-------YL------------WTlPMFHCNGWTFTWGTAAR 251
Cdd:cd05933 155 LIYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLRPATVgqesvvsYLplshiaaqildiWL-PIKVGGQVYFAQPDALK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 252 GGTSVCMRHVTApeiykniemhnvTHMCCVPTVFNIL---LKGNSLDLSP----------RSGPVHVLT---GGSPPP-- 313
Cdd:cd05933 234 GTLVKTLREVRP------------TAFMGVPRVWEKIqekMKAVGAKSGTlkrkiaswakGVGLETNLKlmgGESPSPlf 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 314 ----AALV-KKV-QRLGFQ--------------------------VMHAYGQTEATGPILFCewqdewnrLPENQQmelk 361
Cdd:cd05933 302 yrlaKKLVfKKVrKALGLDrcqkfftgaapisretlefflslnipIMELYGMSETSGPHTIS--------NPQAYR---- 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 362 arqgISILGLADVDVKNKETQKSAprDGktMGEILIKGSSIMKGYLKNPKATFEAFK-HGWLNTGDVGVIHPDGHVEIKD 440
Cdd:cd05933 370 ----LLSCGKALPGCKTKIHNPDA--DG--IGEICFWGRHVFMGYLNMEDKTEEAIDeDGWLHSGDLGKLDEDGFLYITG 441
|
490 500
....*....|....*....|.
gi 15218839 441 RSKDIII-SGGENISSVEVEN 460
Cdd:cd05933 442 RIKELIItAGGENVPPVPIED 462
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
28-544 |
4.20e-22 |
|
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: 99.46 E-value: 4.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 28 PNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRLDATSIAAIL 107
Cdd:cd17650 1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 108 RHAKPKILFLDrsfealareslhllssedsnlnlpvifihendfpkrasfeeldyecliqrgePTpsmvarmfriqdehD 187
Cdd:cd17650 81 EDSGAKLLLTQ----------------------------------------------------PE--------------D 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 188 PISLNYTSGTTADPKGVVISHRGAYlctlSAIIGW----EMGTCPVYLWTLPMFHCNGWTftwGTAAR----GGTSV-CM 258
Cdd:cd17650 95 LAYVIYTSGTTGKPKGVMVEHRNVA----HAAHAWrreyELDSFPVRLLQMASFSFDVFA---GDFARsllnGGTLViCP 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 259 RHVTA--PEIYKNIEMHNVTHMCCVPTVFNILLK---GNSLDLSPrsgpVHVLTGGSPPPAALVKK--VQRLG--FQVMH 329
Cdd:cd17650 168 DEVKLdpAALYDLILKSRITLMESTPALIRPVMAyvyRNGLDLSA----MRLLIVGSDGCKAQDFKtlAARFGqgMRIIN 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 330 AYGQTEATgpILFCEWQDEWNRLPENQQMELK---ARQGISILgladvdvknkeTQKSAPRDGKTMGEILIKGSSIMKGY 406
Cdd:cd17650 244 SYGVTEAT--IDSTYYEEGRDPLGDSANVPIGrplPNTAMYVL-----------DERLQPQPVGVAGELYIGGAGVARGY 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 407 LKNPKATFEAFKHGWL-------NTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLEtAVVAMPHP 479
Cdd:cd17650 311 LNRPELTAERFVENPFapgermyRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDE-AVVAVRED 389
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15218839 480 TWGETP-CAFVVLEksettikedrvDKFQTRErnLIEYCRENLPHFMCPRKVVFLEELPKNGNGKI 544
Cdd:cd17650 390 KGGEARlCAYVVAA-----------ATLNTAE--LRAFLAKELPSYMIPSYYVQLDALPLTPNGKV 442
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
28-544 |
1.47e-21 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 100.03 E-value: 1.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 28 PNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRLDATSIAAIL 107
Cdd:PRK12316 525 PEAPALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYML 604
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 108 RHAKPKILFLDRsfealareslHLLSSEDSNLNLPVIfihendfpkrasfeELDYECLIQRGEPTPSMVARMfriqDEHD 187
Cdd:PRK12316 605 EDSGVQLLLSQS----------HLGRKLPLAAGVQVL--------------DLDRPAAWLEGYSEENPGTEL----NPEN 656
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 188 PISLNYTSGTTADPKGVVISHRG--AYLCTLSAIIGWEMGTcPVYLWTLPMFHCNGWTFtWGTAARGGTsvcmRHVTAPE 265
Cdd:PRK12316 657 LAYVIYTSGSTGKPKGAGNRHRAlsNRLCWMQQAYGLGVGD-TVLQKTPFSFDVSVWEF-FWPLMSGAR----LVVAAPG 730
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 266 IYKN-------IEMHNVTHMCCVPTVFNILLKGNSLD--LSPRSgpvhVLTGGSPPPAALVKKVQRLGFQ--VMHAYGQT 334
Cdd:PRK12316 731 DHRDpaklvelINREGVDTLHFVPSMLQAFLQDEDVAscTSLRR----IVCSGEALPADAQEQVFAKLPQagLYNLYGPT 806
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 335 EATGPILFCEWQDEWNRLPEnqqmelkarQGISILGLA----DVDVKnketqksaPRDGKTMGEILIKGSSIMKGYLKNP 410
Cdd:PRK12316 807 EAAIDVTHWTCVEEGGDSVP---------IGRPIANLAcyilDANLE--------PVPVGVLGELYLAGRGLARGYHGRP 869
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 411 KATFEAF-------KHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPhptwGE 483
Cdd:PRK12316 870 GLTAERFvpspfvaGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GK 945
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15218839 484 TPCAFVVLEKSETTIKEDrvdkfqtrernLIEYCRENLPHFMCPRKVVFLEELPKNGNGKI 544
Cdd:PRK12316 946 QLVGYVVLESEGGDWREA-----------LKAHLAASLPEYMVPAQWLALERLPLTPNGKL 995
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
193-544 |
3.01e-21 |
|
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: 96.74 E-value: 3.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 193 YTSGTTADPKGVVISHRgaylctlsAIIGWEMGTCPVYLWTLPMFHCNGWTFTWGTAAR-------GGTSVCMR----HV 261
Cdd:cd17644 113 YTSGSTGKPKGVMIEHQ--------SLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEeiyvtllSGATLVLRpeemRS 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 262 TAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSPR-SGPVHVLTGGS---PPPAALVKKVQRLGFQVMHAYGQTEAT 337
Cdd:cd17644 185 SLEDFVQYIQQWQLTVLSLPPAYWHLLVLELLLSTIDLpSSLRLVIVGGEavqPELVRQWQKNVGNFIQLINVYGPTEAT 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 338 GPILFCEWqdewNRLPENQQMELKARQGISILGLADVDvknkETQKSAPRDgkTMGEILIKGSSIMKGYLKNPKATFEAF 417
Cdd:cd17644 265 IAATVCRL----TQLTERNITSVPIGRPIANTQVYILD----ENLQPVPVG--VPGELHIGGVGLARGYLNRPELTAEKF 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 418 -KHGWLN--------TGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAF 488
Cdd:cd17644 335 iSHPFNSseserlykTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAY 414
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 15218839 489 VVLEKSETTIKEDrvdkfqtrernLIEYCRENLPHFMCPRKVVFLEELPKNGNGKI 544
Cdd:cd17644 415 IVPHYEESPSTVE-----------LRQFLKAKLPDYMIPSAFVVLEELPLTPNGKI 459
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
36-551 |
3.16e-21 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 96.73 E-value: 3.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 36 GKTrFTWPQTYDRCCRLAASLIS-LNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRLDATSiaailrhakpki 114
Cdd:cd05937 3 GKT-WTYSETYDLVLRYAHWLHDdLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDP------------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 115 lfldrsfealareslhllssedsnlnlpviFIHendfpkrasfeeldyeCLIQRGeptpsmvARmFRIQDEHDPISLNYT 194
Cdd:cd05937 70 ------------------------------LIH----------------CLKLSG-------SR-FVIVDPDDPAILIYT 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 195 SGTTADPKGVVISHRGAYlcTLSAIIGWEMGTCPVYLW--TLPMFHCNGWTFTWGTAARGGTSVCMRH-VTAPEIYKNIE 271
Cdd:cd05937 96 SGTTGLPKAAAISWRRTL--VTSNLLSHDLNLKNGDRTytCMPLYHGTAAFLGACNCLMSGGTLALSRkFSASQFWKDVR 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 272 MHNVTHMCCVPTVFNILLkgnSLDLSP--RSGPVHVLTGGSPPPAALVKKVQRLGFQVMHA-YGQTEAT----------- 337
Cdd:cd05937 174 DSGATIIQYVGELCRYLL---STPPSPydRDHKVRVAWGNGLRPDIWERFRERFNVPEIGEfYAATEGVfaltnhnvgdf 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 338 --------GPIlfcewqdeWNRLPENQQMELKarqgisilgladVDVKNKETQKSaPRDG-------KTMGEILI----K 398
Cdd:cd05937 251 gagaighhGLI--------RRWKFENQVVLVK------------MDPETDDPIRD-PKTGfcvrapvGEPGEMLGrvpfK 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 399 GSSIMKGYLKNPKAT-----FEAFKHG--WLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLET 471
Cdd:cd05937 310 NREAFQGYLHNEDATesklvRDVFRKGdiYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEA 389
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 472 AVVAMPHPTW-GETPCAFVVLEKSETtikeDRVDKFQTRernLIEYCRENLPHFMCPRKVVFLEELPKNGNGKILKPKLR 550
Cdd:cd05937 390 NVYGVKVPGHdGRAGCAAITLEESSA----VPTEFTKSL---LASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLR 462
|
.
gi 15218839 551 D 551
Cdd:cd05937 463 D 463
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
193-544 |
3.53e-21 |
|
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).
Pssm-ID: 341307 [Multi-domain] Cd Length: 436 Bit Score: 96.17 E-value: 3.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 193 YTSGTTADPKGVVISHRGayLCTLSAIIGWEMGTCP---VYLWTLPMFHCNGWTFtWGTAARGGTSVCM-RHVTAP--EI 266
Cdd:cd17652 100 YTSGSTGRPKGVVVTHRG--LANLAAAQIAAFDVGPgsrVLQFASPSFDASVWEL-LMALLAGATLVLApAEELLPgePL 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 267 YKNIEMHNVTHMCCVPTVFNILLKGNSLDLsprsgpVHVLTGGSPPPAALVKKVQRlGFQVMHAYGQTEAT------GPi 340
Cdd:cd17652 177 ADLLREHRITHVTLPPAALAALPPDDLPDL------RTLVVAGEACPAELVDRWAP-GRRMINAYGPTETTvcatmaGP- 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 341 lfcewqdewnrLPENQQMELkarqGISILGlADVDVKNKETQKSAPrdGKTmGEILIKGSSIMKGYLKNPKATFEAFKhg 420
Cdd:cd17652 249 -----------LPGGGVPPI----GRPVPG-TRVYVLDARLRPVPP--GVP-GELYIAGAGLARGYLNRPGLTAERFV-- 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 421 wLN-----------TGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFV 489
Cdd:cd17652 308 -ADpfgapgsrmyrTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYV 386
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 15218839 490 VLEKSETTIKEDrvdkfqtrernLIEYCRENLPHFMCPRKVVFLEELPKNGNGKI 544
Cdd:cd17652 387 VPAPGAAPTAAE-----------LRAHLAERLPGYMVPAAFVVLDALPLTPNGKL 430
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
28-544 |
9.84e-21 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 97.15 E-value: 9.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 28 PNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRLDATSIAAIL 107
Cdd:PRK12467 526 PERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYML 605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 108 RHAKPKILfldrsfeaLAREslHLLSSEDSNLNLPVIFIHENDFPkrasfeeldyecLIQRGEPTPSMVArmfriqdehD 187
Cdd:PRK12467 606 DDSGVRLL--------LTQS--HLLAQLPVPAGLRSLCLDEPADL------------LCGYSGHNPEVAL---------D 654
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 188 PISLNY---TSGTTADPKGVVISHRG--AYLCTLSAIIGWEMGTcPVYLWTLPMFHCNGWTFTWGTAArgGTSVCMR--- 259
Cdd:PRK12467 655 PDNLAYviyTSGSTGQPKGVAISHGAlaNYVCVIAERLQLAADD-SMLMVSTFAFDLGVTELFGALAS--GATLHLLppd 731
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 260 -HVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSPRSGPVHVltGGSPPPAALVKKVQRLGFQ--VMHAYGQTEA 336
Cdd:PRK12467 732 cARDAEAFAALMADQGVTVLKIVPSHLQALLQASRVALPRPQRALVC--GGEALQVDLLARVRALGPGarLINHYGPTET 809
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 337 TGPILFCEWQDE---WNRLPENQQMelkARQGISILglaDVDVknketqksAPRDGKTMGEILIKGSSIMKGYLKNPKAT 413
Cdd:PRK12467 810 TVGVSTYELSDEerdFGNVPIGQPL---ANLGLYIL---DHYL--------NPVPVGVVGELYIGGAGLARGYHRRPALT 875
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 414 FEAF-------KHGWL-NTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTwGETP 485
Cdd:PRK12467 876 AERFvpdpfgaDGGRLyRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDA-GLQL 954
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 486 CAFVVLEKS-ETTIKEDRVDKFQTRernlieyCRENLPHFMCPRKVVFLEELPKNGNGKI 544
Cdd:PRK12467 955 VAYLVPAAVaDGAEHQATRDELKAQ-------LRQVLPDYMVPAHLLLLDSLPLTPNGKL 1007
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
20-552 |
1.34e-20 |
|
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: 95.43 E-value: 1.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 20 LKRASECYPNRTsIIY-----GKTRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPI 94
Cdd:cd05906 16 LLRAAERGPTKG-ITYidadgSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 95 NTRLDATSIAAILRHAK--------PKILFLDRSFEALAReslhlLSSEDSNLNLPVIFIHEndfpkrasfeELDYEcli 166
Cdd:cd05906 95 TVPPTYDEPNARLRKLRhiwqllgsPVVLTDAELVAEFAG-----LETLSGLPGIRVLSIEE----------LLDTA--- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 167 qrgEPTPSmvarmfRIQDEHDPISLNYTSGTTADPKGVVISHRgaylctlsAIIGWEMGTCPVYLWT--------LPMFH 238
Cdd:cd05906 157 ---ADHDL------PQSRPDDLALLMLTSGSTGFPKAVPLTHR--------NILARSAGKIQHNGLTpqdvflnwVPLDH 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 239 CNGWTFTWGTAARGGTSvcMRHVTAPEIYKN-------IEMHNVTHMCCVPTVFNILL------KGNSLDLSP-R---SG 301
Cdd:cd05906 220 VGGLVELHLRAVYLGCQ--QVHVPTEEILADplrwldlIDRYRVTITWAPNFAFALLNdlleeiEDGTWDLSSlRylvNA 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 302 --PVHVLTGgspppAALVKKVQRLGFQ--VMH-AYGQTEATGPILFCEWQDEWNRLPENQQMELkarqGISILGlADVDV 376
Cdd:cd05906 298 geAVVAKTI-----RRLLRLLEPYGLPpdAIRpAFGMTETCSGVIYSRSFPTYDHSQALEFVSL----GRPIPG-VSMRI 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 377 KNkETQKSAPRDgkTMGEILIKGSSIMKGYLKNPKATFEAF-KHGWLNTGDVGVIHpDGHVEIKDRSKDIIISGGENISS 455
Cdd:cd05906 368 VD-DEGQLLPEG--EVGRLQVRGPVVTKGYYNNPEANAEAFtEDGWFRTGDLGFLD-NGNLTITGRTKDTIIVNGVNYYS 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 456 VEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKSETTIKEDRVDkfqtrernLIEYCRENLPHFM--CPRKVVFL 533
Cdd:cd05906 444 HEIEAAVEEVPGVEPSFTAAFAVRDPGAETEELAIFFVPEYDLQDALSE--------TLRAIRSVVSREVgvSPAYLIPL 515
|
570 580
....*....|....*....|.
gi 15218839 534 --EELPKNGNGKILKPKLRDI 552
Cdd:cd05906 516 pkEEIPKTSLGKIQRSKLKAA 536
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
193-479 |
1.48e-20 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 95.65 E-value: 1.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 193 YTSGTTADPKGVVISHRGAYLCTLSAIIGWE-----MGTCPVYLWTLPMFHC-----NGWTFtwgtaaRGGTSVCMRHVT 262
Cdd:PLN02430 227 YTSGTSGDPKGVVLTHEAVATFVRGVDLFMEqfedkMTHDDVYLSFLPLAHIldrmiEEYFF------RKGASVGYYHGD 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 263 APEIYKNIEMHNVTHMCCVPTVFNILLKG--NSL-DLSPR---------------------------------------- 299
Cdd:PLN02430 301 LNALRDDLMELKPTLLAGVPRVFERIHEGiqKALqELNPRrrlifnalykyklawmnrgyshkkaspmadflafrkvkak 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 300 -SGPVHVLTGGSPPPAALVKKVQRL---GFqVMHAYGQTEATGPILFCewqdewnrLPENQQMelkarqgISILGLADV- 374
Cdd:PLN02430 381 lGGRLRLLISGGAPLSTEIEEFLRVtscAF-VVQGYGLTETLGPTTLG--------FPDEMCM-------LGTVGAPAVy 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 375 -DVKNKETQKSA--PRDGKTMGEILIKGSSIMKGYLKNPKATFEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDII-ISGG 450
Cdd:PLN02430 445 nELRLEEVPEMGydPLGEPPRGEICVRGKCLFSGYYKNPELTEEVMKDGWFHTGDIGEILPNGVLKIIDRKKNLIkLSQG 524
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 15218839 451 ENISSVEVENVlYKYPKVLE-------------TAVVAmPHP 479
Cdd:PLN02430 525 EYVALEYLENV-YGQNPIVEdiwvygdsfksmlVAVVV-PNE 564
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
281-553 |
1.83e-20 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 94.29 E-value: 1.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 281 VPTVFNILLKGNSLDLSPRSGpvhVLTGGSPPPAALVKKVQRLGFQVMHAYGQTEATGPILFCEWQDEWNrlpenqqmel 360
Cdd:PRK07445 214 VPTQLQRLLQLRPQWLAQFRT---ILLGGAPAWPSLLEQARQLQLRLAPTYGMTETASQIATLKPDDFLA---------- 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 361 KARQGISILGLADVDVKNKETqksaprdgktmGEILIKGSSIMKGY---LKNPKATFEafkhgwlnTGDVGVIHPDGHVE 437
Cdd:PRK07445 281 GNNSSGQVLPHAQITIPANQT-----------GNITIQAQSLALGYypqILDSQGIFE--------TDDLGYLDAQGYLH 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 438 IKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKSETTikedrVDKFQTRernlieyC 517
Cdd:PRK07445 342 ILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVPKDPSIS-----LEELKTA-------I 409
|
250 260 270
....*....|....*....|....*....|....*.
gi 15218839 518 RENLPHFMCPRKVVFLEELPKNGNGKILKPKLRDIA 553
Cdd:PRK07445 410 KDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQIA 445
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
43-559 |
2.66e-20 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 95.42 E-value: 2.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 43 PQTYDRCCRLAASL---ISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFLDR 119
Cdd:PRK06814 658 PLTYRKLLTGAFVLgrkLKKNTPPGENVGVMLPNANGAAVTFFALQSAGRVPAMINFSAGIANILSACKAAQVKTVLTSR 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 120 SFEALAReslhlLSSEDSNLNLPVIFIHENDFPKRASFEeLDYECLIQRGEPTPSMVARmfriqDEHDPISLNYTSGTTA 199
Cdd:PRK06814 738 AFIEKAR-----LGPLIEALEFGIRIIYLEDVRAQIGLA-DKIKGLLAGRFPLVYFCNR-----DPDDPAVILFTSGSEG 806
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 200 DPKGVVISHRG--AYLCTLSAIIgwEMGTCPVYLWTLPMFHCNGWTftwgtaarGGTSVCM------------RHV-TAP 264
Cdd:PRK06814 807 TPKGVVLSHRNllANRAQVAARI--DFSPEDKVFNALPVFHSFGLT--------GGLVLPLlsgvkvflypspLHYrIIP 876
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 265 E-IYKNiemhNVTHMCCVPTvfniLLKG-----NSLDLspRSgpVHVLTGGSPPPAALVKKV--QRLGFQVMHAYGQTEa 336
Cdd:PRK06814 877 ElIYDT----NATILFGTDT----FLNGyaryaHPYDF--RS--LRYVFAGAEKVKEETRQTwmEKFGIRILEGYGVTE- 943
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 337 TGPILFCewqdewnrlpeNQQMELKARQGISILGLADvdvknketQKSAPRDGKTMGEIL-IKGSSIMKGYLK--NPkAT 413
Cdd:PRK06814 944 TAPVIAL-----------NTPMHNKAGTVGRLLPGIE--------YRLEPVPGIDEGGRLfVRGPNVMLGYLRaeNP-GV 1003
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 414 FEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETpcafVVLEK 493
Cdd:PRK06814 1004 LEPPADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELWPDALHAAVSIPDARKGER----IILLT 1079
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15218839 494 SETTIkedrvdkfqTRErNLIEYCREN-LPHFMCPRKVVFLEELPKNGNGKILKPKLRDIAKGLVVE 559
Cdd:PRK06814 1080 TASDA---------TRA-AFLAHAKAAgASELMVPAEIITIDEIPLLGTGKIDYVAVTKLAEEAAAK 1136
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
28-544 |
2.90e-20 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 95.61 E-value: 2.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 28 PNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRLDATSIAAIL 107
Cdd:PRK12467 1588 PEAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMI 1667
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 108 RHAKPKILFLDRsfealareslHLLSSEDSNLNLPVIFIHENDfpkrasfeeldyECLIQRGEPTPSMVArmfriqdehD 187
Cdd:PRK12467 1668 EDSGIELLLTQS----------HLQARLPLPDGLRSLVLDQED------------DWLEGYSDSNPAVNL---------A 1716
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 188 PISLNY---TSGTTADPKGVVISHrGAYLCTLSAIIGWeMGTCPVYLWTLPM---FHCNGWTFTWgtAARGGTSVCMR-- 259
Cdd:PRK12467 1717 PQNLAYviyTSGSTGRPKGAGNRH-GALVNRLCATQEA-YQLSAADVVLQFTsfaFDVSVWELFW--PLINGARLVIApp 1792
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 260 --HVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSPRSGPVHVLTGGSPPPAALVKKVQRLGF-QVMHAYGQTEA 336
Cdd:PRK12467 1793 gaHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQMDEQVEHPLSLRRVVCGGEALEVEALRPWLERLPDtGLFNLYGPTET 1872
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 337 TGPILF--CEWQDEWNR--LPENQQMelkARQGISILgladvdvknKETQKSAPRdgKTMGEILIKGSSIMKGYLKNPKA 412
Cdd:PRK12467 1873 AVDVTHwtCRRKDLEGRdsVPIGQPI---ANLSTYIL---------DASLNPVPI--GVAGELYLGGVGLARGYLNRPAL 1938
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 413 TFEAF------KHG--WLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTwGET 484
Cdd:PRK12467 1939 TAERFvadpfgTVGsrLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQDGAN-GKQ 2017
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 485 PCAFVVLEKSETTIKEDRVDKFQTRernLIEYCRENLPHFMCPRKVVFLEELPKNGNGKI 544
Cdd:PRK12467 2018 LVAYVVPTDPGLVDDDEAQVALRAI---LKNHLKASLPEYMVPAHLVFLARMPLTPNGKL 2074
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
187-543 |
2.93e-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: 341248 [Multi-domain] Cd Length: 364 Bit Score: 92.83 E-value: 2.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 187 DPISLNYTSGTTADPKGVVISH--------------RGAYLCTLSAIIGWEMGTCPVYLWTLPMFHCNGWtFTWGTAARG 252
Cdd:cd05924 4 DDLYILYTGGTTGMPKGVMWRQedifrmlmggadfgTGEFTPSEDAHKAAAAAAGTVMFPAPPLMHGTGS-WTAFGGLLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 253 GTSVCMRHV--TAPEIYKNIEMHNVTHMCCVPTVF-----NILLKGNSLDLSprsGPVHVLTGGspppAALVKKV-QRLG 324
Cdd:cd05924 83 GQTVVLPDDrfDPEEVWRTIEKHKVTSMTIVGDAMarpliDALRDAGPYDLS---SLFAISSGG----ALLSPEVkQGLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 325 FQVMH-----AYGQTEATGpilfcewqdewnrlpenqqmelkarqgisiLGLADVDVKNKETQKSAPRDGKTM-----GE 394
Cdd:cd05924 156 ELVPNitlvdAFGSSETGF------------------------------TGSGHSAGSGPETGPFTRANPDTVvldddGR 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 395 ILIKGSSIM----------KGYLKNPKATFEAFKH----GWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVEN 460
Cdd:cd05924 206 VVPPGSGGVgwiarrghipLGYYGDEAKTAETFPEvdgvRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEE 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 461 VLYKYPKVLETAVVAMPHPTWGETPCAFVVLEksettikedrvDKFQTRERNLIEYCRENLPHFMCPRKVVFLEELPKNG 540
Cdd:cd05924 286 ALKSHPAVYDVLVVGRPDERWGQEVVAVVQLR-----------EGAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSP 354
|
...
gi 15218839 541 NGK 543
Cdd:cd05924 355 AGK 357
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
20-479 |
3.72e-20 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 94.32 E-value: 3.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 20 LKRASECYPN-----RTSIIYGKT-RFTWP---QTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAV 90
Cdd:PLN02614 51 FRMSVEKYPNnpmlgRREIVDGKPgKYVWQtyqEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLY 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 91 LNPINTRLDATSIAAILRHAKPKILFLDR---------------------SFEALARESlhllSSEDSNLNLpviFIHE- 148
Cdd:PLN02614 131 CVPLYDTLGAGAVEFIISHSEVSIVFVEEkkiselfktcpnsteymktvvSFGGVSREQ----KEEAETFGL---VIYAw 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 149 NDFPKRASFEELDyecliqrgeptpsmvarmFRIQDEHDPISLNYTSGTTADPKGVVISHRGAYLCTLSAI-----IGWE 223
Cdd:PLN02614 204 DEFLKLGEGKQYD------------------LPIKKKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIrllksANAA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 224 MGTCPVYLWTLPMFHCNGWTFTWGTAARGGtSVCMRHVTAPEIYKNIEMHNVTHMCCVPTV------------------- 284
Cdd:PLN02614 266 LTVKDVYLSYLPLAHIFDRVIEECFIQHGA-AIGFWRGDVKLLIEDLGELKPTIFCAVPRVldrvysglqkklsdggflk 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 285 -----------FNILLKGNS-LDLSP-------------RSGPVHVLTGGSPPPAALVKKVQRL--GFQVMHAYGQTEAT 337
Cdd:PLN02614 345 kfvfdsafsykFGNMKKGQShVEASPlcdklvfnkvkqgLGGNVRIILSGAAPLASHVESFLRVvaCCHVLQGYGLTESC 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 338 GPIlFCEWQDEWNRL----PENQQMELKarqgisilgLADVDVKNKETQKSAPRdgktmGEILIKGSSIMKGYLKNPKAT 413
Cdd:PLN02614 425 AGT-FVSLPDELDMLgtvgPPVPNVDIR---------LESVPEMEYDALASTPR-----GEICIRGKTLFSGYYKREDLT 489
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15218839 414 FEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDII-ISGGENISSVEVENV---------LYKYPKVLETAVVAMPHP 479
Cdd:PLN02614 490 KEVLIDGWLHTGDVGEWQPNGSMKIIDRKKNIFkLSQGEYVAVENIENIygevqavdsVWVYGNSFESFLVAIANP 565
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
152-473 |
3.92e-20 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 94.40 E-value: 3.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 152 PKRASFEELDYECLIQRGEPTPsmvaRMFRIQDEHDPISLNYTSGTTADPKGVVISHRGAYLCTLSAIIGWEMGTCPVYL 231
Cdd:PLN02736 191 PSGTGVEIVTYSKLLAQGRSSP----QPFRPPKPEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKFYPSDVHI 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 232 WTLPMFHcngwtftwgTAARGGTSVCMRHVTAPEIYK--------NIEMHNVTHMCCVPTVFN----------------- 286
Cdd:PLN02736 267 SYLPLAH---------IYERVNQIVMLHYGVAVGFYQgdnlklmdDLAALRPTIFCSVPRLYNriydgitnavkesgglk 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 287 -------------ILLKGNSLdlSPR-------------SGPVHVLTGGSPPPAALVKKVQRLGF--QVMHAYGQTEATG 338
Cdd:PLN02736 338 erlfnaaynakkqALENGKNP--SPMwdrlvfnkikaklGGRVRFMSSGASPLSPDVMEFLRICFggRVLEGYGMTETSC 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 339 PILFCewqDEWNRL-----PENQQMELKarqgisilgLADVDVKNKETQ-KSAPRdgktmGEILIKGSSIMKGYLKNPKA 412
Cdd:PLN02736 416 VISGM---DEGDNLsghvgSPNPACEVK---------LVDVPEMNYTSEdQPYPR-----GEICVRGPIIFKGYYKDEVQ 478
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15218839 413 TFEAF-KHGWLNTGDVGVIHPDGHVEIKDRSKDII-ISGGENISSVEVENVLYKYPKVLETAV 473
Cdd:PLN02736 479 TREVIdEDGWLHTGDIGLWLPGGRLKIIDRKKNIFkLAQGEYIAPEKIENVYAKCKFVAQCFV 541
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
28-549 |
2.51e-18 |
|
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: 87.91 E-value: 2.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 28 PNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRLDATSIAAIL 107
Cdd:cd17656 2 PDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 108 RHAKPKILFLDRsfealareslHLLSSEDSNLNLPVIfihENDFPKRASFEELDYEcliqrgeptpsmvarmfriQDEHD 187
Cdd:cd17656 82 LDSGVRVVLTQR----------HLKSKLSFNKSTILL---EDPSISQEDTSNIDYI-------------------NNSDD 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 188 PISLNYTSGTTADPKGVVISHRgaylcTLSAIIGWEmgtcpvYLWTLPMFHCNGWTFT-----------WGTAARGGTSV 256
Cdd:cd17656 130 LLYIIYTSGTTGKPKGVQLEHK-----NMVNLLHFE------REKTNINFSDKVLQFAtcsfdvcyqeiFSTLLSGGTLY 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 257 CMRHVT---APEIYKNIEMHNvTHMCCVPTVFnILLKGNSLDLSPR--SGPVHVLTGGSP--PPAALVKKVQRLGFQVMH 329
Cdd:cd17656 199 IIREETkrdVEQLFDLVKRHN-IEVVFLPVAF-LKFIFSEREFINRfpTCVKHIITAGEQlvITNEFKEMLHEHNVHLHN 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 330 AYGQTEaTGPILFCEW--QDEWNRLPEnqqmelkarQGISIlGLADVDVKNKETQksaPRDGKTMGEILIKGSSIMKGYL 407
Cdd:cd17656 277 HYGPSE-THVVTTYTInpEAEIPELPP---------IGKPI-SNTWIYILDQEQQ---LQPQGIVGELYISGASVARGYL 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 408 KNPKATFEAF-------KHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPT 480
Cdd:cd17656 343 NRQELTAEKFfpdpfdpNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDK 422
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15218839 481 WGETPCAFVVLEKSETTIKedrvdkfqtrernLIEYCRENLPHFMCPRKVVFLEELPKNGNGKILKPKL 549
Cdd:cd17656 423 GEKYLCAYFVMEQELNISQ-------------LREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
193-477 |
2.60e-18 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 88.64 E-value: 2.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 193 YTSGTTADPKGVVISHrGAYLCTLSAI--IGWEMGTCPVYLWTLPMFH-----CNGWTFTWGTAARGGTSVCMRHvTAPE 265
Cdd:PLN02387 257 YTSGSTGLPKGVMMTH-GNIVATVAGVmtVVPKLGKNDVYLAYLPLAHilelaAESVMAAVGAAIGYGSPLTLTD-TSNK 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 266 IYK----NIEMHNVTHMCCVPTV----------------------FNILLKG--------------------NSLDLSP- 298
Cdd:PLN02387 335 IKKgtkgDASALKPTLMTAVPAIldrvrdgvrkkvdakgglakklFDIAYKRrlaaiegswfgawglekllwDALVFKKi 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 299 RS---GPVH-VLTGGSPppaaLVKKVQR-----LGFQVMHAYGQTEATGPILFCEWQDE-----WNRLPenqqmelkarq 364
Cdd:PLN02387 415 RAvlgGRIRfMLSGGAP----LSGDTQRfinicLGAPIGQGYGLTETCAGATFSEWDDTsvgrvGPPLP----------- 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 365 gISILGLADVDVKN-KETQKSAPRdgktmGEILIKGSSIMKGYLKNPKATFEAFK---HG--WLNTGDVGVIHPDGHVEI 438
Cdd:PLN02387 480 -CCYVKLVSWEEGGyLISDKPMPR-----GEIVIGGPSVTLGYFKNQEKTDEVYKvdeRGmrWFYTGDIGQFHPDGCLEI 553
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 15218839 439 KDRSKDII-ISGGENISSVEVENVLYKYPKVLETAVVAMP 477
Cdd:PLN02387 554 IDRKKDIVkLQHGEYVSLGKVEAALSVSPYVDNIMVHADP 593
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
28-544 |
1.53e-17 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 87.32 E-value: 1.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 28 PNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRLDATSIAAIL 107
Cdd:PRK12316 3071 PDAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYML 3150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 108 RHAKPKILFLDRSFEALARESLHLLSSEDSNLNLPvifihENDFPKRASFEELDYecliqrgeptpsmvarmfriqdehd 187
Cdd:PRK12316 3151 EDSGAQLLLSQSHLRLPLAQGVQVLDLDRGDENYA-----EANPAIRTMPENLAY------------------------- 3200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 188 pisLNYTSGTTADPKGVVISHRG--AYLCTLSAIIGWEMGTCPVYLWTLPmFHCNGWTFTWGTAArGGTSVCMRHVTAPE 265
Cdd:PRK12316 3201 ---VIYTSGSTGKPKGVGIRHSAlsNHLCWMQQAYGLGVGDRVLQFTTFS-FDVFVEELFWPLMS-GARVVLAGPEDWRD 3275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 266 IYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSPRSGPVH-VLTGGSPPPAALVKKVQrLGFQVMHAYGQTEATgpilfcE 344
Cdd:PRK12316 3276 PALLVELINSEGVDVLHAYPSMLQAFLEEEDAHRCTSLKrIVCGGEALPADLQQQVF-AGLPLYNLYGPTEAT------I 3348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 345 WQDEWnRLPENQQMELKARQGISILGLADVDVKNKetqksaPRDGKTMGEILIKGSSIMKGYLKNPKATFEAF------- 417
Cdd:PRK12316 3349 TVTHW-QCVEEGKDAVPIGRPIANRACYILDGSLE------PVPVGALGELYLGGEGLARGYHNRPGLTAERFvpdpfvp 3421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 418 KHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPhptwGETPCAFVVLEKSETT 497
Cdd:PRK12316 3422 GERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAVD----GRQLVAYVVPEDEAGD 3497
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 15218839 498 IKEDrvdkfqtrernLIEYCRENLPHFMCPRKVVFLEELPKNGNGKI 544
Cdd:PRK12316 3498 LREA-----------LKAHLKASLPEYMVPAHLLFLERMPLTPNGKL 3533
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
9-544 |
1.89e-17 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 86.64 E-value: 1.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 9 ANNVPLTPMT-FLKRASECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMA 87
Cdd:PRK10252 452 AVEIPETTLSaLVAQQAAKTPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEA 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 88 GAVLNPINTRLDATSIAAILRHAKPKILFLDRSFEALareslhllssedsnlnlpvifihendFPKRASFEELDYECLIQ 167
Cdd:PRK10252 532 GAAWLPLDTGYPDDRLKMMLEDARPSLLITTADQLPR--------------------------FADVPDLTSLCYNAPLA 585
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 168 RGEPTPsmvarmFRIQDEHDPISLNYTSGTTADPKGVVISHRgaylctlsAIIG---W-----EMGTCPVYLWTLPM-FH 238
Cdd:PRK10252 586 PQGAAP------LQLSQPHHTAYIIFTSGSTGRPKGVMVGQT--------AIVNrllWmqnhyPLTADDVVLQKTPCsFD 651
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 239 CNGWTFTWGTAArGGTSVcmrhVTAPEIYKN-------IEMHNVTHMCCVPTVFNILLKGNSLDLSPRSGPV--HVLTGG 309
Cdd:PRK10252 652 VSVWEFFWPFIA-GAKLV----MAEPEAHRDplamqqfFAEYGVTTTHFVPSMLAAFVASLTPEGARQSCASlrQVFCSG 726
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 310 SPPPAALVKKVQRLGFQVMH-AYGQTEA-----------------TG---PILFCEWqdewnrlpeNQQME-LKARQGIS 367
Cdd:PRK10252 727 EALPADLCREWQQLTGAPLHnLYGPTEAavdvswypafgeelaavRGssvPIGYPVW---------NTGLRiLDARMRPV 797
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 368 ILGLAdvdvknketqksaprdgktmGEILIKGSSIMKGYLKNPKATFEAFKHG-------WLNTGDVGVIHPDGHVEIKD 440
Cdd:PRK10252 798 PPGVA--------------------GDLYLTGIQLAQGYLGRPDLTASRFIADpfapgerMYRTGDVARWLDDGAVEYLG 857
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 441 RSKDIIISGGENISSVEVENVLYKYPKVlETAVV-------AMPHPTWGETPCAFVVlekSETTIKEDRVDkfqtrernL 513
Cdd:PRK10252 858 RSDDQLKIRGQRIELGEIDRAMQALPDV-EQAVThacvinqAAATGGDARQLVGYLV---SQSGLPLDTSA--------L 925
|
570 580 590
....*....|....*....|....*....|.
gi 15218839 514 IEYCRENLPHFMCPRKVVFLEELPKNGNGKI 544
Cdd:PRK10252 926 QAQLRERLPPHMVPVVLLQLDQLPLSANGKL 956
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
183-544 |
2.61e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 84.32 E-value: 2.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 183 QDEHDPISLNYTSGTTADPKGV------VISHRGAYLCTLSAiigwEMGTCPVYLwtLPMFHCNGwtFTWGTAA---RGG 253
Cdd:PRK08308 98 YLAEEPSLLQYSSGTTGEPKLIrrswteIDREIEAYNEALNC----EQDETPIVA--CPVTHSYG--LICGVLAaltRGS 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 254 TSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKgnsldLSPRSGPVH-VLTGGSPPPAALVKKVQRLGFQVMHAYG 332
Cdd:PRK08308 170 KPVIITNKNPKFALNILRNTPQHILYAVPLMLHILGR-----LLPGTFQFHaVMTSGTPLPEAWFYKLRERTTYMMQQYG 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 333 QTEAtGPILFCewqdewnrlpenQQMELKARQGISilgLADVDVKNKETqKSAPRdgktmgEILIK--GSSImkgylknp 410
Cdd:PRK08308 245 CSEA-GCVSIC------------PDMKSHLDLGNP---LPHVSVSAGSD-ENAPE------EIVVKmgDKEI-------- 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 411 katfeafkhgwlNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVV 490
Cdd:PRK08308 294 ------------FTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVI 361
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 15218839 491 lekSETTIKEDrvdkfqtrerNLIEYCRENLPHFMCPRKVVFLEELPKNGNGKI 544
Cdd:PRK08308 362 ---SHEEIDPV----------QLREWCIQHLAPYQVPHEIESVTEIPKNANGKV 402
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
21-550 |
2.80e-17 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 85.47 E-value: 2.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 21 KRASECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGavlnpintrlda 100
Cdd:PRK06060 12 EQASEAGWYDRPAFYAADVVTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARG------------ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 101 tsIAAILrhAKPKILFLDRSFEAlaRESLHLLSSEDSNLNlpvifiheNDFPKRASFEELDYECLIQRGEPTpsmvarmf 180
Cdd:PRK06060 80 --VMAFL--ANPELHRDDHALAA--RNTEPALVVTSDALR--------DRFQPSRVAEAAELMSEAARVAPG-------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 181 riqdEHDPIS------LNYTSGTTADPKGVVISHRG------AYLCTLSAIIGWEMGTCPVYLWtlpmFHCNGWTFTWGT 248
Cdd:PRK06060 138 ----GYEPMGgdalayATYTSGTTGPPKAAIHRHADpltfvdAMCRKALRLTPEDTGLCSARMY----FAYGLGNSVWFP 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 249 AARGGTSVCMRHVTAPEIYKNIEMH-NVTHMCCVPTVFNILLKGNSLDlSPRSGPVhVLTGGSPPPAALVKKVQRL--GF 325
Cdd:PRK06060 210 LATGGSAVINSAPVTPEAAAILSARfGPSVLYGVPNFFARVIDSCSPD-SFRSLRC-VVSAGEALELGLAERLMEFfgGI 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 326 QVMHAYGQTEaTGPILFCEWQDEWnrlpenqqmelkaRQGisilGLADVdVKNKETQKSAPrDGKTMG-----EILIKGS 400
Cdd:PRK06060 288 PILDGIGSTE-VGQTFVSNRVDEW-------------RLG----TLGRV-LPPYEIRVVAP-DGTTAGpgvegDLWVRGP 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 401 SIMKGYLKNPKATFEafKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPT 480
Cdd:PRK06060 348 AIAKGYWNRPDSPVA--NEGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVREST 425
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15218839 481 WGETPCAFVVLEKSETtikedrVDKFQTRE--RNLIeycrENLPHFMCPRKVVFLEELPKNGNGKILKPKLR 550
Cdd:PRK06060 426 GASTLQAFLVATSGAT------IDGSVMRDlhRGLL----NRLSAFKVPHRFAVVDRLPRTPNGKLVRGALR 487
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
32-547 |
6.07e-17 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 84.41 E-value: 6.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 32 SIIY-----GKT-RFTWPQTYDRCCRLAASLISLNISKNDVVSV-MAPNTPALYEMhFAVPMAGAVLNPINTRLDATSIA 104
Cdd:PTZ00237 79 ALIYecpylKKTiKLTYYQLYEKVCEFSRVLLNLNISKNDNVLIyMANTLEPLIAM-LSCARIGATHCVLFDGYSVKSLI 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 105 AILRHAKPKIL-------FLDR--SFEALARESLHLLSSEDSNlnlpVIFIHENDFPKRASFEeldyecLIQRGEPTPSM 175
Cdd:PTZ00237 158 DRIETITPKLIittnygiLNDEiiTFTPNLKEAIELSTFKPSN----VITLFRNDITSESDLK------KIETIPTIPNT 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 176 VARMFRIQ----------------DEHDPISLNYTSGTTADPKGVVISHRGAYLCTL---SAIIgwEMGTCPVYLWTlpm 236
Cdd:PTZ00237 228 LSWYDEIKkikennqspfyeyvpvESSHPLYILYTSGTTGNSKAVVRSNGPHLVGLKyywRSII--EKDIPTVVFSH--- 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 237 fHCNGWT----FTWGTAARGGTSVCMR-HVTAPE-----IYKNIEMHNVTHMCCVPTVFNILLK----GNSL----DLSp 298
Cdd:PTZ00237 303 -SSIGWVsfhgFLYGSLSLGNTFVMFEgGIIKNKhieddLWNTIEKHKVTHTLTLPKTIRYLIKtdpeATIIrskyDLS- 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 299 rsGPVHVLTGGSPPPAALVKKV-QRLGFQVMHAYGQTEaTGPILFCEWQDewNRLPenqqmelkarqgISILGLADVDVK 377
Cdd:PTZ00237 381 --NLKEIWCGGEVIEESIPEYIeNKLKIKSSRGYGQTE-IGITYLYCYGH--INIP------------YNATGVPSIFIK 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 378 nketqksaP----RDGKTM-----GEILIK---GSSIMKGYLKNP---KATFEAFKhGWLNTGDVGVIHPDGHVEIKDRS 442
Cdd:PTZ00237 444 --------PsilsEDGKELnvneiGEVAFKlpmPPSFATTFYKNDekfKQLFSKFP-GYYNSGDLGFKDENGYYTIVSRS 514
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 443 KDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKSETTIKEDrVDKFQTRERNLIEycrENLP 522
Cdd:PTZ00237 515 DDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGLLVLKQDQSNQSID-LNKLKNEINNIIT---QDIE 590
|
570 580
....*....|....*....|....*
gi 15218839 523 HFMCPRKVVFLEELPKNGNGKILKP 547
Cdd:PTZ00237 591 SLAVLRKIIIVNQLPKTKTGKIPRQ 615
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
414-555 |
6.21e-17 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 84.42 E-value: 6.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 414 FEAFKHGWLnTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVL-- 491
Cdd:PRK00174 478 FSTFKGMYF-TGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLkg 556
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15218839 492 --EKSETTIKEdrvdkfqtrernLIEYCRENLPHFMCPRKVVFLEELPKNGNGKILKPKLRDIAKG 555
Cdd:PRK00174 557 geEPSDELRKE------------LRNWVRKEIGPIAKPDVIQFAPGLPKTRSGKIMRRILRKIAEG 610
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
28-468 |
6.22e-17 |
|
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: 84.04 E-value: 6.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 28 PNRTSIIYGktrftwpQTYDRCCRLAASLISLN-ISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRLDATSIAAI 106
Cdd:cd17632 63 PRFETITYA-------ELWERVGAVAAAHDPEQpVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPI 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 107 LRHAKPKILFLDRSFEALARESLhLLSSEDSNLnlpVIFIHENDFPKRASFEELDYECLIQRGEP--TPSMVAR------ 178
Cdd:cd17632 136 LAETEPRLLAVSAEHLDLAVEAV-LEGGTPPRL---VVFDHRPEVDAHRAALESARERLAAVGIPvtTLTLIAVrgrdlp 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 179 ---MFRIQDEHDPIS-LNYTSGTTADPKGVVISHRGAYLCTLSAiIGWEMGTCP--VYLWTLPMFHCNGWTFTWGTAARG 252
Cdd:cd17632 212 papLFRPEPDDDPLAlLIYTSGSTGTPKGAMYTERLVATFWLKV-SSIQDIRPPasITLNFMPMSHIAGRISLYGTLARG 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 253 GTSVcmrHVTAPE---IYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSPRSGPVH----------------VLTG----- 308
Cdd:cd17632 291 GTAY---FAAASDmstLFDDLALVRPTELFLVPRVCDMLFQRYQAELDRRSVAGAdaetlaervkaelrerVLGGrllaa 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 309 --GSPPPAALVKKV--QRLGFQVMHAYGQTEATGPILFcewqdewNRLPENQQMELKarqgisilgLADV-DVKNKETQK 383
Cdd:cd17632 368 vcGSAPLSAEMKAFmeSLLDLDLHDGYGSTEAGAVILD-------GVIVRPPVLDYK---------LVDVpELGYFRTDR 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 384 SAPRdgktmGEILIKGSSIMKGYLKNPKATFEAF-KHGWLNTGDV-GVIHPDGHVEIKDRSKDIIISGGENISSVEVENV 461
Cdd:cd17632 432 PHPR-----GELLVKTDTLFPGYYKRPEVTAEVFdEDGFYRTGDVmAELGPDRLVYVDRRNNVLKLSQGEFVTVARLEAV 506
|
....*..
gi 15218839 462 LYKYPKV 468
Cdd:cd17632 507 FAASPLV 513
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
39-553 |
1.24e-16 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 83.41 E-value: 1.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 39 RFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILF-- 116
Cdd:PLN02654 120 SLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVItc 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 117 --LDRSFEALARESL---HLLSSEDSNLNLPVIFIHENDFP-KRASF---EELD--YECLIQRgEPTPSMVARMfriqDE 185
Cdd:PLN02654 200 naVKRGPKTINLKDIvdaALDESAKNGVSVGICLTYENQLAmKREDTkwqEGRDvwWQDVVPN-YPTKCEVEWV----DA 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 186 HDPISLNYTSGTTADPKGVVIShRGAYLCTLSAIIGWEMGTCP--VYLWTLPMFHCNGWTF-TWGTAARGGTSVCMRHV- 261
Cdd:PLN02654 275 EDPLFLLYTSGSTGKPKGVLHT-TGGYMVYTATTFKYAFDYKPtdVYWCTADCGWITGHSYvTYGPMLNGATVLVFEGAp 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 262 ---TAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSPRS-GPVHVLTGGSPP--PAALvkkvqRLGFQVM------- 328
Cdd:PLN02654 354 nypDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGDEYVTRHSrKSLRVLGSVGEPinPSAW-----RWFFNVVgdsrcpi 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 329 -HAYGQTEaTGPILFCEWQDEWNRLPENQQMELKARQGISilgladVDVKNKETqksaprDGKTMGEILIKGS------S 401
Cdd:PLN02654 429 sDTWWQTE-TGGFMITPLPGAWPQKPGSATFPFFGVQPVI------VDEKGKEI------EGECSGYLCVKKSwpgafrT 495
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 402 IMKGYLKNPKATFEAFKhGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTW 481
Cdd:PLN02654 496 LYGDHERYETTYFKPFA-GYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVK 574
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15218839 482 GETPCAFVVLEKSETTIKEDRvdkfqtreRNLIEYCRENLPHFMCPRKVVFLEELPKNGNGKILKPKLRDIA 553
Cdd:PLN02654 575 GQGIYAFVTLVEGVPYSEELR--------KSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKIA 638
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
28-552 |
1.26e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 84.06 E-value: 1.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 28 PNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRLDATSIAAIL 107
Cdd:PRK12467 3109 PEAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMI 3188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 108 rhakpkilfldrsfealareslhllssEDSNLNLPVIFIH-ENDFPKRASFEELDYECLIQRGEPTPSMVARMfriqdeh 186
Cdd:PRK12467 3189 ---------------------------EDSGVKLLLTQAHlLEQLPAPAGDTALTLDRLDLNGYSENNPSTRV------- 3234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 187 DPISLNY---TSGTTADPKGVVISHrGA---YLCTLSAIIGWEMGTcPVYLWTLPMFHCNGWTFTWgTAARGGTSVCM-- 258
Cdd:PRK12467 3235 MGENLAYviyTSGSTGKPKGVGVRH-GAlanHLCWIAEAYELDAND-RVLLFMSFSFDGAQERFLW-TLICGGCLVVRdn 3311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 259 RHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKgnslDLSPRSGPV--HVLTGGSPPPAALVKKVQRLGFQV--MHAYGQT 334
Cdd:PRK12467 3312 DLWDPEELWQAIHAHRISIACFPPAYLQQFAE----DAGGADCASldIYVFGGEAVPPAAFEQVKRKLKPRglTNGYGPT 3387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 335 EAT-GPILFCEWQD---EWNRLPENQQMelkARQGISILgladvdvknkeTQKSAPRDGKTMGEILIKGSSIMKGYLKNP 410
Cdd:PRK12467 3388 EAVvTVTLWKCGGDavcEAPYAPIGRPV---AGRSIYVL-----------DGQLNPVPVGVAGELYIGGVGLARGYHQRP 3453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 411 KATFEAF-------KHGWL-NTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPhPTWG 482
Cdd:PRK12467 3454 SLTAERFvadpfsgSGGRLyRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLARD-GAGG 3532
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 483 ETPCAFVVLEKSETTIKEDRVDKFQTrernlieycreNLPHFMCPRKVVFLEELPKNGNGKILKPKLRDI 552
Cdd:PRK12467 3533 KQLVAYVVPADPQGDWRETLRDHLAA-----------SLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDP 3591
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
14-468 |
1.57e-16 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 82.97 E-value: 1.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 14 LTPMTFLKRASECYPN-----RTSIIYGK----TRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAV 84
Cdd:PLN02861 43 DSPWQFFSDAVKKYPNnqmlgRRQVTDSKvgpyVWLTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEAC 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 85 PMAGAVLNPINTRLDATSIAAILRHAKPKILFLDrsfEALARESLHLLSSEDSNLNLPVIFIHENDFPKRASfEELDYEC 164
Cdd:PLN02861 123 NSQGITYVPLYDTLGANAVEFIINHAEVSIAFVQ---ESKISSILSCLPKCSSNLKTIVSFGDVSSEQKEEA-EELGVSC 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 165 LiqRGEPTPSMVARMFRIQDEH--DPISLNYTSGTTADPKGVVISHRGAYLCTLSA-----IIGWEMGTCPVYLWTLPMF 237
Cdd:PLN02861 199 F--SWEEFSLMGSLDCELPPKQktDICTIMYTSGTTGEPKGVILTNRAIIAEVLSTdhllkVTDRVATEEDSYFSYLPLA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 238 HCNGWTFTWGTAARGgTSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLS-------------------- 297
Cdd:PLN02861 277 HVYDQVIETYCISKG-ASIGFWQGDIRYLMEDVQALKPTIFCGVPRVYDRIYTGIMQKISsggmlrkklfdfaynyklgn 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 298 -----------PR-------------SGPVHVLTGGSPPPAALVKKVQRL--GFQVMHAYGQTEATGPIlFCEWQDEWnr 351
Cdd:PLN02861 356 lrkglkqeeasPRldrlvfdkikeglGGRVRLLLSGAAPLPRHVEEFLRVtsCSVLSQGYGLTESCGGC-FTSIANVF-- 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 352 lpenqqmelkarqgiSILGLADVDVKNKETQ-KSAPRDGKTM------GEILIKGSSIMKGYLKNPKATFEAFKHGWLNT 424
Cdd:PLN02861 433 ---------------SMVGTVGVPMTTIEARlESVPEMGYDAlsdvprGEICLRGNTLFSGYHKRQDLTEEVLIDGWFHT 497
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 15218839 425 GDVGVIHPDGHVEIKDRSKDII-ISGGENISSVEVENVLYKYPKV 468
Cdd:PLN02861 498 GDIGEWQPNGAMKIIDRKKNIFkLSQGEYVAVENLENTYSRCPLI 542
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
184-544 |
1.89e-16 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 82.35 E-value: 1.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 184 DEHDPISLNYTSGTTADPKGVVISHRGAYLCtLSAI---IGWEMGTCPVYLWtLPMFHCNGWT-FTWGTAARGGTSVC-- 257
Cdd:PRK07768 150 GEDDLALMQLTSGSTGSPKAVQITHGNLYAN-AEAMfvaAEFDVETDVMVSW-LPLFHDMGMVgFLTVPMYFGAELVKvt 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 258 -MRHVTAPEIY-KNIEMHNVThMCCVP----TVFNILL----KGNSLDLSP-RsgpvHVLTGGSP-PPAA---LVKKVQR 322
Cdd:PRK07768 228 pMDFLRDPLLWaELISKYRGT-MTAAPnfayALLARRLrrqaKPGAFDLSSlR----FALNGAEPiDPADvedLLDAGAR 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 323 LGFQ---VMHAYGQTEATGPILFCEWqDEWNRLPENQQMELKARQ----------------GISILGLaDVDVKNKETQK 383
Cdd:PRK07768 303 FGLRpeaILPAYGMAEATLAVSFSPC-GAGLVVDEVDADLLAALRravpatkgntrrlatlGPPLPGL-EVRVVDEDGQV 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 384 SAPRDgktMGEILIKGSSIMKGYLK--NPKATFEAfkHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENV 461
Cdd:PRK07768 381 LPPRG---VGVIELRGESVTPGYLTmdGFIPAQDA--DGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERA 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 462 LYKYPKVLETAVVA--MPHPTWGETpcaFVVLekSETTIKEDRVDKFQTReRNLIEYCRENLPhfMCPRKVVFLE--ELP 537
Cdd:PRK07768 456 AARVEGVRPGNAVAvrLDAGHSREG---FAVA--VESNAFEDPAEVRRIR-HQVAHEVVAEVG--VRPRNVVVLGpgSIP 527
|
....*..
gi 15218839 538 KNGNGKI 544
Cdd:PRK07768 528 KTPSGKL 534
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
305-544 |
1.99e-16 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 80.86 E-value: 1.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 305 VLTGGSPPPAALVKKVQRLGFQVMHAYGQTEATGPILFcewqdewnrlpenqqmelkarQGISILGlADVDVKNketqks 384
Cdd:PRK07824 156 VLVGGGPAPAPVLDAAAAAGINVVRTYGMSETSGGCVY---------------------DGVPLDG-VRVRVED------ 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 385 aprdgktmGEILIKGSSIMKGYlKNPkATFEAF-KHGWLNTGDVGVIHpDGHVEIKDRSKDIIISGGENISSVEVENVLY 463
Cdd:PRK07824 208 --------GRIALGGPTLAKGY-RNP-VDPDPFaEPGWFRTDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALA 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 464 KYPKVLETAVVAMPHPTWGETPCAFVVLEKSETTIKEDrvdkfqtrernLIEYCRENLPHFMCPRKVVFLEELPKNGNGK 543
Cdd:PRK07824 277 THPAVADCAVFGLPDDRLGQRVVAAVVGDGGPAPTLEA-----------LRAHVARTLDRTAAPRELHVVDELPRRGIGK 345
|
.
gi 15218839 544 I 544
Cdd:PRK07824 346 V 346
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
25-549 |
3.73e-16 |
|
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.
Pssm-ID: 341300 [Multi-domain] Cd Length: 440 Bit Score: 81.06 E-value: 3.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 25 ECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRLDATSIA 104
Cdd:cd17645 9 ERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGERIA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 105 AILRHAKPKILfldrsfealareslhllssedsnlnlpvifihendfpkrasfeeldyecliqrgeptpsmvarmfrIQD 184
Cdd:cd17645 89 YMLADSSAKIL------------------------------------------------------------------LTN 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 185 EHDPISLNYTSGTTADPKGVVISHRgaylcTLSAIIGWEMGTCPV------YLWTLPMFHCNGW-TFTWGTAargGTSVc 257
Cdd:cd17645 103 PDDLAYVIYTSGSTGLPKGVMIEHH-----NLVNLCEWHRPYFGVtpadksLVYASFSFDASAWeIFPHLTA---GAAL- 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 258 mrHVTAPEIYKNI-------EMHNVThMCCVPTVfnilLKGNSLDLSPRSGPVhVLTGGSpppaaLVKKVQRLGFQVMHA 330
Cdd:cd17645 174 --HVVPSERRLDLdalndyfNQEGIT-ISFLPTG----AAEQFMQLDNQSLRV-LLTGGD-----KLKKIERKGYKLVNN 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 331 YGQTEATGPILFCEWQDEWNRLPENQQMelkARQGISILGladvdvknkETQKSAPRDgkTMGEILIKGSSIMKGYLKNP 410
Cdd:cd17645 241 YGPTENTVVATSFEIDKPYANIPIGKPI---DNTRVYILD---------EALQLQPIG--VAGELCIAGEGLARGYLNRP 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 411 KATFEAF-------KHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGE 483
Cdd:cd17645 307 ELTAEKFivhpfvpGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRK 386
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15218839 484 TPCAFVVLEKsETTIKEDRvdkfqtrernliEYCRENLPHFMCPRKVVFLEELPKNGNGKILKPKL 549
Cdd:cd17645 387 YLVAYVTAPE-EIPHEELR------------EWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
18-479 |
7.90e-16 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 80.33 E-value: 7.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 18 TFLKRASECYPNRTSIIYGKTRFTWPQ-TYD---------RCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMA 87
Cdd:PRK09274 10 RHLPRAAQERPDQLAVAVPGGRGADGKlAYDelsfaeldaRSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 88 GAVLNPINTRLDATSIAAILRHAKP------------KILFLdrsfeaLARESLHLLSSEDSNLNLPVIFIHEndfpkra 155
Cdd:PRK09274 90 GAVPVLVDPGMGIKNLKQCLAEAQPdafigipkahlaRRLFG------WGKPSVRRLVTVGGRLLWGGTTLAT------- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 156 sfeeldyecLIQRGEPTPSMVARMfriqDEHDPISLNYTSGTTADPKGVVISHRG--AYLCTLSAIIGWEMGTcpVYLWT 233
Cdd:PRK09274 157 ---------LLRDGAAAPFPMADL----APDDMAAILFTSGSTGTPKGVVYTHGMfeAQIEALREDYGIEPGE--IDLPT 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 234 LPMFHCNGwtftwgtAARGGTSV--CM---RHVTA-PE-IYKNIEMHNVTHMCCVPTVFNILL---KGNSLDL-SPRSgp 302
Cdd:PRK09274 222 FPLFALFG-------PALGMTSVipDMdptRPATVdPAkLFAAIERYGVTNLFGSPALLERLGrygEANGIKLpSLRR-- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 303 vhVLTGGSPPPAALVKKVQRL---GFQVMHAYGQTEATgPILFCEWQDEwnrLPENQQMelkARQG-------------I 366
Cdd:PRK09274 293 --VISAGAPVPIAVIERFRAMlppDAEILTPYGATEAL-PISSIESREI---LFATRAA---TDNGagicvgrpvdgveV 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 367 SILGLADVDVKNKETQKSAPRDGktMGEILIKGSSIMKGYLKNPKATFEA--------FKHgwlNTGDVGVIHPDGHVEI 438
Cdd:PRK09274 364 RIIAISDAPIPEWDDALRLATGE--IGEIVVAGPMVTRSYYNRPEATRLAkipdgqgdVWH---RMGDLGYLDAQGRLWF 438
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 15218839 439 KDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHP 479
Cdd:PRK09274 439 CGRKAHRVETAGGTLYTIPCERIFNTHPGVKRSALVGVGVP 479
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
27-544 |
1.31e-15 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 79.55 E-value: 1.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 27 YPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPalyEMhfAVPMAGAVLN-----PINTRLDAT 101
Cdd:PRK04813 15 QPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSP---EM--LATFLGAVKAghayiPVDVSSPAE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 102 SIAAILRHAKPKiLFLDRSFEALARESLHLLSSEDsnlnLPVIFIHENDFPKRASFEELDYECLIqrgeptpsmvarmfr 181
Cdd:PRK04813 90 RIEMIIEVAKPS-LIIATEELPLEILGIPVITLDE----LKDIFATGNPYDFDHAVKGDDNYYII--------------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 182 iqdehdpislnYTSGTTADPKGVVISHRgaylcTLSAIIGWE-----MGTCPVYLWTLPmfhcngWTF-----TWG-TAA 250
Cdd:PRK04813 150 -----------FTSGTTGKPKGVQISHD-----NLVSFTNWMledfaLPEGPQFLNQAP------YSFdlsvmDLYpTLA 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 251 RGGTSVCMRH-VTA--PEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSPRSGPVHVLTGGSPPPAALVKK-VQRlgF- 325
Cdd:PRK04813 208 SGGTLVALPKdMTAnfKQLFETLPQLPINVWVSTPSFADMCLLDPSFNEEHLPNLTHFLFCGEELPHKTAKKlLER--Fp 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 326 --QVMHAYGQTEATGPILFCEWQDE----WNRLPenqqmelkarqgisiLGLADVDVK---NKETQKSAPRDGKtmGEIL 396
Cdd:PRK04813 286 saTIYNTYGPTEATVAVTSIEITDEmldqYKRLP---------------IGYAKPDSPlliIDEEGTKLPDGEQ--GEIV 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 397 IKGSSIMKGYLKNPKATFEAF----KHGWLNTGDVGVIhPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVlETA 472
Cdd:PRK04813 349 ISGPSVSKGYLNNPEKTAEAFftfdGQPAYHTGDAGYL-EDGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYV-ESA 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 473 VVAmphPTWGETPC----AFVVLEKSE--------TTIKEDrvdkfqtrernlieyCRENLPHFMCPRKVVFLEELPKNG 540
Cdd:PRK04813 427 VVV---PYNKDHKVqyliAYVVPKEEDferefeltKAIKKE---------------LKERLMEYMIPRKFIYRDSLPLTP 488
|
....
gi 15218839 541 NGKI 544
Cdd:PRK04813 489 NGKI 492
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
191-475 |
2.50e-14 |
|
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: 75.60 E-value: 2.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 191 LNYTSGTTADPKGVVISHRGAYLCTLSAIIGWEMGTCPVYLWTLPMFHCNGWTFTWGTAARGG-------TSVCMRHvta 263
Cdd:cd05908 111 IQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGmnqylmpTRLFIRR--- 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 264 PEIY-KNIEMHNVTHMCCVPTVFNILLK------GNSLDLSPrsgpVHVLTGGSPPPAA-----LVKKVQRLGFQ---VM 328
Cdd:cd05908 188 PILWlKKASEHKATIVSSPNFGYKYFLKtlkpekANDWDLSS----IRMILNGAEPIDYelcheFLDHMSKYGLKrnaIL 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 329 HAYGQTEAT-------------GPILFCEWQDEWNRLPENQQMELKARQGISI-LGLADVDVKNKETQKSAPRDGkTMGE 394
Cdd:cd05908 264 PVYGLAEASvgaslpkaqspfkTITLGRRHVTHGEPEPEVDKKDSECLTFVEVgKPIDETDIRICDEDNKILPDG-YIGH 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 395 ILIKGSSIMKGYLKNPKATFEAF-KHGWLNTGDVGVIHpDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAV 473
Cdd:cd05908 343 IQIRGKNVTPGYYNNPEATAKVFtDDGWLKTGDLGFIR-NGRLVITGREKDIIFVNGQNVYPHDIERIAEELEGVELGRV 421
|
..
gi 15218839 474 VA 475
Cdd:cd05908 422 VA 423
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
193-544 |
3.15e-14 |
|
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: 75.13 E-value: 3.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 193 YTSGTTADPKGVVISHRGA-YLCT-LSAIIGwemGTCPVYLWTLPM------FHCNGWTFtwgtAARGGTSVC-----MR 259
Cdd:cd17648 101 YTSGTTGKPKGVLVEHGSVvNLRTsLSERYF---GRDNGDEAVLFFsnyvfdFFVEQMTL----ALLNGQKLVvppdeMR 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 260 hVTAPEIYKNIEMHNVTHMCCVPTVFNILlkgnslDLSPRSGPVHVLTGGSPPPAALVKKV-QRLGFQVMHAYGQTEATG 338
Cdd:cd17648 174 -FDPDRFYAYINREKVTYLSGTPSVLQQY------DLARLPHLKRVDAAGEEFTAPVFEKLrSRFAGLIINAYGPTETTV 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 339 PILFcewqdewNRLPENQQMELKARQGisiLGLADVDVKNKETQKsAPRDGktMGEILIKGSSIMKGYLKNPKATFEAF- 417
Cdd:cd17648 247 TNHK-------RFFPGDQRFDKSLGRP---VRNTKCYVLNDAMKR-VPVGA--VGELYLGGDGVARGYLNRPELTAERFl 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 418 -------------KHGWL-NTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGE 483
Cdd:cd17648 314 pnpfqteqerargRNARLyKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDASQAQ 393
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15218839 484 TP-----CAFVVLEksettikEDRVDkfqtrERNLIEYCRENLPHFMCPRKVVFLEELPKNGNGKI 544
Cdd:cd17648 394 SRiqkylVGYYLPE-------PGHVP-----ESDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKL 447
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
183-476 |
3.45e-14 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 75.19 E-value: 3.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 183 QDEHDPISLNYTSGTTADPKGVVIShRGAYLCTLSAI---IGWEMGTCPVYLWtLPMFHCNGWTFTWgTAARGGTSVCMR 259
Cdd:PRK05851 149 PDSGGPAVLQGTAGSTGTPRTAILS-PGAVLSNLRGLnarVGLDAATDVGCSW-LPLYHDMGLAFLL-TAALAGAPLWLA 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 260 HVTA----PEIYKNIEMHNVTHMCCVPTV-FNILLKGNS----LDLsprsGPVHV-LTGGSPPPAALVKK----VQRLGF 325
Cdd:PRK05851 226 PTTAfsasPFRWLSWLSDSRATLTAAPNFaYNLIGKYARrvsdVDL----GALRVaLNGGEPVDCDGFERfataMAPFGF 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 326 Q---VMHAYGQTEAT------GP---ILFCEWQDewnrlPENQQMELKARQGISILGLadvDVKNKETQKSAPRDGKTMG 393
Cdd:PRK05851 302 DagaAAPSYGLAESTcavtvpVPgigLRVDEVTT-----DDGSGARRHAVLGNPIPGM---EVRISPGDGAAGVAGREIG 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 394 EILIKGSSIMKGYLKnpKATFEAfkHGWLNTGDVGVIHPDGHVeIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAV 473
Cdd:PRK05851 374 EIEIRGASMMSGYLG--QAPIDP--DDWFPTGDLGYLVDGGLV-VCGRAKELITVAGRNIFPTEIERVAAQVRGVREGAV 448
|
...
gi 15218839 474 VAM 476
Cdd:PRK05851 449 VAV 451
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
52-498 |
2.54e-13 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 72.73 E-value: 2.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 52 LAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNP--INTRL---DA--TSIAAILRHAKPKILFLDRSFEAL 124
Cdd:PRK09192 62 GARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPlpLPMGFggrESyiAQLRGMLASAQPAAIITPDELLPW 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 125 ARESLhllssedSNLNLPVIFIHendfpkrASFEELDyECLIQRGEPTPsmvarmfriqdeHDPISLNYTSGTTADPKGV 204
Cdd:PRK09192 142 VNEAT-------HGNPLLHVLSH-------AWFKALP-EADVALPRPTP------------DDIAYLQYSSGSTRFPRGV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 205 VISHRgAYLCTLSAI-------------IGW-----EMG---------TCPV---YLWT----------LPMFHCNGWTF 244
Cdd:PRK09192 195 IITHR-ALMANLRAIshdglkvrpgdrcVSWlpfyhDMGlvgflltpvATQLsvdYLPTrdfarrplqwLDLISRNRGTI 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 245 TWgtAARGGTSVCMRHVTAPEIykniemhnvthmccvptvfnillkgNSLDLSP-RSGPVhvltGGSPPPA----ALVKK 319
Cdd:PRK09192 274 SY--SPPFGYELCARRVNSKDL-------------------------AELDLSCwRVAGI----GADMIRPdvlhQFAEA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 320 VQRLGFQ---VMHAYGQTEATGPILFcewqdewnrLPENQ--QMELKARQGISILGLA---------------------- 372
Cdd:PRK09192 323 FAPAGFDdkaFMPSYGLAEATLAVSF---------SPLGSgiVVEEVDRDRLEYQGKAvapgaetrrvrtfvncgkalpg 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 373 -DVDVKNKETQKSAPRdgkTMGEILIKGSSIMKGYLKNPKATFEAFKHGWLNTGDVGVIHpDGHVEIKDRSKDIIISGGE 451
Cdd:PRK09192 394 hEIEIRNEAGMPLPER---VVGHICVRGPSLMSGYFRDEESQDVLAADGWLDTGDLGYLL-DGYLYITGRAKDLIIINGR 469
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 15218839 452 NIssvevenvlykYPKVLETAVVAMPHPTWGETpCAFVVLEKSETTI 498
Cdd:PRK09192 470 NI-----------WPQDIEWIAEQEPELRSGDA-AAFSIAQENGEKI 504
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
38-555 |
3.58e-13 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 72.29 E-value: 3.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 38 TRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTP-ALYEMhFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILF 116
Cdd:PRK10524 83 RTYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAeAAFAM-LACARIGAIHSVVFGGFASHSLAARIDDAKPVLIV 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 117 ldrSFEALAR-----ESLHLLsseDSNLNLP------VIFIHEN--DFPKRASfEELDYECLIQRGEPTPSMVARMfriq 183
Cdd:PRK10524 162 ---SADAGSRggkvvPYKPLL---DEAIALAqhkprhVLLVDRGlaPMARVAG-RDVDYATLRAQHLGARVPVEWL---- 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 184 DEHDPISLNYTSGTTADPKGVvisHR--GAYLCTLSAI------------------IGWEMG-TCPVY------LWTLpM 236
Cdd:PRK10524 231 ESNEPSYILYTSGTTGKPKGV---QRdtGGYAVALATSmdtifggkagetffcasdIGWVVGhSYIVYapllagMATI-M 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 237 FHcngwtftwGTAARGGTSVCMRHVtapeiykniEMHNVTHMCCVPTVFNILLKGNS-----LDLSPRSgpvHVLTGGSP 311
Cdd:PRK10524 307 YE--------GLPTRPDAGIWWRIV---------EKYKVNRMFSAPTAIRVLKKQDPallrkHDLSSLR---ALFLAGEP 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 312 ---PPAALVKKVqrLGFQVMHAYGQTEATGPILfcewqdewNRLPENQQMELK-ARQGISILGLaDVDVKNKETQKSAPR 387
Cdd:PRK10524 367 ldePTASWISEA--LGVPVIDNYWQTETGWPIL--------AIARGVEDRPTRlGSPGVPMYGY-NVKLLNEVTGEPCGP 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 388 DGKtmGEILIKG-------SSI-------MKGYlknpkatFEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENI 453
Cdd:PRK10524 436 NEK--GVLVIEGplppgcmQTVwgdddrfVKTY-------WSLFGRQVYSTFDWGIRDADGYYFILGRTDDVINVAGHRL 506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 454 SSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKSETTikEDRvDKFQTRERNLIEYCRENLPHFMCPRKVVFL 533
Cdd:PRK10524 507 GTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSDSL--ADR-EARLALEKEIMALVDSQLGAVARPARVWFV 583
|
570 580
....*....|....*....|..
gi 15218839 534 EELPKNGNGKILKPKLRDIAKG 555
Cdd:PRK10524 584 SALPKTRSGKLLRRAIQAIAEG 605
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
48-553 |
9.84e-13 |
|
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: 70.57 E-value: 9.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 48 RCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKIlfldrsfealare 127
Cdd:cd05910 11 RSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAEPDA------------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 128 slhllssedsnlnlpviFIhendfpkrasfeeldyecliqrGEPTPSmvarmfriqdehDPISLNYTSGTTADPKGVVIS 207
Cdd:cd05910 78 -----------------FI----------------------GIPKAD------------EPAAILFTSGSTGTPKGVVYR 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 208 HR--GAYLCTLSAIIGWEMGTcpVYLWTLPMFHCNGwtftwgtAARGGTSVC--MRHvTAP------EIYKNIEMHNVTH 277
Cdd:cd05910 107 HGtfAAQIDALRQLYGIRPGE--VDLATFPLFALFG-------PALGLTSVIpdMDP-TRParadpqKLVGAIRQYGVSI 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 278 MCCVPTVFNILLKGNSLDLSPRSGPVHVLTGGSPPPAALVKKVQRL---GFQVMHAYGQTEATgPILFCEWQD---EWNR 351
Cdd:cd05910 177 VFGSPALLERVARYCAQHGITLPSLRRVLSAGAPVPIALAARLRKMlsdEAEILTPYGATEAL-PVSSIGSREllaTTTA 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 352 LPENQQMELKARQ--GI--SILGLADVDVKNKETQKSAPRDGktMGEILIKGSSIMKGYLKNPKATFEA----FKHG-WL 422
Cdd:cd05910 256 ATSGGAGTCVGRPipGVrvRIIEIDDEPIAEWDDTLELPRGE--IGEITVTGPTVTPTYVNRPVATALAkiddNSEGfWH 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 423 NTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTwGETPcafVVLEKSETTIKEDR 502
Cdd:cd05910 334 RMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGVGKPG-CQLP---VLCVEPLPGTITPR 409
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 15218839 503 vdkfQTRERNLIEYCRENlPHFMCPRKVVFLEELPKN--GNGKILKPKLRDIA 553
Cdd:cd05910 410 ----ARLEQELRALAKDY-PHTQRIGRFLIHPSFPVDirHNAKIFREKLAVWA 457
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
51-462 |
2.82e-12 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 69.07 E-value: 2.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 51 RLAASLISLNISK--NDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFLDRSFEAlares 128
Cdd:PRK06334 52 RKAVIALATKVSKypDQHIGIMMPASAGAYIAYFATLLSGKIPVMINWSQGLREVTACANLVGVTHVLTSKQLMQ----- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 129 lHLLSSEDSNLNLPVIFIHENDFPKRASFEEldyECLIQRGEPTP-SMVARMFRI--QDEHDPISLNYTSGTTADPKGVV 205
Cdd:PRK06334 127 -HLAQTHGEDAEYPFSLIYMEEVRKELSFWE---KCRIGIYMSIPfEWLMRWFGVsdKDPEDVAVILFTSGTEKLPKGVP 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 206 ISHRGAYLCTLSAIIGWEMGTCPVYLWTLPMFHCNGWTFTWGTAARGGTSVCMRH--VTAPEIYKNIEMHNVTHMCCVPT 283
Cdd:PRK06334 203 LTHANLLANQRACLKFFSPKEDDVMMSFLPPFHAYGFNSCTLFPLLSGVPVVFAYnpLYPKKIVEMIDEAKVTFLGSTPV 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 284 VFNILLKGNSLDLSPRSGPVHVLTGGSPPPAALVKKVQRL--GFQVMHAYGQTEATgPILFCEWQDEwnrlPENQQMelk 361
Cdd:PRK06334 283 FFDYILKTAKKQESCLPSLRFVVIGGDAFKDSLYQEALKTfpHIQLRQGYGTTECS-PVITINTVNS----PKHESC--- 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 362 arQGISILGLaDVDVKNKETQksAPRDGKTMGEILIKGSSIMKGYLKN-PKATF-EAFKHGWLNTGDVGVIHPDGHVEIK 439
Cdd:PRK06334 355 --VGMPIRGM-DVLIVSEETK--VPVSSGETGLVLTRGTSLFSGYLGEdFGQGFvELGGETWYVTGDLGYVDRHGELFLK 429
|
410 420
....*....|....*....|...
gi 15218839 440 DRSKDIIISGGENISSVEVENVL 462
Cdd:PRK06334 430 GRLSRFVKIGAEMVSLEALESIL 452
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
180-463 |
5.10e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 68.59 E-value: 5.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 180 FRIQDEhDP---ISLNYTSGTTADPKGVVISHRGAY-----LCTLSAIIGWEMGTcpvYLWTLPMFHCNGWTFTWGTAAR 251
Cdd:PTZ00342 296 YKIQNE-DPdfiTSIVYTSGTSGKPKGVMLSNKNLYntvvpLCKHSIFKKYNPKT---HLSYLPISHIYERVIAYLSFML 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 252 GGTSvcmrHVTAPEI---YKNIEMHNVTHMCCVPTVF-----NILLKGNSLDLSPRS----------------------G 301
Cdd:PTZ00342 372 GGTI----NIWSKDInyfSKDIYNSKGNILAGVPKVFnriytNIMTEINNLPPLKRFlvkkilslrksnnnggfskfleG 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 302 PVHV---------------LTGGspppAALVKKVQR-----LGFQVMHAYGQTEATGPIlFCEWQDEWNrlPENQqmelk 361
Cdd:PTZ00342 448 ITHIsskikdkvnpnleviLNGG----GKLSPKIAEelsvlLNVNYYQGYGLTETTGPI-FVQHADDNN--TESI----- 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 362 arqGISILGLADVDVKNKETQK---SAPRdgktmGEILIKGSSIMKGYLKNPKATFEAFKH-GWLNTGDVGVIHPDGHVE 437
Cdd:PTZ00342 516 ---GGPISPNTKYKVRTWETYKatdTLPK-----GELLIKSDSIFSGYFLEKEQTKNAFTEdGYFKTGDIVQINKNGSLT 587
|
330 340
....*....|....*....|....*..
gi 15218839 438 IKDRSKDII-ISGGENISSvEVENVLY 463
Cdd:PTZ00342 588 FLDRSKGLVkLSQGEYIET-DMLNNLY 613
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
165-443 |
7.52e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 68.08 E-value: 7.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 165 LIQRGEPTPSMVArmFRIQDEHDPISL-NYTSGTTADPKGVVISHR----GAYLCT--LSAIIGwEMGTCPVYLWTLPMF 237
Cdd:PTZ00216 244 VVAKGHSAGSHHP--LNIPENNDDLALiMYTSGTTGDPKGVMHTHGsltaGILALEdrLNDLIG-PPEEDETYCSYLPLA 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 238 HCNGWTFTWGTAARG-----GTSVCMRHVTA-PeiYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSPRS----------- 300
Cdd:PTZ00216 321 HIMEFGVTNIFLARGaligfGSPRTLTDTFArP--HGDLTEFRPVFLIGVPRIFDTIKKAVEAKLPPVGslkrrvfdhay 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 301 -----------------------------GPVH-VLTGG---SPPPAALVKKVqrLGfQVMHAYGQTE--ATGPILFC-E 344
Cdd:PTZ00216 399 qsrlralkegkdtpywnekvfsapravlgGRVRaMLSGGgplSAATQEFVNVV--FG-MVIQGWGLTEtvCCGGIQRTgD 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 345 WQDEWNRLPENQQmELKarqgisilgLADVDvKNKETQKSAPRdgktmGEILIKGSSIMKGYLKNPKATFEAF-KHGWLN 423
Cdd:PTZ00216 476 LEPNAVGQLLKGV-EMK---------LLDTE-EYKHTDTPEPR-----GEILLRGPFLFKGYYKQEELTREVLdEDGWFH 539
|
330 340
....*....|....*....|
gi 15218839 424 TGDVGVIHPDGHVEIKDRSK 443
Cdd:PTZ00216 540 TGDVGSIAANGTLRIIGRVK 559
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
193-550 |
7.95e-11 |
|
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: 64.37 E-value: 7.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 193 YTSGTTADPKGVVISHRGAYlcTLSAIIGWEMGTCP---VYLwTLPMFHCNGWTFTWGTAARGGTSVCMRH-VTAPEIYK 268
Cdd:cd05939 111 YTSGTTGLPKAAVIVHSRYY--RIAAGAYYAFGMRPedvVYD-CLPLYHSAGGIMGVGQALLHGSTVVIRKkFSASNFWD 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 269 NIEMHNVTHMCCVPTVFNILLKGNSLDlSPRSGPVHVLTGGSPPPAALVKKVQRLGF-QVMHAYGQTEAT---------- 337
Cdd:cd05939 188 DCVKYNCTIVQYIGEICRYLLAQPPSE-EEQKHNVRLAVGNGLRPQIWEQFVRRFGIpQIGEFYGATEGNsslvnidnhv 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 338 GPILFCewqdewNRLPEN-----------QQMEL-KARQGISILgladvdvknkeTQKSAPrdGKTMGEIlIKGSSIMK- 404
Cdd:cd05939 267 GACGFN------SRILPSvypirlikvdeDTGELiRDSDGLCIP-----------CQPGEP--GLLVGKI-IQNDPLRRf 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 405 -GYLK----NPKATFEAFKHG--WLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAV--VA 475
Cdd:cd05939 327 dGYVNegatNKKIARDVFKKGdsAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVygVE 406
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15218839 476 MPHpTWGETPCAFVVLEKSETTikedrVDKF-QTRERNLIEYCRenlPHFmcprkVVFLEELPKNGNGKILKPKLR 550
Cdd:cd05939 407 VPG-VEGRAGMAAIVDPERKVD-----LDRFsAVLAKSLPPYAR---PQF-----IRLLPEVDKTGTFKLQKTDLQ 468
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
35-549 |
3.10e-10 |
|
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: 62.69 E-value: 3.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 35 YGKTRFTWPQTYDRCCRLAASLIS-LNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPK 113
Cdd:cd05938 1 FEGETYTYRDVDRRSNQAARALLAhAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 114 ILFLDRSFEALARESLHLLSSEdsnlNLPVIFIHENDFPK--RASFEELDYecliQRGEPTPsmvarmfriQDEHDPISL 191
Cdd:cd05938 81 VLVVAPELQEAVEEVLPALRAD----GVSVWYLSHTSNTEgvISLLDKVDA----ASDEPVP---------ASLRAHVTI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 192 N------YTSGTTADPKGVVISHRGAYLCTLsaiIGWEMGTCP---VYLwTLPMFHCNGWTFTW-GTAARGGTSVCMRHV 261
Cdd:cd05938 144 KspalyiYTSGTTGLPKAARISHLRVLQCSG---FLSLCGVTAddvIYI-TLPLYHSSGFLLGIgGCIELGATCVLKPKF 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 262 TAPEIYKNIEMHNVT----------HMCCVP-----TVFNILLK-GNSL------DLSPRSGPVHVLtggspppaalvkk 319
Cdd:cd05938 220 SASQFWDDCRKHNVTviqyigellrYLCNQPqspndRDHKVRLAiGNGLradvwrEFLRRFGPIRIR------------- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 320 vqrlgfqvmHAYGQTEatGPILFcewqdewnrlpenqqMELKARQG----ISILG--LADVDVKNKETQKSAP-RD--GK 390
Cdd:cd05938 287 ---------EFYGSTE--GNIGF---------------FNYTGKIGavgrVSYLYklLFPFELIKFDVEKEEPvRDaqGF 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 391 TM----GE--ILIkgSSIMK-----GYLKNPKAT-----FEAFKHG--WLNTGDVGVIHPDGHVEIKDRSKDIIISGGEN 452
Cdd:cd05938 341 CIpvakGEpgLLV--AKITQqspflGYAGDKEQTekkllRDVFKKGdvYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGEN 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 453 ISSVEVENVLYKYPKVLETAVVAMPHPTW-GETPCAFVVLeKSETTIKEDRvdkfqtrernLIEYCRENLPHFMCPRKVV 531
Cdd:cd05938 419 VATTEVADVLGLLDFLQEVNVYGVTVPGHeGRIGMAAVKL-KPGHEFDGKK----------LYQHVREYLPAYARPRFLR 487
|
570
....*....|....*...
gi 15218839 532 FLEELPKNGNGKILKPKL 549
Cdd:cd05938 488 IQDSLEITGTFKQQKVRL 505
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
191-544 |
3.15e-10 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 63.65 E-value: 3.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 191 LNYTSGTTADPKGVVISHrGAYLCTLSAII---GWEMGTCPVYLWTLpmfHCNGWTFTWGTAARGGTSVCMR---HVTAP 264
Cdd:PRK05691 2338 LIYTSGSTGKPKGVVVSH-GEIAMHCQAVIerfGMRADDCELHFYSI---NFDAASERLLVPLLCGARVVLRaqgQWGAE 2413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 265 EIYKNIEMHNVTHMCCVPTVFNIL---LKGNSLDLSPRSgpvhVLTGGSpppAALVKKVQRL--GFQ---VMHAYGQTEA 336
Cdd:PRK05691 2414 EICQLIREQQVSILGFTPSYGSQLaqwLAGQGEQLPVRM----CITGGE---ALTGEHLQRIrqAFApqlFFNAYGPTET 2486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 337 TGPILFCEWQDewnRLPENQ-QMELKARQGISILGLADVDVknketqksAPRDGKTMGEILIKGSSIMKGYLKNPKATFE 415
Cdd:PRK05691 2487 VVMPLACLAPE---QLEEGAaSVPIGRVVGARVAYILDADL--------ALVPQGATGELYVGGAGLAQGYHDRPGLTAE 2555
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 416 AF-------KHGWL-NTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTwGETPCA 487
Cdd:PRK05691 2556 RFvadpfaaDGGRLyRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLALDTPS-GKQLAG 2634
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 15218839 488 FVVLEKSEttikEDRVDKFQTRERnLIEYCRENLPHFMCPRKVVFLEELPKNGNGKI 544
Cdd:PRK05691 2635 YLVSAVAG----QDDEAQAALREA-LKAHLKQQLPDYMVPAHLILLDSLPLTANGKL 2686
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
164-549 |
3.42e-10 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 62.49 E-value: 3.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 164 CLIQRGEPTPSmvARMFRIQDEHDPISLNY-------TSGTTADPKGVVISHRgaylCTLSAIIG----WEMGTCPVYLW 232
Cdd:cd17654 91 YLLQNKELDNA--PLSFTPEHRHFNIRTDEclayvihTSGTTGTPKIVAVPHK----CILPNIQHfrslFNITSEDILFL 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 233 TLPMFHCNGWTFTWGTAARGGTSVCMRHVTAPEIYK----NIEMHNVTHMCCVPTVFNILLKGNSLD--LSPRSGPVHVL 306
Cdd:cd17654 165 TSPLTFDPSVVEIFLSLSSGATLLIVPTSVKVLPSKladiLFKRHRITVLQATPTLFRRFGSQSIKStvLSATSSLRVLA 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 307 TGGSPPPAALVKKVQR---LGFQVMHAYGQTEAtgpilfCEWQdEWNRLPENQQMElkaRQGISILGLAD--VDVKNKET 381
Cdd:cd17654 245 LGGEPFPSLVILSSWRgkgNRTRIFNIYGITEV------SCWA-LAYKVPEEDSPV---QLGSPLLGTVIevRDQNGSEG 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 382 QksaprdgktmGEILIKGSS---IMKGYLKNPKATFEAfkhgwlnTGDVgVIHPDGHVEIKDRSKDIIISGGENISSVEV 458
Cdd:cd17654 315 T----------GQVFLGGLNrvcILDDEVTVPKGTMRA-------TGDF-VTVKDGELFFLGRKDSQIKRRGKRINLDLI 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 459 ENVLYKYPKVLETAVvamphpTW--GETPCAFVVLEKSETTIKEDRVdkfqtrernlieycRENLPHFMCPRKVVFLEEL 536
Cdd:cd17654 377 QQVIESCLGVESCAV------TLsdQQRLIAFIVGESSSSRIHKELQ--------------LTLLSSHAIPDTFVQIDKL 436
|
410
....*....|...
gi 15218839 537 PKNGNGKILKPKL 549
Cdd:cd17654 437 PLTSHGKVDKSEL 449
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
393-543 |
2.81e-09 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 60.11 E-value: 2.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 393 GEILIKGSSIMKGYLK-------------NPKATFEAfkhGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVE 459
Cdd:PRK08043 554 GRLQLKGPNIMNGYLRvekpgvlevptaeNARGEMER---GWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVE 630
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 460 NVLYKYPKVLETAVVAMPHPTWGEtpcAFVVLekseTTikedrvDKFQTRERnLIEYCREN-LPHFMCPRKVVFLEELPK 538
Cdd:PRK08043 631 QLALGVSPDKQHATAIKSDASKGE---ALVLF----TT------DSELTREK-LQQYAREHgVPELAVPRDIRYLKQLPL 696
|
....*
gi 15218839 539 NGNGK 543
Cdd:PRK08043 697 LGSGK 701
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
173-470 |
7.58e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 58.59 E-value: 7.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 173 PSMVARMF-RIQDEHDPIS-LNYTSGTTADPKGVVISHRGAYLCTLSAI--IGWEMGTCPVYlWtLPMFHCNGWTFTWGT 248
Cdd:PRK07769 165 PDEVGATWvPPEANEDTIAyLQYTSGSTRIPAGVQITHLNLPTNVLQVIdaLEGQEGDRGVS-W-LPFFHDMGLITVLLP 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 249 AARGGTSVCMR---HVTAPeiYKNI-EMHNVTHMccVPTVFNIL---------LKG------NSLDLSPRSGpvhVLTGG 309
Cdd:PRK07769 243 ALLGHYITFMSpaaFVRRP--GRWIrELARKPGG--TGGTFSAApnfafehaaARGlpkdgePPLDLSNVKG---LLNGS 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 310 SPPPAALVKKVQR----LGFQ---VMHAYGQTEATgpiLFCE---WQDEwNRLPENQQMELKARQGISIlglaDVDVKNK 379
Cdd:PRK07769 316 EPVSPASMRKFNEafapYGLPptaIKPSYGMAEAT---LFVSttpMDEE-PTVIYVDRDELNAGRFVEV----PADAPNA 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 380 ETQKSAPR----------DGKT--------MGEILIKGSSIMKGYLKNPKATFEAFK----------HG--------WLN 423
Cdd:PRK07769 388 VAQVSAGKvgvsewavivDPETaselpdgqIGEIWLHGNNIGTGYWGKPEETAATFQnilksrlsesHAegapddalWVR 467
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 15218839 424 TGDVGVIHpDGHVEIKDRSKDIIISGGENissvevenvlyKYPKVLE 470
Cdd:PRK07769 468 TGDYGVYF-DGELYITGRVKDLVIIDGRN-----------HYPQDLE 502
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
392-549 |
8.28e-09 |
|
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.
Pssm-ID: 274582 [Multi-domain] Cd Length: 1389 Bit Score: 58.92 E-value: 8.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 392 MGEILIKGSSIMKGYLKNPKATFEAFKHGWL-----------------------------NTGDVGVIHPDGHVEIKDRS 442
Cdd:TIGR03443 621 VGEIYVRAGGLAEGYLGLPELNAEKFVNNWFvdpshwidldkennkperefwlgprdrlyRTGDLGRYLPDGNVECCGRA 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 443 KDIIISGGENISSVEVENVLYKYPKVLE-------------TAVVAM-PHPTWGEtpcafvvLEK----SETTIKEDRVD 504
Cdd:TIGR03443 701 DDQVKIRGFRIELGEIDTHLSQHPLVREnvtlvrrdkdeepTLVSYIvPQDKSDE-------LEEfkseVDDEESSDPVV 773
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15218839 505 KFQTRERNLI----EYCRENLPHFMCPRKVVFLEELPKNGNGKILKPKL 549
Cdd:TIGR03443 774 KGLIKYRKLIkdirEYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKPAL 822
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
392-544 |
1.36e-08 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 58.26 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 392 MGEILIKGSSIMKGYLKNPKATFEAF-KHG---WLNTGDVGVIHpDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPK 467
Cdd:PRK05691 397 VGEIWASGPSIAHGYWRNPEASAKTFvEHDgrtWLRTGDLGFLR-DGELFVTGRLKDMLIVRGHNLYPQDIEKTVEREVE 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 468 VLETAVVAmphptwgetpcAFVVLEKSETTIK-----EDRVDKFQTRE------RNLI-EYCREnlphfmCPRKVVFLE- 534
Cdd:PRK05691 476 VVRKGRVA-----------AFAVNHQGEEGIGiaaeiSRSVQKILPPQaliksiRQAVaEACQE------APSVVLLLNp 538
|
170
....*....|.
gi 15218839 535 -ELPKNGNGKI 544
Cdd:PRK05691 539 gALPKTSSGKL 549
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
392-549 |
2.38e-08 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 56.76 E-value: 2.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 392 MGEILIKGSSIMKGYLKNPKATFEAFKHGWL-----------------------------NTGDVGVIHPDGHVEIKDRS 442
Cdd:cd17647 315 VGEIYVRAGGLAEGYRGLPELNKEKFVNNWFvepdhwnyldkdnnepwrqfwlgprdrlyRTGDLGRYLPNGDCECCGRA 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 443 KDIIISGGENISSVEVENVLYKYPKVLETavVAMPHPTWGETPC--AFVV--LEKSETT----------IKEDRVDKFQT 508
Cdd:cd17647 395 DDQVKIRGFRIELGEIDTHISQHPLVREN--ITLVRRDKDEEPTlvSYIVprFDKPDDEsfaqedvpkeVSTDPIVKGLI 472
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15218839 509 RERNLI----EYCRENLPHFMCPRKVVFLEELPKNGNGKILKPKL 549
Cdd:cd17647 473 GYRKLIkdirEFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKL 517
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
37-560 |
3.15e-08 |
|
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.
Pssm-ID: 341265 [Multi-domain] Cd Length: 629 Bit Score: 56.51 E-value: 3.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 37 KTRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILF 116
Cdd:cd05943 96 RTEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFGVPGVLDRFGQIEPKVLF 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 117 LDRSFEALARESLHLlssedSNLN-----LP----VIFIH------ENDFPKRASFeeLDYECLIQRGEPTPSMVARM-F 180
Cdd:cd05943 176 AVDAYTYNGKRHDVR-----EKVAelvkgLPsllaVVVVPytvaagQPDLSKIAKA--LTLEDFLATGAAGELEFEPLpF 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 181 riqdEHdPISLNYTSGTTADPKGVVISHRGAYLCTLSA-IIGWEMGTCPVYLWtlpmFHCNGWTFtWGTAARG---GTSV 256
Cdd:cd05943 249 ----DH-PLYILYSSGTTGLPKCIVHGAGGTLLQHLKEhILHCDLRPGDRLFY----YTTCGWMM-WNWLVSGlavGATI 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 257 CMR-----HVTAPEIYKNIEMHNVTHMCCVPTVFNILLK-----GNSLDLSP-RsgpvHVLTGGSPPPA---ALVKKVQR 322
Cdd:cd05943 319 VLYdgspfYPDTNALWDLADEEGITVFGTSAKYLDALEKaglkpAETHDLSSlR----TILSTGSPLKPesfDYVYDHIK 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 323 LGFQVMHAYGQTEATGPILFCewqdewNRLPENQQMELKARqgisILGLAdvdvknketQKSAPRDGKT----MGEILIK 398
Cdd:cd05943 395 PDVLLASISGGTDIISCFVGG------NPLLPVYRGEIQCR----GLGMA---------VEAFDEEGKPvwgeKGELVCT 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 399 GS--SIMKGYLKNP------KATFEAFKHGWLNtGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLE 470
Cdd:cd05943 456 KPfpSMPVGFWNDPdgsryrAAYFAKYPGVWAH-GDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVED 534
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 471 TAVVAMPHPTWGETPCAFVVLeKSETTIKEDRVDKFQTRernlieyCRENL-PHFMcPRKVVFLEELPKNGNGKILKPKL 549
Cdd:cd05943 535 SLVVGQEWKDGDERVILFVKL-REGVELDDELRKRIRST-------IRSALsPRHV-PAKIIAVPDIPRTLSGKKVEVAV 605
|
570
....*....|.
gi 15218839 550 RDIAKGLVVED 560
Cdd:cd05943 606 KKIIAGRPVKN 616
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
39-426 |
6.71e-08 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 55.27 E-value: 6.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 39 RFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTP-----ALYEMHFAVPMAgaVLNPINTRL--DATSIAAILRHAK 111
Cdd:PRK08180 69 RLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIehallALAAMYAGVPYA--PVSPAYSLVsqDFGKLRHVLELLT 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 112 PKILFLDRSfEALAReSLHLLSSEDsnlnLPVIfIHENDFPKRA--SFEELdyecliQRGEPTPSMVARMFRIqDEHDPI 189
Cdd:PRK08180 147 PGLVFADDG-AAFAR-ALAAVVPAD----VEVV-AVRGAVPGRAatPFAAL------LATPPTAAVDAAHAAV-GPDTIA 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 190 SLNYTSGTTADPKGVVISHRgaYLCTLSAIIG--W-EMGTC-PVYL-WtLP---MF---HCNGWTFTWG----------T 248
Cdd:PRK08180 213 KFLFTSGSTGLPKAVINTHR--MLCANQQMLAqtFpFLAEEpPVLVdW-LPwnhTFggnHNLGIVLYNGgtlyiddgkpT 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 249 AARGGTSV-CMRHVtAPEIYKNiemhnvthmccVPTVFNILLKGNSLDLSPRS---GPVHVLT-GGSPPPAALVKKVQRL 323
Cdd:PRK08180 290 PGGFDETLrNLREI-SPTVYFN-----------VPKGWEMLVPALERDAALRRrffSRLKLLFyAGAALSQDVWDRLDRV 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 324 GFQV-------MHAYGQTEATGPILFCEWQDEwnrlpenqqmelkaRQGISILGLADVDVknketqKSAPRDGKTmgEIL 396
Cdd:PRK08180 358 AEATcgerirmMTGLGMTETAPSATFTTGPLS--------------RAGNIGLPAPGCEV------KLVPVGGKL--EVR 415
|
410 420 430
....*....|....*....|....*....|.
gi 15218839 397 IKGSSIMKGYLKNPKATFEAF-KHGWLNTGD 426
Cdd:PRK08180 416 VKGPNVTPGYWRAPELTAEAFdEEGYYRSGD 446
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
393-544 |
2.15e-06 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 50.94 E-value: 2.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 393 GEILIKGSSIMKGYLKNPKATFEAF---KHG-----WLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYK 464
Cdd:PRK05691 4067 GELCVAGTGVGRGYVGDPLRTALAFvphPFGapgerLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHE 4146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 465 YPKVLETAVVAMPHPTwGETPCAFVVLEKSETTiKEDRVDKFQTRernlieyCRENLPHFMCPRKVVFLEELPKNGNGKI 544
Cdd:PRK05691 4147 QAEVREAAVAVQEGVN-GKHLVGYLVPHQTVLA-QGALLERIKQR-------LRAELPDYMVPLHWLWLDRLPLNANGKL 4217
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
38-426 |
5.51e-06 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 49.35 E-value: 5.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 38 TRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPIN-----TRLDATSIAAILRHAKP 112
Cdd:cd05921 24 RRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSpayslMSQDLAKLKHLFELLKP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 113 KILFLDrSFEALARESLHLLSsedsnLNLPVIFIHeNDFPKRA--SFEEL-DYECLIQ----RGEPTPSMVARMFriqde 185
Cdd:cd05921 104 GLVFAQ-DAAPFARALAAIFP-----LGTPLVVSR-NAVAGRGaiSFAELaATPPTAAvdaaFAAVGPDTVAKFL----- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 186 hdpislnYTSGTTADPKGVVISHRgaYLCTLSAII----GWEMGTCPVYLWTLPmfhcngWTFTWGTAA-------RGGT 254
Cdd:cd05921 172 -------FTSGSTGLPKAVINTQR--MLCANQAMLeqtyPFFGEEPPVLVDWLP------WNHTFGGNHnfnlvlyNGGT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 255 SVCMRHVTAP----EIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSPRS---GPVHVLT-GGSPPPAALVKKVQRLGFQ 326
Cdd:cd05921 237 LYIDDGKPMPggfeETLRNLREISPTVYFNVPAGWEMLVAALEKDEALRRrffKRLKLMFyAGAGLSQDVWDRLQALAVA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 327 -------VMHAYGQTEATGPILFCEWqdewnrlpenqqmeLKARQGISILGLADVDVKnketqkSAPRDGKTmgEILIKG 399
Cdd:cd05921 317 tvgeripMMAGLGATETAPTATFTHW--------------PTERSGLIGLPAPGTELK------LVPSGGKY--EVRVKG 374
|
410 420
....*....|....*....|....*...
gi 15218839 400 SSIMKGYLKNPKATFEAF-KHGWLNTGD 426
Cdd:cd05921 375 PNVTPGYWRQPELTAQAFdEEGFYCLGD 402
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
391-452 |
2.00e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 47.63 E-value: 2.00e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15218839 391 TMGEILIKGSSIMKGYLKNPKATFEAFkHG-------------WLNTGDVGVIHpDGHVEIKDRSKDIIISGGEN 452
Cdd:PRK05850 396 TVGEIWVHGDNVAAGYWQKPEETERTF-GAtlvdpspgtpegpWLRTGDLGFIS-EGELFIVGRIKDLLIVDGRN 468
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
172-449 |
2.76e-05 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 46.96 E-value: 2.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 172 TPSMVARMFriqdehdpislnYTSGTTADPKGVVISHRgaylcTLSAIIGWEMGT--------CPVYLWTLPMFHCNGWT 243
Cdd:PRK12582 218 TPDTVAKYL------------FTSGSTGMPKAVINTQR-----MMCANIAMQEQLrprepdppPPVSLDWMPWNHTMGGN 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 244 FTWGTAARGGTSVcmrHVTA----PEIY----KNIEMHNVTHMCCVPTVFNILLKGNSLDLSPRSGPVHVLT----GGSP 311
Cdd:PRK12582 281 ANFNGLLWGGGTL---YIDDgkplPGMFeetiRNLREISPTVYGNVPAGYAMLAEAMEKDDALRRSFFKNLRlmayGGAT 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 312 PPAALVKKVQRL-----GFQV--MHAYGQTEATGPILFCEWQDEwnrlpenqqmelkaRQGISILGLADVDVKnketqkS 384
Cdd:PRK12582 358 LSDDLYERMQALavrttGHRIpfYTGYGATETAPTTTGTHWDTE--------------RVGLIGLPLPGVELK------L 417
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15218839 385 APrDGKTMgEILIKGSSIMKGYLKNPKATFEAF-KHGWLNTGDVGV-IHPDghveikDRSKDIIISG 449
Cdd:PRK12582 418 AP-VGDKY-EVRVKGPNVTPGYHKDPELTAAAFdEEGFYRLGDAARfVDPD------DPEKGLIFDG 476
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
70-554 |
3.44e-05 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 46.73 E-value: 3.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 70 MAPNTPALYemhFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFLD----RSFEALARESLHLLSSEDSNLNLPVIf 145
Cdd:PLN03051 3 MTVDAVIIY---LAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFTQdvvlRGGRALPLYSKVVEAAPAKAIVLPAA- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 146 ihENDFPKRASFEELDYECLIQRGEPTPSMVARMFR--IQDEHDPISLNYTSGTTADPKGVVISHRGAYLCTLSAI---- 219
Cdd:PLN03051 79 --GEPVAVPLREQDLSWCDFLGVAAAQGSVGGNEYSpvYAPVESVTNILFSSGTTGEPKAIPWTHLSPLRCASDGWahmd 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 220 ------------IGWEMGTcpvylWTLPMFHCNGWTFtwgtAARGGTSvcmrhvTAPEIYKNIEMHNVTHMCCVPTVFNI 287
Cdd:PLN03051 157 iqpgdvvcwptnLGWMMGP-----WLLYSAFLNGATL----ALYGGAP------LGRGFGKFVQDAGVTVLGLVPSIVKA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 288 LLKGNS-----LDLSprsgpvHVLTGGSPPPAALVKKVqrLGFQVMHAY--------GQTE-ATGPILFCEWQdewnrlP 353
Cdd:PLN03051 222 WRHTGAfamegLDWS------KLRVFASTGEASAVDDV--LWLSSVRGYykpvieycGGTElASGYISSTLLQ------P 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 354 ENQQMELKARQGISILGLADVDVknketqkSAPRDGKTMGEI----LIKGSSIMKGYLKNPKATFEAFKHGWLNT----- 424
Cdd:PLN03051 288 QAPGAFSTASLGTRFVLLNDNGV-------PYPDDQPCVGEValapPMLGASDRLLNADHDKVYYKGMPMYGSKGmplrr 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 425 -GDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPK-VLETAVVAMPHPTWG-ETPCAFVVLEKSETTIKED 501
Cdd:PLN03051 361 hGDIMKRTPGGYFCVQGRADDTMNLGGIKTSSVEIERACDRAVAgIAETAAVGVAPPDGGpELLVIFLVLGEEKKGFDQA 440
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 15218839 502 RVDKFQTRERNLIeycRENL-PHFMCPRkVVFLEELPKNGNGKILKPKLRDIAK 554
Cdd:PLN03051 441 RPEALQKKFQEAI---QTNLnPLFKVSR-VKIVPELPRNASNKLLRRVLRDQLK 490
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
28-213 |
7.01e-05 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 45.94 E-value: 7.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 28 PNRTSIIY-----GKTRFTWPQTYDRCCRLAASLISLNISKNDVVSVMAPNTPalyemHFAVPMagavlnpintrLDATS 102
Cdd:PRK03584 98 DDRPAIIFrgedgPRRELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIP-----ETVVAM-----------LATAS 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 103 IAAI----------------LRHAKPKILF-----------LDRSfEALARESLHLLSSED----SNLNLPvifiHENDF 151
Cdd:PRK03584 162 LGAIwsscspdfgvqgvldrFGQIEPKVLIavdgyryggkaFDRR-AKVAELRAALPSLEHvvvvPYLGPA----AAAAA 236
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15218839 152 PKRAsfeeLDYECLIQRGEPTPSMVARM-FriqdEHdPISLNYTSGTTADPKGVVISHRGAYL 213
Cdd:PRK03584 237 LPGA----LLWEDFLAPAEAAELEFEPVpF----DH-PLWILYSSGTTGLPKCIVHGHGGILL 290
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
425-551 |
1.63e-04 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 44.68 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 425 GDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYK-YPKVLETAVVAMPHPTWG-ETPCAFVVL--EKSETTIKE 500
Cdd:PLN03052 594 GDIFERTSGGYYRAHGRADDTMNLGGIKVSSVEIERVCNAaDESVLETAAIGVPPPGGGpEQLVIAAVLkdPPGSNPDLN 673
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 15218839 501 DRVDKFQTR-ERNLieycreNlPHFMCpRKVVFLEELPKNGNGKILKPKLRD 551
Cdd:PLN03052 674 ELKKIFNSAiQKKL------N-PLFKV-SAVVIVPSFPRTASNKVMRRVLRQ 717
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
41-473 |
2.16e-04 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 44.35 E-value: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 41 TWPQTYDRCCRLAASLISLnISKNDVVSVMAPNTPALYEMHFAVPMAGAVLNPI--------NTRLDAtsiaaILRHAKP 112
Cdd:PRK12476 70 TWTQLGVRLRAVGARLQQV-AGPGDRVAILAPQGIDYVAGFFAAIKAGTIAVPLfapelpghAERLDT-----ALRDAEP 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 113 KILFLDrsfeALARESLHLLSSEDSNLNLP-VIFIHEndfpkrasfeeldyecliqrgepTPSMVARMF-RIQDEHDPIS 190
Cdd:PRK12476 144 TVVLTT----TAAAEAVEGFLRNLPRLRRPrVIAIDA-----------------------IPDSAGESFvPVELDTDDVS 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 191 -LNYTSGTTADPKGVVISHRGAYLCTLSAIIG---WEMGTCPVYlWtLPMFHCNGWTFTWGTAARGGTSVCM-------- 258
Cdd:PRK12476 197 hLQYTSGSTRPPVGVEITHRAVGTNLVQMILSidlLDRNTHGVS-W-LPLYHDMGLSMIGFPAVYGGHSTLMsptafvrr 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 259 ---------------RHVTAPEIYKniemHNVTHMCCVPTvfnillKGNSLDLSPRsgpvhVLTGGSPP----------- 312
Cdd:PRK12476 275 pqrwikalsegsrtgRVVTAAPNFA----YEWAAQRGLPA------EGDDIDLSNV-----VLIIGSEPvsidavttfnk 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 313 -------PAALVKKvqrlgfqvmhAYGQTEATgpiLFCEwqdewNRLPENQ-------QMELKARQGISILGLADVDVKN 378
Cdd:PRK12476 340 afapyglPRTAFKP----------SYGIAEAT---LFVA-----TIAPDAEpsvvyldREQLGAGRAVRVAADAPNAVAH 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218839 379 KETQKSAP---------------RDGkTMGEILIKGSSIMKGYLKNPKATFEAFK-----------HG--------WLNT 424
Cdd:PRK12476 402 VSCGQVARsqwavivdpdtgaelPDG-EVGEIWLHGDNIGRGYWGRPEETERTFGaklqsrlaegsHAdgaaddgtWLRT 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 15218839 425 GDVGViHPDGHVEIKDRSKDIIISGGENissvevenvlyKYPKVLETAV 473
Cdd:PRK12476 481 GDLGV-YLDGELYITGRIADLIVIDGRN-----------HYPQDIEATV 517
|
|
| |
