|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
1-578 |
0e+00 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 1274.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 1 MDNLALCEANNVPLTPITFLKRASECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEM 80
Cdd:PLN03102 1 MDNLALCEANNVPLTPITFLKRASECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 81 HFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFIYRSFEPLAREILQLLSSEDSNLNLPVIFIHEIDFPKRVSSEES 160
Cdd:PLN03102 81 HFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFVDRSFEPLAREVLHLLSSEDSNLNLPVIFIHEIDFPKRPSSEEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 161 DYECLIQRGEPTPLLLARMFCIQDEHDPISLNYTSGTTADPKGVVISHRGAYLSTLSAIIGWEMGTCPVYLWTLPMFHCN 240
Cdd:PLN03102 161 DYECLIQRGEPTPSLVARMFRIQDEHDPISLNYTSGTTADPKGVVISHRGAYLSTLSAIIGWEMGTCPVYLWTLPMFHCN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 241 GWTFTWGTAARGGTSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSHRSGPVHVLTGGSPPPAALVKKV 320
Cdd:PLN03102 241 GWTFTWGTAARGGTSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSPRSGPVHVLTGGSPPPAALVKKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 321 QRLGFQVMHAYGLTEATGPVLFCEWQDEWNRLPENQQMELKARQGLSILGLTEVDVRNKETQESVPRDGKTMGEIVMKGS 400
Cdd:PLN03102 321 QRLGFQVMHAYGLTEATGPVLFCEWQDEWNRLPENQQMELKARQGVSILGLADVDVKNKETQESVPRDGKTMGEIVIKGS 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 401 SIMKGYLKNPKATYEAFKHGWLNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPT 480
Cdd:PLN03102 401 SIMKGYLKNPKATSEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPT 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 481 WGETPCAFVVLEKGETNNEDREDKLVTKERDLIEYCRENLPHFMCPRKVVFLDELPKNGNGKILKPKLRDIAKGLVAEDE 560
Cdd:PLN03102 481 WGETPCAFVVLEKGETTKEDRVDKLVTRERDLIEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKLRDIAKGLVVEDE 560
|
570
....*....|....*....
gi 15218840 561 VNVRSKV-QRPVEHFTSRL 578
Cdd:PLN03102 561 DNVIKKVhQRPVEHFSSRL 579
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
11-550 |
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: 864.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 11 NVPLTPITFLKRASECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAV 90
Cdd:cd12118 1 YVPLTPLSFLERAAAVYPDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 91 LNPINTRLDATSIAAILRHAKPKILFIYRSFEplareilqllssedsnlnlpvifiheidfpkrvsseesdYECLIQRGE 170
Cdd:cd12118 81 LNALNTRLDAEEIAFILRHSEAKVLFVDREFE---------------------------------------YEDLLAEGD 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 171 PTPLLLarmfCIQDEHDPISLNYTSGTTADPKGVVISHRGAYLSTLSAIIGWEMGTCPVYLWTLPMFHCNGWTFTWGTAA 250
Cdd:cd12118 122 PDFEWI----PPADEWDPIALNYTSGTTGRPKGVVYHHRGAYLNALANILEWEMKQHPVYLWTLPMFHCNGWCFPWTVAA 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 251 RGGTSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSHRSGPVHVLTGGSPPPAALVKKVQRLGFQVMHA 330
Cdd:cd12118 198 VGGTNVCLRKVDAKAIYDLIEKHKVTHFCGAPTVLNMLANAPPSDARPLPHRVHVMTAGAPPPAAVLAKMEELGFDVTHV 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 331 YGLTEATGPVLFCEWQDEWNRLPENQQMELKARQGLSILGLTEVDVRNKETQESVPRDGKTMGEIVMKGSSIMKGYLKNP 410
Cdd:cd12118 278 YGLTETYGPATVCAWKPEWDELPTEERARLKARQGVRYVGLEEVDVLDPETMKPVPRDGKTIGEIVFRGNIVMKGYLKNP 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 411 KATYEAFKHGWLNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPTWGETPCAFVV 490
Cdd:cd12118 358 EATAEAFRGGWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVE 437
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 491 LEKGETnnedredklvTKERDLIEYCRENLPHFMCPRKVVFlDELPKNGNGKILKPKLRD 550
Cdd:cd12118 438 LKEGAK----------VTEEEIIAFCREHLAGFMVPKTVVF-GELPKTSTGKIQKFVLRD 486
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
2-560 |
0e+00 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 742.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 2 DNLALCEANNVPLTPITFLKRASECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMH 81
Cdd:PRK08162 6 QGLDRNAANYVPLTPLSFLERAAEVYPDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 82 FAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFIYRSFEPLAREILQLLSsedsNLNLPVIFIHEIDFPKRVSSEESD 161
Cdd:PRK08162 86 FGVPMAGAVLNTLNTRLDAASIAFMLRHGEAKVLIVDTEFAEVAREALALLP----GPKPLVIDVDDPEYPGGRFIGALD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 162 YECLIQRGEPT-----PlllarmfciQDEHDPISLNYTSGTTADPKGVVISHRGAYLSTLSAIIGWEMGTCPVYLWTLPM 236
Cdd:PRK08162 162 YEAFLASGDPDfawtlP---------ADEWDAIALNYTSGTTGNPKGVVYHHRGAYLNALSNILAWGMPKHPVYLWTLPM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 237 FHCNGWTFTWGTAARGGTSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSHRSGPVHVLTGGSPPPAAL 316
Cdd:PRK08162 233 FHCNGWCFPWTVAARAGTNVCLRKVDPKLIFDLIREHGVTHYCGAPIVLSALINAPAEWRAGIDHPVHAMVAGAAPPAAV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 317 VKKVQRLGFQVMHAYGLTEATGPVLFCEWQDEWNRLPENQQMELKARQGLSILGLTEVDVRNKETQESVPRDGKTMGEIV 396
Cdd:PRK08162 313 IAKMEEIGFDLTHVYGLTETYGPATVCAWQPEWDALPLDERAQLKARQGVRYPLQEGVTVLDPDTMQPVPADGETIGEIM 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 397 MKGSSIMKGYLKNPKATYEAFKHGWLNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAM 476
Cdd:PRK08162 393 FRGNIVMKGYLKNPKATEEAFAGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAK 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 477 PHPTWGETPCAFVVLEKGETNNEDredklvtkerDLIEYCRENLPHFMCPRKVVFlDELPKNGNGKILKPKLRDIAKGLV 556
Cdd:PRK08162 473 PDPKWGEVPCAFVELKDGASATEE----------EIIAHCREHLAGFKVPKAVVF-GELPKTSTGKIQKFVLREQAKSLK 541
|
....
gi 15218840 557 AEDE 560
Cdd:PRK08162 542 AIDL 545
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
1-555 |
0e+00 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 626.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 1 MDNLALCEANNVPLTPITFLKRASECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEM 80
Cdd:PLN02479 7 IDDLPKNAANYTALTPLWFLERAAVVHPTRKSVVHGSVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 81 HFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFIYRSFEPLAREILQLLSSED-SNLNLPVIFIHEIDFPKRVSSEE 159
Cdd:PLN02479 87 HFGVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEVVMVDQEFFTLAEEALKILAEKKkSSFKPPLLIVIGDPTCDPKSLQY 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 160 S------DYECLIQRGEPT-----PlllarmfciQDEHDPISLNYTSGTTADPKGVVISHRGAYLSTLSAIIGWEMGTCP 228
Cdd:PLN02479 167 AlgkgaiEYEKFLETGDPEfawkpP---------ADEWQSIALGYTSGTTASPKGVVLHHRGAYLMALSNALIWGMNEGA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 229 VYLWTLPMFHCNGWTFTWGTAARGGTSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKG----NSLDLSHrsgPVH 304
Cdd:PLN02479 238 VYLWTLPMFHCNGWCFTWTLAALCGTNICLRQVTAKAIYSAIANYGVTHFCAAPVVLNTIVNApkseTILPLPR---VVH 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 305 VLTGGSPPPAALVKKVQRLGFQVMHAYGLTEATGPVLFCEWQDEWNRLPENQQMELKARQGLSILGLTEVDVRNKETQES 384
Cdd:PLN02479 315 VMTAGAAPPPSVLFAMSEKGFRVTHTYGLSETYGPSTVCAWKPEWDSLPPEEQARLNARQGVRYIGLEGLDVVDTKTMKP 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 385 VPRDGKTMGEIVMKGSSIMKGYLKNPKATYEAFKHGWLNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYK 464
Cdd:PLN02479 395 VPADGKTMGEIVMRGNMVMKGYLKNPKANEEAFANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYT 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 465 YPKVLETAVVAMPHPTWGETPCAFVVLEKGetnnEDREDKLVTkERDLIEYCRENLPHFMCPRKVVFlDELPKNGNGKIL 544
Cdd:PLN02479 475 HPAVLEASVVARPDERWGESPCAFVTLKPG----VDKSDEAAL-AEDIMKFCRERLPAYWVPKSVVF-GPLPKTATGKIQ 548
|
570
....*....|.
gi 15218840 545 KPKLRDIAKGL 555
Cdd:PLN02479 549 KHVLRAKAKEM 559
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
19-558 |
4.35e-157 |
|
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: 456.96 E-value: 4.35e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 19 FLKRASECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRL 98
Cdd:COG0318 4 LLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 99 DATSIAAILRHAKPKILFIyrsfeplareilqllssedsnlnlpvifiheidfpkrvsseesdyeCLIQrgeptplllar 178
Cdd:COG0318 84 TAEELAYILEDSGARALVT----------------------------------------------ALIL----------- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 179 mfciqdehdpislnYTSGTTADPKGVVISHRGAYLSTLSAIIGWEMGTCPVYLWTLPMFHCNGWTFTWGTA-ARGGTSVC 257
Cdd:COG0318 107 --------------YTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPlLAGATLVL 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 258 MRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLK---GNSLDLSH-RsgpvHVLTGGSPPPAALVKKVQ-RLGFQVMHAYG 332
Cdd:COG0318 173 LPRFDPERVLELIERERVTVLFGVPTMLARLLRhpeFARYDLSSlR----LVVSGGAPLPPELLERFEeRFGVRIVEGYG 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 333 LTEaTGPVLFCEWQDEWNRLPenqqmelkARQGLSILGlTEVDVRNKETQEsVPRDgkTMGEIVMKGSSIMKGYLKNPKA 412
Cdd:COG0318 249 LTE-TSPVVTVNPEDPGERRP--------GSVGRPLPG-VEVRIVDEDGRE-LPPG--EVGEIVVRGPNVMKGYWNDPEA 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 413 TYEAFKHGWLNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPTWGETPCAFVVLE 492
Cdd:COG0318 316 TAEAFRDGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLR 395
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15218840 493 KGETNNEDredklvtkerDLIEYCRENLPHFMCPRKVVFLDELPKNGNGKILKPKLRDIAKGLVAE 558
Cdd:COG0318 396 PGAELDAE----------ELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRERYAAGALE 451
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
9-550 |
3.81e-153 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 449.64 E-value: 3.81e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 9 ANNVPLTPITFLKRASECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAG 88
Cdd:PRK06187 1 MQDYPLTIGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 89 AVLNPINTRLDATSIAAILRHAKPKILFIYRSFEPLAREILQLLSSEDSnlnlpVIFIHEIDfPKRVSSEESDYECLIQR 168
Cdd:PRK06187 81 AVLHPINIRLKPEEIAYILNDAEDRVVLVDSEFVPLLAAILPQLPTVRT-----VIVEGDGP-AAPLAPEVGEYEELLAA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 169 GEPTPLllarmFCIQDEHDPISLNYTSGTTADPKGVVISHRGAYLSTLSAIIGWEMGTCPVYLWTLPMFHCNGWTftWGT 248
Cdd:PRK06187 155 ASDTFD-----FPDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPMFHVHAWG--LPY 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 249 AA--RGGTSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLK---GNSLDLSHRSgpvHVLTGGSPPPAALVKK-VQR 322
Cdd:PRK06187 228 LAlmAGAKQVIPRRFDPENLLDLIETERVTFFFAVPTIWQMLLKaprAYFVDFSSLR---LVIYGGAALPPALLREfKEK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 323 LGFQVMHAYGLTEaTGPVLFCewqdewNRLPENQQMELKAR--QGLSILGLtEVDVRNKETQEsVPRDGKTMGEIVMKGS 400
Cdd:PRK06187 305 FGIDLVQGYGMTE-TSPVVSV------LPPEDQLPGQWTKRrsAGRPLPGV-EARIVDDDGDE-LPPDGGEVGEIIVRGP 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 401 SIMKGYLKNPKATYEAFKHGWLNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPT 480
Cdd:PRK06187 376 WLMQGYWNRPEATAETIDGGWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEK 455
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 481 WGETPCAFVVLEKGETnnedredklvTKERDLIEYCRENLPHFMCPRKVVFLDELPKNGNGKILKPKLRD 550
Cdd:PRK06187 456 WGERPVAVVVLKPGAT----------LDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLRE 515
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
19-550 |
8.00e-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. 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: 412.79 E-value: 8.00e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 19 FLKRASECYPNRTsIIY-----GKTRFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNP 93
Cdd:cd12119 1 LLEHAARLHGDRE-IVSrthegEVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 94 INTRLDATSIAAILRHAKPKILFIYRSFEPLAREILQllssedsnlNLPVIfIHEIDFPKRVSSEES------DYECLIQ 167
Cdd:cd12119 80 INPRLFPEQIAYIINHAEDRVVFVDRDFLPLLEAIAP---------RLPTV-EHVVVMTDDAAMPEPagvgvlAYEELLA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 168 RGEPTplllaRMFCIQDEHDPISLNYTSGTTADPKGVVISHRGAYLSTLSAIIGWEMGTCP--VYLWTLPMFHCNGWTFT 245
Cdd:cd12119 150 AESPE-----YDWPDFDENTAAAICYTSGTTGNPKGVVYSHRSLVLHAMAALLTDGLGLSEsdVVLPVVPMFHVNAWGLP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 246 WgTAARGGTSVCM--RHVTAPEIYKNIEMHNVTHMCCVPTVFNILL---KGNSLDLSHRsgpVHVLTGGSPPPAALVKKV 320
Cdd:cd12119 225 Y-AAAMVGAKLVLpgPYLDPASLAELIEREGVTFAAGVPTVWQGLLdhlEANGRDLSSL---RRVVIGGSAVPRSLIEAF 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 321 QRLGFQVMHAYGLTEaTGPVLFCEW-QDEWNRLPENQQMELKARQGLSILGLtEVDVRNKETQEsVPRDGKTMGEIVMKG 399
Cdd:cd12119 301 EERGVRVIHAWGMTE-TSPLGTVARpPSEHSNLSEDEQLALRAKQGRPVPGV-ELRIVDDDGRE-LPWDGKAVGELQVRG 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 400 SSIMKGYLKNPKATYEAFKHGWLNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHP 479
Cdd:cd12119 378 PWVTKSYYKNDEESEALTEDGWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHP 457
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15218840 480 TWGETPCAFVVLEKGETnnedredklVTKErDLIEYCRENLPHFMCPRKVVFLDELPKNGNGKILKPKLRD 550
Cdd:cd12119 458 KWGERPLAVVVLKEGAT---------VTAE-ELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
13-549 |
1.44e-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. 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: 406.82 E-value: 1.44e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 13 PLTPITFLKRASECYPNRTsiiYGKTRFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLN 92
Cdd:cd05915 1 LERAAALFGRKEVVSRLHT---GEVHRTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 93 PINTRLDATSIAAILRHAKPKILFIYRSFEPLAREILQLLSSEDSNlnlpvifiheidfPKRVSSEESdYECLIQRGEPT 172
Cdd:cd05915 78 TANPRLSPKEIAYILNHAEDKVLLFDPNLLPLVEAIRGELKTVQHF-------------VVMDEKAPE-GYLAYEEALGE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 173 --PLLLArmfciqDEHDPISLNYTSGTTADPKGVVISHRGAYLSTLSAIIGWEMGT--CPVYLWTLPMFHCNGWTFTWGT 248
Cdd:cd05915 144 eaDPVRV------PERAACGMAYTTGTTGLPKGVVYSHRALVLHSLAASLVDGTALseKDVVLPVVPMFHVNAWCLPYAA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 249 AARGGTSVCMRHVTAPE-IYKNIEMHNVTHMCCVPTVFNILlkGNSLDLSHRSGP--VHVLTGGSPPPAALVkKVQRLG- 324
Cdd:cd05915 218 TLVGAKQVLPGPRLDPAsLVELFDGEGVTFTAGVPTVWLAL--ADYLESTGHRLKtlRRLVVGGSAAPRSLI-ARFERMg 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 325 FQVMHAYGLTEATGPVLFCEWQDEWNRLPENQQMELKARQGLSILGlTEVDVRNKETQeSVPRDGKTMGEIVMKGSSIMK 404
Cdd:cd05915 295 VEVRQGYGLTETSPVVVQNFVKSHLESLSEEEKLTLKAKTGLPIPL-VRLRVADEEGR-PVPKDGKALGEVQLKGPWITG 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 405 GYLKNPKAT-YEAFKHGWLNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPTWGE 483
Cdd:cd05915 373 GYYGNEEATrSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQE 452
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15218840 484 TPCAFVVLEKGEtnnedredklvTKERDLIEYCRENLPHF-MCPRKVVFLDELPKNGNGKILKPKLR 549
Cdd:cd05915 453 RPLAVVVPRGEK-----------PTPEELNEHLLKAGFAKwQLPDAYVFAEEIPRTSAGKFLKRALR 508
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
20-545 |
7.11e-132 |
|
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: 391.97 E-value: 7.11e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 20 LKRASECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRLD 99
Cdd:cd17631 1 LRRRARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 100 ATSIAAILRHAKPKILFiyrsfeplareilqllssedsnlnlpvifiheidfpkrvsseesdyecliqrgeptplllarm 179
Cdd:cd17631 81 PPEVAYILADSGAKVLF--------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 180 fciqdeHDPISLNYTSGTTADPKGVVISHRGAYLSTLSAIIGWEMGTCPVYLWTLPMFHCNGW-TFTWGTAARGGTSVCM 258
Cdd:cd17631 98 ------DDLALLMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDLGPDDVLLVVAPLFHIGGLgVFTLPTLLRGGTVVIL 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 259 RHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSHRSGPVHVLTGGSPPPAALVKKVQRLGFQVMHAYGLTEATG 338
Cdd:cd17631 172 RKFDPETVLDLIERHRVTSFFLVPTMIQALLQHPRFATTDLSSLRAVIYGGAPMPERLLRALQARGVKFVQGYGMTETSP 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 339 PVLFcewqdewnrLPENQQMELKARQGLSILGlTEVDVRNKETQEsVPRDgkTMGEIVMKGSSIMKGYLKNPKATYEAFK 418
Cdd:cd17631 252 GVTF---------LSPEDHRRKLGSAGRPVFF-VEVRIVDPDGRE-VPPG--EVGEIVVRGPHVMAGYWNRPEATAAAFR 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 419 HGWLNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETNN 498
Cdd:cd17631 319 DGWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGAELD 398
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 15218840 499 EDredklvtkerDLIEYCRENLPHFMCPRKVVFLDELPKNGNGKILK 545
Cdd:cd17631 399 ED----------ELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
20-449 |
3.05e-113 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 343.53 E-value: 3.05e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 20 LKRASECYPNRTSI-IYGKTRFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRL 98
Cdd:pfam00501 1 LERQAARTPDKTALeVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 99 DATSIAAILRHAKPKILFIYRsfEPLAREILQLLSSEDSnlnlpVIFIHEIDFPKRVSSEESDYECLIQRGEPTPLLLAr 178
Cdd:pfam00501 81 PAEELAYILEDSGAKVLITDD--ALKLEELLEALGKLEV-----VKLVLVLDRDPVLKEEPLPEEAKPADVPPPPPPPP- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 179 mfciqDEHDPISLNYTSGTTADPKGVVISHRGAYLSTLSAII----GWEMGTCPVYLWTLPMFHCNGWT-FTWGTAARGG 253
Cdd:pfam00501 153 -----DPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRvrprGFGLGPDDRVLSTLPLFHDFGLSlGLLGPLLAGA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 254 TSVCMRHVTAP---EIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSHRSGPVHVLTGGSPPPAALVKKV-QRLGFQVMH 329
Cdd:pfam00501 228 TVVLPPGFPALdpaALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLPPELARRFrELFGGALVN 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 330 AYGLTEATGPVlfcewqdeWNRLPENQQMELKARQGLSILGlTEVDVRNKETQESVPRDGKtmGEIVMKGSSIMKGYLKN 409
Cdd:pfam00501 308 GYGLTETTGVV--------TTPLPLDEDLRSLGSVGRPLPG-TEVKIVDDETGEPVPPGEP--GELCVRGPGVMKGYLND 376
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 15218840 410 PKATYEAFKH-GWLNSGDVGVIHPDGHVEIKDRSKDIIISG 449
Cdd:pfam00501 377 PELTAEAFDEdGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
10-550 |
4.16e-105 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 326.09 E-value: 4.16e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 10 NNVPLTPITFLKRASECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGA 89
Cdd:PRK07656 1 DNEWMTLPELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 90 VLNPINTRLDATSIAAILRHAKPKILFIYRSFEPLAREILQLLssedsnLNLPVIFIHEIDFPKRVSSEESDYECLIQRG 169
Cdd:PRK07656 81 VVVPLNTRYTADEAAYILARGDAKALFVLGLFLGVDYSATTRL------PALEHVVICETEEDDPHTEKMKTFTDFLAAG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 170 EPtplllARMFCIQDEHDPISLNYTSGTTADPKGVVISHRgaylSTLSAIIGW----EMGTCPVYLWTLPMFHCNGWTFT 245
Cdd:PRK07656 155 DP-----AERAPEVDPDDVADILFTSGTTGRPKGAMLTHR----QLLSNAADWaeylGLTEGDRYLAANPFFHVFGYKAG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 246 WGTA-ARGGTSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILL---KGNSLDLSH-RSGpvhvLTGGSPPPAALVKKV 320
Cdd:PRK07656 226 VNAPlMRGATILPLPVFDPDEVFRLIETERITVLPGPPTMYNSLLqhpDRSAEDLSSlRLA----VTGAASMPVALLERF 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 321 Q-RLGFQ-VMHAYGLTEATGPVLFCEWQDEWNRLPenqqmelkARQGLSILGlTEVDVRNKETQESVPRDgktMGEIVMK 398
Cdd:PRK07656 302 EsELGVDiVLTGYGLSEASGVTTFNRLDDDRKTVA--------GTIGTAIAG-VENKIVNELGEEVPVGE---VGELLVR 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 399 GSSIMKGYLKNPKATYEAFKH-GWLNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMP 477
Cdd:PRK07656 370 GPNVMKGYYDDPEATAAAIDAdGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVP 449
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15218840 478 HPTWGETPCAFVVLEKGETNNEDredklvtkerDLIEYCRENLPHFMCPRKVVFLDELPKNGNGKILKPKLRD 550
Cdd:PRK07656 450 DERLGEVGKAYVVLKPGAELTEE----------ELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRALRE 512
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
187-544 |
4.01e-101 |
|
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: 309.60 E-value: 4.01e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 187 DPISLNYTSGTTADPKGVVISHRG--AYLSTLSAIIGWEMGTcpVYLWTLPMFHCNGWTFTWGTAARGGTSVCMRHVTAP 264
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNllAAAAALAASGGLTEGD--VFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKFDPE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 265 EIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSHRSGPVHVLTGGSPPPAALVKKV-QRLGFQVMHAYGLTEATGPVLFC 343
Cdd:cd04433 79 AALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPPELLERFeEAPGIKLVNGYGLTETGGTVATG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 344 eWQDEWNRLPENQqmelkarqGLSILGlTEVDVRNKETQESVPRdgkTMGEIVMKGSSIMKGYLKNPKATYEAFKHGWLN 423
Cdd:cd04433 159 -PPDDDARKPGSV--------GRPVPG-VEVRIVDPDGGELPPG---EIGELVVRGPSVMKGYWNNPEATAAVDEDGWYR 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 424 SGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETNNEDred 503
Cdd:cd04433 226 TGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDAE--- 302
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 15218840 504 klvtkerDLIEYCRENLPHFMCPRKVVFLDELPKNGNGKIL 544
Cdd:cd04433 303 -------ELRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
19-555 |
4.61e-101 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 315.72 E-value: 4.61e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 19 FLKRASECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRL 98
Cdd:PRK08316 16 ILRRSARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFML 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 99 DATSIAAILRHAKPKILFIYRSFEPLAREILQLLSSEDSNLNLPVIfiheidfPKRVSSEESDYECLIQRGEPTPLLLAr 178
Cdd:PRK08316 96 TGEELAYILDHSGARAFLVDPALAPTAEAALALLPVDTLILSLVLG-------GREAPGGWLDFADWAEAGSVAEPDVE- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 179 mfcIQDEhDPISLNYTSGTTADPKGVVISHRGAYLSTLSAIIGWEMGTCPVYLWTLPMFHCNGW-TFTWGTAARGGTSVC 257
Cdd:PRK08316 168 ---LADD-DLAQILYTSGTESLPKGAMLTHRALIAEYVSCIVAGDMSADDIPLHALPLYHCAQLdVFLGPYLYVGATNVI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 258 MRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLkgNSLDLSHR--SGPVHVLTGGSPPPAALVKKVQ-RL-GFQVMHAYGL 333
Cdd:PRK08316 244 LDAPDPELILRTIEAERITSFFAPPTVWISLL--RHPDFDTRdlSSLRKGYYGASIMPVEVLKELReRLpGLRFYNCYGQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 334 TE----ATgpVLfcewqdewnrLPEnQQMELKARQGLSILgltevdvrNKETQ------ESVPRDgkTMGEIVMKGSSIM 403
Cdd:PRK08316 322 TEiaplAT--VL----------GPE-EHLRRPGSAGRPVL--------NVETRvvdddgNDVAPG--EVGEIVHRSPQLM 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 404 KGYLKNPKATYEAFKHGWLNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPTWGE 483
Cdd:PRK08316 379 LGYWDDPEKTAEAFRGGWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIE 458
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15218840 484 TPCAFVVLEKGETNNEDredklvtkerDLIEYCRENLPHFMCPRKVVFLDELPKNGNGKILKPKLRDIAKGL 555
Cdd:PRK08316 459 AVTAVVVPKAGATVTED----------ELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKRELRERYAGA 520
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
20-549 |
2.62e-97 |
|
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: 304.49 E-value: 2.62e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 20 LKRASECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRLD 99
Cdd:cd05936 5 LEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 100 ATSIAAILRHAKPKILFIYRSFEPLareilqllssedsnlnlpvifiheidfpkrvsseesdyeclIQRGEPTPLLLARm 179
Cdd:cd05936 85 PRELEHILNDSGAKALIVAVSFTDL-----------------------------------------LAAGAPLGERVAL- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 180 fciqDEHDPISLNYTSGTTADPKGVVISHRGAYLSTLS--AIIGWEMGTCPVYLWTLPMFHcngwTFTWGTA-----ARG 252
Cdd:cd05936 123 ----TPEDVAVLQYTSGTTGVPKGAMLTHRNLVANALQikAWLEDLLEGDDVVLAALPLFH----VFGLTVAlllplALG 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 253 GTSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILL---KGNSLDLSH-RSgpvhVLTGGSPPPAALVKKVQRL-GFQV 327
Cdd:cd05936 195 ATIVLIPRFRPIGVLKEIRKHRVTIFPGVPTMYIALLnapEFKKRDFSSlRL----CISGGAPLPVEVAERFEELtGVPI 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 328 MHAYGLTEaTGPVLFCewqdewNRLPENQqmelKARQ-GLSILGlTEVDVRNKETQEsVPrDGKTmGEIVMKGSSIMKGY 406
Cdd:cd05936 271 VEGYGLTE-TSPVVAV------NPLDGPR----KPGSiGIPLPG-TEVKIVDDDGEE-LP-PGEV-GELWVRGPQVMKGY 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 407 LKNPKATYEAFKHGWLNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPTWGETPC 486
Cdd:cd05936 336 WNRPEETAEAFVDGWLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVK 415
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15218840 487 AFVVLEKGETnnedredklVTkERDLIEYCRENLPHFMCPRKVVFLDELPKNGNGKILKPKLR 549
Cdd:cd05936 416 AFVVLKEGAS---------LT-EEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
38-549 |
6.47e-88 |
|
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: 278.41 E-value: 6.47e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 38 TRFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFI 117
Cdd:cd05934 2 RRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 118 yrsfeplareilqllssedsnlnlpvifiheidfpkrvsseesdyecliqrgeptplllarmfciqdehDPISLNYTSGT 197
Cdd:cd05934 82 ---------------------------------------------------------------------DPASILYTSGT 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 198 TADPKGVVISHRGAYLSTLSAIigWEMGTCP--VYLWTLPMFHCNGWTFTW-GTAARGGTSVCMRHVTAPEIYKNIEMHN 274
Cdd:cd05934 93 TGPPKGVVITHANLTFAGYYSA--RRFGLGEddVYLTVLPLFHINAQAVSVlAALSVGATLVLLPRFSASRFWSDVRRYG 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 275 VTHMCCVPTVFNILLKGNSLDlSHRSGPVHVlTGGSPPPAALVKKV-QRLGFQVMHAYGLTEATGPVlfcewqdeWNRLP 353
Cdd:cd05934 171 ATVTNYLGAMLSYLLAQPPSP-DDRAHRLRA-AYGAPNPPELHEEFeERFGVRLLEGYGMTETIVGV--------IGPRD 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 354 ENQQMELKARQGLSIlgltEVDVRNKETQEsVPRDgkTMGEIVMK---GSSIMKGYLKNPKATYEAFKHGWLNSGDVGVI 430
Cdd:cd05934 241 EPRRPGSIGRPAPGY----EVRIVDDDGQE-LPAG--EPGELVIRglrGWGFFKGYYNMPEATAEAMRNGWFHTGDLGYR 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 431 HPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETNNEDredklvtker 510
Cdd:cd05934 314 DADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDPE---------- 383
|
490 500 510
....*....|....*....|....*....|....*....
gi 15218840 511 DLIEYCRENLPHFMCPRKVVFLDELPKNGNGKILKPKLR 549
Cdd:cd05934 384 ELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
13-550 |
4.88e-85 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 274.71 E-value: 4.88e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 13 PLTPITFLKRASECYPNR---TSIIYGK-TRFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAG 88
Cdd:PRK06018 9 PLLCHRIIDHAARIHGNRevvTRSVEGPiVRTTYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 89 AVLNPINTRLDATSIAAILRHAKPKILFIYRSFEPLAREILQLLSSedsnLNLPVIFIHEIDFPKRVSSEESDYECLIqr 168
Cdd:PRK06018 89 AICHTVNPRLFPEQIAWIINHAEDRVVITDLTFVPILEKIADKLPS----VERYVVLTDAAHMPQTTLKNAVAYEEWI-- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 169 GEPTPLLLARMFciqDEHDPISLNYTSGTTADPKGVVISHRGAYLSTLSAIIGWEMGTCP--VYLWTLPMFHCNGWTFTW 246
Cdd:PRK06018 163 AEADGDFAWKTF---DENTAAGMCYTSGTTGDPKGVLYSHRSNVLHALMANNGDALGTSAadTMLPVVPLFHANSWGIAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 247 gTAARGGTSVCM--RHVTAPEIYKNIEMHNVTHMCCVPTVFNILLK---GNSLDLSHRSgpvHVLTGGSPPPAALVKKVQ 321
Cdd:PRK06018 240 -SAPSMGTKLVMpgAKLDGASVYELLDTEKVTFTAGVPTVWLMLLQymeKEGLKLPHLK---MVVCGGSAMPRSMIKAFE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 322 RLGFQVMHAYGLTEaTGPV-LFCEWQDEWNRLPENQQMELKARQGLSILGLtEVDVRNKETQEsVPRDGKTMGEIVMKGS 400
Cdd:PRK06018 316 DMGVEVRHAWGMTE-MSPLgTLAALKPPFSKLPGDARLDVLQKQGYPPFGV-EMKITDDAGKE-LPWDGKTFGRLKVRGP 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 401 SIMKGYLKNPKATYEAfkHGWLNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPT 480
Cdd:PRK06018 393 AVAAAYYRVDGEILDD--DGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPK 470
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 481 WGETPCAFVVLEKGETnnedredklVTKErDLIEYCRENLPHFMCPRKVVFLDELPKNGNGKILKPKLRD 550
Cdd:PRK06018 471 WDERPLLIVQLKPGET---------ATRE-EILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALRE 530
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
38-544 |
2.12e-84 |
|
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: 271.39 E-value: 2.12e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 38 TRFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFI 117
Cdd:cd05911 9 KELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 118 YRSFEPLAREILQLLSSED-----SNLNLPVIFIHEIDFPKRVSSEESDYECLIQRGEptplllarmfciqdehDPISLN 192
Cdd:cd05911 89 DPDGLEKVKEAAKELGPKDkiivlDDKPDGVLSIEDLLSPTLGEEDEDLPPPLKDGKD----------------DTAAIL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 193 YTSGTTADPKGVVISHRGAYLSTLSA--IIGWEMGTCPVYLWTLPMFHCNGWTFTWGTAARGGTSVCMRHVTAPEIYKNI 270
Cdd:cd05911 153 YSSGTTGLPKGVCLSHRNLIANLSQVqtFLYGNDGSNDVILGFLPLYHIYGLFTTLASLLNGATVIIMPKFDSELFLDLI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 271 EMHNVTHMCCVPTVFNILLKgNSLDLSHRSGPV-HVLTGGSPPPAALVKKVQRLGFQ--VMHAYGLTEATGPVLFCEWQD 347
Cdd:cd05911 233 EKYKITFLYLVPPIAAALAK-SPLLDKYDLSSLrVILSGGAPLSKELQELLAKRFPNatIKQGYGMTETGGILTVNPDGD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 348 EWN----RLPENqqMELKarqglsilgltevdVRNKETQESVPRDgkTMGEIVMKGSSIMKGYLKNPKATYEAF-KHGWL 422
Cdd:cd05911 312 DKPgsvgRLLPN--VEAK--------------IVDDDGKDSLGPN--EPGEICVRGPQVMKGYYNNPEATKETFdEDGWL 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 423 NSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETNNEDre 502
Cdd:cd05911 374 HTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEKLTEK-- 451
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 15218840 503 dklvtkerDLIEYCRENLPHFmcprK-----VVFLDELPKNGNGKIL 544
Cdd:cd05911 452 --------EVKDYVAKKVASY----KqlrggVVFVDEIPKSASGKIL 486
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
19-559 |
4.84e-83 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 270.06 E-value: 4.84e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 19 FLKRASECYPNRTSIIY-----GKTRFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNP 93
Cdd:COG0365 14 CLDRHAEGRGDKVALIWegedgEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 94 INTRLDATSIAAILRHAKPKILF-----IYRSFE----PLAREILQLLSSEDS-----NLNLPVIFIHEIDFPKRVSSEE 159
Cdd:COG0365 94 VFPGFGAEALADRIEDAEAKVLItadggLRGGKVidlkEKVDEALEELPSLEHvivvgRTGADVPMEGDLDWDELLAAAS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 160 SDYECliqrgEPTplllarmfciqDEHDPISLNYTSGTTADPKGVVISHRG---AYLSTLSAIIGWEMGTcpVYLWTLPM 236
Cdd:COG0365 174 AEFEP-----EPT-----------DADDPLFILYTSGTTGKPKGVVHTHGGylvHAATTAKYVLDLKPGD--VFWCTADI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 237 fhcnGW-TFTWGTA----ARGGTSVCMR----HVTAPEIYKNIEMHNVTHMCCVPTVFNILLK-----GNSLDLSH-Rsg 301
Cdd:COG0365 236 ----GWaTGHSYIVygplLNGATVVLYEgrpdFPDPGRLWELIEKYGVTVFFTAPTAIRALMKagdepLKKYDLSSlR-- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 302 pvHVLTGGSPPPAALVKKVQR-LGFQVMHAYGLTEATGPVLFCewqdewnrLPEnqqMELKARQ-GLSILGLtEVDVRNK 379
Cdd:COG0365 310 --LLGSAGEPLNPEVWEWWYEaVGVPIVDGWGQTETGGIFISN--------LPG---LPVKPGSmGKPVPGY-DVAVVDE 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 380 ETQEsVPRDgkTMGEIVMKGS--SIMKGYLKNPKATYEAFKH---GWLNSGDVGVIHPDGHVEIKDRSKDIIISGGENIS 454
Cdd:COG0365 376 DGNP-VPPG--EEGELVIKGPwpGMFRGYWNDPERYRETYFGrfpGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIG 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 455 SVEVENIIYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETNNEDredkLVtkeRDLIEYCRENLPHFMCPRKVVFLDE 534
Cdd:COG0365 453 TAEIESALVSHPAVAEAAVVGVPDEIRGQVVKAFVVLKPGVEPSDE----LA---KELQAHVREELGPYAYPREIEFVDE 525
|
570 580
....*....|....*....|....*
gi 15218840 535 LPKNGNGKILKPKLRDIAKGLVAED 559
Cdd:COG0365 526 LPKTRSGKIMRRLLRKIAEGRPLGD 550
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
39-556 |
2.51e-81 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 265.03 E-value: 2.51e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 39 RFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFIY 118
Cdd:PRK07008 39 RYTYRDCERRAKQLAQALAALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRLFPEQIAYIVNHAEDRYVLFD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 119 RSFEPLAREILQ---------LLSSEDSnlnLPVIFIHEIDFPKRVSSEESDYECliqrgeptPLLlarmfciqDEHDPI 189
Cdd:PRK07008 119 LTFLPLVDALAPqcpnvkgwvAMTDAAH---LPAGSTPLLCYETLVGAQDGDYDW--------PRF--------DENQAS 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 190 SLNYTSGTTADPKGVVISHRGAYLSTLSAIIGWEMGTCP--VYLWTLPMFHCNGWTFTWGTAARGGTSVCM-RHVTAPEI 266
Cdd:PRK07008 180 SLCYTSGTTGNPKGALYSHRSTVLHAYGAALPDAMGLSArdAVLPVVPMFHVNAWGLPYSAPLTGAKLVLPgPDLDGKSL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 267 YKNIEMHNVTHMCCVPTVFNILL---KGNSLDLSHRSGPVhvlTGGSPPPAALVKKVQR-LGFQVMHAYGLTEATGPVLF 342
Cdd:PRK07008 260 YELIEAERVTFSAGVPTVWLGLLnhmREAGLRFSTLRRTV---IGGSACPPAMIRTFEDeYGVEVIHAWGMTEMSPLGTL 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 343 CEWQDEWNRLPENQQMELKARQGLSILGlteVDVR--NKETQEsVPRDGKTMGEIVMKGSSIMKGYLKNpkaTYEAFKHG 420
Cdd:PRK07008 337 CKLKWKHSQLPLDEQRKLLEKQGRVIYG---VDMKivGDDGRE-LPWDGKAFGDLQVRGPWVIDRYFRG---DASPLVDG 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 421 WLNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETnned 500
Cdd:PRK07008 410 WFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRPGAE---- 485
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 15218840 501 redklVTKErDLIEYCRENLPHFMCPRKVVFLDELPKNGNGKILKPKLRDIAKGLV 556
Cdd:PRK07008 486 -----VTRE-ELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLREQFRDYV 535
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
10-548 |
3.48e-78 |
|
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: 255.62 E-value: 3.48e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 10 NNVPLTPITFLkrASECYPNRTSIIYGKT--RFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMA 87
Cdd:cd05904 3 TDLPLDSVSFL--FASAHPSRPALIDAATgrALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 88 GAVL---NPINTrldATSIAAILRHAKPKILFIYRS-FEPLAReilqllssedsnLNLPVIFIHEIDFpkrvssEESDYE 163
Cdd:cd05904 81 GAVVttaNPLST---PAEIAKQVKDSGAKLAFTTAElAEKLAS------------LALPVVLLDSAEF------DSLSFS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 164 CLIQRGEPTPLLLARMfciqDEHDPISLNYTSGTTADPKGVVISHRGAYLSTLSAIIGWEMGTCP--VYLWTLPMFHCNG 241
Cdd:cd05904 140 DLLFEADEAEPPVVVI----KQDDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEGSNSDSedVFLCVLPMFHIYG 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 242 WT-FTWGTAARGGTSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSHRSGPVHVLTGGSPPPAALVKKV 320
Cdd:cd05904 216 LSsFALGLLRLGATVVVMPRFDLEELLAAIERYKVTHLPVVPPIVLALVKSPIVDKYDLSSLRQIMSGAAPLGKELIEAF 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 321 -QRL-GFQVMHAYGLTEATGPVLFCEwqdewnrlpenQQMELKARQGLS--ILGLTEVDVRNKETQESVPRdGKTmGEIV 396
Cdd:cd05904 296 rAKFpNVDLGQGYGMTESTGVVAMCF-----------APEKDRAKYGSVgrLVPNVEAKIVDPETGESLPP-NQT-GELW 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 397 MKGSSIMKGYLKNPKATYEAF-KHGWLNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVA 475
Cdd:cd05904 363 IRGPSIMKGYLNNPEATAATIdKEGWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIP 442
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15218840 476 MPHPTWGETPCAFVVLEKGETNNEDredklvtkerDLIEYCRENLPHFMCPRKVVFLDELPKNGNGKILKPKL 548
Cdd:cd05904 443 YPDEEAGEVPMAFVVRKPGSSLTED----------EIMDFVAKQVAPYKKVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
28-555 |
2.08e-76 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 250.26 E-value: 2.08e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 28 PNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAIL 107
Cdd:PRK03640 16 PDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 108 RHAKPKILFIYRSFEPLAREILQLLSSEDSNLNLPVIFIheidfpkrvsseESDYecliqrgeptplllarmfciqDEHD 187
Cdd:PRK03640 96 DDAEVKCLITDDDFEAKLIPGISVKFAELMNGPKEEAEI------------QEEF---------------------DLDE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 188 PISLNYTSGTTADPKGVVISHRGAYLSTLSAIIgwEMG----TCpvYLWTLPMFHCNGWTFTWGTAARGGTSVCMRHVTA 263
Cdd:PRK03640 143 VATIMYTSGTTGKPKGVIQTYGNHWWSAVGSAL--NLGltedDC--WLAAVPIFHISGLSILMRSVIYGMRVVLVEKFDA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 264 PEIYKNIEMHNVTHMCCVPTVFNILLKgnslDLSHRSGPVH---VLTGGSPPPAALVKKVQRLGFQVMHAYGLTEATgpv 340
Cdd:PRK03640 219 EKINKLLQTGGVTIISVVSTMLQRLLE----RLGEGTYPSSfrcMLLGGGPAPKPLLEQCKEKGIPVYQSYGMTETA--- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 341 lfcewqdewnrlpeNQQMELKARQGLSILG-----LTEVDVR-NKETQESVPRDgktMGEIVMKGSSIMKGYLKNPKATY 414
Cdd:PRK03640 292 --------------SQIVTLSPEDALTKLGsagkpLFPCELKiEKDGVVVPPFE---EGEIVVKGPNVTKGYLNREDATR 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 415 EAFKHGWLNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPTWGETPCAFVVLEKG 494
Cdd:PRK03640 355 ETFQDGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVKSGE 434
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15218840 495 ETNNEdredklvtkerdLIEYCRENLPHFMCPRKVVFLDELPKNGNGKILKPKLRDIAKGL 555
Cdd:PRK03640 435 VTEEE------------LRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQLVEEM 483
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
9-560 |
4.38e-76 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 251.65 E-value: 4.38e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 9 ANNVPLTPIT---FLKRASECYPNRTSIIY--GKTRFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFA 83
Cdd:PRK08315 8 PTDVPLLEQTigqLLDRTAARYPDREALVYrdQGLRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 84 VPMAGAVLNPINTRLDATSIAAILRHAKPKILFIYRSF------EPLAREILQLLSSEDSNLN---LP----VIFIHEID 150
Cdd:PRK08315 88 TAKIGAILVTINPAYRLSELEYALNQSGCKALIAADGFkdsdyvAMLYELAPELATCEPGQLQsarLPelrrVIFLGDEK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 151 FPKRVSSEEsdyecLIQRGE--PTPLLLARMFCIqDEHDPISLNYTSGTTADPKGVVISHRG----AYLstlsaiIGWEM 224
Cdd:PRK08315 168 HPGMLNFDE-----LLALGRavDDAELAARQATL-DPDDPINIQYTSGTTGFPKGATLTHRNilnnGYF------IGEAM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 225 G-------TCPVylwtlPMFHCNGWTFtwGTAA---RGGTSVCMRHVTAPE-IYKNIEMHNVTHMCCVPTVFNILLKG-- 291
Cdd:PRK08315 236 KlteedrlCIPV-----PLYHCFGMVL--GNLAcvtHGATMVYPGEGFDPLaTLAAVEEERCTALYGVPTMFIAELDHpd 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 292 -NSLDLSH-RSGpvhvLTGGSPPPAALVKKVQRLgfqvMH------AYGLTEaTGPVLFCEWQDEwnrlPENQQMELKAR 363
Cdd:PRK08315 309 fARFDLSSlRTG----IMAGSPCPIEVMKRVIDK----MHmsevtiAYGMTE-TSPVSTQTRTDD----PLEKRVTTVGR 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 364 qglsILGLTEVDVRNKETQESVPRdGKTmGEIVMKGSSIMKGYLKNPKATYEAFKH-GWLNSGDVGVIHPDGHVEIKDRS 442
Cdd:PRK08315 376 ----ALPHLEVKIVDPETGETVPR-GEQ-GELCTRGYSVMKGYWNDPEKTAEAIDAdGWMHTGDLAVMDEEGYVNIVGRI 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 443 KDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETNNEDredklvtkerDLIEYCRENLPH 522
Cdd:PRK08315 450 KDMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGATLTEE----------DVRDFCRGKIAH 519
|
570 580 590
....*....|....*....|....*....|....*...
gi 15218840 523 FMCPRKVVFLDELPKNGNGKILKPKLRDIAKGLVAEDE 560
Cdd:PRK08315 520 YKIPRYIRFVDEFPMTVTGKIQKFKMREMMIEELGLQA 557
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
51-550 |
1.35e-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: 1.35e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 51 RLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFI-YRSFEPLAReil 129
Cdd:cd05926 26 DLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVLTpKGELGPASR--- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 130 qllssedsNLNLPVIFIHEIDFPKRVSSEESDYE----CLIQRGEPTPLLLARmfciqdEHDPISLNYTSGTTADPKGVV 205
Cdd:cd05926 103 --------AASKLGLAILELALDVGVLIRAPSAEslsnLLADKKNAKSEGVPL------PDDLALILHTSGTTGRPKGVP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 206 ISHRGAYLSTLSAIIGWEMGTCPVYLWTLPMFHCNGWTFT-WGTAARGGTSVCMRHVTAPEIYKNIEMHNVTHMCCVPTV 284
Cdd:cd05926 169 LTHRNLAASATNITNTYKLTPDDRTLVVMPLFHVHGLVASlLSTLAAGGSVVLPPRFSASTFWPDVRDYNATWYTAVPTI 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 285 FNILLKgnsldlSHRSGPVHVL-------TGGSP-PPAALVKKVQRLGFQVMHAYGLTEATGPVlFCewqdewNRLPENQ 356
Cdd:cd05926 249 HQILLN------RPEPNPESPPpklrfirSCSASlPPAVLEALEATFGAPVLEAYGMTEAAHQM-TS------NPLPPGP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 357 QmelkaRQGLsiLGL---TEVDVRNkETQESVPrDGKTmGEIVMKGSSIMKGYLKNPKATYE-AFKHGWLNSGDVGVIHP 432
Cdd:cd05926 316 R-----KPGS--VGKpvgVEVRILD-EDGEILP-PGVV-GEICLRGPNVTRGYLNNPEANAEaAFKDGWFRTGDLGYLDA 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 433 DGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETnnedredklVTKErDL 512
Cdd:cd05926 386 DGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGAS---------VTEE-EL 455
|
490 500 510
....*....|....*....|....*....|....*...
gi 15218840 513 IEYCRENLPHFMCPRKVVFLDELPKNGNGKILKPKLRD 550
Cdd:cd05926 456 RAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
28-553 |
2.12e-74 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 245.54 E-value: 2.12e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 28 PNRTSIIYGKTRFTWPQTYDRCCRLAASLI-SLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAI 106
Cdd:PRK06839 16 PDRIAIITEEEEMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 107 LRHAKPKILFIYRSFEPLAREILQLLSSEdsnlnlPVIFIHEidfPKRVSSEESDYecLIQRGEPTPLLLArmfciqdeh 186
Cdd:PRK06839 96 LKDSGTTVLFVEKTFQNMALSMQKVSYVQ------RVISITS---LKEIEDRKIDN--FVEKNESASFIIC--------- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 187 dpislnYTSGTTADPKGVVISHRGAYLSTLSAIIGWEMGTCPVYLWTLPMFHCNGWT-FTWGTAARGGTSVCMRHVTAPE 265
Cdd:PRK06839 156 ------YTSGTTGKPKGAVLTQENMFWNALNNTFAIDLTMHDRSIVLLPLFHIGGIGlFAFPTLFAGGVIIVPRKFEPTK 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 266 IYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSHRSGPVHVLTGGSPPPAALVKKVQRLGFQVMHAYGLTEaTGPVLFCEW 345
Cdd:PRK06839 230 ALSMIEKHKVTVVMGVPTIHQALINCSKFETTNLQSVRWFYNGGAPCPEELMREFIDRGFLFGQGFGMTE-TSPTVFMLS 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 346 QDEWNRLPenqqmelkARQGLSILgLTEVDVRNKETQEsVPRDGktMGEIVMKGSSIMKGYLKNPKATYEAFKHGWLNSG 425
Cdd:PRK06839 309 EEDARRKV--------GSIGKPVL-FCDYELIDENKNK-VEVGE--VGELLIRGPNVMKEYWNRPDATEETIQDGWLCTG 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 426 DVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGEtnnedredkl 505
Cdd:PRK06839 377 DLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSS---------- 446
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 15218840 506 VTKERDLIEYCRENLPHFMCPRKVVFLDELPKNGNGKILKPKLRDIAK 553
Cdd:PRK06839 447 VLIEKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVNQLK 494
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
28-550 |
7.00e-73 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 241.33 E-value: 7.00e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 28 PNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAIL 107
Cdd:PRK06145 16 PDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYIL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 108 RHAKPKILFIyrsfeplareilqllsseDSNLNLPVIFIHeidfPKRVSSE--ESDYECLIQRGEPTPLLLARMfciqdE 185
Cdd:PRK06145 96 GDAGAKLLLV------------------DEEFDAIVALET----PKIVIDAaaQADSRRLAQGGLEIPPQAAVA-----P 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 186 HDPISLNYTSGTTADPKGVVISHRGAYLSTLSAIIGWEMGTCPVYLWTLPMFHCNGWTFTwGTA--ARGGTSVCMRHVTA 263
Cdd:PRK06145 149 TDLVRLMYTSGTTDRPKGVMHSYGNLHWKSIDHVIALGLTASERLLVVGPLYHVGAFDLP-GIAvlWVGGTLRIHREFDP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 264 PEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSHRSGPVHVLTGGSPPPAALVKKVQRL--GFQVMHAYGLTEATGPVL 341
Cdd:PRK06145 228 EAVLAAIERHRLTCAWMAPVMLSRVLTVPDRDRFDLDSLAWCIGGGEKTPESRIRDFTRVftRARYIDAYGLTETCSGDT 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 342 FCEwqdewnrlpENQQMELKARQGLSiLGLTEVDVRNKETQESVPrdgKTMGEIVMKGSSIMKGYLKNPKATYEAFKHGW 421
Cdd:PRK06145 308 LME---------AGREIEKIGSTGRA-LAHVEIRIADGAGRWLPP---NMKGEICMRGPKVTKGYWKDPEKTAEAFYGDW 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 422 LNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETNNEDr 501
Cdd:PRK06145 375 FRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGATLTLE- 453
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 15218840 502 edklvtkerDLIEYCRENLPHFMCPRKVVFLDELPKNGNGKILKPKLRD 550
Cdd:PRK06145 454 ---------ALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLRD 493
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
41-550 |
3.28e-72 |
|
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: 237.24 E-value: 3.28e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 41 TWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKilfiyrs 120
Cdd:cd05912 3 TFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVK------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 121 FEPLAreilqllssedsnlnlpvifiheidfpkrvsseesdyecliqrgeptplllarmfciqdehdpiSLNYTSGTTAD 200
Cdd:cd05912 76 LDDIA----------------------------------------------------------------TIMYTSGTTGK 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 201 PKGVVISHRGAYLSTLSAI--IGWEMGTCpvYLWTLPMFHCNGWTFTWGTAARGGTSVCMRHVTAPEIYKNIEMHNVTHM 278
Cdd:cd05912 92 PKGVQQTFGNHWWSAIGSAlnLGLTEDDN--WLCALPLFHISGLSILMRSVIYGMTVYLVDKFDAEQVLHLINSGKVTII 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 279 CCVPTVFNILLKgnsldLSHRSGPVH---VLTGGSPPPAALVKKVQRLGFQVMHAYGLTEATGPVLFCEWQDEWNRlpen 355
Cdd:cd05912 170 SVVPTMLQRLLE-----ILGEGYPNNlrcILLGGGPAPKPLLEQCKEKGIPVYQSYGMTETCSQIVTLSPEDALNK---- 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 356 qqmelkarqgLSILGLTEVDVRNKETQESVPRdgKTMGEIVMKGSSIMKGYLKNPKATYEAFKHGWLNSGDVGVIHPDGH 435
Cdd:cd05912 241 ----------IGSAGKPLFPVELKIEDDGQPP--YEVGEILLKGPNVTKGYLNRPDATEESFENGWFKTGDIGYLDEEGF 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 436 VEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETNNEdredklvtkerdLIEY 515
Cdd:cd05912 309 LYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSERPISEEE------------LIAY 376
|
490 500 510
....*....|....*....|....*....|....*
gi 15218840 516 CRENLPHFMCPRKVVFLDELPKNGNGKILKPKLRD 550
Cdd:cd05912 377 CSEKLAKYKVPKKIYFVDELPRTASGKLLRHELKQ 411
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
186-549 |
2.61e-70 |
|
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: 230.24 E-value: 2.61e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 186 HDPISLNYTSGTTADPKGVVISHRGayLSTLSAIIGWEMGT-------CPVylwtlPMFHCNGWTF-TWGTAARGGTSVC 257
Cdd:cd05917 2 DDVINIQFTSGTTGSPKGATLTHHN--IVNNGYFIGERLGLteqdrlcIPV-----PLFHCFGSVLgVLACLTHGATMVF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 258 M-RHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSL---DLSH-RSGpvhvLTGGSPPPAALVKKV-QRLGFQVMH-A 330
Cdd:cd05917 75 PsPSFDPLAVLEAIEKEKCTALHGVPTMFIAELEHPDFdkfDLSSlRTG----IMAGAPCPPELMKRViEVMNMKDVTiA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 331 YGLTEATgPVLFCEWQDEwnrlpenqQMELKARQGLSILGLTEVDVRNKETQESVPRDGKtmGEIVMKGSSIMKGYLKNP 410
Cdd:cd05917 151 YGMTETS-PVSTQTRTDD--------SIEKRVNTVGRIMPHTEAKIVDPEGGIVPPVGVP--GELCIRGYSVMKGYWNDP 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 411 KATYEAFKH-GWLNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPTWGETPCAFV 489
Cdd:cd05917 220 EKTAEAIDGdGWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWI 299
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 490 VLEKGETnnedredklvTKERDLIEYCRENLPHFMCPRKVVFLDELPKNGNGKILKPKLR 549
Cdd:cd05917 300 RLKEGAE----------LTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
20-559 |
4.26e-69 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 233.13 E-value: 4.26e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 20 LKRASECYPNRTSIIYGK--TRFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTR 97
Cdd:PRK12583 24 FDATVARFPDREALVVRHqaLRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 98 LDATSIAAILRHAKPKILFI---YRSFEPLAreILQLLSSEDSNLNlPVIFIHEiDFPK-----RVSSEESD----YECL 165
Cdd:PRK12583 104 YRASELEYALGQSGVRWVICadaFKTSDYHA--MLQELLPGLAEGQ-PGALACE-RLPElrgvvSLAPAPPPgflaWHEL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 166 IQRGEPtpLLLARMFCIQ---DEHDPISLNYTSGTTADPKGVVISH----RGAYLSTLSAIIGWEMGTC-PVylwtlPMF 237
Cdd:PRK12583 180 QARGET--VSREALAERQaslDRDDPINIQYTSGTTGFPKGATLSHhnilNNGYFVAESLGLTEHDRLCvPV-----PLY 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 238 HCNGWTFTwgtaarggTSVCMRH---VTAPEIY-------KNIEMHNVTHMCCVPTVFNILL---KGNSLDLSH-RSGpv 303
Cdd:PRK12583 253 HCFGMVLA--------NLGCMTVgacLVYPNEAfdplatlQAVEEERCTALYGVPTMFIAELdhpQRGNFDLSSlRTG-- 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 304 hvLTGGSPPPAALVKKVqrlgFQVMH------AYGLTEaTGPVLFcewqdewnRLPENQQMELKarqgLSILGLTEVDVR 377
Cdd:PRK12583 323 --IMAGAPCPIEVMRRV----MDEMHmaevqiAYGMTE-TSPVSL--------QTTAADDLERR----VETVGRTQPHLE 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 378 NKETQ---ESVPRDgkTMGEIVMKGSSIMKGYLKNPKATYEAF-KHGWLNSGDVGVIHPDGHVEIKDRSKDIIISGGENI 453
Cdd:PRK12583 384 VKVVDpdgATVPRG--EIGELCTRGYSVMKGYWNNPEATAESIdEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENI 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 454 SSVEVENIIYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETNNEDredklvtkerDLIEYCRENLPHFMCPRKVVFLD 533
Cdd:PRK12583 462 YPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHPGHAASEE----------ELREFCKARIAHFKVPRYFRFVD 531
|
570 580
....*....|....*....|....*.
gi 15218840 534 ELPKNGNGKILKPKLRDIAKGLVAED 559
Cdd:PRK12583 532 EFPMTVTGKVQKFRMREISIEELALP 557
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
41-548 |
1.58e-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: 225.41 E-value: 1.58e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 41 TWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFIYRS 120
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 121 FEplaREILQLLSsedsnlnlpvifIHEIDFPKRVSSEESDYecliqrgeptplllarmfcIQDEhDPISLNYTSGTTAD 200
Cdd:TIGR01923 81 LE---EKDFQADS------------LDRIEAAGRYETSLSAS-------------------FNMD-QIATLMFTSGTTGK 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 201 PKGVVISHRGAYLSTLSAI--IGWEMGTCpvYLWTLPMFHCNGWTFTWGTAARGGTSVCmrHVTAPEIYKNIEMHNVTHM 278
Cdd:TIGR01923 126 PKAVPHTFRNHYASAVGSKenLGFTEDDN--WLLSLPLYHISGLSILFRWLIEGATLRI--VDKFNQLLEMIANERVTHI 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 279 CCVPTVFNILLKGNSLDLSHRSgpvhVLTGGSPPPAALVKKVQRLGFQVMHAYGLTEATGPVLFCEWQDewnrlpenqqm 358
Cdd:TIGR01923 202 SLVPTQLNRLLDEGGHNENLRK----ILLGGSAIPAPLIEEAQQYGLPIYLSYGMTETCSQVTTATPEM----------- 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 359 eLKARQGLSILgLTEVDVRnketqesVPRDGKT-MGEIVMKGSSIMKGYLKNPKATYEAFKHGWLNSGDVGVIHPDGHVE 437
Cdd:TIGR01923 267 -LHARPDVGRP-LAGREIK-------IKVDNKEgHGEIMVKGANLMKGYLYQGELTPAFEQQGWFNTGDIGELDGEGFLY 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 438 IKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETNNEdredklvtkerdLIEYCR 517
Cdd:TIGR01923 338 VLGRRDDLIISGGENIYPEEIETVLYQHPGIQEAVVVPKPDAEWGQVPVAYIVSESDISQAK------------LIAYLT 405
|
490 500 510
....*....|....*....|....*....|.
gi 15218840 518 ENLPHFMCPRKVVFLDELPKNGNGKILKPKL 548
Cdd:TIGR01923 406 EKLAKYKVPIAFEKLDELPYNASGKILRNQL 436
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
39-549 |
2.29e-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: 219.94 E-value: 2.29e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 39 RFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFIY 118
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 119 RSFeplareilqllssedsnlnlpvifiheidfpkrvsseesdyecliqrgeptplllaRMFCIQDEHDPIS-LNYTSGT 197
Cdd:cd05903 81 ERF--------------------------------------------------------RQFDPAAMPDAVAlLLFTSGT 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 198 TADPKGVVISHRGAYLSTLSAIIGWEMGTCPVYLWTLPMFHCNGwtFTWGTAA---RGGTSVCMRHVTAPEIYKNIEMHN 274
Cdd:cd05903 105 TGEPKGVMHSHNTLSASIRQYAERLGLGPGDVFLVASPMAHQTG--FVYGFTLpllLGAPVVLQDIWDPDKALALMREHG 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 275 VTHMCCVPTVFNILLKGNSLDLSHRSGPVHVLTGGSPPPAALVKKVQ-RLGFQVMHAYGLTEATGPVLFCEWQDEWNRLP 353
Cdd:cd05903 183 VTFMMGATPFLTDLLNAVEEAGEPLSRLRTFVCGGATVPRSLARRAAeLLGAKVCSAYGSTECPGAVTSITPAPEDRRLY 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 354 ENqqmelkarqGLSILGLtEVDVrnketqesVPRDGKTM-----GEIVMKGSSIMKGYLKNPKATYEAFKHGWLNSGDVG 428
Cdd:cd05903 263 TD---------GRPLPGV-EIKV--------VDDTGATLapgveGELLSRGPSVFLGYLDRPDLTADAAPEGWFRTGDLA 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 429 VIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETNNEDredklvtk 508
Cdd:cd05903 325 RLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGALLTFD-------- 396
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 15218840 509 erDLIEYC-RENLPHFMCPRKVVFLDELPKNGNGKILKPKLR 549
Cdd:cd05903 397 --ELVAYLdRQGVAKQYWPERLVHVDDLPRTPSGKVQKFRLR 436
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
18-560 |
1.01e-64 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 220.68 E-value: 1.01e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 18 TFLKRASECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTR 97
Cdd:PRK07470 11 HFLRQAARRFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 98 LDATSIAAILRHAKPKILFIYRSFEPLAREILQLLSSEDSnlnlpVIFIHEIDFpkrvsseESDYECLIQRGEPTPLLLA 177
Cdd:PRK07470 91 QTPDEVAYLAEASGARAMICHADFPEHAAAVRAASPDLTH-----VVAIGGARA-------GLDYEALVARHLGARVANA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 178 RMfciqDEHDPISLNYTSGTTADPKGVVISH-RGAYLST--LSAIIGwemGTCP--VYLWTLPMFHCNGwTFTWGTAARG 252
Cdd:PRK07470 159 AV----DHDDPCWFFFTSGTTGRPKAAVLTHgQMAFVITnhLADLMP---GTTEqdASLVVAPLSHGAG-IHQLCQVARG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 253 GTSVCM--RHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSHRSGPVHVLTGGSPPPAALVKK-VQRLGFQVMH 329
Cdd:PRK07470 231 AATVLLpsERFDPAEVWALVERHRVTNLFTVPTILKMLVEHPAVDRYDHSSLRYVIYAGAPMYRADQKRaLAKLGKVLVQ 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 330 AYGLTEATG-----PVLFCEWQDEwnrlPEnqqmelkARQGLSILGLT--EVDVRNKETQESVPrdGKTmGEIVMKGSSI 402
Cdd:PRK07470 311 YFGLGEVTGnitvlPPALHDAEDG----PD-------ARIGTCGFERTgmEVQIQDDEGRELPP--GET-GEICVIGPAV 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 403 MKGYLKNPKATYEAFKHGWLNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPTWG 482
Cdd:PRK07470 377 FAGYYNNPEANAKAFRDGWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWG 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 483 ETPCAFVVLEKGETNNEDredklvtkerDLIEYCRENLPHFMCPRKVVFLDELPKNGNGKILKPKLRD--IAKGLVAEDE 560
Cdd:PRK07470 457 EVGVAVCVARDGAPVDEA----------ELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVREelEERGLLDLER 526
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
22-549 |
1.24e-62 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 214.85 E-value: 1.24e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 22 RASECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMyemhFAVPMAGAV-------LNPI 94
Cdd:PRK06188 20 SALKRYPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEV----LMAIGAAQLaglrrtaLHPL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 95 NTRLDAtsiAAILRHAKPKIL------FIYRSFEPLAR--EILQLLSSEDSNlnlpvifiheidfpkrvssEESDYECLI 166
Cdd:PRK06188 96 GSLDDH---AYVLEDAGISTLivdpapFVERALALLARvpSLKHVLTLGPVP-------------------DGVDLLAAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 167 QRGEPTPLLlarmfCIQDEHDPISLNYTSGTTADPKGVVISHRGayLSTLSAII--GWEMGTCPVYLWTLPMFHCNGWTF 244
Cdd:PRK06188 154 AKFGPAPLV-----AAALPPDIAGLAYTGGTTGKPKGVMGTHRS--IATMAQIQlaEWEWPADPRFLMCTPLSHAGGAFF 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 245 TwGTAARGGTSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSHRSGPVHVLTGGSP-PPAALVKKVQRL 323
Cdd:PRK06188 227 L-PTLLRGGTVIVLAKFDPAEVLRAIEEQRITATFLVPTMIYALLDHPDLRTRDLSSLETVYYGASPmSPVRLAEAIERF 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 324 GFQVMHAYGLTEATGPVLFCEWQDEWNRLPEnqqmeLKARQGLSILGLtEVDVRNKETQEsVPRDgkTMGEIVMKGSSIM 403
Cdd:PRK06188 306 GPIFAQYYGQTEAPMVITYLRKRDHDPDDPK-----RLTSCGRPTPGL-RVALLDEDGRE-VAQG--EVGEICVRGPLVM 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 404 KGYLKNPKATYEAFKHGWLNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPTWGE 483
Cdd:PRK06188 377 DGYWNRPEETAEAFRDGWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGE 456
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15218840 484 TPCAFVVLEKGETNNEDredklvtkerDLIEYCRENLPHFMCPRKVVFLDELPKNGNGKILKPKLR 549
Cdd:PRK06188 457 AVTAVVVLRPGAAVDAA----------ELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALR 512
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
30-550 |
1.30e-62 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 214.38 E-value: 1.30e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 30 RTSIIYGK-TRFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILR 108
Cdd:PRK08276 1 PAVIMAPSgEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 109 HAKPKILFIYRSFEPLAREILQLLSsedsnLNLPVIFIheidFPKRVSSEESdYECLIQRGEPTPlllarmfcIQDEHDP 188
Cdd:PRK08276 81 DSGAKVLIVSAALADTAAELAAELP-----AGVPLLLV----VAGPVPGFRS-YEEALAAQPDTP--------IADETAG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 189 ISLNYTSGTTADPKGVVISHRG----AYLSTLSAIIGWEMGTCP--VYLWTLPMFHCNGWTFTWGTAARGGTSVCMRHVT 262
Cdd:PRK08276 143 ADMLYSSGTTGRPKGIKRPLPGldpdEAPGMMLALLGFGMYGGPdsVYLSPAPLYHTAPLRFGMSALALGGTVVVMEKFD 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 263 APEIYKNIEMHNVTHMCCVPTVFNILLK-----GNSLDLSHRSGPVHvltGGSPPPAAlVKK--VQRLGFQVMHAYGLTE 335
Cdd:PRK08276 223 AEEALALIERYRVTHSQLVPTMFVRMLKlpeevRARYDVSSLRVAIH---AAAPCPVE-VKRamIDWWGPIIHEYYASSE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 336 ATGpVLFCEWQDeWNRLPenqqmelkARQGLSILGltEVDVRNKETQESVPRdgkTMGEIVMKGSSIMKGYLKNPKATYE 415
Cdd:PRK08276 299 GGG-VTVITSED-WLAHP--------GSVGKAVLG--EVRILDEDGNELPPG---EIGTVYFEMDGYPFEYHNDPEKTAA 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 416 AF-KHGWLNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPTWGETPCAFVVLEKG 494
Cdd:PRK08276 364 ARnPHGWVTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQPADG 443
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 15218840 495 ETNNEDREDklvtkerDLIEYCRENLPHFMCPRKVVFLDELPKNGNGKILKPKLRD 550
Cdd:PRK08276 444 ADAGDALAA-------ELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLRD 492
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
8-549 |
5.33e-61 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 212.89 E-value: 5.33e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 8 EANNVPLTPITFLKRASECYPNRTSIIYGKT--------RFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPamyE 79
Cdd:PRK07529 19 AARDLPASTYELLSRAAARHPDAPALSFLLDadpldrpeTWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLP---E 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 80 MHFAV--PMAGAVLNPINTRLDATSIAAILRHAKPKILFIYRSF---------EPLAREILQLLssedsnlnlPVIfihE 148
Cdd:PRK07529 96 THFALwgGEAAGIANPINPLLEPEQIAELLRAAGAKVLVTLGPFpgtdiwqkvAEVLAALPELR---------TVV---E 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 149 IDFPKRVSSEES---------------DYECLIQRGEPTPLLLARMFciqDEHDPISLNYTSGTTADPKGVVISHRG--- 210
Cdd:PRK07529 164 VDLARYLPGPKRlavplirrkaharilDFDAELARQPGDRLFSGRPI---GPDDVAAYFHTGGTTGMPKLAQHTHGNeva 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 211 -AYLSTLSAIIGwEMGT--CPvylwtLPMFHCNGwTFTWGTA--ARGG-----TSVCMRHvtaPEIYKN----IEMHNVT 276
Cdd:PRK07529 241 nAWLGALLLGLG-PGDTvfCG-----LPLFHVNA-LLVTGLAplARGAhvvlaTPQGYRG---PGVIANfwkiVERYRIN 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 277 HMCCVPTVFNILLK--GNSLDLSHRSGpvhVLTGGSPPPAALVKKVQ-RLGFQVMHAYGLTEATGPVlfcewqdewNRLP 353
Cdd:PRK07529 311 FLSGVPTVYAALLQvpVDGHDISSLRY---ALCGAAPLPVEVFRRFEaATGVRIVEGYGLTEATCVS---------SVNP 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 354 ENQQMelkaRQGlSIlGL----TEVDVRNKETQESVPRDGKT--MGEIVMKGSSIMKGYL---KNPKATYEAfkhGWLNS 424
Cdd:PRK07529 379 PDGER----RIG-SV-GLrlpyQRVRVVILDDAGRYLRDCAVdeVGVLCIAGPNVFSGYLeaaHNKGLWLED---GWLNT 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 425 GDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETNNEDRedk 504
Cdd:PRK07529 450 GDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYVQLKPGASATEAE--- 526
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 15218840 505 lvtkerdLIEYCRENLPHFMC-PRKVVFLDELPKNGNGKILKPKLR 549
Cdd:PRK07529 527 -------LLAFARDHIAERAAvPKHVRILDALPKTAVGKIFKPALR 565
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
12-554 |
1.36e-60 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 209.82 E-value: 1.36e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 12 VPLTPITF-LKRASECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLIS-LNIGKNDVVSVVAPNTPAMYEMHFAVPMAGA 89
Cdd:PRK08314 7 LPETSLFHnLEVSARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQQeCGVRKGDRVLLYMQNSPQFVIAYYAILRANA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 90 VLNPINTRLDATSIAAILRHAKPKILFIYRSfepLAREILQLLS----------------SEDSNLNLPVIFIHEidfPK 153
Cdd:PRK08314 87 VVVPVNPMNREEELAHYVTDSGARVAIVGSE---LAPKVAPAVGnlrlrhvivaqysdylPAEPEIAVPAWLRAE---PP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 154 RVSSEESDY----ECLIQRGEPTPLllarmfciQDEHDPIS-LNYTSGTTADPKGVVISHRGAYLSTLSAIIgWEMGTC- 227
Cdd:PRK08314 161 LQALAPGGVvawkEALAAGLAPPPH--------TAGPDDLAvLPYTSGTTGVPKGCMHTHRTVMANAVGSVL-WSNSTPe 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 228 PVYLWTLPMFHCNGWTFTWGTA-ARGGTSVCM----RHvTAPEIyknIEMHNVTHMCCVPTVFNILLKGNSLDLSHRSGP 302
Cdd:PRK08314 232 SVVLAVLPLFHVTGMVHSMNAPiYAGATVVLMprwdRE-AAARL---IERYRVTHWTNIPTMVVDFLASPGLAERDLSSL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 303 VHVLTGGSPPPAALVKKVQRL-GFQVMHAYGLTEATGPVLFcewqdewNrlPenqqmelKARQGLSILG--LTEVDVR-- 377
Cdd:PRK08314 308 RYIGGGGAAMPEAVAERLKELtGLDYVEGYGLTETMAQTHS-------N--P-------PDRPKLQCLGipTFGVDARvi 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 378 NKETQESVPrDGKTmGEIVMKGSSIMKGYLKNPKATYEAF-----KHgWLNSGDVGVIHPDGHVEIKDRSKDIIISGGEN 452
Cdd:PRK08314 372 DPETLEELP-PGEV-GEIVVHGPQVFKGYWNRPEATAEAFieidgKR-FFRTGDLGRMDEEGYFFITDRLKRMINASGFK 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 453 ISSVEVENIIYKYPKVLETAVVAMPHPTWGETPCAFVVLekgetnNEDREDKlvTKERDLIEYCRENLPHFMCPRKVVFL 532
Cdd:PRK08314 449 VWPAEVENLLYKHPAIQEACVIATPDPRRGETVKAVVVL------RPEARGK--TTEEEIIAWAREHMAAYKYPRIVEFV 520
|
570 580
....*....|....*....|..
gi 15218840 533 DELPKNGNGKILKPKLRDIAKG 554
Cdd:PRK08314 521 DSLPKSGSGKILWRQLQEQEKA 542
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
20-549 |
3.54e-60 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 208.86 E-value: 3.54e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 20 LKRASECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRLD 99
Cdd:PRK07786 23 LARHALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 100 ATSIAAILRHAKPKILFIYRSFEPLAREILQLLSSEDSnlnlpVIFIHEidfpkrvSSEES--DYECLI-QRGEPTPLLl 176
Cdd:PRK07786 103 PPEIAFLVSDCGAHVVVTEAALAPVATAVRDIVPLLST-----VVVAGG-------SSDDSvlGYEDLLaEAGPAHAPV- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 177 armfciqD--EHDPISLNYTSGTTADPKGVVISHRGAYLSTLSAIIGWEMGT-CPVYLWTLPMFHCNGWTFTWGTAARGG 253
Cdd:PRK07786 170 -------DipNDSPALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGADInSDVGFVGVPLFHIAGIGSMLPGLLLGA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 254 TSVC--MRHVTAPEIYKNIEMHNVTHMCCVPTVFNILL---KGNSLDLSHRsgpvhVLT-GGSPPPAALVKKVQRL--GF 325
Cdd:PRK07786 243 PTVIypLGAFDPGQLLDVLEAEKVTGIFLVPAQWQAVCaeqQARPRDLALR-----VLSwGAAPASDTLLRQMAATfpEA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 326 QVMHAYGLTEATgPVLfCEwqdewnrlpenqqmeLKARQGLSILG-----LTEVDVR-NKETQESVPRDgkTMGEIVMKG 399
Cdd:PRK07786 318 QILAAFGQTEMS-PVT-CM---------------LLGEDAIRKLGsvgkvIPTVAARvVDENMNDVPVG--EVGEIVYRA 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 400 SSIMKGYLKNPKATYEAFKHGWLNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHP 479
Cdd:PRK07786 379 PTLMSGYWNNPEATAEAFAGGWFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADE 458
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 480 TWGETPCAFVVLekgetNNEDREDKLvtkeRDLIEYCRENLPHFMCPRKVVFLDELPKNGNGKILKPKLR 549
Cdd:PRK07786 459 KWGEVPVAVAAV-----RNDDAALTL----EDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTELR 519
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
193-545 |
1.62e-59 |
|
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: 201.19 E-value: 1.62e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 193 YTSGTTADPKGVVISHRgaylSTLSAIIGW----EMGTCPVYLWTLPMFHCNGWTFTWGTA-ARGGTSVCMRHVTAPEIY 267
Cdd:cd17638 7 FTSGTTGRSKGVMCAHR----QTLRAAAAWadcaDLTEDDRYLIINPFFHTFGYKAGIVAClLTGATVVPVAVFDVDAIL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 268 KNIEMHNVTHMCCVPTVFNILL---KGNSLDLSH-RSGpvhvLTGGSPPPAALVKKVQ-RLGFQ-VMHAYGLTEAtGPVL 341
Cdd:cd17638 83 EAIERERITVLPGPPTLFQSLLdhpGRKKFDLSSlRAA----VTGAATVPVELVRRMRsELGFEtVLTAYGLTEA-GVAT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 342 FCEwqdewnrlPENQQMELKARQGLSILGlTEVDVRNKetqesvprdgktmGEIVMKGSSIMKGYLKNPKATYEAF-KHG 420
Cdd:cd17638 158 MCR--------PGDDAETVATTCGRACPG-FEVRIADD-------------GEVLVRGYNVMQGYLDDPEATAEAIdADG 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 421 WLNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETNNED 500
Cdd:cd17638 216 WLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGVTLTEE 295
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 15218840 501 redklvtkerDLIEYCRENLPHFMCPRKVVFLDELPKNGNGKILK 545
Cdd:cd17638 296 ----------DVIAWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
39-544 |
6.99e-59 |
|
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: 202.32 E-value: 6.99e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 39 RFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFIY 118
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 119 RSFEPLAreilqllssedsnlnlpVIFiheidfpkrvsseesdyecliqrgeptplllarmfciqdehdpislnYTSGTT 198
Cdd:cd05935 81 SELDDLA-----------------LIP-----------------------------------------------YTSGTT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 199 ADPKGVVISHRGAYLSTLSAIIgWEMGTCP-VYLWTLPMFHCNGWTFTWGTA-ARGGTSVCMRHVTAPEIYKNIEMHNVT 276
Cdd:cd05935 97 GLPKGCMHTHFSAAANALQSAV-WTGLTPSdVILACLPLFHVTGFVGSLNTAvYVGGTYVLMARWDRETALELIEKYKVT 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 277 HMCCVPTVFNILLkgNSLDLSHR--SGPVHVLTGGSPPPAALVKKV-QRLGFQVMHAYGLTEATGPVlfcewqdewnrlp 353
Cdd:cd05935 176 FWTNIPTMLVDLL--ATPEFKTRdlSSLKVLTGGGAPMPPAVAEKLlKLTGLRFVEGYGLTETMSQT------------- 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 354 enqQMELKARQGLSILGL--TEVDVR--NKETQESVPrDGKTmGEIVMKGSSIMKGYLKNPKATYEAFKH----GWLNSG 425
Cdd:cd05935 241 ---HTNPPLRPKLQCLGIp*FGVDARviDIETGRELP-PNEV-GEIVVRGPQIFKGYWNRPEETEESFIEikgrRFFRTG 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 426 DVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPTWGETPCAFVVLekgetnneDREDKL 505
Cdd:cd05935 316 DLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVL--------RPEYRG 387
|
490 500 510
....*....|....*....|....*....|....*....
gi 15218840 506 VTKERDLIEYCRENLPHFMCPRKVVFLDELPKNGNGKIL 544
Cdd:cd05935 388 KVTEEDIIEWAREQMAAYKYPREVEFVDELPRSASGKIL 426
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
20-550 |
8.15e-59 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 206.00 E-value: 8.15e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 20 LKRASECYPNRTSI-IYGKTRfTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVL---NPIN 95
Cdd:PRK05605 38 YDNAVARFGDRPALdFFGATT-TYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVvehNPLY 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 96 TrldatsiAAILRHA----KPKILFIYRSFEPLAREILQLLSSED---------------SNLNLPVIFIHE-------- 148
Cdd:PRK05605 117 T-------AHELEHPfedhGARVAIVWDKVAPTVERLRRTTPLETivsvnmiaampllqrLALRLPIPALRKaraaltgp 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 149 ----IDFPKRVSSEESDYECLIQRGEPTPlllarmfciqdeHDPISLNYTSGTTADPKGVVISHRGAYlstLSAIIG--W 222
Cdd:PRK05605 190 apgtVPWETLVDAAIGGDGSDVSHPRPTP------------DDVALILYTSGTTGKPKGAQLTHRNLF---ANAAQGkaW 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 223 --EMGTCP-VYLWTLPMFHCNGWTFTwGTAAR--GGTSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKG---NSL 294
Cdd:PRK05605 255 vpGLGDGPeRVLAALPMFHAYGLTLC-LTLAVsiGGELVLLPAPDIDLILDAMKKHPPTWLPGVPPLYEKIAEAaeeRGV 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 295 DLshrSGPVHVLTGGSPPPAALVKKVQRL-GFQVMHAYGLTEaTGPVLFCewqdewNRLPENQqmelkaRQGLsiLGL-- 371
Cdd:PRK05605 334 DL---SGVRNAFSGAMALPVSTVELWEKLtGGLLVEGYGLTE-TSPIIVG------NPMSDDR------RPGY--VGVpf 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 372 --TEVDVRNKET-QESVPrDGkTMGEIVMKGSSIMKGYLKNPKATYEAFKHGWLNSGDVGVIHPDGHVEIKDRSKDIIIS 448
Cdd:PRK05605 396 pdTEVRIVDPEDpDETMP-DG-EEGELLVRGPQVFKGYWNRPEETAKSFLDGWFRTGDVVVMEEDGFIRIVDRIKELIIT 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 449 GGENISSVEVENIIYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETNNEDredklvtkerDLIEYCRENLPHFMCPRK 528
Cdd:PRK05605 474 GGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPGAALDPE----------GLRAYCREHLTRYKVPRR 543
|
570 580
....*....|....*....|..
gi 15218840 529 VVFLDELPKNGNGKILKPKLRD 550
Cdd:PRK05605 544 FYHVDELPRDQLGKVRRREVRE 565
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
29-550 |
1.86e-58 |
|
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: 201.75 E-value: 1.86e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 29 NRTSIIYGKTRFTWPQTYDRCCRLAASLI-SLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAIL 107
Cdd:cd05941 1 DRIAIVDDGDSITYADLVARAARLANRLLaLGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 108 RHAKPKILfiyrsfeplareilqllssedsnLNLPVIFiheidfpkrvsseesdyecliqrgeptplllarmfciqdehd 187
Cdd:cd05941 81 TDSEPSLV-----------------------LDPALIL------------------------------------------ 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 188 pislnYTSGTTADPKGVVISHRgAYLSTLSAII-GWEMGTCPVYLWTLPMFHCNGWTFT-WGTAARGGTSVCMRHVTAPE 265
Cdd:cd05941 96 -----YTSGTTGRPKGVVLTHA-NLAANVRALVdAWRWTEDDVLLHVLPLHHVHGLVNAlLCPLFAGASVEFLPKFDPKE 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 266 IYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSHRSG-------PVHVLTGGSP--PPAALVKKVQRLGFQVMHAYGLTEa 336
Cdd:cd05941 170 VAISRLMPSITVFMGVPTIYTRLLQYYEAHFTDPQFaraaaaeRLRLMVSGSAalPVPTLEEWEAITGHTLLERYGMTE- 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 337 TGPVLFcewqdewNRLpenqqmELKARQGLSILGLTEVDVRNKETQESVPRDGKTMGEIVMKGSSIMKGYLKNPKATYEA 416
Cdd:cd05941 249 IGMALS-------NPL------DGERRPGTVGMPLPGVQARIVDEETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEE 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 417 FKH-GWLNSGDVGVIHPDGHVEIKDRSK-DIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPTWGETPCAFVVLEKG 494
Cdd:cd05941 316 FTDdGWFKTGDLGVVDEDGYYWILGRSSvDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAG 395
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 15218840 495 ETNNEdredklvtkERDLIEYCRENLPHFMCPRKVVFLDELPKNGNGKILKPKLRD 550
Cdd:cd05941 396 AAALS---------LEELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
20-551 |
1.34e-57 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 201.91 E-value: 1.34e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 20 LKRASECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRLD 99
Cdd:PRK06155 27 LARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 100 ATSIAAILRHAKPKILFIYRSFEPLAREIlqllssEDSNLNLPVIFIheIDFPKRVSSEES-DYECLIQRGEPTPLLLAR 178
Cdd:PRK06155 107 GPQLEHILRNSGARLLVVEAALLAALEAA------DPGDLPLPAVWL--LDAPASVSVPAGwSTAPLPPLDAPAPAAAVQ 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 179 mfciqdEHDPISLNYTSGTTADPKGVVISHRGAYLSTLSAIIGWEMGTCPVYLWTLPMFHCNGWTFTWGTAARGGTSVCM 258
Cdd:PRK06155 179 ------PGDTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTLPLFHTNALNAFFQALLAGATYVLE 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 259 RHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDlSHRSGPVHVLTGGSPPPAALVKKVQRLGFQVMHAYGLTEATG 338
Cdd:PRK06155 253 PRFSASGFWPAVRRHGATVTYLLGAMVSILLSQPARE-SDRAHRVRVALGPGVPAALHAAFRERFGVDLLDGYGSTETNF 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 339 PVlfcewqdeWNRLPENQQMEL-KARQGLSIlglTEVDvrnkETQESVPrDGkTMGEIVMKGS---SIMKGYLKNPKATY 414
Cdd:PRK06155 332 VI--------AVTHGSQRPGSMgRLAPGFEA---RVVD----EHDQELP-DG-EPGELLLRADepfAFATGYFGMPEKTV 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 415 EAFKHGWLNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPTWGETPCAFVVLEKG 494
Cdd:PRK06155 395 EAWRNLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDG 474
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 15218840 495 ETNNEDredklvtkerDLIEYCRENLPHFMCPRKVVFLDELPKNGNGKILKPKLRDI 551
Cdd:PRK06155 475 TALEPV----------ALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLREQ 521
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
20-548 |
1.60e-57 |
|
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: 200.43 E-value: 1.60e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 20 LKRASECYPNRTSIIY--GKTRFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTR 97
Cdd:cd05923 7 LRRAASRAPDACAIADpaRGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 98 LDATSIAAILRHAKpkilfIYRSFEPLAREILQllssEDSNLNLPVIFIHEIDfpkRVSSEESDyecliqrgepTPLLLA 177
Cdd:cd05923 87 LKAAELAELIERGE-----MTAAVIAVDAQVMD----AIFQSGVRVLALSDLV---GLGEPESA----------GPLIED 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 178 RMfciQDEHDPISLNYTSGTTADPKGVVISHRGAYLSTL--SAIIGWEMGTCPVYLWTLPMFHCNG-WTFTWGTAARGGT 254
Cdd:cd05923 145 PP---REPEQPAFVFYTSGTTGLPKGAVIPQRAAESRVLfmSTQAGLRHGRHNVVLGLMPLYHVIGfFAVLVAALALDGT 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 255 SVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILL---KGNSLDLSHRSgpvHVLTGGSPPPAALVKKVQRL--GFQVMH 329
Cdd:cd05923 222 YVVVEEFDPADALKLIEQERVTSLFATPTHLDALAaaaEFAGLKLSSLR---HVTFAGATMPDAVLERVNQHlpGEKVNI 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 330 aYGLTEATGPvLFCEWQDEWNRLPENQQMELKArqgLSILGLTEVDVRNKETqesvprdgktmGEIVMK--GSSIMKGYL 407
Cdd:cd05923 299 -YGTTEAMNS-LYMRDARTGTEMRPGFFSEVRI---VRIGGSPDEALANGEE-----------GELIVAaaADAAFTGYL 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 408 KNPKATYEAFKHGWLNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPTWGETPCA 487
Cdd:cd05923 363 NQPEATAKKLQDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTA 442
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15218840 488 FVVLEKGeTNNEDREDklvtkerdliEYCREN-LPHFMCPRKVVFLDELPKNGNGKILKPKL 548
Cdd:cd05923 443 CVVPREG-TLSADELD----------QFCRASeLADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
19-553 |
5.70e-56 |
|
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: 197.29 E-value: 5.70e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 19 FLKRASECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVlnPINT-- 96
Cdd:COG1021 30 LLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAI--PVFAlp 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 97 --RldATSIAAILRHAKPKILFI---YRSF--EPLAREILQLLSSEDsnlnlPVIFIHEidfpkrvSSEESDYECLIQrg 169
Cdd:COG1021 108 ahR--RAEISHFAEQSEAVAYIIpdrHRGFdyRALARELQAEVPSLR-----HVLVVGD-------AGEFTSLDALLA-- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 170 EPTPLLLARmfciQDEHDPISLNYTSGTTADPKGVVISHRG-AYLSTLSAII-GWEMGTcpVYLWTLPMFH-----CNGW 242
Cdd:COG1021 172 APADLSEPR----PDPDDVAFFQLSGGTTGLPKLIPRTHDDyLYSVRASAEIcGLDADT--VYLAALPAAHnfplsSPGV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 243 TftwGTAARGGTSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILL---KGNSLDLShrSGPVhVLTGGSPPPAALVKK 319
Cdd:COG1021 246 L---GVLYAGGTVVLAPDPSPDTAFPLIERERVTVTALVPPLALLWLdaaERSRYDLS--SLRV-LQVGGAKLSPELARR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 320 V-QRLGFQVMHAYGLTEatGPVLFCEWQDewnrlPEnqqmELKAR-QGLSILGLTEVDVRNkETQESVPrDGKTmGEIVM 397
Cdd:COG1021 320 VrPALGCTLQQVFGMAE--GLVNYTRLDD-----PE----EVILTtQGRPISPDDEVRIVD-EDGNPVP-PGEV-GELLT 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 398 KGSSIMKGYLKNPKATYEAF-KHGWLNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAM 476
Cdd:COG1021 386 RGPYTIRGYYRAPEHNARAFtPDGFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAM 465
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15218840 477 PHPTWGETPCAFVVLekgetnnedREDKLvtKERDLIEYCRE-NLPHFMCPRKVVFLDELPKNGNGKILKPKLRDIAK 553
Cdd:COG1021 466 PDEYLGERSCAFVVP---------RGEPL--TLAELRRFLRErGLAAFKLPDRLEFVDALPLTAVGKIDKKALRAALA 532
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
58-549 |
7.34e-55 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 195.00 E-value: 7.34e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 58 SLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFIyrsfEP-LAREILQLLSSED 136
Cdd:PRK05620 58 ELGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIVA----DPrLAEQLGEILKECP 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 137 SNLNLPVIFIHEIDFPKRVSSEE---SDYECLIQrGEPT----PlllarmfcIQDEHDPISLNYTSGTTADPKGVVISHR 209
Cdd:PRK05620 134 CVRAVVFIGPSDADSAAAHMPEGikvYSYEALLD-GRSTvydwP--------ELDETTAAAICYSTGTTGAPKGVVYSHR 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 210 GAYLSTLSAI----IGWEMGTCpvYLWTLPMFHcngwTFTWG---TAARGGTSVCM--RHVTAPEIYKNIE--MHNVTHm 278
Cdd:PRK05620 205 SLYLQSLSLRttdsLAVTHGES--FLCCVPIYH----VLSWGvplAAFMSGTPLVFpgPDLSAPTLAKIIAtaMPRVAH- 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 279 cCVPTVFNILLKGNSLDLSHRSGPVHVLTGGSPPPAALVKK-VQRLGFQVMHAYGLTEaTGPVlfcewqDEWNRLPENQQ 357
Cdd:PRK05620 278 -GVPTLWIQLMVHYLKNPPERMSLQEIYVGGSAVPPILIKAwEERYGVDVVHVWGMTE-TSPV------GTVARPPSGVS 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 358 MELKAR----QGLSILGLTEVDVRNKETQESVPRDgktMGEIVMKGSSIMKGYLKNPKATYEAFKH-------------- 419
Cdd:PRK05620 350 GEARWAyrvsQGRFPASLEYRIVNDGQVMESTDRN---EGEIQVRGNWVTASYYHSPTEEGGGAAStfrgedvedandrf 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 420 ---GWLNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGET 496
Cdd:PRK05620 427 tadGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGIE 506
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 15218840 497 NNEDredklvTKERdLIEYCRENLPHFMCPRKVVFLDELPKNGNGKILKPKLR 549
Cdd:PRK05620 507 PTRE------TAER-LRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLR 552
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
28-550 |
1.34e-54 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 192.98 E-value: 1.34e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 28 PNRTSIIYGKTR--FTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAA 105
Cdd:PRK13391 11 PDKPAVIMASTGevVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 106 ILRHAKPKILFIYRSFEPLAREILQLLSsedsNLNLPVIFIHEIDFPKRVsseesDYECLIQRGEPTPlllarmfcIQDE 185
Cdd:PRK13391 91 IVDDSGARALITSAAKLDVARALLKQCP----GVRHRLVLDGDGELEGFV-----GYAEAVAGLPATP--------IADE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 186 HDPISLNYTSGTTADPKGVV-------ISHRGAYLSTLSAIIGWEMGTcpVYLWTLPMFHCNGWTFTWGTAARGGTSVCM 258
Cdd:PRK13391 154 SLGTDMLYSSGTTGRPKGIKrplpeqpPDTPLPLTAFLQRLWGFRSDM--VYLSPAPLYHSAPQRAVMLVIRLGGTVIVM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 259 RHVTAPEIYKNIEMHNVTHMCCVPTVFNILLK-----GNSLDLSHRSGPVHvltGGSPPPAaLVKK--VQRLGFQVMHAY 331
Cdd:PRK13391 232 EHFDAEQYLALIEEYGVTHTQLVPTMFSRMLKlpeevRDKYDLSSLEVAIH---AAAPCPP-QVKEqmIDWWGPIIHEYY 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 332 GLTEATGpVLFCEWQdEWnrlpenqqMELKARQGLSILGltEVDVRNKETQESVPrdgKTMGEIVMKGSSIMKgYLKNPK 411
Cdd:PRK13391 308 AATEGLG-FTACDSE-EW--------LAHPGTVGRAMFG--DLHILDDDGAELPP---GEPGTIWFEGGRPFE-YLNDPA 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 412 ATYEAfKH---GWLNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPTWGETPCAF 488
Cdd:PRK13391 372 KTAEA-RHpdgTWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAV 450
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15218840 489 VVLEKGETNNEDRedklvtkERDLIEYCRENLPHFMCPRKVVFLDELPKNGNGKILKPKLRD 550
Cdd:PRK13391 451 VQPVDGVDPGPAL-------AAELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLRD 505
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
19-548 |
1.07e-53 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 191.79 E-value: 1.07e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 19 FLKRASECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRL 98
Cdd:PRK06710 29 YVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLY 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 99 DATSIAAILRHAKPKILFIYRSFEPL------AREILQLLSSEDSNL-----NLPVIFIHEIDFPKRVSSEESDYECLIQ 167
Cdd:PRK06710 109 TERELEYQLHDSGAKVILCLDLVFPRvtnvqsATKIEHVIVTRIADFlpfpkNLLYPFVQKKQSNLVVKVSESETIHLWN 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 168 RGEPTPLLLARMFCiQDEHDPISLNYTSGTTADPKGVVISHRGAYLSTLSAIiGWeMGTC----PVYLWTLPMFHCNGWT 243
Cdd:PRK06710 189 SVEKEVNTGVEVPC-DPENDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGV-QW-LYNCkegeEVVLGVLPFFHVYGMT 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 244 FTWG-TAARGGTSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSHRSGPVHVLTGGSPPPAALVKKVQR 322
Cdd:PRK06710 266 AVMNlSIMQGYKMVLIPKFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIRACISGSAPLPVEVQEKFET 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 323 L-GFQVMHAYGLTEATgPVLFCEWQDEwNRLPENqqmelkarqglsiLGL----TEVDVRNKETQESVPRDgkTMGEIVM 397
Cdd:PRK06710 346 VtGGKLVEGYGLTESS-PVTHSNFLWE-KRVPGS-------------IGVpwpdTEAMIMSLETGEALPPG--EIGEIVV 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 398 KGSSIMKGYLKNPKATYEAFKHGWLNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMP 477
Cdd:PRK06710 409 KGPQIMKGYWNKPEETAAVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVP 488
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15218840 478 HPTWGETPCAFVVLEKGEtnnedredklVTKERDLIEYCRENLPHFMCPRKVVFLDELPKNGNGKILKPKL 548
Cdd:PRK06710 489 DPYRGETVKAFVVLKEGT----------ECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
51-550 |
2.12e-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: 187.54 E-value: 2.12e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 51 RLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILfiyrsfeplareilq 130
Cdd:cd05972 12 KAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAI--------------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 131 llssedsnlnlpvifiheidfpkrvsseesdyecliqrgeptplllarmfcIQDEHDPISLNYTSGTTADPKGVVISHRG 210
Cdd:cd05972 77 ---------------------------------------------------VTDAEDPALIYFTSGTTGLPKGVLHTHSY 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 211 AY--LSTLSAIIGWEMGTCpvyLWTL--PmfhcnGW-TFTWGT----AARGGTSVC--MRHVTAPEIYKNIEMHNVTHMC 279
Cdd:cd05972 106 PLghIPTAAYWLGLRPDDI---HWNIadP-----GWaKGAWSSffgpWLLGATVFVyeGPRFDAERILELLERYGVTSFC 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 280 CVPTVFNILLKgnsLDLSHR--SGPVHVLTGGSP-PPAALVKKVQRLGFQVMHAYGLTEATGPVLFCEWQDewnrlpenq 356
Cdd:cd05972 178 GPPTAYRMLIK---QDLSSYkfSHLRLVVSAGEPlNPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMP--------- 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 357 qmelkARQGlSILGLT---EVDVRNKETQESVPrdgKTMGEIVMKGS--SIMKGYLKNPKATYEAFKHGWLNSGDVGVIH 431
Cdd:cd05972 246 -----VKPG-SMGRPTpgyDVAIIDDDGRELPP---GEEGDIAIKLPppGLFLGYVGDPEKTEASIRGDYYLTGDRAYRD 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 432 PDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETnnedREDKLVtkeRD 511
Cdd:cd05972 317 EDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYE----PSEELA---EE 389
|
490 500 510
....*....|....*....|....*....|....*....
gi 15218840 512 LIEYCRENLPHFMCPRKVVFLDELPKNGNGKILKPKLRD 550
Cdd:cd05972 390 LQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRVELRD 428
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
38-554 |
3.27e-53 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 189.88 E-value: 3.27e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 38 TRFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFI 117
Cdd:PRK13295 54 RRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAESKVLVV 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 118 YRSF-----EPLAREILQLLSSEDSnlnlpVIFIH---EIDFPKRVSSEESDYEcliqRGEPTPLLLARMfciqDEHDPI 189
Cdd:PRK13295 134 PKTFrgfdhAAMARRLRPELPALRH-----VVVVGgdgADSFEALLITPAWEQE----PDAPAILARLRP----GPDDVT 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 190 SLNYTSGTTADPKGVVISHRgaylSTLSAIIGW----EMGTCPVYLWTLPMFHCNGWTFTWGTAARGGTSVCMRHVTAP- 264
Cdd:PRK13295 201 QLIYTSGTTGEPKGVMHTAN----TLMANIVPYaerlGLGADDVILMASPMAHQTGFMYGLMMPVMLGATAVLQDIWDPa 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 265 EIYKNIEMHNVTH-MCCVPTVFNILlkgNSLDLSHRsgPVHVLT----GGSPPPAALVKKVQR-LGFQVMHAYGLTEaTG 338
Cdd:PRK13295 277 RAAELIRTEGVTFtMASTPFLTDLT---RAVKESGR--PVSSLRtflcAGAPIPGALVERARAaLGAKIVSAWGMTE-NG 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 339 PVLFCEWQDEWNRLPEnqqmelkaRQGLSILGLtEVDVRNKETQEsVPRDgkTMGEIVMKGSSIMKGYLKNPKATYEAFK 418
Cdd:PRK13295 351 AVTLTKLDDPDERAST--------TDGCPLPGV-EVRVVDADGAP-LPAG--QIGRLQVRGCSNFGGYLKRPQLNGTDAD 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 419 hGWLNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETnn 498
Cdd:PRK13295 419 -GWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPGQS-- 495
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 15218840 499 edredklVTKErDLIEYCREN---LPHFmcPRKVVFLDELPKNGNGKILKPKLRDIAKG 554
Cdd:PRK13295 496 -------LDFE-EMVEFLKAQkvaKQYI--PERLVVRDALPRTPSGKIQKFRLREMLRG 544
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
65-550 |
1.31e-52 |
|
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: 186.81 E-value: 1.31e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 65 DVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFIYRSFEPLAREILQLLSSEDSNLNLPVI 144
Cdd:cd05929 21 DVYSIALNRNARAAAAEGVWIADGVYIYLINSILTVFAAAAAWKCGACPAYKSSRAPRAEACAIIEIKAAALVCGLFTGG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 145 FIHEIDfpkrvsseESDYECLiqRGEPTPLllarmfcIQDEHDPISLNYTSGTTADPKGVVISHRGAYLSTLsAIIGWEM 224
Cdd:cd05929 101 GALDGL--------EDYEAAE--GGSPETP-------IEDEAAGWKMLYSGGTTGRPKGIKRGLPGGPPDND-TLMAAAL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 225 GTCP----VYLWTLPMFHCNGWTFTWGTAARGGTSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLK-----GNSLD 295
Cdd:cd05929 163 GFGPgadsVYLSPAPLYHAAPFRWSMTALFMGGTLVLMEKFDPEEFLRLIERYRVTFAQFVPTMFVRLLKlpeavRNAYD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 296 LSHRSGPVHVltgGSPPPAALVKKVQRLGFQVMHA-YGLTEATGpVLFCEwQDEWnrlpenqqmeLKARQGLSILGLTEV 374
Cdd:cd05929 243 LSSLKRVIHA---AAPCPPWVKEQWIDWGGPIIWEyYGGTEGQG-LTIIN-GEEW----------LTHPGSVGRAVLGKV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 375 DVRNKETQESVPRdgkTMGEIVMKGSSiMKGYLKNPKATYEAF-KHGWLNSGDVGVIHPDGHVEIKDRSKDIIISGGENI 453
Cdd:cd05929 308 HILDEDGNEVPPG---EIGEVYFANGP-GFEYTNDPEKTAAARnEGGWSTLGDVGYLDEDGYLYLTDRRSDMIISGGVNI 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 454 SSVEVENIIYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETNNEDREDklvtkerDLIEYCRENLPHFMCPRKVVFLD 533
Cdd:cd05929 384 YPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQPAPGADAGTALAE-------ELIAFLRDRLSRYKCPRSIEFVA 456
|
490
....*....|....*..
gi 15218840 534 ELPKNGNGKILKPKLRD 550
Cdd:cd05929 457 ELPRDDTGKLYRRLLRD 473
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
19-534 |
4.75e-52 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 188.00 E-value: 4.75e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 19 FLKRASEcYPNRTSIIY----GKTRFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPI 94
Cdd:COG1022 17 LRRRAAR-FPDRVALREkedgIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVPI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 95 NTRLDATSIAAILRHAKPKILFIyrSFEPLAREILQLLSsedsnlNLP----VIFIHEIDfpKRVSSEESDYECLIQRGE 170
Cdd:COG1022 96 YPTSSAEEVAYILNDSGAKVLFV--EDQEQLDKLLEVRD------ELPslrhIVVLDPRG--LRDDPRLLSLDELLALGR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 171 P--TPLLLARMFCIQDEHDPISLNYTSGTTADPKGVVISHRgAYLSTLSAIIG-WEMGTCPVYLWTLPMFHCNGWTFTWG 247
Cdd:COG1022 166 EvaDPAELEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHR-NLLSNARALLErLPLGPGDRTLSFLPLAHVFERTVSYY 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 248 TAARGGTsvcmrhVTAPEIYKNIeMHNV-----THMCCVPTVF-----NILLKGNS------------LDLSHRSGPvHV 305
Cdd:COG1022 245 ALAAGAT------VAFAESPDTL-AEDLrevkpTFMLAVPRVWekvyaGIQAKAEEagglkrklfrwaLAVGRRYAR-AR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 306 LTGGSPPP--------------------------------AALVKKVQR----LGFQVMHAYGLTEATGPVLFcewqdew 349
Cdd:COG1022 317 LAGKSPSLllrlkhaladklvfsklrealggrlrfavsggAALGPELARffraLGIPVLEGYGLTETSPVITV------- 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 350 NRLPENQqmelkarqglsiLG-----LTEVDVRnketqesVPRDGktmgEIVMKGSSIMKGYLKNPKATYEAF-KHGWLN 423
Cdd:COG1022 390 NRPGDNR------------IGtvgppLPGVEVK-------IAEDG----EILVRGPNVMKGYYKNPEATAEAFdADGWLH 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 424 SGDVGVIHPDGHVEIKDRSKDIII-SGGENISSVEVENIIYKYPKVLETAVVA--MPHPTwgetpcAFVVL--------- 491
Cdd:COG1022 447 TGDIGELDEDGFLRITGRKKDLIVtSGGKNVAPQPIENALKASPLIEQAVVVGdgRPFLA------ALIVPdfealgewa 520
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 15218840 492 -EKG---ETNNEDREDKLVTKE-RDLIEYCRENLPHFMCPRKVVFLDE 534
Cdd:COG1022 521 eENGlpyTSYAELAQDPEVRALiQEEVDRANAGLSRAEQIKRFRLLPK 568
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
18-548 |
1.78e-51 |
|
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: 183.68 E-value: 1.78e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 18 TFLKRASECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVlnPINT- 96
Cdd:cd05920 19 DLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAV--PVLAl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 97 -RLDATSIAAILRHAKPKILFIYRSFEP-----LAREILqllssedsnlnlpvifiHEIdfpkrvsseesdyecliqrGE 170
Cdd:cd05920 97 pSHRRSELSAFCAHAEAVAYIVPDRHAGfdhraLARELA-----------------ESI-------------------PE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 171 PTPLLLarmfciqdehdpislnyTSGTTADPKGVVISHRG-AYLSTLSAIIGWeMGTCPVYLWTLPMFH-----CNGwtf 244
Cdd:cd05920 141 VALFLL-----------------SGGTTGTPKLIPRTHNDyAYNVRASAEVCG-LDQDTVYLAVLPAAHnfplaCPG--- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 245 TWGTAARGGTSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVfnILLKGNSLDLSHRS-GPVHVLTGG----SPPPAALVKK 319
Cdd:cd05920 200 VLGTLLAGGRVVLAPDPSPDAAFPLIEREGVTVTALVPAL--VSLWLDAAASRRADlSSLRLLQVGgarlSPALARRVPP 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 320 VqrLGFQVMHAYGLTEAtgpvLFCewqdeWNRL--PENQQMElkaRQGLSILGLTEVDVRNKETQEsVPrDGkTMGEIVM 397
Cdd:cd05920 278 V--LGCTLQQVFGMAEG----LLN-----YTRLddPDEVIIH---TQGRPMSPDDEIRVVDEEGNP-VP-PG-EEGELLT 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 398 KGSSIMKGYLKNPKATYEAF-KHGWLNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAM 476
Cdd:cd05920 341 RGPYTIRGYYRAPEHNARAFtPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAM 420
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15218840 477 PHPTWGETPCAFVVLEKGETNNEDREDKLvtKERDLIEYCRenlphfmcPRKVVFLDELPKNGNGKILKPKL 548
Cdd:cd05920 421 PDELLGERSCAFVVLRDPPPSAAQLRRFL--RERGLAAYKL--------PDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
27-549 |
3.05e-51 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 184.12 E-value: 3.05e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 27 YPNRTSIIY----GKTR-FTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRLDAT 101
Cdd:PRK08008 20 YGHKTALIFessgGVVRrYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLRE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 102 SIAAILRHAKPKILFIYRSFEPLAREILQllssEDSNLnLPVIFIheidfpKRVSSEESDYECLIQRgeptplLLARMFC 181
Cdd:PRK08008 100 ESAWILQNSQASLLVTSAQFYPMYRQIQQ----EDATP-LRHICL------TRVALPADDGVSSFTQ------LKAQQPA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 182 IQDEHDPISLN------YTSGTTADPKGVVISH-----RGAYLStlsaiigWE--MGTCPVYLWTLPMFH----CNGW-- 242
Cdd:PRK08008 163 TLCYAPPLSTDdtaeilFTSGTTSRPKGVVITHynlrfAGYYSA-------WQcaLRDDDVYLTVMPAFHidcqCTAAma 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 243 TFTwgtaaRGGTSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLkgnsldlshrsgpvhvltggSPPPAALVKK--- 319
Cdd:PRK08008 236 AFS-----AGATFVLLEKYSARAFWGQVCKYRATITECIPMMIRTLM--------------------VQPPSANDRQhcl 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 320 -----------------VQRLGFQVMHAYGLTEATGPVLFCEWQDEwNRLPEnqqmelKARQGLSIlgltEVDVRNKETQ 382
Cdd:PRK08008 291 revmfylnlsdqekdafEERFGVRLLTSYGMTETIVGIIGDRPGDK-RRWPS------IGRPGFCY----EAEIRDDHNR 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 383 ESVPrdgKTMGEIVMKG---SSIMKGYLKNPKATYEAFK-HGWLNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEV 458
Cdd:PRK08008 360 PLPA---GEIGEICIKGvpgKTIFKEYYLDPKATAKVLEaDGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVEL 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 459 ENIIYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETNNEDredklvtkerDLIEYCRENLPHFMCPRKVVFLDELPKN 538
Cdd:PRK08008 437 ENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEE----------EFFAFCEQNMAKFKVPSYLEIRKDLPRN 506
|
570
....*....|.
gi 15218840 539 GNGKILKPKLR 549
Cdd:PRK08008 507 CSGKIIKKNLK 517
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
22-560 |
6.35e-50 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 181.10 E-value: 6.35e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 22 RASECYPNRTSIIYGK-TRFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRLDA 100
Cdd:PRK06087 31 QTARAMPDKIAVVDNHgASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWRE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 101 TSIAAILRHAKPKILFI-----YRSFEPLAREILQLLSSEDsnlnlPVIFIheiDFPKRVSSEESdYECLIQRGEPTpll 175
Cdd:PRK06087 111 AELVWVLNKCQAKMFFAptlfkQTRPVDLILPLQNQLPQLQ-----QIVGV---DKLAPATSSLS-LSQIIADYEPL--- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 176 laRMFCIQDEHDPISLNYTSGTTADPKGVVISHRG------AYLSTLSaiIGWEmgtcPVYLWTLPMFHCNGwtFTWGTA 249
Cdd:PRK06087 179 --TTAITTHGDELAAVLFTSGTEGLPKGVMLTHNNilaserAYCARLN--LTWQ----DVFMMPAPLGHATG--FLHGVT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 250 AR---GGTSVCMRHVTAPEIYKNIEMHNVT-HMCCVPTVFNILlkgNSLDlshrSGPVHV------LTGGSPPPAALVKK 319
Cdd:PRK06087 249 APfliGARSVLLDIFTPDACLALLEQQRCTcMLGATPFIYDLL---NLLE----KQPADLsalrffLCGGTTIPKKVARE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 320 VQRLGFQVMHAYGLTEATgPVLFCEWQD--EWNrlpenqqmelKARQGLSILGLtEVDVRNKETQEsVPRDgkTMGEIVM 397
Cdd:PRK06087 322 CQQRGIKLLSVYGSTESS-PHAVVNLDDplSRF----------MHTDGYAAAGV-EIKVVDEARKT-LPPG--CEGEEAS 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 398 KGSSIMKGYLKNPKATYEAF-KHGWLNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAM 476
Cdd:PRK06087 387 RGPNVFMGYLDEPELTARALdEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAM 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 477 PHPTWGETPCAFVVLeKGETNNEDREdklvtkerDLIEY-CRENLPHFMCPRKVVFLDELPKNGNGKILKPKLR-DIAKG 554
Cdd:PRK06087 467 PDERLGERSCAYVVL-KAPHHSLTLE--------EVVAFfSRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRkDIMRR 537
|
....*.
gi 15218840 555 LVAEDE 560
Cdd:PRK06087 538 LTQDVC 543
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
25-549 |
8.86e-50 |
|
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: 179.87 E-value: 8.86e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 25 ECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIA 104
Cdd:cd05959 15 EGRGDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 105 AILRHAKPKILFIYRSFEPLAREILQLLSSEDSNLNLPVifiheidfPKRVSSEESDYECLIqRGEPTPLLLARMFCiqd 184
Cdd:cd05959 95 YYLEDSRARVVVVSGELAPVLAAALTKSEHTLVVLIVSG--------GAGPEAGALLLAELV-AAEAEQLKPAATHA--- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 185 eHDPISLNYTSGTTADPKGVVISHRGAYlSTLSAIIGWEMGTCP--VYLWTLPMFHC----NGWTFTWGTaarGGTSVCM 258
Cdd:cd05959 163 -DDPAFWLYSSGSTGRPKGVVHLHADIY-WTAELYARNVLGIREddVCFSAAKLFFAyglgNSLTFPLSV---GATTVLM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 259 -RHVTAPEIYKNIEMHNVTHMCCVPTVFNILLkgNSLDLSHRsGPVHV---LTGGSPPPAALVKKVQ-RLGFQVMHAYGL 333
Cdd:cd05959 238 pERPTPAAVFKRIRRYRPTVFFGVPTLYAAML--AAPNLPSR-DLSSLrlcVSAGEALPAEVGERWKaRFGLDILDGIGS 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 334 TEATGpvLFCEwqdewNRlPENQQMelkARQGLSILGLtEVDVRNKETQEsVPrDGKTmGEIVMKGSSIMKGYLKNPKAT 413
Cdd:cd05959 315 TEMLH--IFLS-----NR-PGRVRY---GTTGKPVPGY-EVELRDEDGGD-VA-DGEP-GELYVRGPSSATMYWNNRDKT 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 414 YEAFKHGWLNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPTWGETPCAFVVLEK 493
Cdd:cd05959 380 RDTFQGEWTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRP 459
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 15218840 494 GETNNEdredklvTKERDLIEYCRENLPHFMCPRKVVFLDELPKNGNGKILKPKLR 549
Cdd:cd05959 460 GYEDSE-------ALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
20-549 |
1.26e-49 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 180.38 E-value: 1.26e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 20 LKRASECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRLD 99
Cdd:PLN02860 13 LTRLATLRGNAVVTISGNRRRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 100 ATSIAAILRHAKPKILFIYRS----FEPLARE-----ILQLLSSEDSNlnlpVIFIHEIDFpkrVSSEEsdyecLIQRGE 170
Cdd:PLN02860 93 FEEAKSAMLLVRPVMLVTDETcsswYEELQNDrlpslMWQVFLESPSS----SVFIFLNSF---LTTEM-----LKQRAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 171 PTPLLlarMFCIQDEhDPISLNYTSGTTADPKGVVISHRGAYLSTLS--AIIGWemGTCPVYLWTLPMFHCNGWTFTWGT 248
Cdd:PLN02860 161 GTTEL---DYAWAPD-DAVLICFTSGTTGRPKGVTISHSALIVQSLAkiAIVGY--GEDDVYLHTAPLCHIGGLSSALAM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 249 AARGGTSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSHRSGPV--HVLTGGSPPPAALVKKVQRL--G 324
Cdd:PLN02860 235 LMVGACHVLLPKFDAKAALQAIKQHNVTSMITVPAMMADLISLTRKSMTWKVFPSvrKILNGGGSLSSRLLPDAKKLfpN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 325 FQVMHAYGLTEATGPVLFCEWQDEWNRLPENQQMELKARQGLSI-------LGLTEVDVRNKETQESVPRDGKtmgeIVM 397
Cdd:PLN02860 315 AKLFSAYGMTEACSSLTFMTLHDPTLESPKQTLQTVNQTKSSSVhqpqgvcVGKPAPHVELKIGLDESSRVGR----ILT 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 398 KGSSIMKGYLKNPKATYEAF-KHGWLNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAM 476
Cdd:PLN02860 391 RGPHVMLGYWGQNSETASVLsNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGV 470
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15218840 477 PHPTWGETPCAFVVLEKG----ETNNEDREDKLVTKERDLIEYCRE-NLPHFMCPRK-VVFLDELPKNGNGKILKPKLR 549
Cdd:PLN02860 471 PDSRLTEMVVACVRLRDGwiwsDNEKENAKKNLTLSSETLRHHCREkNLSRFKIPKLfVQWRKPFPLTTTGKIRRDEVR 549
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
28-543 |
3.94e-49 |
|
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: 176.56 E-value: 3.94e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 28 PNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAIL 107
Cdd:cd05930 1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 108 RHAKPKILFiyrsfeplareilqllsSEDSNLNlPVIfiheidfpkrvsseesdyecliqrgeptplllarmfciqdehd 187
Cdd:cd05930 81 EDSGAKLVL-----------------TDPDDLA-YVI------------------------------------------- 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 188 pislnYTSGTTADPKGVVISHRG--AYLSTLSAIIGweMGTCPVYL-WTLPMFHCNGWTFtWGTAARGGTSVCMR---HV 261
Cdd:cd05930 100 -----YTSGSTGKPKGVMVEHRGlvNLLLWMQEAYP--LTPGDRVLqFTSFSFDVSVWEI-FGALLAGATLVVLPeevRK 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 262 TAPEIYKNIEMHNVTHMCCVPTVFNILLkgNSLDLSHRSGPVHVLTGGSPPPAALVKKVQRLGF--QVMHAYGLTEATGP 339
Cdd:cd05930 172 DPEALADLLAEEGITVLHLTPSLLRLLL--QELELAALPSLRLVLVGGEALPPDLVRRWRELLPgaRLVNLYGPTEATVD 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 340 VLFCewqdewnRLPENqqmELKARQ---GLSILGlTEVDVRNkETQESVPrDGKtMGEIVMKGSSIMKGYLKNPKATYEA 416
Cdd:cd05930 250 ATYY-------RVPPD---DEEDGRvpiGRPIPN-TRVYVLD-ENLRPVP-PGV-PGELYIGGAGLARGYLNRPELTAER 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 417 FKHGWLN-------SGDVGVIHPDGHVEIKDRSKDII-ISG-----GEnissveVENIIYKYPKVLETAVVAMPHPTWGE 483
Cdd:cd05930 316 FVPNPFGpgermyrTGDLVRWLPDGNLEFLGRIDDQVkIRGyrielGE------IEAALLAHPGVREAAVVAREDGDGEK 389
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 484 TPCAFVVLEKGETNNEDredklvtkerDLIEYCRENLPHFMCPRKVVFLDELPKNGNGKI 543
Cdd:cd05930 390 RLVAYVVPDEGGELDEE----------ELRAHLAERLPDYMVPSAFVVLDALPLTPNGKV 439
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
40-547 |
4.87e-49 |
|
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: 176.25 E-value: 4.87e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 40 FTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFIyr 119
Cdd:cd05907 6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFV-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 120 sfeplareilqllssedsnlnlpvifiheidfpkrvsseesdyecliqrGEPTplllarmfciqdehDPISLNYTSGTTA 199
Cdd:cd05907 84 -------------------------------------------------EDPD--------------DLATIIYTSGTTG 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 200 DPKGVVISHRGaYLSTLSAIIG-WEMGTCPVYLWTLPMFHCNGWTF-TWGTAARGgtsVCMRHVTAPE-IYKNIEMHNVT 276
Cdd:cd05907 101 RPKGVMLSHRN-ILSNALALAErLPATEGDRHLSFLPLAHVFERRAgLYVPLLAG---ARIYFASSAEtLLDDLSEVRPT 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 277 HMCCVPTVFNILLKGNSLDLSHR---------SGP--VHVLTGGSPPPAALVKKVQRLGFQVMHAYGLTEATGPVLFCEW 345
Cdd:cd05907 177 VFLAVPRVWEKVYAAIKVKAVPGlkrklfdlaVGGrlRFAASGGAPLPAELLHFFRALGIPVYEGYGLTETSAVVTLNPP 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 346 QDewNRLpenqqmelkARQGLSILGlteVDVRNKETqesvprdgktmGEIVMKGSSIMKGYLKNPKATYEAFKH-GWLNS 424
Cdd:cd05907 257 GD--NRI---------GTVGKPLPG---VEVRIADD-----------GEILVRGPNVMLGYYKNPEATAEALDAdGWLHT 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 425 GDVGVIHPDGHVEIKDRSKDIII-SGGENISSVEVENIIYKYPKVLETAVVA--MPHPTwgetpcAFVVL---------- 491
Cdd:cd05907 312 GDLGEIDEDGFLHITGRKKDLIItSGGKNISPEPIENALKASPLISQAVVIGdgRPFLV------ALIVPdpealeawae 385
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15218840 492 EKGETNNEDRE---DKLVTKE-RDLIEYCRENLPHFMCPRKVVFLDELPKNGNGKI---LKPK 547
Cdd:cd05907 386 EHGIAYTDVAElaaNPAVRAEiEAAVEAANARLSRYEQIKKFLLLPEPFTIENGELtptLKLK 448
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
39-550 |
6.47e-49 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 176.92 E-value: 6.47e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 39 RFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILfiy 118
Cdd:PRK09088 22 RWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLL--- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 119 rsfepLAREILQLLSSEDSNLNlpvIFIHEIDfpkrvsSEESDYECLIQRGEPTPLLlarmfciqdehdpislnYTSGTT 198
Cdd:PRK09088 99 -----LGDDAVAAGRTDVEDLA---AFIASAD------ALEPADTPSIPPERVSLIL-----------------FTSGTS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 199 ADPKGVVISHRGAYLSTLSAIIGWEMGTCPVYLWTLPMFHCNGW-TFTWGTAARGGT---------SVCMRHVTAPEIyk 268
Cdd:PRK09088 148 GQPKGVMLSERNLQQTAHNFGVLGRVDAHSSFLCDAPMFHIIGLiTSVRPVLAVGGSilvsngfepKRTLGRLGDPAL-- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 269 niemhNVTHMCCVPTVFNILLKGNSLDLSHRSGPVHVLTGGSPPPAALVKKVQRLGFQVMHAYGLTEAtGPVLfcewqde 348
Cdd:PRK09088 226 -----GITHYFCVPQMAQAFRAQPGFDAAALRHLTALFTGGAPHAAEDILGWLDDGIPMVDGFGMSEA-GTVF------- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 349 wnRLPENQQMeLKARQGLSILGLTEVDVRNKETQESVPRDGKTmGEIVMKGSSIMKGYLKNPKATYEAF-KHGWLNSGDV 427
Cdd:PRK09088 293 --GMSVDCDV-IRAKAGAAGIPTPTVQTRVVDDQGNDCPAGVP-GELLLRGPNLSPGYWRRPQATARAFtGDGWFRTGDI 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 428 GVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETNNEDRedklvt 507
Cdd:PRK09088 369 ARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAPLDLER------ 442
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 15218840 508 kerdLIEYCRENLPHFMCPRKVVFLDELPKNGNGKILKPKLRD 550
Cdd:PRK09088 443 ----IRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLRD 481
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
23-551 |
1.09e-48 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 177.43 E-value: 1.09e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 23 ASECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRLDATS 102
Cdd:PRK07788 58 AARRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQ 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 103 IAAILRHAKPKILFIYRSFEPLAREIlqllssEDSNLNLPVIFIHEIDFPKRVSSEESdYECLIQRGEPTPLLLARmfci 182
Cdd:PRK07788 138 LAEVAAREGVKALVYDDEFTDLLSAL------PPDLGRLRAWGGNPDDDEPSGSTDET-LDDLIAGSSTAPLPKPP---- 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 183 qdEHDPISLnYTSGTTADPKGVVISHRGAyLSTLSAI---IGWEMGTcpVYLWTLPMFHCNGW-TFTWGTAArGGTSVCM 258
Cdd:PRK07788 207 --KPGGIVI-LTSGTTGTPKGAPRPEPSP-LAPLAGLlsrVPFRAGE--TTLLPAPMFHATGWaHLTLAMAL-GSTVVLR 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 259 RHVTAPEIYKNIEMHNVTHMCCVPTVFNILLK-----GNSLDLShrSGPVhVLTGGSPPPAALVKKVQ-RLGFQVMHAYG 332
Cdd:PRK07788 280 RRFDPEATLEDIAKHKATALVVVPVMLSRILDlgpevLAKYDTS--SLKI-IFVSGSALSPELATRALeAFGPVLYNLYG 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 333 LTE----------------ATG--PVLFCE---WQDEWNRLPENQQMELKARQGLSILGLTevDVRNKETqesvprdgkt 391
Cdd:PRK07788 357 STEvafatiatpedlaeapGTVgrPPKGVTvkiLDENGNEVPRGVVGRIFVGNGFPFEGYT--DGRDKQI---------- 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 392 mgeivmkgssimkgylknpkatyeafKHGWLNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLET 471
Cdd:PRK07788 425 --------------------------IDGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEA 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 472 AVVAMPHPTWGETPCAFVVLEKGETNNEDredklvtkerDLIEYCRENLPHFMCPRKVVFLDELPKNGNGKILKPKLRDI 551
Cdd:PRK07788 479 AVIGVDDEEFGQRLRAFVVKAPGAALDED----------AIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELREM 548
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
59-551 |
4.72e-48 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 176.19 E-value: 4.72e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 59 LNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFIyrsfeplAREILQLLSSedsn 138
Cdd:PLN02574 87 MGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFT-------SPENVEKLSP---- 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 139 LNLPVIFIHE-IDFPKRVSSEESDYECLIQRGEPTPLLLARmfciqdEHDPISLNYTSGTTADPKGVVISHRGaYLSTLS 217
Cdd:PLN02574 156 LGVPVIGVPEnYDFDSKRIEFPKFYELIKEDFDFVPKPVIK------QDDVAAIMYSSGTTGASKGVVLTHRN-LIAMVE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 218 AIIGWEM------GTCPVYLWTLPMFHCNGWT-FTWGTAARGGTSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLK 290
Cdd:PLN02574 229 LFVRFEAsqyeypGSDNVYLAALPMFHIYGLSlFVVGLLSLGSTIVVMRRFDASDMVKVIDRFKVTHFPVVPPILMALTK 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 291 ------GNSLDlshrsGPVHVLTGGSPPPAALVKK-VQRLG-FQVMHAYGLTEATGPvlfcewqdewnrlpENQQMELKA 362
Cdd:PLN02574 309 kakgvcGEVLK-----SLKQVSCGAAPLSGKFIQDfVQTLPhVDFIQGYGMTESTAV--------------GTRGFNTEK 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 363 RQGLSILGLTEVDVRNK----ETQESVPRDGKtmGEIVMKGSSIMKGYLKNPKAT-YEAFKHGWLNSGDVGVIHPDGHVE 437
Cdd:PLN02574 370 LSKYSSVGLLAPNMQAKvvdwSTGCLLPPGNC--GELWIQGPGVMKGYLNNPKATqSTIDKDGWLRTGDIAYFDEDGYLY 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 438 IKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETnnedredklvTKERDLIEYCR 517
Cdd:PLN02574 448 IVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGST----------LSQEAVINYVA 517
|
490 500 510
....*....|....*....|....*....|....
gi 15218840 518 ENLPHFMCPRKVVFLDELPKNGNGKILKPKLRDI 551
Cdd:PLN02574 518 KQVAPYKKVRKVVFVQSIPKSPAGKILRRELKRS 551
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
9-549 |
5.04e-48 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 175.55 E-value: 5.04e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 9 ANNVPLTPITFlKRASEcYPNRTSIIYGKT--RFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPM 86
Cdd:PLN02246 20 PNHLPLHDYCF-ERLSE-FSDRPCLIDGATgrVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 87 AGAVL---NPINTrldATSIAAILRHAKPKILFIyrsfEPLAREILQLLSSEDsnlNLPVIFIHE-----IDFPKRVSSE 158
Cdd:PLN02246 98 RGAVTttaNPFYT---PAEIAKQAKASGAKLIIT----QSCYVDKLKGLAEDD---GVTVVTIDDppegcLHFSELTQAD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 159 ESDyecliqrgEPTPLllarmfcIQDEhDPISLNYTSGTTADPKGVVISHRGAYLSTLSAIIG----WEMGTCPVYLWTL 234
Cdd:PLN02246 168 ENE--------LPEVE-------ISPD-DVVALPYSSGTTGLPKGVMLTHKGLVTSVAQQVDGenpnLYFHSDDVILCVL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 235 PMFHCNGWTFTWGTAAR-GGTSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKG---NSLDLSH-RSgpvhVLTGG 309
Cdd:PLN02246 232 PMFHIYSLNSVLLCGLRvGAAILIMPKFEIGALLELIQRHKVTIAPFVPPIVLAIAKSpvvEKYDLSSiRM----VLSGA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 310 SPppaaLVKKVQR----------LGfqvmHAYGLTEAtGPVL-----FCEwqdewnrlpenQQMELKARQGLSILGLTEV 374
Cdd:PLN02246 308 AP----LGKELEDafraklpnavLG----QGYGMTEA-GPVLamclaFAK-----------EPFPVKSGSCGTVVRNAEL 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 375 DVRNKETQESVPRDgkTMGEIVMKGSSIMKGYLKNPKATYEAF-KHGWLNSGDVGVIHPDGHVEIKDRSKDIIISGGENI 453
Cdd:PLN02246 368 KIVDPETGASLPRN--QPGEICIRGPQIMKGYLNDPEATANTIdKDGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQV 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 454 SSVEVENIIYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETNNEDREDKLVTKErdLIEYCRENlphfmcprKVVFLD 533
Cdd:PLN02246 446 APAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNGSEITEDEIKQFVAKQ--VVFYKRIH--------KVFFVD 515
|
570
....*....|....*.
gi 15218840 534 ELPKNGNGKILKPKLR 549
Cdd:PLN02246 516 SIPKAPSGKILRKDLR 531
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
23-550 |
1.48e-47 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 174.18 E-value: 1.48e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 23 ASECyPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRLDATS 102
Cdd:PRK13382 53 AQRC-PDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 103 IAAILRHAKPKILFIYRSFEPL----------AREILQLLSSEDSNLNLPVIFIHEIDFPKRvsseesdyecliqRGEPT 172
Cdd:PRK13382 132 LAEVVTREGVDTVIYDEEFSATvdraladcpqATRIVAWTDEDHDLTVEVLIAAHAGQRPEP-------------TGRKG 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 173 PLLLarmfciqdehdpislnYTSGTTADPKGVVISHRGAYlSTLSAI---IGWEMGTcPVYLwTLPMFHcngwtfTWG-- 247
Cdd:PRK13382 199 RVIL----------------LTSGTTGTPKGARRSGPGGI-GTLKAIldrTPWRAEE-PTVI-VAPMFH------AWGfs 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 248 ---TAARGGTSVCMRHVTAPE-IYKNIEMHNVTHMCCVPTVFNILLK--GNSLD-LSHRSGPVHVLTGGSPPPAALVKKV 320
Cdd:PRK13382 254 qlvLAASLACTIVTRRRFDPEaTLDLIDRHRATGLAVVPVMFDRIMDlpAEVRNrYSGRSLRFAAASGSRMRPDVVIAFM 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 321 QRLGFQVMHAYGLTEATgpVLFCEWQDEWNRLPENQQmelKARQGlsilglTEVDVRNKETQEsVPrDGKTmGEIVMKGS 400
Cdd:PRK13382 334 DQFGDVIYNNYNATEAG--MIATATPADLRAAPDTAG---RPAEG------TEIRILDQDFRE-VP-TGEV-GTIFVRND 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 401 SIMKGYlkNPKATYEaFKHGWLNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPT 480
Cdd:PRK13382 400 TQFDGY--TSGSTKD-FHDGFMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQ 476
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 481 WGETPCAFVVLekgetnnedrEDKLVTKERDLIEYCRENLPHFMCPRKVVFLDELPKNGNGKILKPKLRD 550
Cdd:PRK13382 477 YGQRLAAFVVL----------KPGASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQA 536
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
33-550 |
3.03e-47 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 172.96 E-value: 3.03e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 33 IIYGKTRFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKP 112
Cdd:PRK12406 5 IISGDRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 113 KILFIYRS-FEPLAREILQllssedsnlNLPVIFIH---EIDFPKRVSSEES-------DYECLIQRGEP-TPLLLARmf 180
Cdd:PRK12406 85 RVLIAHADlLHGLASALPA---------GVTVLSVPtppEIAAAYRISPALLtppagaiDWEGWLAQQEPyDGPPVPQ-- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 181 ciqdehdPISLNYTSGTTADPKGV-----VISHRGAYLSTLSAIIGWEMGTcpVYLWTLPMFHCNGWTFTWGTAARGGTS 255
Cdd:PRK12406 154 -------PQSMIYTSGTTGHPKGVrraapTPEQAAAAEQMRALIYGLKPGI--RALLTGPLYHSAPNAYGLRAGRLGGVL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 256 VCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLK-----GNSLDLSHRSgpvHVLTGGSPPPAAlVKK--VQRLGFQVM 328
Cdd:PRK12406 225 VLQPRFDPEELLQLIERHRITHMHMVPTMFIRLLKlpeevRAKYDVSSLR---HVIHAAAPCPAD-VKRamIEWWGPVIY 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 329 HAYGLTEaTGPVLFCEWQDeWNRLPENQQmelKARQG--LSILGltevdvrnkETQESVPrDGkTMGEIVMKGSSIMK-G 405
Cdd:PRK12406 301 EYYGSTE-SGAVTFATSED-ALSHPGTVG---KAAPGaeLRFVD---------EDGRPLP-QG-EIGEIYSRIAGNPDfT 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 406 YLKNPKATYEAFKHGWLNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPTWGETP 485
Cdd:PRK12406 365 YHNKPEKRAEIDRGGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEAL 444
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15218840 486 CAFVVLEKGETNNEDredklvtkerDLIEYCRENLPHFMCPRKVVFLDELPKNGNGKILKPKLRD 550
Cdd:PRK12406 445 MAVVEPQPGATLDEA----------DIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLRD 499
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
193-549 |
7.27e-47 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 170.94 E-value: 7.27e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 193 YTSGTTADPKGVVIShRGAYLSTLSAII-GWEmgtcpvylWT--------LPMFHCNGWTF-TWGTAARGGTsvcMRHVT 262
Cdd:PRK07787 135 YTSGTTGPPKGVVLS-RRAIAADLDALAeAWQ--------WTaddvlvhgLPLFHVHGLVLgVLGPLRIGNR---FVHTG 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 263 --APEIYKNIEMHNVTHMCCVPTVFNILlkGNSLDLSHRSGPVHVLTGGSPP-PAALVKKVQRL-GFQVMHAYGLTE--- 335
Cdd:PRK07787 203 rpTPEAYAQALSEGGTLYFGVPTVWSRI--AADPEAARALRGARLLVSGSAAlPVPVFDRLAALtGHRPVERYGMTEtli 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 336 -----ATGPvlfcewqdewnrlpenqqmelkARQGLSILGLTEVDVR-NKETQESVPRDGKTMGEIVMKGSSIMKGYLKN 409
Cdd:PRK07787 281 tlstrADGE----------------------RRPGWVGLPLAGVETRlVDEDGGPVPHDGETVGELQVRGPTLFDGYLNR 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 410 PKATYEAF-KHGWLNSGDVGVIHPDGHVEIKDR-SKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPTWGETPCA 487
Cdd:PRK07787 339 PDATAAAFtADGWFRTGDVAVVDPDGMHRIVGReSTDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVA 418
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15218840 488 FVVLEKGETnnedredklvtkERDLIEYCRENLPHFMCPRKVVFLDELPKNGNGKILKPKLR 549
Cdd:PRK07787 419 YVVGADDVA------------ADELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLL 468
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
37-551 |
6.50e-46 |
|
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: 169.63 E-value: 6.50e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 37 KTRFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTpamyeMHFAVPM-----AGAVLNPINTRLDATSIAAILRHAK 111
Cdd:cd17642 42 GVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENS-----LQFFLPViaglfIGVGVAPTNDIYNERELDHSLNISK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 112 PKILFIYRsfeplaREILQLLSSEDSNLNLPVIFIheIDFPKRVSSEESDYEcLIQRGEPtPLLLARMFCIQ--DEHDPI 189
Cdd:cd17642 117 PTIVFCSK------KGLQKVLNVQKKLKIIKTIII--LDSKEDYKGYQCLYT-FITQNLP-PGFNEYDFKPPsfDRDEQV 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 190 SL-NYTSGTTADPKGVVISHRGAyLSTLSAIIGWEMGTCPV----YLWTLPMFHCNGWTFTWGTAARGGTSVCMRHVTAP 264
Cdd:cd17642 187 ALiMNSSGSTGLPKGVQLTHKNI-VARFSHARDPIFGNQIIpdtaILTVIPFHHGFGMFTTLGYLICGFRVVLMYKFEEE 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 265 EIYKNIEMHNVTHMCCVPTVFNILLKG---NSLDLSHrsgpVHVLTGGSPPPAA----LVKKVQRLGFqVMHAYGLTEAT 337
Cdd:cd17642 266 LFLRSLQDYKVQSALLVPTLFAFFAKStlvDKYDLSN----LHEIASGGAPLSKevgeAVAKRFKLPG-IRQGYGLTETT 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 338 GPVLFcewqdewnrlpenqQMELKARQGLS--ILGLTEVDVRNKETqesvprdGKTMG-----EIVMKGSSIMKGYLKNP 410
Cdd:cd17642 341 SAILI--------------TPEGDDKPGAVgkVVPFFYAKVVDLDT-------GKTLGpnergELCVKGPMIMKGYVNNP 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 411 KATYEAF-KHGWLNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPTWGETPCAFV 489
Cdd:cd17642 400 EATKALIdKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVV 479
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15218840 490 VLEKGETNNedredklvtkERDLIEYCRENlphfMCPRK-----VVFLDELPKNGNGKILKPKLRDI 551
Cdd:cd17642 480 VLEAGKTMT----------EKEVMDYVASQ----VSTAKrlrggVKFVDEVPKGLTGKIDRRKIREI 532
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
30-549 |
4.47e-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: 165.33 E-value: 4.47e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 30 RTSIIYGKTRFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRH 109
Cdd:cd05919 1 KTAFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 110 AKPKILfiyrsfeplareilqllssedsnlnlpvifiheidfpkrvsseesdyecliqrgeptplllarmfcIQDEHDPI 189
Cdd:cd05919 81 CEARLV------------------------------------------------------------------VTSADDIA 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 190 SLNYTSGTTADPKGVVISHRGAYL-------------------STLSAIIGWEMGtcpvylwtlpmfhcNGWTFTWGTaa 250
Cdd:cd05919 95 YLLYSSGTTGPPKGVMHAHRDPLLfadamarealgltpgdrvfSSAKMFFGYGLG--------------NSLWFPLAV-- 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 251 rGGTSVCMRH-VTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSHRSGPVHVLTGGSPPPAALVKK-VQRLGFQVM 328
Cdd:cd05919 159 -GASAVLNPGwPTAERVLATLARFRPTVLYGVPTFYANLLDSCAGSPDALRSLRLCVSAGEALPRGLGERwMEHFGGPIL 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 329 HAYGLTEaTGPVLFCEWQDEWnrlpenqqmelkaRQGLSILGLTEVDVRnketqeSVPRDGKTM-----GEIVMKGSSIM 403
Cdd:cd05919 238 DGIGATE-VGHIFLSNRPGAW-------------RLGSTGRPVPGYEIR------LVDEEGHTIppgeeGDLLVRGPSAA 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 404 KGYLKNPKATYEAFKHGWLNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPTWGE 483
Cdd:cd05919 298 VGYWNNPEKSRATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLS 377
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15218840 484 TPCAFVVLEKGETNNEdredKLVtkeRDLIEYCRENLPHFMCPRKVVFLDELPKNGNGKILKPKLR 549
Cdd:cd05919 378 RLTAFVVLKSPAAPQE----SLA---RDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
191-558 |
4.59e-45 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 167.92 E-value: 4.59e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 191 LNYTSGTTADPKGVVISHR----------GAYLSTLSAiiGWEMGTCPvylwtLPMFH-----CNGWTFTwgtaARGGTS 255
Cdd:PRK08974 211 LQYTGGTTGVAKGAMLTHRnmlanleqakAAYGPLLHP--GKELVVTA-----LPLYHifaltVNCLLFI----ELGGQN 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 256 VCM---RHVtaPEIYKNIEMHNVTHMCCVPTVFNILLKG---NSLDLSHRSGPVhvlTGGSPPPAALVKKVQRL-GFQVM 328
Cdd:PRK08974 280 LLItnpRDI--PGFVKELKKYPFTAITGVNTLFNALLNNeefQELDFSSLKLSV---GGGMAVQQAVAERWVKLtGQYLL 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 329 HAYGLTEATgPVLFCEwqdewnrlPENqqmeLKARQGlSIlGL----TEVDVRNKETQEsVPRdGKTmGEIVMKGSSIMK 404
Cdd:PRK08974 355 EGYGLTECS-PLVSVN--------PYD----LDYYSG-SI-GLpvpsTEIKLVDDDGNE-VPP-GEP-GELWVKGPQVML 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 405 GYLKNPKATYEAFKHGWLNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPTWGET 484
Cdd:PRK08974 417 GYWQRPEATDEVIKDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEA 496
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15218840 485 PCAFVVlekgetnnedREDKLVTKErDLIEYCRENLPHFMCPRKVVFLDELPKNGNGKILKPKLRDIAKGLVAE 558
Cdd:PRK08974 497 VKIFVV----------KKDPSLTEE-ELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRDEARAKVDN 559
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
28-556 |
4.69e-45 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 167.91 E-value: 4.69e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 28 PNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAIL 107
Cdd:PRK06178 47 PQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYEL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 108 RHAKPKILFIYRSFEPLAREILQLLSSED-----------SNLNLPVIFihEIDFPKRVSSEESDYECLIqRGEPTPLLL 176
Cdd:PRK06178 127 NDAGAEVLLALDQLAPVVEQVRAETSLRHvivtsladvlpAEPTLPLPD--SLRAPRLAAAGAIDLLPAL-RACTAPVPL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 177 ARMfciqDEHDPISLNYTSGTTADPKGVVISHRG-AYLSTLSAIIGWEMGTCPVYLWTLPMFHCNGWTFtwGT---AARG 252
Cdd:PRK06178 204 PPP----ALDALAALNYTGGTTGMPKGCEHTQRDmVYTAAAAYAVAVVGGEDSVFLSFLPEFWIAGENF--GLlfpLFSG 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 253 GTSVCMRHVTAPEIYKNIEMHNVTHMccvptvfnILLKGNSLDL-SHRSGPVHVLTGGSPPPAA-LVKKV-----QR--- 322
Cdd:PRK06178 278 ATLVLLARWDAVAFMAAVERYRVTRT--------VMLVDNAVELmDHPRFAEYDLSSLRQVRVVsFVKKLnpdyrQRwra 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 323 LGFQVMH--AYGLTEA-TGPVLFCEWQDEwnrlpenqQMELKARQ---GLSILGlTEVDVRNKETQESVPRDGKtmGEIV 396
Cdd:PRK06178 350 LTGSVLAeaAWGMTEThTCDTFTAGFQDD--------DFDLLSQPvfvGLPVPG-TEFKICDFETGELLPLGAE--GEIV 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 397 MKGSSIMKGYLKNPKATYEAFKHGWLNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAM 476
Cdd:PRK06178 419 VRTPSLLKGYWNKPEATAEALRDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGR 498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 477 PHPTWGETPCAFVVLEKGETNNEDredklvtkerDLIEYCRENLPHFMCPrKVVFLDELPKNGNGKILKPKLRDIAKGLV 556
Cdd:PRK06178 499 PDPDKGQVPVAFVQLKPGADLTAA----------ALQAWCRENMAVYKVP-EIRIVDALPMTATGKVRKQDLQALAEELK 567
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
187-543 |
8.32e-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: 161.67 E-value: 8.32e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 187 DPISLNYTSGTTADPKGVVISHRGAYLSTLSAIIGWEMGTCPVYLWTLPMFHCNGWTFTWGTAARGGTSVCMRHVTAPEI 266
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAGLNLALATFHAGGANVVMEKFDPAEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 267 YKNIEMHNVTHMCCVPTV-FNIL--LKGNSLDLSHRSgpvHVLTGGSPPPAALVKKVQRLGFQVMhaYGLTEATGPVLFC 343
Cdd:cd17637 81 LELIEEEKVTLMGSFPPIlSNLLdaAEKSGVDLSSLR---HVLGLDAPETIQRFEETTGATFWSL--YGQTETSGLVTLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 344 EWQDewnrlpenqqmelkaRQGLS--ILGLTEVDVRNKETQEsVPRdGKTmGEIVMKGSSIMKGYLKNPKATYEAFKHGW 421
Cdd:cd17637 156 PYRE---------------RPGSAgrPGPLVRVRIVDDNDRP-VPA-GET-GEIVVRGPLVFQGYWNLPELTAYTFRNGW 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 422 LNSGDVGVIHPDGHVEIKDRS--KDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETnne 499
Cdd:cd17637 218 HHTGDLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPGAT--- 294
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 15218840 500 dredklVTkERDLIEYCRENLPHFMCPRKVVFLDELPKNGNGKI 543
Cdd:cd17637 295 ------LT-ADELIEFVGSRIARYKKPRYVVFVEALPKTADGSI 331
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
25-548 |
3.22e-43 |
|
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: 160.49 E-value: 3.22e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 25 ECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIA 104
Cdd:cd05945 2 AANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 105 AILRHAKPKILfiyrsfeplareilqllssedsnlnlpvifiheidfpkrvsseesdyecliqrgeptplllarmfcIQD 184
Cdd:cd05945 82 EILDAAKPALL------------------------------------------------------------------IAD 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 185 EHDPISLNYTSGTTADPKGVVISHRGaylstLSAIIGWE-----MGTCPVYLWTLPmFHCNGWTFTW-GTAARGGTSVCM 258
Cdd:cd05945 96 GDDNAYIIFTSGSTGRPKGVQISHDN-----LVSFTNWMlsdfpLGPGDVFLNQAP-FSFDLSVMDLyPALASGATLVPV 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 259 RHvtapEIYKN-------IEMHNVTHMCCVPTVFNILLKGNSLDLSHRSGPVHVLTGGSPPPAALVKKVQRL--GFQVMH 329
Cdd:cd05945 170 PR----DATADpkqlfrfLAEHGITVWVSTPSFAAMCLLSPTFTPESLPSLRHFLFCGEVLPHKTARALQQRfpDARIYN 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 330 AYGLTEATGPVLFCEWQDE----WNRLPenqqmelkarqglsiLGLTEVDVRNK-ETQESVPRDGKTMGEIVMKGSSIMK 404
Cdd:cd05945 246 TYGPTEATVAVTYIEVTPEvldgYDRLP---------------IGYAKPGAKLViLDEDGRPVPPGEKGELVISGPSVSK 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 405 GYLKNPKATYEAF----KHGWLNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPT 480
Cdd:cd05945 311 GYLNNPEKTAAAFfpdeGQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGE 390
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15218840 481 WGETPCAFVVLEKGEtnnedrEDKLVTkerDLIEYCRENLPHFMCPRKVVFLDELPKNGNGKILKPKL 548
Cdd:cd05945 391 KVTELIAFVVPKPGA------EAGLTK---AIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
20-543 |
4.13e-43 |
|
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: 161.49 E-value: 4.13e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 20 LKRASECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRLD 99
Cdd:TIGR03098 6 LEDAAARLPDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 100 ATSIAAILRHAKPKILFIyrsfeplAREILQLLSSEDSNLNLPVIFIH----EIDFPKRVSSEESDYECLIQRGEPTPLl 175
Cdd:TIGR03098 86 AEQVAHILADCNVRLLVT-------SSERLDLLHPALPGCHDLRTLIIvgdpAHASEGHPGEEPASWPKLLALGDADPP- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 176 larMFCIQDehDPISLNYTSGTTADPKGVVISHRGAYLSTLSAIIGWEMGTCPVYLWTLPMfhcngwTFTWG-----TA- 249
Cdd:TIGR03098 158 ---HPVIDS--DMAAILYTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPL------SFDYGfnqltTAf 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 250 ARGGTSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFnilLKGNSLDLSHRSGPvHVL----TGGSPPPAALVKKVQRLGF 325
Cdd:TIGR03098 227 YVGATVVLHDYLLPRDVLKALEKHGITGLAAVPPLW---AQLAQLDWPESAAP-SLRyltnSGGAMPRATLSRLRSFLPN 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 326 QVMH-AYGLTEA----TGPvlfcewqdewnrlPEnqqmELKARQGlSI---LGLTEVDVRNKETQESVPRDgktMGEIVM 397
Cdd:TIGR03098 303 ARLFlMYGLTEAfrstYLP-------------PE----EVDRRPD-SIgkaIPNAEVLVLREDGSECAPGE---EGELVH 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 398 KGSSIMKGYLKNPKATYEAFK-----HGWLN-------SGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKY 465
Cdd:TIGR03098 362 RGALVAMGYWNDPEKTAERFRplppfPGELHlpelavwSGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYAT 441
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15218840 466 PKVLETAVVAMPHPTWGETPCAFVVLEKGEtnNEDREdklvtkerDLIEYCRENLPHFMCPRKVVFLDELPKNGNGKI 543
Cdd:TIGR03098 442 GLVAEAVAFGVPDPTLGQAIVLVVTPPGGE--ELDRA--------ALLAECRARLPNYMVPALIHVRQALPRNANGKI 509
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
14-550 |
4.30e-43 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 162.07 E-value: 4.30e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 14 LTPITFLKRASECYPNRTSII---YGKTrFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAV 90
Cdd:PLN02330 28 LTLPDFVLQDAELYADKVAFVeavTGKA-VTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 91 LNPINTRLDATSIAAILRHAKPKilfiyrsfeplareilqLLSSEDSN------LNLPVIFIHEIDFPKRVSSEEsdyec 164
Cdd:PLN02330 107 FSGANPTALESEIKKQAEAAGAK-----------------LIVTNDTNygkvkgLGLPVIVLGEEKIEGAVNWKE----- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 165 LIQRGEPTPLLLARMFCIQDehDPISLNYTSGTTADPKGVVISHRGAYLSTLSAI--IGWEMGTCPVYLWTLPMFHCNGW 242
Cdd:PLN02330 165 LLEAADRAGDTSDNEEILQT--DLCALPFSSGTTGISKGVMLTHRNLVANLCSSLfsVGPEMIGQVVTLGLIPFFHIYGI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 243 T-FTWGTAARGGTSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKG---NSLDLSH---RSgpvhVLTGGSPPPAA 315
Cdd:PLN02330 243 TgICCATLRNKGKVVVMSRFELRTFLNALITQEVSFAPIVPPIILNLVKNpivEEFDLSKlklQA----IMTAAAPLAPE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 316 LVKKVQRL--GFQVMHAYGLTEATGPVLFcewqdewNRLPENQQMELKARQGLSILGLTEVDVRNKETQESVPRDgkTMG 393
Cdd:PLN02330 319 LLTAFEAKfpGVQVQEAYGLTEHSCITLT-------HGDPEKGHGIAKKNSVGFILPNLEVKFIDPDTGRSLPKN--TPG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 394 EIVMKGSSIMKGYLKNPKATYEAF-KHGWLNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETA 472
Cdd:PLN02330 390 ELCVRSQCVMQGYYNNKEETDRTIdEDGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAA 469
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15218840 473 VVAMPHPTWGETPCAFVVLekgetNNEDREdklvtKERDLIEYCRENLPHFMCPRKVVFLDELPKNGNGKILKPKLRD 550
Cdd:PLN02330 470 VVPLPDEEAGEIPAACVVI-----NPKAKE-----SEEDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKE 537
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
193-552 |
8.04e-43 |
|
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: 156.87 E-value: 8.04e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 193 YTSGTTADPKGVVISHRGAYLStlsaiiGWEMGTCPVY------LWTLPMFHCNGWTFTWGTAARGGTSVCM------RH 260
Cdd:cd05944 9 HTGGTTGTPKLAQHTHSNEVYN------AWMLALNSLFdpddvlLCGLPLFHVNGSVVTLLTPLASGAHVVLagpagyRN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 261 VTA-PEIYKNIEMHNVTHMCCVPTVFNILLK--GNSlDLSHRSGpvhVLTGGSPPPAALVKKVQ-RLGFQVMHAYGLTEA 336
Cdd:cd05944 83 PGLfDNFWKLVERYRITSLSTVPTVYAALLQvpVNA-DISSLRF---AMSGAAPLPVELRARFEdATGLPVVEGYGLTEA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 337 TGPVlfcewqdewNRLPENQQMELKArQGLSI-LGLTEVDVRNKETQESVPRDGKTMGEIVMKGSSIMKGYLKNPKATYE 415
Cdd:cd05944 159 TCLV---------AVNPPDGPKRPGS-VGLRLpYARVRIKVLDGVGRLLRDCAPDEVGEICVAGPGVFGGYLYTEGNKNA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 416 AFKHGWLNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGE 495
Cdd:cd05944 229 FVADGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGA 308
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 15218840 496 TnnedredklVTKErDLIEYCRENLPH-FMCPRKVVFLDELPKNGNGKILKPKLRDIA 552
Cdd:cd05944 309 V---------VEEE-ELLAWARDHVPErAAVPKHIEVLEELPVTAVGKVFKPALRADA 356
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
39-557 |
1.11e-41 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 157.34 E-value: 1.11e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 39 RFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKiLFIY 118
Cdd:PRK07514 28 RYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAEPA-LVVC 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 119 RsfePLAREILQLLSSEdsnlnLPVIFIHEIDfPKRVSSeesdyecLIQRGEPTPLLLARMFCiqDEHDPISLNYTSGTT 198
Cdd:PRK07514 107 D---PANFAWLSKIAAA-----AGAPHVETLD-ADGTGS-------LLEAAAAAPDDFETVPR--GADDLAAILYTSGTT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 199 ADPKGVVISHRGAYLSTLSAIIGWEMGTCPVYLWTLPMFHCNGwTF--TWGTAARGGTSVCMRHVTAPEIYKniEMHNVT 276
Cdd:PRK07514 169 GRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIHALPIFHTHG-LFvaTNVALLAGASMIFLPKFDPDAVLA--LMPRAT 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 277 HMCCVPTVFNILLKGNSLDLSHRSGpVHVLTGGSPPPAALVKKV--QRLGFQVMHAYGLTEA----TGPvlfceWQDEwn 350
Cdd:PRK07514 246 VMMGVPTFYTRLLQEPRLTREAAAH-MRLFISGSAPLLAETHREfqERTGHAILERYGMTETnmntSNP-----YDGE-- 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 351 RLPenqqmelkARQGLSILGlTEVDVRNKETQESVPRDGktMGEIVMKGSSIMKGYLKNPKATYEAFKH-GWLNSGDVGV 429
Cdd:PRK07514 318 RRA--------GTVGFPLPG-VSLRVTDPETGAELPPGE--IGMIEVKGPNVFKGYWRMPEKTAEEFRAdGFFITGDLGK 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 430 IHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETNNEDredklvtke 509
Cdd:PRK07514 387 IDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPGAALDEA--------- 457
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 15218840 510 rDLIEYCRENLPHFMCPRKVVFLDELPKNGNGKILKPKLRDIAKGLVA 557
Cdd:PRK07514 458 -AILAALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLLREQYADLFA 504
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
28-544 |
1.38e-41 |
|
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: 158.51 E-value: 1.38e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 28 PNRTSIIY------GKTRFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRLDAT 101
Cdd:cd17634 67 GDRTAIIYegddtsQSRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 102 SIAAILRHAKPKILFIYRSFEPLAREIlQLLSSEDSNLNLPVIFIHEIDFPKRVSSE-------ESDYECLIQRGEPTpL 174
Cdd:cd17634 147 AVAGRIIDSSSRLLITADGGVRAGRSV-PLKKNVDDALNPNVTSVEHVIVLKRTGSDidwqegrDLWWRDLIAKASPE-H 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 175 LLARMfciqDEHDPISLNYTSGTTADPKGVVISHRG--AYLSTLSAIIgWEMGTCPVYLWTLPMfhcnGWT-----FTWG 247
Cdd:cd17634 225 QPEAM----NAEDPLFILYTSGTTGKPKGVLHTTGGylVYAATTMKYV-FDYGPGDIYWCTADV----GWVtghsyLLYG 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 248 TAARGGTSVCMR----HVTAPEIYKNIEMHNVTHMCCVPTVFNILLK-GNSLDLSHRSGPVHVLTG-GSP----PPAALV 317
Cdd:cd17634 296 PLACGATTLLYEgvpnWPTPARMWQVVDKHGVNILYTAPTAIRALMAaGDDAIEGTDRSSLRILGSvGEPinpeAYEWYW 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 318 KKVQRLGFQVMHAYGLTEATGPVLfcewqdewnrLPENQQMELKARQGLSILGLTEVDVRNKETQesvPRDGKTMGEIVM 397
Cdd:cd17634 376 KKIGKEKCPVVDTWWQTETGGFMI----------TPLPGAIELKAGSATRPVFGVQPAVVDNEGH---PQPGGTEGNLVI 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 398 KGS--SIMKGYLKNPKATYEA----FKHGWLnSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLET 471
Cdd:cd17634 443 TDPwpGQTRTLFGDHERFEQTyfstFKGMYF-SGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEA 521
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15218840 472 AVVAMPHPTWGETPCAFVVLEKGETNNEDREDKLVtkerdliEYCRENLPHFMCPRKVVFLDELPKNGNGKIL 544
Cdd:cd17634 522 AVVGIPHAIKGQAPYAYVVLNHGVEPSPELYAELR-------NWVRKEIGPLATPDVVHWVDSLPKTRSGKIM 587
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
40-552 |
2.48e-41 |
|
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: 154.97 E-value: 2.48e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 40 FTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPIntrldatsiaailrhakpkilfiYR 119
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPL-----------------------FS 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 120 SFEPLAreILQLLssedsnlnlpvifiheidfpkrvssEESDYECLIQrgepTPLLLARMfciqDEHDPISLNYTSGTTA 199
Cdd:cd05969 58 AFGPEA--IRDRL-------------------------ENSEAKVLIT----TEELYERT----DPEDPTLLHYTSGTTG 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 200 DPKGVVISHRGAYLSTLSAiiGWEMGTCPVylwtlPMFHCN---GW---TF--TWGTAARGGTSVCMRHVTAPE-IYKNI 270
Cdd:cd05969 103 TPKGVLHVHDAMIFYYFTG--KYVLDLHPD-----DIYWCTadpGWvtgTVygIWAPWLNGVTNVVYEGRFDAEsWYGII 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 271 EMHNVTHMCCVPTVFNILLK-----GNSLDLSHRSgpvHVLTGGSP-PPAALVKKVQRLGFQVMHAYGLTEaTGPVLFCE 344
Cdd:cd05969 176 ERVKVTVWYTAPTAIRMLMKegdelARKYDLSSLR---FIHSVGEPlNPEAIRWGMEVFGVPIHDTWWQTE-TGSIMIAN 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 345 WQdewnrlpenqQMELKA-RQGLSILGLTEVDVRNKetQESVPRDgkTMGEIVMKGS--SIMKGYLKNPKATYEAFKHGW 421
Cdd:cd05969 252 YP----------CMPIKPgSMGKPLPGVKAAVVDEN--GNELPPG--TKGILALKPGwpSMFRGIWNDEERYKNSFIDGW 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 422 LNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGetnnEDR 501
Cdd:cd05969 318 YLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEG----FEP 393
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 15218840 502 EDKLvtkERDLIEYCRENLPHFMCPRKVVFLDELPKNGNGKILKPKLRDIA 552
Cdd:cd05969 394 SDEL---KEEIINFVRQKLGAHVAPREIEFVDNLPKTRSGKIMRRVLKAKE 441
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
50-549 |
2.28e-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: 341246 [Multi-domain] Cd Length: 457 Bit Score: 152.59 E-value: 2.28e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 50 CRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRH----AKPKILFIYRSFEPLA 125
Cdd:cd05922 4 SAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRLGLVFVPLNPTLKESVLRYlvadAGGRIVLADAGAADRL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 126 REILQLLSSEDSNLNLPVIFIHEIDFPKRVSSEEsdyecliqrgeptplllarmfciqdehDPISLNYTSGTTADPKGVV 205
Cdd:cd05922 84 RDALPASPDPGTVLDADGIRAARASAPAHEVSHE---------------------------DLALLLYTSGSTGSPKLVR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 206 ISHRgAYLSTLSAIIGWeMGTCP--VYLWTLPMFHCNGWTFTWGTAARGGTSVC-MRHVTAPEIYKNIEMHNVTHMCCVP 282
Cdd:cd05922 137 LSHQ-NLLANARSIAEY-LGITAddRALTVLPLSYDYGLSVLNTHLLRGATLVLtNDGVLDDAFWEDLREHGATGLAGVP 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 283 TVFNILLkgnSLDLSHRSGPV--HVLTGGSPPPAALVKKVQRL--GFQVMHAYGLTEATGPVLFcewqdewnrLPENQQM 358
Cdd:cd05922 215 STYAMLT---RLGFDPAKLPSlrYLTQAGGRLPQETIARLRELlpGAQVYVMYGQTEATRRMTY---------LPPERIL 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 359 ELKARQGLSILGlTEVDVRNKETQESVPrdgKTMGEIVMKGSSIMKGYLKNPKA-TYEAFKHGWLNSGDVGVIHPDGHVE 437
Cdd:cd05922 283 EKPGSIGLAIPG-GEFEILDDDGTPTPP---GEPGEIVHRGPNVMKGYWNDPPYrRKEGRGGGVLHTGDLARRDEDGFLF 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 438 IKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPhPTWGETPCAFVVLEKGETnnedredklvtkERDLIEYCR 517
Cdd:cd05922 359 IVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLP-DPLGEKLALFVTAPDKID------------PKDVLRSLA 425
|
490 500 510
....*....|....*....|....*....|..
gi 15218840 518 ENLPHFMCPRKVVFLDELPKNGNGKILKPKLR 549
Cdd:cd05922 426 ERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
191-550 |
4.30e-40 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 153.77 E-value: 4.30e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 191 LNYTSGTTADPKGVVISHRG--AYLSTLSAIIGWEMGT-CPVYLWTLPMFHCNGWTFTWG-TAARGGTSVCM---RHVta 263
Cdd:PRK05677 212 LQYTGGTTGVAKGAMLTHRNlvANMLQCRALMGSNLNEgCEILIAPLPLYHIYAFTFHCMaMMLIGNHNILIsnpRDL-- 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 264 PEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSHRSGPVHVLTGGSPPPAALVKKVQRL-GFQVMHAYGLTEaTGPVLF 342
Cdd:PRK05677 290 PAMVKELGKWKFSGFVGLNTLFVALCNNEAFRKLDFSALKLTLSGGMALQLATAERWKEVtGCAICEGYGMTE-TSPVVS 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 343 CEwqdewnrLPENQQMelkARQGLSILGlTEVDVRNKETQEsVPRdGKTmGEIVMKGSSIMKGYLKNPKATYEAF-KHGW 421
Cdd:PRK05677 369 VN-------PSQAIQV---GTIGIPVPS-TLCKVIDDDGNE-LPL-GEV-GELCVKGPQVMKGYWQRPEATDEILdSDGW 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 422 LNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETnnedr 501
Cdd:PRK05677 435 LKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKPGET----- 509
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 15218840 502 edklVTKERdLIEYCRENLPHFMCPRKVVFLDELPKNGNGKILKPKLRD 550
Cdd:PRK05677 510 ----LTKEQ-VMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRRELRD 553
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
187-541 |
1.15e-39 |
|
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: 147.45 E-value: 1.15e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 187 DPISLNYTSGTTADPKGVVISHRGAYLSTLSAIIGWEMGTCPVYLWTLPMFHCNGWTFTWGTAARGGTSVCMRHVTAPEI 266
Cdd:cd17636 1 DPVLAIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLNSGPLFHIGTLMFTLATFHAGGTNVFVRRVDAEEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 267 YKNIEMHNVTH-MCCVPTVFNI--LLKGNSLDLSH-RSGPvhvltgGSPPPAALVKKVQRLGFQVMHAYGLTEATGPVLF 342
Cdd:cd17636 81 LELIEAERCTHaFLLPPTIDQIveLNADGLYDLSSlRSSP------AAPEWNDMATVDTSPWGRKPGGYGQTEVMGLATF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 343 cEWQdewnrlpenqqmelkARQGLSILG----LTEVDVRNKETQEsVPrDGKTmGEIVMKGSSIMKGYLKNPKATYEAFK 418
Cdd:cd17636 155 -AAL---------------GGGAIGGAGrpspLVQVRILDEDGRE-VP-DGEV-GEIVARGPTVMAGYWNRPEVNARRTR 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 419 HGWLNSGDVGVIHPDGHVEI---KDRskdIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGE 495
Cdd:cd17636 216 GGWHHTNDLGRREPDGSLSFvgpKTR---MIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGA 292
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 15218840 496 TNNEDredklvtkerDLIEYCRENLPHFMCPRKVVFLDELPKNGNG 541
Cdd:cd17636 293 SVTEA----------ELIEHCRARIASYKKPKSVEFADALPRTAGG 328
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
28-549 |
3.99e-39 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 150.16 E-value: 3.99e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 28 PNRTSIIYGKT--RFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAA 105
Cdd:PRK13390 11 PDRPAVIVAETgeQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 106 ILRHAKPKILFIYRSFEPLAREIlqllsseDSNLNLPVIFIHEID-FpkrvsseeSDYECLIQRGEPTpllLARMFCiqd 184
Cdd:PRK13390 91 IVGDSGARVLVASAALDGLAAKV-------GADLPLRLSFGGEIDgF--------GSFEAALAGAGPR---LTEQPC--- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 185 ehDPISLnYTSGTTADPKGVVISHRGAYLST----LSAIIG--WEMGTCPVYLWTLPMFHCNGWTFTWGTAARGGTSVCM 258
Cdd:PRK13390 150 --GAVML-YSSGTTGFPKGIQPDLPGRDVDApgdpIVAIARafYDISESDIYYSSAPIYHAAPLRWCSMVHALGGTVVLA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 259 RHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNS-----LDLSHRSGPVHvltGGSPPPAAlVKK--VQRLGFQVMHAY 331
Cdd:PRK13390 227 KRFDAQATLGHVERYRITVTQMVPTMFVRLLKLDAdvrtrYDVSSLRAVIH---AAAPCPVD-VKHamIDWLGPIVYEYY 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 332 GLTEATGPVLfcewqdewnrLPENQQMELKARQGLSILGltEVDVRNKETQEsVPrdGKTMGEIVMKGSSIMKGYLKNPK 411
Cdd:PRK13390 303 SSTEAHGMTF----------IDSPDWLAHPGSVGRSVLG--DLHICDDDGNE-LP--AGRIGTVYFERDRLPFRYLNDPE 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 412 ATYEAfKHG----WLNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPTWGETPCA 487
Cdd:PRK13390 368 KTAAA-QHPahpfWTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKA 446
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15218840 488 FVVLEKGetnnEDREDKLVtkeRDLIEYCRENLPHFMCPRKVVFLDELPKNGNGKILKPKLR 549
Cdd:PRK13390 447 VIQLVEG----IRGSDELA---RELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
28-554 |
8.02e-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: 150.93 E-value: 8.02e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 28 PNRTSIIY------GKTRFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTP-AMYEMhFAVPMAGAVLNPINTRLDA 100
Cdd:cd05967 65 GDQIALIYdspvtgTERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPeAAIAM-LACARIGAIHSVVFGGFAA 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 101 TSIAAILRHAKPKiLFIYRSF--EPlaREILQLLSSEDSNLNLP------VIFIHEIDFPKR--VSSEESDYECLIQRGE 170
Cdd:cd05967 144 KELASRIDDAKPK-LIVTASCgiEP--GKVVPYKPLLDKALELSghkphhVLVLNRPQVPADltKPGRDLDWSELLAKAE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 171 PTPLLLArmfciqDEHDPISLNYTSGTTADPKGVVishR--GAYLSTLSaiigWEMGTC------PVYLWTLPMfhcnGW 242
Cdd:cd05967 221 PVDCVPV------AATDPLYILYTSGTTGKPKGVV---RdnGGHAVALN----WSMRNIygikpgDVWWAASDV----GW 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 243 T-----FTWGTAARGGTSVC-----MRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKgnsldlshrsgpvhvltggSPP 312
Cdd:cd05967 284 VvghsyIVYGPLLHGATTVLyegkpVGTPDPGAFWRVIEKYQVNALFTAPTAIRAIRK-------------------EDP 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 313 PAALVKKVQRLGFQVMHAYG----------LTEATG-PVLFCEWQDE--WNrLPEN----QQMELKARQ-GLSILGLtEV 374
Cdd:cd05967 345 DGKYIKKYDLSSLRTLFLAGerldpptlewAENTLGvPVIDHWWQTEtgWP-ITANpvglEPLPIKAGSpGKPVPGY-QV 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 375 DVRNKETQESVPRdgkTMGEIVMKGS---SIMKGYLKNPkatyEAFKHGWLN-------SGDVGVIHPDGHVEIKDRSKD 444
Cdd:cd05967 423 QVLDEDGEPVGPN---ELGNIVIKLPlppGCLLTLWKND----ERFKKLYLSkfpgyydTGDAGYKDEDGYLFIMGRTDD 495
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 445 IIISGGENISSVEVENIIYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETNNEDredklvTKERDLIEYCRENLPHFM 524
Cdd:cd05967 496 VINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEGVKITAE------ELEKELVALVREQIGPVA 569
|
570 580 590
....*....|....*....|....*....|
gi 15218840 525 CPRKVVFLDELPKNGNGKILKPKLRDIAKG 554
Cdd:cd05967 570 AFRLVIFVKRLPKTRSGKILRRTLRKIADG 599
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
47-558 |
1.09e-38 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 149.51 E-value: 1.09e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 47 DRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFIYRSFE--PL 124
Cdd:PRK06164 43 ALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARWLVVWPGFKgiDF 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 125 AReILQLLSsEDSNLNLPVIFIHEI---DFPKRVSSEESDYeCLIQRGEPTPLLLARmfciQDEHDPISLNYT-SGTTAD 200
Cdd:PRK06164 123 AA-ILAAVP-PDALPPLRAIAVVDDaadATPAPAPGARVQL-FALPDPAPPAAAGER----AADPDAGALLFTtSGTTSG 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 201 PKGVVisHRGAYLSTLSAIIGWEMGTCP--VYLWTLPMFHCNGWTFTWGTAARGGTSVCMRHVTAPEIYKNIEMHNVTHM 278
Cdd:PRK06164 196 PKLVL--HRQATLLRHARAIARAYGYDPgaVLLAALPFCGVFGFSTLLGALAGGAPLVCEPVFDAARTARALRRHRVTHT 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 279 CCVPTVFNILLK--GNSLDLSHrsgpVHVLTGGSPPPAA--LVKKVQRLGFQVMHAYGLTEATGpvLFCEWQDEwnrLPE 354
Cdd:PRK06164 274 FGNDEMLRRILDtaGERADFPS----ARLFGFASFAPALgeLAALARARGVPLTGLYGSSEVQA--LVALQPAT---DPV 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 355 NQQMElkaRQGLSILGLTEVDVRNKETQESVPrDGKTmGEIVMKGSSIMKGYLKNPKATYEAFK-HGWLNSGDVGVIHPD 433
Cdd:PRK06164 345 SVRIE---GGGRPASPEARVRARDPQDGALLP-DGES-GEIEIRAPSLMRGYLDNPDATARALTdDGYFRTGDLGYTRGD 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 434 GHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPtwGET-PCAFVVLEKGETnnedredklvTKERDL 512
Cdd:PRK06164 420 GQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGATRD--GKTvPVAFVIPTDGAS----------PDEAGL 487
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 15218840 513 IEYCRENLPHFMCPRKVVFLDELP--KNGNG-KILKPKLRDIAKGLVAE 558
Cdd:PRK06164 488 MAACREALAGFKVPARVQVVEAFPvtESANGaKIQKHRLREMAQARLAA 536
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
191-553 |
1.51e-37 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 146.32 E-value: 1.51e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 191 LNYTSGTTADPKGVVISHRGAYLSTLSAIIgWeMGTC---------PVYLWTLPMFHCNGWTFTWGTAAR-GGTSVCM-- 258
Cdd:PRK07059 209 LQYTGGTTGVSKGATLLHRNIVANVLQMEA-W-LQPAfekkprpdqLNFVCALPLYHIFALTVCGLLGMRtGGRNILIpn 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 259 -RHVtaPEIYKNIEMHNVTHMCCVPTVFNILLKG---NSLDLSHRsgpVHVLTGGSPPPAALVKK-VQRLGFQVMHAYGL 333
Cdd:PRK07059 287 pRDI--PGFIKELKKYQVHIFPAVNTLYNALLNNpdfDKLDFSKL---IVANGGGMAVQRPVAERwLEMTGCPITEGYGL 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 334 TEaTGPVLFCewqdewNRLPENqqmELKARQGLSILGlTEVDVRNKETQEsVPRDgkTMGEIVMKGSSIMKGYLKNPKAT 413
Cdd:PRK07059 362 SE-TSPVATC------NPVDAT---EFSGTIGLPLPS-TEVSIRDDDGND-LPLG--EPGEICIRGPQVMAGYWNRPDET 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 414 YEA-FKHGWLNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPTWGETPCAFVVle 492
Cdd:PRK07059 428 AKVmTADGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFVV-- 505
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15218840 493 kgetnnedREDKLVTkERDLIEYCRENLPHFMCPRKVVFLDELPKNGNGKILKPKLRDIAK 553
Cdd:PRK07059 506 --------KKDPALT-EEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRRELRDGKA 557
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
52-543 |
3.38e-37 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 145.03 E-value: 3.38e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 52 LAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFIYRS-----FEPLAR 126
Cdd:PRK05852 56 LAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLIDADgphdrAEPTTR 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 127 EILQLLS-SEDSNLNLPVIFIHeidfpkrvsseesdyecLIQRGEPTPLLLARMFCiqdEHDPISLNYTSGTTADPKGVV 205
Cdd:PRK05852 136 WWPLTVNvGGDSGPSGGTLSVH-----------------LDAATEPTPATSTPEGL---RPDDAMIMFTGGTTGLPKMVP 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 206 ISHRGAYLSTLSAIIGWEMGTCPVYLWTLPMFHCNGWTFTW-GTAARGGTSVCMRH--VTAPEIYKNIEMHNVTHMCCVP 282
Cdd:PRK05852 196 WTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALlATLASGGAVLLPARgrFSAHTFWDDIKAVGATWYTAVP 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 283 TVFNILLKGNSLDLSHRS-GPVHVLTGGSPP--PAALVKKVQRLGFQVMHAYGLTEATGPVlfCEWQDEWNRLPENQQME 359
Cdd:PRK05852 276 TIHQILLERAATEPSGRKpAALRFIRSCSAPltAETAQALQTEFAAPVVCAFGMTEATHQV--TTTQIEGIGQTENPVVS 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 360 --LKARQGLSilgltEVDVRNKETQESVPrdgKTMGEIVMKGSSIMKGYLKNPKATYEAFKHGWLNSGDVGVIHPDGHVE 437
Cdd:PRK05852 354 tgLVGRSTGA-----QIRIVGSDGLPLPA---GAVGEVWLRGTTVVRGYLGDPTITAANFTDGWLRTGDLGSLSAAGDLS 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 438 IKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPTWGETPCAFVVlekgetnneDREDKLVTKErDLIEYCR 517
Cdd:PRK05852 426 IRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIV---------PRESAPPTAE-ELVQFCR 495
|
490 500
....*....|....*....|....*.
gi 15218840 518 ENLPHFMCPRKVVFLDELPKNGNGKI 543
Cdd:PRK05852 496 ERLAAFEIPASFQEASGLPHTAKGSL 521
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
178-553 |
4.30e-37 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 145.02 E-value: 4.30e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 178 RMFCIQDEHDPIS-LNYTSGTTADPKGVVISHRGaYLSTLSAIIGWEMGT------CPVYLWTLPMFH-----CNGWTFT 245
Cdd:PRK08751 199 SMPTLQIEPDDIAfLQYTGGTTGVAKGAMLTHRN-LVANMQQAHQWLAGTgkleegCEVVITALPLYHifaltANGLVFM 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 246 wgtaARGGtsvCMRHVTAPE----IYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSHRSGPVHVLTGGSPPPAALVKKVQ 321
Cdd:PRK08751 278 ----KIGG---CNHLISNPRdmpgFVKELKKTRFTAFTGVNTLFNGLLNTPGFDQIDFSSLKMTLGGGMAVQRSVAERWK 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 322 RL-GFQVMHAYGLTEATgpvlfcewqdewnrlPEN--QQMELKARQGLSILGLTEVDVRNKETQESVPRDGKtMGEIVMK 398
Cdd:PRK08751 351 QVtGLTLVEAYGLTETS---------------PAAciNPLTLKEYNGSIGLPIPSTDACIKDDAGTVLAIGE-IGELCIK 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 399 GSSIMKGYLKNPKATYEAFK-HGWLNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMP 477
Cdd:PRK08751 415 GPQVMKGYWKRPEETAKVMDaDGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVP 494
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15218840 478 HPTWGETPCAFVVlekgetnnedREDKLVTKErDLIEYCRENLPHFMCPRKVVFLDELPKNGNGKILKPKLRDIAK 553
Cdd:PRK08751 495 DEKSGEIVKVVIV----------KKDPALTAE-DVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRRELRDAAK 559
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
194-552 |
5.90e-37 |
|
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: 139.77 E-value: 5.90e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 194 TSGTTADPKGVVISHRgAYLSTLSAIIGWEMGTCP-VYLWTLPMFHCNGWTFTWGTAARGGTSVCMRHvtAPEIYKNIEM 272
Cdd:cd17630 8 TSGSTGTPKAVVHTAA-NLLASAAGLHSRLGFGGGdSWLLSLPLYHVGGLAILVRSLLAGAELVLLER--NQALAEDLAP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 273 HNVTHMCCVPTVFNILLKgNSLDLSHRSGPVHVLTGGSPPPAALVKKVQRLGFQVMHAYGLTEATGPVlfCEWqdewnRL 352
Cdd:cd17630 85 PGVTHVSLVPTQLQRLLD-SGQGPAALKSLRAVLLGGAPIPPELLERAADRGIPLYTTYGMTETASQV--ATK-----RP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 353 PENQQMELKarqglSILGLTEVDVRNKetqesvprdgktmGEIVMKGSSIMKGYLKNPKaTYEAFKHGWLNSGDVGVIHP 432
Cdd:cd17630 157 DGFGRGGVG-----VLLPGRELRIVED-------------GEIWVGGASLAMGYLRGQL-VPEFNEDGWFTTKDLGELHA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 433 DGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETnnedredklvtkERDL 512
Cdd:cd17630 218 DGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGPAD------------PAEL 285
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 15218840 513 IEYCRENLPHFMCPRKVVFLDELPKNGNGKILKPKLRDIA 552
Cdd:cd17630 286 RAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRAWL 325
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
34-543 |
1.27e-36 |
|
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: 142.20 E-value: 1.27e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 34 IYGKTRFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPK 113
Cdd:cd05914 2 YYGGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 114 ILFIyrsfeplareilqllssedsnlnlpvifiheidfpkrvsseesdyecliqrgeptplllarmfciQDEHDPISLNY 193
Cdd:cd05914 82 AIFV-----------------------------------------------------------------SDEDDVALINY 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 194 TSGTTADPKGVVISHRGaYLSTLSAIIGWEM-GTCPVYLWTLPMFHCNGWTFTWGTAARGGTSVCMRHVTAPEIYKNIEM 272
Cdd:cd05914 97 TSGTTGNSKGVMLTYRN-IVSNVDGVKEVVLlGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDKIPSAKIIALAF 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 273 HNVTHMCCVPTVFNIL---------------------LKGNSLDLSHRSG-PVH---------VLTGGSPPPAALVKKVQ 321
Cdd:cd05914 176 AQVTPTLGVPVPLVIEkifkmdiipkltlkkfkfklaKKINNRKIRKLAFkKVHeafggnikeFVIGGAKINPDVEEFLR 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 322 RLGFQVMHAYGLTEaTGPVLFcewQDEWNRLpenqqmelkarqglsILGLTEVDVRNKETQESVPRDGKTMGEIVMKGSS 401
Cdd:cd05914 256 TIGFPYTIGYGMTE-TAPIIS---YSPPNRI---------------RLGSAGKVIDGVEVRIDSPDPATGEGEIIVRGPN 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 402 IMKGYLKNPKATYEAF-KHGWLNSGDVGVIHPDGHVEIKDRSKDIIISG-GENISSVEVENIIYKYPKVLETAVV----- 474
Cdd:cd05914 317 VMKGYYKNPEATAEAFdKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSsGKNIYPEEIEAKINNMPFVLESLVVvqekk 396
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15218840 475 ----AMPHPTwgetpcAFVVLEKGETNNEDRedklvTKERDLIEYCReNLPHFMCPRKV-VFLDELPKNGNGKI 543
Cdd:cd05914 397 lvalAYIDPD------FLDVKALKQRNIIDA-----IKWEVRDKVNQ-KVPNYKKISKVkIVKEEFEKTPKGKI 458
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
161-549 |
5.43e-36 |
|
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: 139.92 E-value: 5.43e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 161 DYECLIQRGEPTPLLLARMFCIQDehDPISLNYTSGTTADPKGVVISHRgaylSTLSAIIGWE---MGTCP--VYLWTLP 235
Cdd:cd05958 74 ELAYILDKARITVALCAHALTASD--DICILAFTSGTTGAPKATMHFHR----DPLASADRYAvnvLRLREddRFVGSPP 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 236 MFhcngwtFTWGtaaRGGTSVCMRHV----------TAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSHRSGPVHV 305
Cdd:cd05958 148 LA------FTFG---LGGVLLFPFGVgasgvlleeaTPDLLLSAIARYKPTVLFTAPTAYRAMLAHPDAAGPDLSSLRKC 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 306 LTGGSPPPAALVKKVQR-LGFQVMHAYGLTEatgpvlfcewqdewnrlpeNQQMELKARQGLSILGLTEVDVRNKETqES 384
Cdd:cd05958 219 VSAGEALPAALHRAWKEaTGIPIIDGIGSTE-------------------MFHIFISARPGDARPGATGKPVPGYEA-KV 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 385 VPRDGK-----TMGEIVMKGSSIMKGYLKNPKATYeaFKHGWLNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVE 459
Cdd:cd05958 279 VDDEGNpvpdgTIGRLAVRGPTGCRYLADKRQRTY--VQGGWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVE 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 460 NIIYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETNNEDredkLVtkeRDLIEYCRENLPHFMCPRKVVFLDELPKNG 539
Cdd:cd05958 357 DVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPGPV----LA---RELQDHAKAHIAPYKYPRAIEFVTELPRTA 429
|
410
....*....|
gi 15218840 540 NGKILKPKLR 549
Cdd:cd05958 430 TGKLQRFALR 439
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
186-552 |
1.45e-35 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 140.73 E-value: 1.45e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 186 HDPIS-LNYTSGTTADPKGVVISHRG--AYLSTLSAIIG---------WEMGTcPVYLWTLPMFHCngWTFTwgtaargG 253
Cdd:PRK12492 206 LDDIAvLQYTGGTTGLAKGAMLTHGNlvANMLQVRACLSqlgpdgqplMKEGQ-EVMIAPLPLYHI--YAFT-------A 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 254 TSVCM----RH---VTAPE----IYKNIEMHNVTHMCCVPTVFNILLKG---NSLDLSHRSGpvhVLTGGSpppaALVKK 319
Cdd:PRK12492 276 NCMCMmvsgNHnvlITNPRdipgFIKELGKWRFSALLGLNTLFVALMDHpgfKDLDFSALKL---TNSGGT----ALVKA 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 320 V-----QRLGFQVMHAYGLTEaTGPVLFCEWQDEWNRLpenqqmelkARQGLSILGlTEVDVRNKETQEsVPRDGKtmGE 394
Cdd:PRK12492 349 TaerweQLTGCTIVEGYGLTE-TSPVASTNPYGELARL---------GTVGIPVPG-TALKVIDDDGNE-LPLGER--GE 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 395 IVMKGSSIMKGYLKNPKATYEAF-KHGWLNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAV 473
Cdd:PRK12492 415 LCIKGPQVMKGYWQQPEATAEALdAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAA 494
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15218840 474 VAMPHPTWGETPCAFVVlekgetnneDREDKLVTKErdLIEYCRENLPHFMCPRKVVFLDELPKNGNGKILKPKLRDIA 552
Cdd:PRK12492 495 IGVPDERSGEAVKLFVV---------ARDPGLSVEE--LKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELRDIA 562
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
38-550 |
1.56e-35 |
|
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: 138.72 E-value: 1.56e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 38 TRFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAailrhakpkilfi 117
Cdd:cd05971 5 EKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALE------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 118 YRsfeplareilqLLSSEdsnlnlpvifiheidfPKRVSSEESDyecliqrgeptplllarmfciqdehDPISLNYTSGT 197
Cdd:cd05971 72 YR-----------LSNSG----------------ASALVTDGSD-------------------------DPALIIYTSGT 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 198 TADPKGVVISHRgaYLstlsaiigweMGTCPVYLWTLPMFHCNGWTFtWGTAARG---------------GTSVC---MR 259
Cdd:cd05971 100 TGPPKGALHAHR--VL----------LGHLPGVQFPFNLFPRDGDLY-WTPADWAwigglldvllpslyfGVPVLahrMT 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 260 HVTAPEIYKNIEMHNVTHMCCVPTVFNIL-LKGNSLD---LSHRSgpvhVLTGGSPPPAALVKKVQR-LGFQVMHAYGLT 334
Cdd:cd05971 167 KFDPKAALDLMSRYGVTTAFLPPTALKMMrQQGEQLKhaqVKLRA----IATGGESLGEELLGWAREqFGVEVNEFYGQT 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 335 EA-----TGPVLFCewqdewnrlPENQQMelkarqGLSILGLTeVDVRNKETQEsVPRDgkTMGEIVMK--GSSIMKGYL 407
Cdd:cd05971 243 ECnlvigNCSALFP---------IKPGSM------GKPIPGHR-VAIVDDNGTP-LPPG--EVGEIAVElpDPVAFLGYW 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 408 KNPKATYEAFKHGWLNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPTWGETPCA 487
Cdd:cd05971 304 NNPSATEKKMAGDWLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKA 383
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15218840 488 FVVLEKGETNNedreDKLVtkeRDLIEYCRENLPHFMCPRKVVFLDELPKNGNGKILKPKLRD 550
Cdd:cd05971 384 FVVLNPGETPS----DALA---REIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRRELRA 439
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
18-553 |
1.86e-35 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 139.14 E-value: 1.86e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 18 TFLKRASEcYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNiGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTR 97
Cdd:PRK07638 6 EYKKHASL-QPNKIAIKENDRVLTYKDWFESVCKVANWLNEKE-SKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 98 LDATSIAAILRHAKPKILFIYRSFeplareiLQLLSSEDSnlnlPVIfihEIDFPKRVSSEESdyecliqrgePTPLlla 177
Cdd:PRK07638 84 WKQDELKERLAISNADMIVTERYK-------LNDLPDEEG----RVI---EIDEWKRMIEKYL----------PTYA--- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 178 rmFCIQDEHDPISLNYTSGTTADPKGVVISHRGAYLSTLSAIIGWEMGTCPVYLWTLPMFHCNgwtFTWG---TAARGGT 254
Cdd:PRK07638 137 --PIENVQNAPFYMGFTSGSTGKPKAFLRAQQSWLHSFDCNVHDFHMKREDSVLIAGTLVHSL---FLYGaisTLYVGQT 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 255 SVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLdlshRSGPVHVLTGGSPPPAALVKKVQRlgfQVMHA---- 330
Cdd:PRK07638 212 VHLMRKFIPNQVLDKLETENISVMYTVPTMLESLYKENRV----IENKMKIISSGAKWEAEAKEKIKN---IFPYAklye 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 331 -YGLTEATgpvlFCEW--QDEWNRLP-------ENQQMElkarqglsilgltevdVRNKETQESVPRDgktMGEIVMKGS 400
Cdd:PRK07638 285 fYGASELS----FVTAlvDEESERRPnsvgrpfHNVQVR----------------ICNEAGEEVQKGE---IGTVYVKSP 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 401 SIMKGYLKNPKATYEAFKHGWLNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPT 480
Cdd:PRK07638 342 QFFMGYIIGGVLARELNADGWMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSY 421
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15218840 481 WGETPCAFVvleKGETNnedredklvtkERDLIEYCRENLPHFMCPRKVVFLDELPKNGNGKILKPKLRDIAK 553
Cdd:PRK07638 422 WGEKPVAII---KGSAT-----------KQQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAKSWIE 480
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
187-543 |
5.89e-35 |
|
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: 134.70 E-value: 5.89e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 187 DPISLNYTSGTTADPKGVVISHRGAYLSTLSAII-GWEMGTCPVYLWTLPMFHCNG-WTFTWGTAARGGTSVCMRHVTAP 264
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKeGLNWVVGDVTYLPLPATHIGGlWWILTCLIHGGLCVTGGENTTYK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 265 EIYKNIEMHNVTHMCCVPTVFN--ILLKGNSLDLSHRSGPVHVltGGSPPPAALVKKVQRLGF-QVMHAYGLTEaTGPVL 341
Cdd:cd17635 82 SLFKILTTNAVTTTCLVPTLLSklVSELKSANATVPSLRLIGY--GGSRAIAADVRFIEATGLtNTAQVYGLSE-TGTAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 342 FCEWQDEwnrlpenqQMELKArQGLSILGLtEVDVRNKETQEsVPRDGKtmGEIVMKGSSIMKGYLKNPKATYEAFKHGW 421
Cdd:cd17635 159 CLPTDDD--------SIEINA-VGRPYPGV-DVYLAATDGIA-GPSASF--GTIWIKSPANMLGYWNNPERTAEVLIDGW 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 422 LNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPTWGETPCAFVVleKGETNNEDR 501
Cdd:cd17635 226 VNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVV--ASAELDENA 303
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 15218840 502 edklvtkERDLIEYCRENLPHFMCPRKVVFLDELPKNGNGKI 543
Cdd:cd17635 304 -------IRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKV 338
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
28-549 |
1.19e-34 |
|
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: 138.39 E-value: 1.19e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 28 PNRTSIIY----GKTR-FTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRLDATS 102
Cdd:cd05968 75 RTRPALRWegedGTSRtLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEA 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 103 IAAILRHAKPKILFIYRSFEPLAREILQLLSSEDSNLNLP----VIFIHEIDFPkrVSSEESDYECLIQRGEPTPLLLAR 178
Cdd:cd05968 155 AATRLQDAEAKALITADGFTRRGREVNLKEEADKACAQCPtvekVVVVRHLGND--FTPAKGRDLSYDEEKETAGDGAER 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 179 MfciqDEHDPISLNYTSGTTADPKGVVISHRGAYL-STLSAIIGWEMGTCPVYLWTLPMfhcnGWT----FTWGTAARGG 253
Cdd:cd05968 233 T----ESEDPLMIIYTSGTTGKPKGTVHVHAGFPLkAAQDMYFQFDLKPGDLLTWFTDL----GWMmgpwLIFGGLILGA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 254 TSVCMR----HVTAPEIYKNIEMHNVTHMCCVPTVFNILL-KGNSLDLSHRSGPVHVLTG-GSP----PPAALVKKVQRL 323
Cdd:cd05968 305 TMVLYDgapdHPKADRLWRMVEDHEITHLGLSPTLIRALKpRGDAPVNAHDLSSLRVLGStGEPwnpePWNWLFETVGKG 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 324 GFQVMHAYGLTEATGPVLFCewqdewnrlpeNQQMELKARQGLSILGLTEVDVRNKETQESVPrdgkTMGEIVMKGS--S 401
Cdd:cd05968 385 RNPIINYSGGTEISGGILGN-----------VLIKPIKPSSFNGPVPGMKADVLDESGKPARP----EVGELVLLAPwpG 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 402 IMKGYLKNPKATYEAFKHGWLN---SGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPH 478
Cdd:cd05968 450 MTRGFWRDEDRYLETYWSRFDNvwvHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPH 529
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15218840 479 PTWGETPCAFVVLEKGETNNEDREDklvtkerDLIEYCRENLPHFMCPRKVVFLDELPKNGNGKILKPKLR 549
Cdd:cd05968 530 PVKGEAIVCFVVLKPGVTPTEALAE-------ELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIR 593
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
38-474 |
1.39e-34 |
|
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: 136.33 E-value: 1.39e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 38 TRFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFi 117
Cdd:cd17640 4 KRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALV- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 118 yrsfeplareilqllssedsnlnlpvifiheidfpkrVSSEESDYECLIqrgeptplllarmfciqdehdpislnYTSGT 197
Cdd:cd17640 83 -------------------------------------VENDSDDLATII--------------------------YTSGT 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 198 TADPKGVVISHRGAY--LSTLSAIIGWEMGTcpVYLWTLPMFHCNGWTFTWGTAARGGTSVCMRHVTAPEIYKNIemhNV 275
Cdd:cd17640 100 TGNPKGVMLTHANLLhqIRSLSDIVPPQPGD--RFLSILPIWHSYERSAEYFIFACGCSQAYTSIRTLKDDLKRV---KP 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 276 THMCCVPTVFNILLKGnsLDLSHRSGP----------------VHVLTGGSPPPAALVKKVQRLGFQVMHAYGLTEaTGP 339
Cdd:cd17640 175 HYIVSVPRLWESLYSG--IQKQVSKSSpikqflflfflsggifKFGISGGGALPPHVDTFFEAIGIEVLNGYGLTE-TSP 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 340 VLFCewqdewNRLPENqqmeLKARQGLSILGlTEVDVRNKETQESVPRDGKtmGEIVMKGSSIMKGYLKNPKATYEAF-K 418
Cdd:cd17640 252 VVSA------RRLKCN----VRGSVGRPLPG-TEIKIVDPEGNVVLPPGEK--GIVWVRGPQVMKGYYKNPEATSKVLdS 318
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 15218840 419 HGWLNSGDVGVIHPDGHVEIKDRSKD-IIISGGENISSVEVENIIYKYPkVLETAVV 474
Cdd:cd17640 319 DGWFNTGDLGWLTCGGELVLTGRAKDtIVLSNGENVEPQPIEEALMRSP-FIEQIMV 374
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
28-542 |
2.12e-34 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 136.94 E-value: 2.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 28 PNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAIL 107
Cdd:PRK07798 17 PDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 108 RHAKPKILFIYRSFEPLAREILqllsSEDSNLNLPVIFIHEIDFPKRVSSEesDYECLIQRGEPTPLLLARmfciqdEHD 187
Cdd:PRK07798 97 DDSDAVALVYEREFAPRVAEVL----PRLPKLRTLVVVEDGSGNDLLPGAV--DYEDALAAGSPERDFGER------SPD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 188 PISLNYTSGTTADPKGVVISHRGAYLSTLSAI---IG------WEM------GTCPVYLWTLPMFHCNG-WTfTWGTAAR 251
Cdd:PRK07798 165 DLYLLYTGGTTGMPKGVMWRQEDIFRVLLGGRdfaTGepiedeEELakraaaGPGMRRFPAPPLMHGAGqWA-AFAALFS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 252 GGTSVCMRHVT--APEIYKNIEMHNVTHMCCVPTVF-----NILLKGNSLDLShrsGPVHVLTGGspppAALVKKVQRlG 324
Cdd:PRK07798 244 GQTVVLLPDVRfdADEVWRTIEREKVNVITIVGDAMarpllDALEARGPYDLS---SLFAIASGG----ALFSPSVKE-A 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 325 FQ-------VMHAYGLTEaTGpvlfcewqdewnrlpeNQQMELKARQGLSILGLT-----EVDVRNKETQESVPRDGKtM 392
Cdd:PRK07798 316 LLellpnvvLTDSIGSSE-TG----------------FGGSGTVAKGAVHTGGPRftigpRTVVLDEDGNPVEPGSGE-I 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 393 GEIVMKGSsIMKGYLKNPKATYEAFK----HGWLNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKV 468
Cdd:PRK07798 378 GWIARRGH-IPLGYYKDPEKTAETFPtidgVRYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDV 456
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15218840 469 LETAVVAMPHPTWGETPCAFVVLEKGETNNEDredklvtkerDLIEYCRENLPHFMCPRKVVFLDELPKNGNGK 542
Cdd:PRK07798 457 ADALVVGVPDERWGQEVVAVVQLREGARPDLA----------ELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
51-550 |
9.97e-34 |
|
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: 134.90 E-value: 9.97e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 51 RLAASLIS--LNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFIYRSFEPLAREI 128
Cdd:cd05928 52 RKAANVLSgaCGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSDELAPEVDSV 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 129 lqllSSEDSNLNLpvifiheidfpKRVSSEES-----DYECLIQRGEPTPLllarmfCIQDEH-DPISLNYTSGTTADPK 202
Cdd:cd05928 132 ----ASECPSLKT-----------KLLVSEKSrdgwlNFKELLNEASTEHH------CVETGSqEPMAIYFTSGTTGSPK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 203 GVVISHrGAYLSTLSAIIGWEMGTCPV-YLWTLPMfhcNGWT-FTWGTA----ARGGTSVC--MRHVTAPEIYKNIEMHN 274
Cdd:cd05928 191 MAEHSH-SSLGLGLKVNGRYWLDLTASdIMWNTSD---TGWIkSAWSSLfepwIQGACVFVhhLPRFDPLVILKTLSSYP 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 275 VTHMCCVPTVFNILLKGnslDLSHRSGPV--HVLTGGSP-PPAALVKKVQRLGFQVMHAYGLTEAtgpVLFCEWQdewnr 351
Cdd:cd05928 267 ITTFCGAPTVYRMLVQQ---DLSSYKFPSlqHCVTGGEPlNPEVLEKWKAQTGLDIYEGYGQTET---GLICANF----- 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 352 lpenQQMELKArqGLSILGLTEVDVRNKETQESVPRDGKTmGEIVMKGS-----SIMKGYLKNPKATYEAFKHGWLNSGD 426
Cdd:cd05928 336 ----KGMKIKP--GSMGKASPPYDVQIIDDNGNVLPPGTE-GDIGIRVKpirpfGLFSGYVDNPEKTAATIRGDFYLTGD 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 427 VGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPTWGETPCAFVVLeKGETNNEDREDklV 506
Cdd:cd05928 409 RGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVL-APQFLSHDPEQ--L 485
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 15218840 507 TKErdLIEYCRENLPHFMCPRKVVFLDELPKNGNGKILKPKLRD 550
Cdd:cd05928 486 TKE--LQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRD 527
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
30-561 |
1.27e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 134.42 E-value: 1.27e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 30 RTSIIYGKTRFTWPQTYDRCCRLAASLIS-LNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILR 108
Cdd:PRK07867 19 DRGLYFEDSFTSWREHIRGSAARAAALRArLDPTRPPHVGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDIA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 109 HAKPKILFIYRSFEPLAreilqllssEDSNLNLPVIfiheidfpkRVSSEESDYECLIQRGEPTPLLLArmfciqDEHDP 188
Cdd:PRK07867 99 HADCQLVLTESAHAELL---------DGLDPGVRVI---------NVDSPAWADELAAHRDAEPPFRVA------DPDDL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 189 ISLNYTSGTTADPKGVVISHR-----GAYLSTlsaiigwEMGTCP---VYLwTLPMFHCNGWTFTWGTAARGGTSVCMRH 260
Cdd:PRK07867 155 FMLIFTSGTSGDPKAVRCTHRkvasaGVMLAQ-------RFGLGPddvCYV-SMPLFHSNAVMAGWAVALAAGASIALRR 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 261 -VTAPEIYKNIEMHNVTHMCCV--PTVFnILLKGNSLDlsHRSGPVHVLTGGSPPPAALVKKVQRLGFQVMHAYGLTEat 337
Cdd:PRK07867 227 kFSASGFLPDVRRYGATYANYVgkPLSY-VLATPERPD--DADNPLRIVYGNEGAPGDIARFARRFGCVVVDGFGSTE-- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 338 GPVLFcewqdewNRLPENQQMEL-KARQGLSILgltevdvrNKETQESVPR-----DGKT-----MGEIV-MKGSSIMKG 405
Cdd:PRK07867 302 GGVAI-------TRTPDTPPGALgPLPPGVAIV--------DPDTGTECPPaedadGRLLnadeaIGELVnTAGPGGFEG 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 406 YLKNPKATYEAFKHGWLNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPTWGETP 485
Cdd:PRK07867 367 YYNDPEADAERMRGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQV 446
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15218840 486 CAFVVLEKGETNNEDREDKLVTKERDlieycrenLPHFMCPRKVVFLDELPKNGNGKILKPKLRdiAKGLVAEDEV 561
Cdd:PRK07867 447 MAALVLAPGAKFDPDAFAEFLAAQPD--------LGPKQWPSYVRVCAELPRTATFKVLKRQLS--AEGVDCADPV 512
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
54-557 |
1.15e-32 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 133.90 E-value: 1.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 54 ASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVlnPINtrLDATSIAAILRHA--KPKILFIYRSfeplaREILQL 131
Cdd:PRK08633 655 ARLLKRELKDEENVGILLPPSVAGALANLALLLAGKV--PVN--LNYTASEAALKSAieQAQIKTVITS-----RKFLEK 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 132 LSSEDSNLNLP----VIFIHeiDFPKRVSSEESDYECLIQRGEPTPLLLARMFCIQDEHDPISLNYTSGTTADPKGVVIS 207
Cdd:PRK08633 726 LKNKGFDLELPenvkVIYLE--DLKAKISKVDKLTALLAARLLPARLLKRLYGPTFKPDDTATIIFSSGSEGEPKGVMLS 803
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 208 HRGaYLSTLSAIIgweMGTCP----VYLWTLPMFHCNGWTFT-WGTAARGGTSVCmrHVT---APEIYKNIEMHNVTHMC 279
Cdd:PRK08633 804 HHN-ILSNIEQIS---DVFNLrnddVILSSLPFFHSFGLTVTlWLPLLEGIKVVY--HPDptdALGIAKLVAKHRATILL 877
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 280 CVPTVFNILLKGN--------SLDLshrsgpvhVLTGGSPPPAALVKKVQ-RLGFQVMHAYGLTEaTGPVLFCEwqdewn 350
Cdd:PRK08633 878 GTPTFLRLYLRNKklhplmfaSLRL--------VVAGAEKLKPEVADAFEeKFGIRILEGYGATE-TSPVASVN------ 942
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 351 rLP---ENQQMELKARQ----GLSILGlTEVDVRNKETQESVPrdGKTMGEIVMKGSSIMKGYLKNPKATYEAFKH---- 419
Cdd:PRK08633 943 -LPdvlAADFKRQTGSKegsvGMPLPG-VAVRIVDPETFEELP--PGEDGLILIGGPQVMKGYLGDPEKTAEVIKDidgi 1018
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 420 GWLNSGDVGVIHPDGHVEIKDR----SKdIiisGGENISSVEVENIIYK--YPKVLETAVVAMPHPTWGEtpcAFVVLek 493
Cdd:PRK08633 1019 GWYVTGDKGHLDEDGFLTITDRysrfAK-I---GGEMVPLGAVEEELAKalGGEEVVFAVTAVPDEKKGE---KLVVL-- 1089
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15218840 494 gETNNEDREDKLvtkeRDLIEYCreNLPHFMCPRKVVFLDELPKNGNGKI-LKpKLRDIAKGLVA 557
Cdd:PRK08633 1090 -HTCGAEDVEEL----KRAIKES--GLPNLWKPSRYFKVEALPLLGSGKLdLK-GLKELALALLG 1146
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
28-543 |
5.13e-32 |
|
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: 129.32 E-value: 5.13e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 28 PNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAIL 107
Cdd:cd17646 12 PDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAYML 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 108 RHAKPKILFIYRSFEPLAREILqllsseDSNLNLPVIFIHEIDFPKRVSSEESDYECLIqrgeptplllarmfciqdehd 187
Cdd:cd17646 92 ADAGPAVVLTTADLAARLPAGG------DVALLGDEALAAPPATPPLVPPRPDNLAYVI--------------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 188 pislnYTSGTTADPKGVVISHRGaylstLSAIIGWEMGTCP------VYLWTLPMFHCNGWTFTWGTAArGGTSVCMR-- 259
Cdd:cd17646 145 -----YTSGSTGRPKGVMVTHAG-----IVNRLLWMQDEYPlgpgdrVLQKTPLSFDVSVWELFWPLVA-GARLVVARpg 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 260 -HVTAPEIYKNIEMHNVTHMCCVPTVFNILLkgNSLDLSHRSGPVHVLTGGSPPPAALVKKV-QRLGFQVMHAYGLTEAT 337
Cdd:cd17646 214 gHRDPAYLAALIREHGVTTCHFVPSMLRVFL--AEPAAGSCASLRRVFCSGEALPPELAARFlALPGAELHNLYGPTEAA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 338 GPVLFCEWQDEWNRLPenqqmelkarqgLSI---LGLTEVDVRNkETQESVPrDGkTMGEIVMKGSSIMKGYLKNPKATY 414
Cdd:cd17646 292 IDVTHWPVRGPAETPS------------VPIgrpVPNTRLYVLD-DALRPVP-VG-VPGELYLGGVQLARGYLGRPALTA 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 415 EAFKHGWLN-------SGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPTWGETPCA 487
Cdd:cd17646 357 ERFVPDPFGpgsrmyrTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVG 436
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 15218840 488 FVVLEKGETNNEDREdklvtkerdLIEYCRENLPHFMCPRKVVFLDELPKNGNGKI 543
Cdd:cd17646 437 YVVPAAGAAGPDTAA---------LRAHLAERLPEYMVPAAFVVLDALPLTANGKL 483
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
41-543 |
9.80e-32 |
|
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: 129.28 E-value: 9.80e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 41 TWPQTYDRCCRLAASLISLNiGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPI----NTRLDATsIAAILRHAKPKILF 116
Cdd:cd05931 26 TYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLppptPGRHAER-LAAILADAGPRVVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 117 IYRSFEPLAREILqllsSEDSNLNLPVIFIHEIdfpkrVSSEESDYECLIQRGEPTPLLLarmfciQdehdpislnYTSG 196
Cdd:cd05931 104 TTAAALAAVRAFA----ASRPAAGTPRLLVVDL-----LPDTSAADWPPPSPDPDDIAYL------Q---------YTSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 197 TTADPKGVVISHRGAyLSTLSAII-GWEMG-TCPVYLWtLPMFHCNGWTFTWGTAA-RGGTSVCM---RHVTAPEIY-KN 269
Cdd:cd05931 160 STGTPKGVVVTHRNL-LANVRQIRrAYGLDpGDVVVSW-LPLYHDMGLIGGLLTPLySGGPSVLMspaAFLRRPLRWlRL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 270 IEMHNVTHMCcVPT-VFNILLK------GNSLDLSHrsgpVHVLTGGSPP--PAAL---VKKVQRLGF--QVMH-AYGLT 334
Cdd:cd05931 238 ISRYRATISA-APNfAYDLCVRrvrdedLEGLDLSS----WRVALNGAEPvrPATLrrfAEAFAPFGFrpEAFRpSYGLA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 335 EAT----------GPVLfcewqDEWNRLPENQQMELKARQGLSILGL---------TEVDVRNKETQESVPrDGkTMGEI 395
Cdd:cd05931 313 EATlfvsggppgtGPVV-----LRVDRDALAGRAVAVAADDPAARELvscgrplpdQEVRIVDPETGRELP-DG-EVGEI 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 396 VMKGSSIMKGYLKNPKATYEAFK-------HGWLNSGDVGVIHpDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKV 468
Cdd:cd05931 386 WVRGPSVASGYWGRPEATAETFGalaatdeGGWLRTGDLGFLH-DGELYITGRLKDLIIVRGRNHYPQDIEATAEEAHPA 464
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15218840 469 L-ETAVVAMPHPTWGETPcAFVVLEKGETNNEDREDKLVTKERDLIeyCREnlpHFMCPRKVVFL--DELPKNGNGKI 543
Cdd:cd05931 465 LrPGCVAAFSVPDDGEER-LVVVAEVERGADPADLAAIAAAIRAAV--ARE---HGVAPADVVLVrpGSIPRTSSGKI 536
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
30-550 |
3.03e-31 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 127.84 E-value: 3.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 30 RTSIIYGKTRFTWPQTYDRCCRLAASLISLNIGKNDV-VSVVAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILR 108
Cdd:PRK13388 17 TIAVRYGDRTWTWREVLAEAAARAAALIALADPDRPLhVGVLLGNTPEMLFWLAAAALGGYVLVGLNTTRRGAALAADIR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 109 HAKPKILFIyrsfeplAREILQLLSSedsnLNLPVIFIHEIDFPkrvsseesDYECLIQR-GEPTPLLLArmfciqDEHD 187
Cdd:PRK13388 97 RADCQLLVT-------DAEHRPLLDG----LDLPGVRVLDVDTP--------AYAELVAAaGALTPHREV------DAMD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 188 PISLNYTSGTTADPKGVVISHRGAYLSTLSAIIGWEMGTCPVYLWTLPMFHCNGWTFTWGTAARGGTSVCMR-HVTAPEI 266
Cdd:PRK13388 152 PFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDDVCYVSMPLFHSNAVMAGWAPAVASGAAVALPaKFSASGF 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 267 YKNIEMHNVTHMCCVPTVFNILLKGNSLDlSHRSGPVHVLTGGSPPPAALVKKVQRLGFQVMHAYGLTEATGPVLfcewq 346
Cdd:PRK13388 232 LDDVRRYGATYFNYVGKPLAYILATPERP-DDADNPLRVAFGNEASPRDIAEFSRRFGCQVEDGYGSSEGAVIVV----- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 347 dewnRLPENQQMEL-KARQGLSILgltevdvrNKETQESVPR-----DGK------TMGEIVMK-GSSIMKGYLKNPKAT 413
Cdd:PRK13388 306 ----REPGTPPGSIgRGAPGVAIY--------NPETLTECAVarfdaHGAllnadeAIGELVNTaGAGFFEGYYNNPEAT 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 414 YEAFKHGWLNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPTWGETPCAFVVLEK 493
Cdd:PRK13388 374 AERMRHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVMAALVLRD 453
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 15218840 494 GETNNEDREDKLVTKERDlieycrenLPHFMCPRKVVFLDELPKNGNGKILKPKLRD 550
Cdd:PRK13388 454 GATFDPDAFAAFLAAQPD--------LGTKAWPRYVRIAADLPSTATNKVLKRELIA 502
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
28-543 |
9.01e-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: 125.78 E-value: 9.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 28 PNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAIL 107
Cdd:cd12117 11 PDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAERLAFML 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 108 RHAKPKILFIYRSFEPLAREilqllssedsnlnLPVIFIHEIDFPKRVSSEEsdyecliqrgePTPLLLARMFCIqdehd 187
Cdd:cd12117 91 ADAGAKVLLTDRSLAGRAGG-------------LEVAVVIDEALDAGPAGNP-----------AVPVSPDDLAYV----- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 188 pislNYTSGTTADPKGVVISHRGaylstlsaIIGWEMGTCpvYLWTLP----MFHCN-GW---TF-TWGTAARGGTSVCM 258
Cdd:cd12117 142 ----MYTSGSTGRPKGVAVTHRG--------VVRLVKNTN--YVTLGPddrvLQTSPlAFdasTFeIWGALLNGARLVLA 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 259 RH---VTAPEIYKNIEMHNVTHMCCVPTVFNILLkgnSLDLSHRSGPVHVLTGGSPPPAALVKKVQRL--GFQVMHAYGL 333
Cdd:cd12117 208 PKgtlLDPDALGALIAEEGVTVLWLTAALFNQLA---DEDPECFAGLRELLTGGEVVSPPHVRRVLAAcpGLRLVNGYGP 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 334 TEATGPVLFCEWQDEwnrlpenqqmelkARQGLSI-----LGLTEVDVRNkETQESVPRDgkTMGEIVMKGSSIMKGYLK 408
Cdd:cd12117 285 TENTTFTTSHVVTEL-------------DEVAGSIpigrpIANTRVYVLD-EDGRPVPPG--VPGELYVGGDGLALGYLN 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 409 NPKATYEAF-KHGWLN------SGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPTW 481
Cdd:cd12117 349 RPALTAERFvADPFGPgerlyrTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGG 428
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15218840 482 GETPCAFVVLEKGETNNEDREdklvtkerdlieYCRENLPHFMCPRKVVFLDELPKNGNGKI 543
Cdd:cd12117 429 DKRLVAYVVAEGALDAAELRA------------FLRERLPAYMVPAAFVVLDELPLTANGKV 478
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
28-543 |
4.48e-30 |
|
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: 123.56 E-value: 4.48e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 28 PNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAIL 107
Cdd:cd12116 1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 108 RHAKPKILFIyrsfEPLAREILqllssedsNLNLPVIFIHEIDFPKrvsseesdyecliQRGEPTPLllarmfciQDEHD 187
Cdd:cd12116 81 EDAEPALVLT----DDALPDRL--------PAGLPVLLLALAAAAA-------------APAAPRTP--------VSPDD 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 188 PISLNYTSGTTADPKGVVISHRGayLSTLSAIIGWEMGTCPVYLW---TLPMFHCNGWTFTWGTAARGGTSVCMR-HVTA 263
Cdd:cd12116 128 LAYVIYTSGSTGRPKGVVVSHRN--LVNFLHSMRERLGLGPGDRLlavTTYAFDISLLELLLPLLAGARVVIAPReTQRD 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 264 PEIYKN-IEMHNVTHMCCVPTVFNILLKGNSLDLSHrsgpVHVLTGGSPPPAALVKKVQRLGFQVMHAYGLTEATGPVLF 342
Cdd:cd12116 206 PEALARlIEAHSITVMQATPATWRMLLDAGWQGRAG----LTALCGGEALPPDLAARLLSRVGSLWNLYGPTETTIWSTA 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 343 CEWQDEWNRLPenqqmelkarQGLSILGlTEVDVRNkETQESVPRDgkTMGEIVMKGSSIMKGYLKNPKATYEAFKHG-- 420
Cdd:cd12116 282 ARVTAAAGPIP----------IGRPLAN-TQVYVLD-AALRPVPPG--VPGELYIGGDGVAQGYLGRPALTAERFVPDpf 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 421 ------WLNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAmpHPTWGETP-CAFVVLEK 493
Cdd:cd12116 348 agpgsrLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVV--REDGGDRRlVAYVVLKA 425
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 15218840 494 GETNNEDRedklvtkerdLIEYCRENLPHFMCPRKVVFLDELPKNGNGKI 543
Cdd:cd12116 426 GAAPDAAA----------LRAHLRATLPAYMVPSAFVRLDALPLTANGKL 465
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
20-550 |
4.55e-30 |
|
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: 124.14 E-value: 4.55e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 20 LKRASECYPNRTSII----YGKTR-FTWPQTYDRCCRLAASLISLNIGKNDVVSVVapnTPAMYEMHFAVP---MAGAVL 91
Cdd:cd05970 23 VDAMAKEYPDKLALVwcddAGEERiFTFAELADYSDKTANFFKAMGIGKGDTVMLT---LKRRYEFWYSLLalhKLGAIA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 92 NPINTRLDATSIaaILRHAKPKILFIYRSFEPLAREILQLLSSEDSNLnlpvifiheidfPKRVSSEES------DYECL 165
Cdd:cd05970 100 IPATHQLTAKDI--VYRIESADIKMIVAIAEDNIPEEIEKAAPECPSK------------PKLVWVGDPvpegwiDFRKL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 166 IQrgEPTPLLLARMFCIQDEHDPISLNY-TSGTTADPKgvVISHRGAYlsTLSAIIgwemgtcpvylwTLPMFHC---NG 241
Cdd:cd05970 166 IK--NASPDFERPTANSYPCGEDILLVYfSSGTTGMPK--MVEHDFTY--PLGHIV------------TAKYWQNvreGG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 242 WTFT-----WGTAARG---GTSVC--------MRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGnslDLSHR--SGPV 303
Cdd:cd05970 228 LHLTvadtgWGKAVWGkiyGQWIAgaavfvydYDKFDPKALLEKLSKYGVTTFCAPPTIYRFLIRE---DLSRYdlSSLR 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 304 HVLTGGSP-PPAALVKKVQRLGFQVMHAYGLTEATGPVLFCEWqdewnrlpenqqMELK-ARQGLSILGLtEVDVrnket 381
Cdd:cd05970 305 YCTTAGEAlNPEVFNTFKEKTGIKLMEGFGQTETTLTIATFPW------------MEPKpGSMGKPAPGY-EIDL----- 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 382 qesVPRDGKTM-----GEIVMKGSS-----IMKGYLKNPKATYEAFKHGWLNSGDVGVIHPDGHVEIKDRSKDIIISGGE 451
Cdd:cd05970 367 ---IDREGRSCeageeGEIVIRTSKgkpvgLFGGYYKDAEKTAEVWHDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGY 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 452 NISSVEVENIIYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETNNEDredklVTKErdLIEYCRENLPHFMCPRKVVF 531
Cdd:cd05970 444 RIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVLAKGYEPSEE-----LKKE--LQDHVKKVTAPYKYPRIVEF 516
|
570
....*....|....*....
gi 15218840 532 LDELPKNGNGKILKPKLRD 550
Cdd:cd05970 517 VDELPKTISGKIRRVEIRE 535
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
29-545 |
8.15e-30 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 123.85 E-value: 8.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 29 NRTSIIY----GKTRFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIA 104
Cdd:PRK04319 59 DKVALRYldasRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVR 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 105 AILRHAKPKILFIYRSFepLAREILQ--------LLSSEDSNLNLPVIfiheiDFPKRVSSEESDYECliqrgEPTplll 176
Cdd:PRK04319 139 DRLEDSEAKVLITTPAL--LERKPADdlpslkhvLLVGEDVEEGPGTL-----DFNALMEQASDEFDI-----EWT---- 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 177 armfciqDEHDPISLNYTSGTTADPKGV------VISHR--GAYLSTL--------SAIIGWEMGTcpVYLWTLPMFHcn 240
Cdd:PRK04319 203 -------DREDGAILHYTSGSTGKPKGVlhvhnaMLQHYqtGKYVLDLheddvywcTADPGWVTGT--SYGIFAPWLN-- 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 241 gwtftwgtaarGGTSVCMRHVTAPEI-YKNIEMHNVTHMCCVPTVFNILLKGNS-----LDLSH-RsgpvHVLTGGSP-P 312
Cdd:PRK04319 272 -----------GATNVIDGGRFSPERwYRILEDYKVTVWYTAPTAIRMLMGAGDdlvkkYDLSSlR----HILSVGEPlN 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 313 PAALV--KKVqrLGFQVMHAYGLTEaTGPVLFCEWQdewnrlpenqQMELK-ARQGLSILGLTEVDVRNKEtqESVPRDg 389
Cdd:PRK04319 337 PEVVRwgMKV--FGLPIHDNWWMTE-TGGIMIANYP----------AMDIKpGSMGKPLPGIEAAIVDDQG--NELPPN- 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 390 kTMGEIVMKGS--SIMKGYLKNPKATYEAFKHGWLNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPK 467
Cdd:PRK04319 401 -RMGNLAIKKGwpSMMRGIWNNPEKYESYFAGDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPA 479
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15218840 468 VLETAVVAMPHPTWGETPCAFVVLEKG-ETNNEDREdklvtkerDLIEYCRENLPHFMCPRKVVFLDELPKNGNGKILK 545
Cdd:PRK04319 480 VAEAGVIGKPDPVRGEIIKAFVALRPGyEPSEELKE--------EIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMR 550
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
40-549 |
1.26e-29 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 121.47 E-value: 1.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 40 FTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTrldatsiaailrhakpkilfiyr 119
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFT----------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 120 SFEPLAreILQLLSSEDSNLnlpviFIHEIDfpkrvsseesdyecliQRGEPTPLLLARMFciqdehdpislnyTSGTTA 199
Cdd:cd05973 58 AFGPKA--IEHRLRTSGARL-----VVTDAA----------------NRHKLDSDPFVMMF-------------TSGTTG 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 200 DPKGVVISHRgaYLSTLSAIIGWEMGTCP--VYlWTL--PmfhcnGWTFTWGTAARG----GTSVCMRH--VTAPEIYKN 269
Cdd:cd05973 102 LPKGVPVPLR--ALAAFGAYLRDAVDLRPedSF-WNAadP-----GWAYGLYYAITGplalGHPTILLEggFSVESTWRV 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 270 IEMHNVTHMCCVPTVFNILLKGNSLDLSHRSGPVHVLTGGSPP--PAALVKKVQRLGFQVMHAYGLTEaTGPVLFCEWQD 347
Cdd:cd05973 174 IERLGVTNLAGSPTAYRLLMAAGAEVPARPKGRLRRVSSAGEPltPEVIRWFDAALGVPIHDHYGQTE-LGMVLANHHAL 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 348 EwnrlpenqqMELKA-RQGLSILGLtEVDVRNKETQESVPRDgktMGEIVM--KGSSIM--KGYLKNPKAtyeAFKHGWL 422
Cdd:cd05973 253 E---------HPVHAgSAGRAMPGW-RVAVLDDDGDELGPGE---PGRLAIdiANSPLMwfRGYQLPDTP---AIDGGYY 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 423 NSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETNNEDRE 502
Cdd:cd05973 317 LTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGTPALA 396
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 15218840 503 DKLVTkerdlieYCRENLPHFMCPRKVVFLDELPKNGNGKILKPKLR 549
Cdd:cd05973 397 DELQL-------HVKKRLSAHAYPRTIHFVDELPKTPSGKIQRFLLR 436
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
40-502 |
8.09e-29 |
|
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: 120.27 E-value: 8.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 40 FTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFIYR 119
Cdd:cd05932 7 FTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFVGK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 120 sfeplareilqLLSSEDSNLNLPVIFIHEIDFPKRVSSEESDYECLIQRGEPtplllarmfcIQDE--HDP---ISLNYT 194
Cdd:cd05932 87 -----------LDDWKAMAPGVPEGLISISLPPPSAANCQYQWDDLIAQHPP----------LEERptRFPeqlATLIYT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 195 SGTTADPKGVVISHrGAYLSTLSAIIGwEMGTCP--VYLWTLPMFHCNGWTFTWGTAARGGTSVCMRHV--TAPEiykNI 270
Cdd:cd05932 146 SGTTGQPKGVMLTF-GSFAWAAQAGIE-HIGTEEndRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAESldTFVE---DV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 271 EMHNVTHMCCVP---TVF-------------NILLK------------GNSLDLSHrsgpVHVLTGGSPP-PAALVKKVQ 321
Cdd:cd05932 221 QRARPTLFFSVPrlwTKFqqgvqdkipqqklNLLLKipvvnslvkrkvLKGLGLDQ----CRLAGCGSAPvPPALLEWYR 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 322 RLGFQVMHAYGLTEATGPVLFCEwqdewnrlPENQQMEL--KARQGlsilglteVDVRNKETqesvprdgktmGEIVMKG 399
Cdd:cd05932 297 SLGLNILEAYGMTENFAYSHLNY--------PGRDKIGTvgNAGPG--------VEVRISED-----------GEILVRS 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 400 SSIMKGYLKNPKATYEAF-KHGWLNSGDVGVIHPDGHVEIKDRSKDII-ISGGENISSVEVENIIYKYPKVLETAVVA-- 475
Cdd:cd05932 350 PALMMGYYKDPEATAEAFtADGFLRTGDKGELDADGNLTITGRVKDIFkTSKGKYVAPAPIENKLAEHDRVEMVCVIGsg 429
|
490 500 510
....*....|....*....|....*....|
gi 15218840 476 MPHPTwgetpcAFVVLEKG---ETNNEDRE 502
Cdd:cd05932 430 LPAPL------ALVVLSEEarlRADAFARA 453
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
67-552 |
8.72e-29 |
|
C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.
Pssm-ID: 341235 [Multi-domain] Cd Length: 490 Bit Score: 119.74 E-value: 8.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 67 VSVVAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFIYRSFEplarEILQLLSSEDSNLNLPVIFI 146
Cdd:cd05909 34 VGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLTSKQFI----EKLKLHHLFDVEYDARIVYL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 147 HEIDfpKRVSSEEsdyECL--IQRGEPTPLLLARMFCI-QDEHDPISLNYTSGTTADPKGVVISHRGAY--LSTLSAIIg 221
Cdd:cd05909 110 EDLR--AKISKAD---KCKafLAGKFPPKWLLRIFGVApVQPDDPAVILFTSGSEGLPKGVVLSHKNLLanVEQITAIF- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 222 wEMGTCPVYLWTLPMFHCNGWTFT-WGTAARGGTSVCMRHVTAPE-IYKNIEMHNVTHMCCVPTVFNILLK-GNSLDLSh 298
Cdd:cd05909 184 -DPNPEDVVFGALPFFHSFGLTGClWLPLLSGIKVVFHPNPLDYKkIPELIYDKKATILLGTPTFLRGYARaAHPEDFS- 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 299 rsGPVHVLTGGSPPPAALVKKVQ-RLGFQVMHAYGLTEATgPVLFCewqdewNRlpenQQMELKARQ-GLSILGLtEVDV 376
Cdd:cd05909 262 --SLRLVVAGAEKLKDTLRQEFQeKFGIRILEGYGTTECS-PVISV------NT----PQSPNKEGTvGRPLPGM-EVKI 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 377 RNKETQESVPrDGKTmGEIVMKGSSIMKGYLKNPKATYEAFKHGWLNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSV 456
Cdd:cd05909 328 VSVETHEEVP-IGEG-GLLLVRGPNVMLGYLNEPELTSFAFGDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLE 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 457 EVENIIYK-YPKVLETAVVAMPHPTWGETPCAFVVlekgeTNNEDREdklvtkerDLIEYCRE-NLPHFMCPRKVVFLDE 534
Cdd:cd05909 406 AIEDILSEiLPEDNEVAVVSVPDGRKGEKIVLLTT-----TTDTDPS--------SLNDILKNaGISNLAKPSYIHQVEE 472
|
490
....*....|....*...
gi 15218840 535 LPKNGNGKILKPKLRDIA 552
Cdd:cd05909 473 IPLLGTGKPDYVTLKALA 490
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
39-550 |
1.48e-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: 118.18 E-value: 1.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 39 RFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILfIY 118
Cdd:cd17653 22 SLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARIQAILRTSGATLL-LT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 119 rsfeplareilqlLSSEDsnlnlpvifiheidfpkrvsseesDYECLIqrgeptplllarmfciqdehdpislnYTSGTT 198
Cdd:cd17653 101 -------------TDSPD------------------------DLAYII--------------------------FTSGST 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 199 ADPKGVVISHRG--AYLSTLSAiigwEMGTCP---VYLWTLPMFHCNGWTFtWGTAARGGTsVCMRHVTAPEIYKnIEMH 273
Cdd:cd17653 118 GIPKGVMVPHRGvlNYVSQPPA----RLDVGPgsrVAQVLSIAFDACIGEI-FSTLCNGGT-LVLADPSDPFAHV-ARTV 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 274 NVTHmcCVPTVFNILlKGNSLDLSHRsgpvhVLTGGSPPPAALVKKvQRLGFQVMHAYGLTEATGPVLFCEWqdewnrLP 353
Cdd:cd17653 191 DALM--STPSILSTL-SPQDFPNLKT-----IFLGGEAVPPSLLDR-WSPGRRLYNAYGPTECTISSTMTEL------LP 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 354 ENQQMELKARQGLSILGLtevdvrNKETQEsVPRDGKtmGEIVMKGSSIMKGYLKNPKATYEAFK-----HGWL--NSGD 426
Cdd:cd17653 256 GQPVTIGKPIPNSTCYIL------DADLQP-VPEGVV--GEICISGVQVARGYLGNPALTASKFVpdpfwPGSRmyRTGD 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 427 VGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPhptwGETPCAFVVlekGETNNEDRedklv 506
Cdd:cd17653 327 YGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQSQPEVTQAAAIVV----NGRLVAFVT---PETVDVDG----- 394
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 15218840 507 tkerdLIEYCRENLPHFMCPRKVVFLDELPKNGNGKILKPKLRD 550
Cdd:cd17653 395 -----LRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
28-543 |
1.89e-28 |
|
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: 118.24 E-value: 1.89e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 28 PNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPintrLDATSIAAIL 107
Cdd:cd17649 1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVP----LDPEYPAERL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 108 RHakpkilfiyrsfeplareILqllssEDSNLnlpvifiheidfpkrvsseesdyecliqrgeptPLLLArmfciqdeHD 187
Cdd:cd17649 77 RY------------------ML-----EDSGA---------------------------------GLLLT--------HH 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 188 PISLN---YTSGTTADPKGVVISHrgAYLSTLSAIIG--WEMGTCPVYLWTLPmFHCNGWTFTWGTAARGGTSVCMRH-- 260
Cdd:cd17649 93 PRQLAyviYTSGSTGTPKGVAVSH--GPLAAHCQATAerYGLTPGDRELQFAS-FNFDGAHEQLLPPLICGACVVLRPde 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 261 --VTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSHRSGPVHVL-TGGSPPPAALVKKVQRLGFQVMHAYGLTEAT 337
Cdd:cd17649 170 lwASADELAEMVRELGVTVLDLPPAYLQQLAEEADRTGDGRPPSLRLYiFGGEALSPELLRRWLKAPVRLFNAYGPTEAT 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 338 -GPVLF-CEWQDE--WNRLPENqqmelkarqglSILGLTEVDVRNKETQEsVPrDGKTmGEIVMKGSSIMKGYLKNPKAT 413
Cdd:cd17649 250 vTPLVWkCEAGAAraGASMPIG-----------RPLGGRSAYILDADLNP-VP-VGVT-GELYIGGEGLARGYLGRPELT 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 414 YEAF------KHG--WLNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPTwGETP 485
Cdd:cd17649 316 AERFvpdpfgAPGsrLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAG-GKQL 394
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 15218840 486 CAFVVLEKGETNNEDREDklvtkerdLIEYCRENLPHFMCPRKVVFLDELPKNGNGKI 543
Cdd:cd17649 395 VAYVVLRAAAAQPELRAQ--------LRTALRASLPDYMVPAHLVFLARLPLTPNGKL 444
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
22-543 |
4.14e-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: 117.83 E-value: 4.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 22 RASECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRLDAT 101
Cdd:cd17651 3 RQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 102 SIAAILRHAKPKILfiyrsfepLAREILQLLSSEDSNLNLPvifiheIDFPKRVSSEESdyecliqrgEPTPLLlarmfc 181
Cdd:cd17651 83 RLAFMLADAGPVLV--------LTHPALAGELAVELVAVTL------LDQPGAAAGADA---------EPDPAL------ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 182 iqDEHDPISLNYTSGTTADPKGVVISHRgaylsTLSAIIGW---EMGTCP---VYLWTLPMFHCNGWTfTWGTAARGGTs 255
Cdd:cd17651 134 --DADDLAYVIYTSGSTGRPKGVVMPHR-----SLANLVAWqarASSLGPgarTLQFAGLGFDVSVQE-IFSTLCAGAT- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 256 vcmRHVTAPEIYKN-------IEMHNVTHmCCVPTVFNILLKGNSLDLSHRSGPV-HVLTGGSPPP--AALVKKVQRLGF 325
Cdd:cd17651 205 ---LVLPPEEVRTDppalaawLDEQRISR-VFLPTVALRALAEHGRPLGVRLAALrYLLTGGEQLVltEDLREFCAGLPG 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 326 QVMH-AYGLTEATgpVLFCEW----QDEWNRLPenqqmelkarqglSI---LGLTEVDVRNkETQESVPrDGKTmGEIVM 397
Cdd:cd17651 281 LRLHnHYGPTETH--VVTALSlpgdPAAWPAPP-------------PIgrpIDNTRVYVLD-AALRPVP-PGVP-GELYI 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 398 KGSSIMKGYLKNPKATYEAF-KHGWLN------SGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLE 470
Cdd:cd17651 343 GGAGLARGYLNRPELTAERFvPDPFVPgarmyrTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVRE 422
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15218840 471 TAVVAMPHPTWGETPCAFVVLekgetnneDREDKLVTKErdLIEYCRENLPHFMCPRKVVFLDELPKNGNGKI 543
Cdd:cd17651 423 AVVLAREDRPGEKRLVAYVVG--------DPEAPVDAAE--LRAALATHLPEYMVPSAFVLLDALPLTPNGKL 485
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
19-564 |
4.72e-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: 119.96 E-value: 4.72e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 19 FLKRAsECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRL 98
Cdd:COG1020 482 FEAQA-ARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAY 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 99 DATSIAAILRHAKPKILfiyrsfepLAREILQllsSEDSNLNLPVIFIheidfpkrvsseesDYECLIQRGEPTPLLLAR 178
Cdd:COG1020 561 PAERLAYMLEDAGARLV--------LTQSALA---ARLPELGVPVLAL--------------DALALAAEPATNPPVPVT 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 179 mfciqdEHDPISLNYTSGTTADPKGVVISHRGAyLSTLSAIIGW-EMGTCPVYLWTLPMfhcngwTF------TWGTAAR 251
Cdd:COG1020 616 ------PDDLAYVIYTSGSTGRPKGVMVEHRAL-VNLLAWMQRRyGLGPGDRVLQFASL------SFdasvweIFGALLS 682
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 252 GGTSVCMR---HVTAPEIYKNIEMHNVTHMCCVPTVFNILLkgnSLDLSHRSGPVHVLTGGSPPPAALVKKVQRL--GFQ 326
Cdd:COG1020 683 GATLVLAPpeaRRDPAALAELLARHRVTVLNLTPSLLRALL---DAAPEALPSLRLVLVGGEALPPELVRRWRARlpGAR 759
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 327 VMHAYGLTEATGPVLFCEWQDE---WNRLP-----ENQQMELkarqglsilglteVDvrnkETQESVPrDGkTMGEIVMK 398
Cdd:COG1020 760 LVNLYGPTETTVDSTYYEVTPPdadGGSVPigrpiANTRVYV-------------LD----AHLQPVP-VG-VPGELYIG 820
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 399 GSSIMKGYLKNPKATYEAF------KHG--WLNSGDVGVIHPDGHVEIKDRS----KdiiISG-----GenissvEVENI 461
Cdd:COG1020 821 GAGLARGYLNRPELTAERFvadpfgFPGarLYRTGDLARWLPDGNLEFLGRAddqvK---IRGfrielG------EIEAA 891
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 462 IYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETNNEDREDKLVtkerdlieycRENLPHFMCPRKVVFLDELPKNGNG 541
Cdd:COG1020 892 LLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLAL----------ALLLPPYMVPAAVVLLLPLPLTGNG 961
|
570 580
....*....|....*....|...
gi 15218840 542 KILKPKLRDIAKGLVAEDEVNVR 564
Cdd:COG1020 962 KLDRLALPAPAAAAAAAAAAPPA 984
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
16-554 |
7.20e-28 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 117.80 E-value: 7.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 16 PITFLKRASECYPNRTSIIY-----GKTRFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAV 90
Cdd:PRK05857 13 PSTVLDRVFEQARQQPEAIAlrrcdGTSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 91 LNPINTRLDATSIAAILRHAKPKILFIYRSFEPLAREILQLLSSedsnlnLPVIFIH-EIDFPKRVSSEESDYecliQRG 169
Cdd:PRK05857 93 AVMADGNLPIAAIERFCQITDPAAALVAPGSKMASSAVPEALHS------IPVIAVDiAAVTRESEHSLDAAS----LAG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 170 EPTplllarmfciQDEHDPISLNYTSGTTADPKGVVISHRgaylsTLSAI-----------IGWEMGTCPVYlwTLPMFH 238
Cdd:PRK05857 163 NAD----------QGSEDPLAMIFTSGTTGEPKAVLLANR-----TFFAVpdilqkeglnwVTWVVGETTYS--PLPATH 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 239 CNGWTFTWGTAARGGTSVCMRHVTApEIYKNIEMHNVTHMCCVPTVFNILLkgNSLDLSHRSGPVHVLT--GGSPPPAAL 316
Cdd:PRK05857 226 IGGLWWILTCLMHGGLCVTGGENTT-SLLEILTTNAVATTCLVPTLLSKLV--SELKSANATVPSLRLVgyGGSRAIAAD 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 317 VKKVQRLGFQVMHAYGLTEaTGPVLFCewqdewnrLPENQQMELKARQGLSILGLTEVDVRNKETQESVPR-----DGKT 391
Cdd:PRK05857 303 VRFIEATGVRTAQVYGLSE-TGCTALC--------LPTDDGSIVKIEAGAVGRPYPGVDVYLAATDGIGPTapgagPSAS 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 392 MGEIVMKGSSIMKGYLKNPKATYEAFKHGWLNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLET 471
Cdd:PRK05857 374 FGTLWIKSPANMLGYWNNPERTAEVLIDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREA 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 472 AVVAMPHPTWGetpcAFVVLEKGETNNEDREDKLVTKERDLIEYCRENlPHFMCPRKVVFLDELPKNGNGKILKPKLRDI 551
Cdd:PRK05857 454 ACYEIPDEEFG----ALVGLAVVASAELDESAARALKHTIAARFRRES-EPMARPSTIVIVTDIPRTQSGKVMRASLAAA 528
|
...
gi 15218840 552 AKG 554
Cdd:PRK05857 529 ATA 531
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
41-479 |
1.06e-27 |
|
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: 117.32 E-value: 1.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 41 TWPQTYDRCCRLAASLISLNI--GKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFIY 118
Cdd:cd05927 7 SYKEVAERADNIGSALRSLGGkpAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVFCD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 119 RSFEPLA-REILQLlsSEDSNLNLPvifiheidfpkrvsseesdyecliqrgEPTPLLLArmfciqdehdpiSLNYTSGT 197
Cdd:cd05927 87 AGVKVYSlEEFEKL--GKKNKVPPP---------------------------PPKPEDLA------------TICYTSGT 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 198 TADPKGVVISHRGAYLSTLSAIIGWEMGTCP----VYLWTLPMFHCNGWTFTWGTAARGGtSVCMRHVTAPEIYKNIEMH 273
Cdd:cd05927 126 TGNPKGVMLTHGNIVSNVAGVFKILEILNKInptdVYISYLPLAHIFERVVEALFLYHGA-KIGFYSGDIRLLLDDIKAL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 274 NVTHMCCVPTVFNILLKG------------------------NSLDLSHRS------------------GPVHVLTGGSP 311
Cdd:cd05927 205 KPTVFPGVPRVLNRIYDKifnkvqakgplkrklfnfalnyklAELRSGVVRaspfwdklvfnkikqalgGNVRLMLTGSA 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 312 PPAALVKKVQR--LGFQVMHAYGLTEATGPVlFCEWQDEWNR------LPeNQQMELKarqglsilgltevdvrnketqe 383
Cdd:cd05927 285 PLSPEVLEFLRvaLGCPVLEGYGQTECTAGA-TLTLPGDTSVghvggpLP-CAEVKLV---------------------- 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 384 SVP------RDGKTMGEIVMKGSSIMKGYLKNPKATYEAF-KHGWLNSGDVGVIHPDGHVEIKDRSKDII-ISGGENISS 455
Cdd:cd05927 341 DVPemnydaKDPNPRGEVCIRGPNVFSGYYKDPEKTAEALdEDGWLHTGDIGEWLPNGTLKIIDRKKNIFkLSQGEYVAP 420
|
490 500 510
....*....|....*....|....*....|...
gi 15218840 456 VEVENI---------IYKYPKVLETAVVAMPHP 479
Cdd:cd05927 421 EKIENIyarspfvaqIFVYGDSLKSFLVAIVVP 453
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
28-543 |
1.20e-27 |
|
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: 115.87 E-value: 1.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 28 PNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAIL 107
Cdd:cd17643 1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 108 RHAKPKILfiyrsfeplareilqllssedsnlnlpvifiheidfpkrvsseesdyecliqrgeptplllarmfcIQDEHD 187
Cdd:cd17643 81 ADSGPSLL------------------------------------------------------------------LTDPDD 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 188 PISLNYTSGTTADPKGVVISHRGayLSTLSAIIGWEMGTCPVYLWTlpMFHCNGWTFT----WGTAARGGTSVCMRHVTA 263
Cdd:cd17643 95 LAYVIYTSGSTGRPKGVVVSHAN--VLALFAATQRWFGFNEDDVWT--LFHSYAFDFSvweiWGALLHGGRLVVVPYEVA 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 264 --PEIYKN-IEMHNVTHMCCVPTVFNILLKGNSLDLSHRSGPVHVLTGGSPPPAALVKK-VQRLGF---QVMHAYGLTEA 336
Cdd:cd17643 171 rsPEDFARlLRDEGVTVLNQTPSAFYQLVEAADRDGRDPLALRYVIFGGEALEAAMLRPwAGRFGLdrpQLVNMYGITET 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 337 TGPVLFcewqdewnRLPENQQMELKARQ----GLSILGLTEVDvrnkETQESVPRDGktMGEIVMKGSSIMKGYLKNPKA 412
Cdd:cd17643 251 TVHVTF--------RPLDAADLPAAAASpigrPLPGLRVYVLD----ADGRPVPPGV--VGELYVSGAGVARGYLGRPEL 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 413 TYEAFKHGWLN--------SGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPTWGET 484
Cdd:cd17643 317 TAERFVANPFGgpgsrmyrTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTR 396
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 15218840 485 PCAFVVLEKGETnnEDRedklvtkeRDLIEYCRENLPHFMCPRKVVFLDELPKNGNGKI 543
Cdd:cd17643 397 LVAYVVADDGAA--ADI--------AELRALLKELLPDYMVPARYVPLDALPLTVNGKL 445
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
12-557 |
1.99e-27 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 116.24 E-value: 1.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 12 VPLTPItfLKRasECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVl 91
Cdd:PRK10946 25 LPLTDI--LTR--HAASDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGVA- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 92 nPINT-----RLDATSIAailRHAKPKILFIYRSFEPLA-REILQLLSSEDSNLNLpVIFIHEidfpkrvsSEESDYECL 165
Cdd:PRK10946 100 -PVNAlfshqRSELNAYA---SQIEPALLIADRQHALFSdDDFLNTLVAEHSSLRV-VLLLND--------DGEHSLDDA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 166 IQRGE------PTPlllarmfciQDEHDPISLnyTSGTTADPKGVVISHRGAYLSTL-SAIIgWEMGTCPVYLWTLPMFH 238
Cdd:PRK10946 167 INHPAedftatPSP---------ADEVAFFQL--SGGSTGTPKLIPRTHNDYYYSVRrSVEI-CGFTPQTRYLCALPAAH 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 239 cngwTFT------WGTAARGGTSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKG----------NSLDLshrsgp 302
Cdd:PRK10946 235 ----NYPmsspgaLGVFLAGGTVVLAPDPSATLCFPLIEKHQVNVTALVPPAVSLWLQAiaeggsraqlASLKL------ 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 303 vhVLTGGSPPPAALVKKV-QRLGFQVMHAYGLTEatGPVlfcewqdEWNRLPENQQMELKArQGLSILGLTEVDVRNKET 381
Cdd:PRK10946 305 --LQVGGARLSETLARRIpAELGCQLQQVFGMAE--GLV-------NYTRLDDSDERIFTT-QGRPMSPDDEVWVADADG 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 382 QEsVPRdGKTmGEIVMKGSSIMKGYLKNPKATYEAF-KHGWLNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVEN 460
Cdd:PRK10946 373 NP-LPQ-GEV-GRLMTRGPYTFRGYYKSPQHNASAFdANGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIEN 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 461 IIYKYPKVLETAVVAMPHPTWGETPCAFVVLekgetnnedRED-KLVTKERDLIEycrENLPHFMCPRKVVFLDELPKNG 539
Cdd:PRK10946 450 LLLRHPAVIHAALVSMEDELMGEKSCAFLVV---------KEPlKAVQLRRFLRE---QGIAEFKLPDRVECVDSLPLTA 517
|
570
....*....|....*...
gi 15218840 540 NGKILKPKLRDIAKGLVA 557
Cdd:PRK10946 518 VGKVDKKQLRQWLASRAS 535
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
16-548 |
5.29e-27 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 114.71 E-value: 5.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 16 PITFLKRASECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPIN 95
Cdd:PRK13383 37 PYTLLAVTAARWPGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPIS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 96 TRLDATSIAAILRHAKPKILFIYRSFeplareILQLLSSEDSnlnlpvifIHEIDfPKRVSSEESDyecliqrGEPTPLL 175
Cdd:PRK13383 117 TEFRSDALAAALRAHHISTVVADNEF------AERIAGADDA--------VAVID-PATAGAEESG-------GRPAVAA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 176 LARMFCIqdehdpislnyTSGTTADPKGV-----VISHRGAYLSTLSAI---IGWEMGTcpvylwTLPMFHCNGWTFTWG 247
Cdd:PRK13383 175 PGRIVLL-----------TSGTTGKPKGVprapqLRSAVGVWVTILDRTrlrTGSRISV------AMPMFHGLGLGMLML 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 248 TAARGGTSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFnillkGNSLDLSHR---SGPVHVL-----TGGSPPPAALVKK 319
Cdd:PRK13383 238 TIALGGTVLTHRHFDAEAALAQASLHRADAFTAVPVVL-----ARILELPPRvraRNPLPQLrvvmsSGDRLDPTLGQRF 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 320 VQRLGFQVMHAYGLTE------ATgPVLFCEWqdewnrlPENQqmelkarqGLSILGlTEVDVRNKETQESVPRdgkTMG 393
Cdd:PRK13383 313 MDTYGDILYNGYGSTEvgigalAT-PADLRDA-------PETV--------GKPVAG-CPVRILDRNNRPVGPR---VTG 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 394 EIVMKGSSIMKGYlknPKATYEAFKHGWLNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAV 473
Cdd:PRK13383 373 RIFVGGELAGTRY---TDGGGKAVVDGMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAV 449
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15218840 474 VAMPHPTWGETPCAFVVLEKGETNNEDRedklvtkerdLIEYCRENLPHFMCPRKVVFLDELPKNGNGKILKPKL 548
Cdd:PRK13383 450 IGVPDERFGHRLAAFVVLHPGSGVDAAQ----------LRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
45-474 |
8.44e-27 |
|
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: 112.74 E-value: 8.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 45 TY----DRCCRLAASLISL-NIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFIYR 119
Cdd:TIGR01733 1 TYreldERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 120 SFEPLAREilqllssedsnLNLPVIFIheidfpkrvsseESDYECLIQRGEPTPLLlarmfciQDEHDPISLNY---TSG 196
Cdd:TIGR01733 81 ALASRLAG-----------LVLPVILL------------DPLELAALDDAPAPPPP-------DAPSGPDDLAYviyTSG 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 197 TTADPKGVVISHRGaylstLSAIIGWeMGTCPVYLWTLPMFHCNGWTF------TWGTAARGGTSVC----MRHVTAPEI 266
Cdd:TIGR01733 131 STGRPKGVVVTHRS-----LVNLLAW-LARRYGLDPDDRVLQFASLSFdasveeIFGALLAGATLVVppedEERDDAALL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 267 YKNIEMHNVTHMCCVPTVFNILLKGNSLDLSH-RsgpvHVLTGGSPPPAALVKKVQRL--GFQVMHAYGLTEATGPVLFC 343
Cdd:TIGR01733 205 AALIAEHPVTVLNLTPSLLALLAAALPPALASlR----LVILGGEALTPALVDRWRARgpGARLINLYGPTETTVWSTAT 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 344 EWQDEWNRLPENqqmelkarqgLSI---LGLTEVDVRNkETQESVPRDGktMGEIVMKGSSIMKGYLKNPKATYEAF--- 417
Cdd:TIGR01733 281 LVDPDDAPRESP----------VPIgrpLANTRLYVLD-DDLRPVPVGV--VGELYIGGPGVARGYLNRPELTAERFvpd 347
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15218840 418 ------KHGWLNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVlETAVV 474
Cdd:TIGR01733 348 pfaggdGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGV-REAVV 409
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
193-539 |
2.53e-26 |
|
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: 112.69 E-value: 2.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 193 YTSGTTADPKGVVISHRG--AYLSTLSAIIGWEMGTCPVYLWTLPMFHCNGWTFTWGTAARGGT----SVcmRHVTaPEI 266
Cdd:cd17639 95 YTSGSTGNPKGVMLTHGNlvAGIAGLGDRVPELLGPDDRYLAYLPLAHIFELAAENVCLYRGGTigygSP--RTLT-DKS 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 267 YKN----IEMHNVTHMCCVPTVF-----NILLKGNSL--------DLSH-------RSGP--------V----------- 303
Cdd:cd17639 172 KRGckgdLTEFKPTLMVGVPAIWdtirkGVLAKLNPMgglkrtlfWTAYqsklkalKEGPgtplldelVfkkvraalggr 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 304 --HVLTGGSPppaaLVKKVQR----LGFQVMHAYGLTE--ATGPVLFcewqdewnrlPENQQmelkarqgLSILG--LTE 373
Cdd:cd17639 252 lrYMLSGGAP----LSADTQEflniVLCPVIQGYGLTEtcAGGTVQD----------PGDLE--------TGRVGppLPC 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 374 VDVRNKETQE-------SVPRdgktmGEIVMKGSSIMKGYLKNPKATYEAFK-HGWLNSGDVGVIHPDGHVEIKDRSKDI 445
Cdd:cd17639 310 CEIKLVDWEEggystdkPPPR-----GEILIRGPNVFKGYYKNPEKTKEAFDgDGWFHTGDIGEFHPDGTLKIIDRKKDL 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 446 I-ISGGENISSVEVENIIYKYPKVLETAVVAMPHPTWgetPCAFVV---------LEKGETNNEDRED--------KLVT 507
Cdd:cd17639 385 VkLQNGEYIALEKLESIYRSNPLVNNICVYADPDKSY---PVAIVVpnekhltklAEKHGVINSEWEElcedkklqKAVL 461
|
410 420 430
....*....|....*....|....*....|....*
gi 15218840 508 KErdLIEYCRE-NLPHFMCPRKVVFLDEL--PKNG 539
Cdd:cd17639 462 KS--LAETARAaGLEKFEIPQGVVLLDEEwtPENG 494
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
19-548 |
4.15e-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: 112.04 E-value: 4.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 19 FLKRASECyPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRL 98
Cdd:cd17655 3 FEEQAEKT-PDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 99 DATSIAAILRHAKPKILFIyrsfeplareilqllsseDSNLNLPVIFIHEIDFPKRVSSEESDYECLIQRGEPTPLllar 178
Cdd:cd17655 82 PEERIQYILEDSGADILLT------------------QSHLQPPIAFIGLIDLLDEDTIYHEESENLEPVSKSDDL---- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 179 MFCIqdehdpislnYTSGTTADPKGVVISHRGA--YLSTLS-AIIGWEMGTCPVY------LWTLPMFHcngwtftwgTA 249
Cdd:cd17655 140 AYVI----------YTSGSTGKPKGVMIEHRGVvnLVEWANkVIYQGEHLRVALFasisfdASVTEIFA---------SL 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 250 ARGGTSVCMRHVT---APEIYKNIEMHNVTHMCCVPTVFNILlkgNSLDLSHRSGPVHVLTGGSPPPAALVKKV---QRL 323
Cdd:cd17655 201 LSGNTLYIVRKETvldGQALTQYIRQNRITIIDLTPAHLKLL---DAADDSEGLSLKHLIVGGEALSTELAKKIielFGT 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 324 GFQVMHAYGLTEAT-GPVLFcewqdewnrlpenqQMELKARQGLSI-----LGLTEV---DVRNKETQESVPrdgktmGE 394
Cdd:cd17655 278 NPTITNAYGPTETTvDASIY--------------QYEPETDQQVSVpigkpLGNTRIyilDQYGRPQPVGVA------GE 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 395 IVMKGSSIMKGYLKNPKATYEAF-KHGWL------NSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPK 467
Cdd:cd17655 338 LYIGGEGVARGYLNRPELTAEKFvDDPFVpgermyRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPD 417
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 468 VLETAVVAMPHPTWGETPCAFVVlekgeTNNEdredklvTKERDLIEYCRENLPHFMCPRKVVFLDELPKNGNGKILKPK 547
Cdd:cd17655 418 IKEAVVIARKDEQGQNYLCAYIV-----SEKE-------LPVAQLREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKA 485
|
.
gi 15218840 548 L 548
Cdd:cd17655 486 L 486
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
457-542 |
5.31e-26 |
|
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: 101.08 E-value: 5.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 457 EVENIIYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETnnedredklvTKERDLIEYCRENLPHFMCPRKVVFLDELP 536
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVE----------LLEEELVAHVREELGPYAVPKEVVFVDELP 70
|
....*.
gi 15218840 537 KNGNGK 542
Cdd:pfam13193 71 KTRSGK 76
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
18-543 |
5.79e-26 |
|
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: 110.87 E-value: 5.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 18 TFLKRASECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTR 97
Cdd:cd12115 3 DLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 98 LDATSIAAILRHAKPKILfiyrsfeplareilqllssedsnlnlpvifiheidfpkrvsseesdyecliqrgeptpllla 177
Cdd:cd12115 83 YPPERLRFILEDAQARLV-------------------------------------------------------------- 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 178 rmfcIQDEHDPISLNYTSGTTADPKGVVISHRGAylstlSAIIGWEMGTCPVYLWT-----------LPMFHcngwtfTW 246
Cdd:cd12115 101 ----LTDPDDLAYVIYTSGSTGRPKGVAIEHRNA-----AAFLQWAAAAFSAEELAgvlastsicfdLSVFE------LF 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 247 GTAARGGTSVCMRHVTAPEIYKNIEmhNVTHMCCVPTVFNILLKGNSLDLSHRSgpvhVLTGGSPPPAALVKKVQRL--G 324
Cdd:cd12115 166 GPLATGGKVVLADNVLALPDLPAAA--EVTLINTVPSAAAELLRHDALPASVRV----VNLAGEPLPRDLVQRLYARlqV 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 325 FQVMHAYGLTEATGPVLFCEwqdewnrlpenqqMELKARQGLSI---LGLTEVDVRNKETQeSVPrDGkTMGEIVMKGSS 401
Cdd:cd12115 240 ERVVNLYGPSEDTTYSTVAP-------------VPPGASGEVSIgrpLANTQAYVLDRALQ-PVP-LG-VPGELYIGGAG 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 402 IMKGYLKNPKATYEAF----KHGWL---NSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVV 474
Cdd:cd12115 304 VARGYLGRPGLTAERFlpdpFGPGArlyRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVV 383
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15218840 475 AMPHPTWGETPCAFVVLEKGETNNEDredklvtkerDLIEYCRENLPHFMCPRKVVFLDELPKNGNGKI 543
Cdd:cd12115 384 AIGDAAGERRLVAYIVAEPGAAGLVE----------DLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKI 442
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
28-554 |
1.32e-25 |
|
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: 111.11 E-value: 1.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 28 PNRTSIIY-----GKTR-FTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTP-AMYEMhFAVPMAGAVLNPINTRLDA 100
Cdd:cd05966 67 GDKVAIIWegdepDQSRtITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPeLVIAM-LACARIGAVHSVVFAGFSA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 101 TSIAAILRHAKPKILFI----YRSFEPL-----AREILQLLSSEDS-----NLNLPVIFIHEIDFP-KRVSSEESDYeCl 165
Cdd:cd05966 146 ESLADRINDAQCKLVITadggYRGGKVIplkeiVDEALEKCPSVEKvlvvkRTGGEVPMTEGRDLWwHDLMAKQSPE-C- 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 166 iqrgEPTPLllarmfciqDEHDPISLNYTSGTTADPKGVVISHRG----AYLSTL-------------SAIIGWEMG-TC 227
Cdd:cd05966 224 ----EPEWM---------DSEDPLFILYTSGSTGKPKGVVHTTGGyllyAATTFKyvfdyhpddiywcTADIGWITGhSY 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 228 PVYLwtlPMfhCNGWTftwgTAARGGTsvcMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLK-GNSLDLSHRSGPVHVL 306
Cdd:cd05966 291 IVYG---PL--ANGAT----TVMFEGT---PTYPDPGRYWDIVEKHKVTIFYTAPTAIRALMKfGDEWVKKHDLSSLRVL 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 307 -TGGSP-PPAA---LVKKVQRLGFQVMHAYGLTEATGPVLFCewqdewnrLPenQQMELK-ARQGLSILGLtEVDVRNKE 380
Cdd:cd05966 359 gSVGEPiNPEAwmwYYEVIGKERCPIVDTWWQTETGGIMITP--------LP--GATPLKpGSATRPFFGI-EPAILDEE 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 381 TQESVPRDGktmGEIVMKGS--SIMKGYLKNPKA---TY-EAFKhGWLNSGDVGVIHPDGHVEIKDRSKDIIISGGENIS 454
Cdd:cd05966 428 GNEVEGEVE---GYLVIKRPwpGMARTIYGDHERyedTYfSKFP-GYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLG 503
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 455 SVEVENIIYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETnnedREDKLVTkerDLIEYCRENLPHFMCPRKVVFLDE 534
Cdd:cd05966 504 TAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEE----PSDELRK---ELRKHVRKEIGPIATPDKIQFVPG 576
|
570 580
....*....|....*....|
gi 15218840 535 LPKNGNGKILKPKLRDIAKG 554
Cdd:cd05966 577 LPKTRSGKIMRRILRKIAAG 596
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
28-545 |
1.58e-25 |
|
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: 110.05 E-value: 1.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 28 PNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAIL 107
Cdd:cd12114 1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 108 RHAKPKILFIyrsfeplAREILQLLSSEDSNLNLPVIFIH-EIDFPKRVSseesdyecliqrgeptplllarmfciqDEH 186
Cdd:cd12114 81 ADAGARLVLT-------DGPDAQLDVAVFDVLILDLDALAaPAPPPPVDV---------------------------APD 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 187 DPISLNYTSGTTADPKGVVISHRGAyLSTLSAIIG-WEMGTCPVYLwTLPMFHCNGWTF-TWGTAARGGTSVCMRHVTAP 264
Cdd:cd12114 127 DLAYVIFTSGSTGTPKGVMISHRAA-LNTILDINRrFAVGPDDRVL-ALSSLSFDLSVYdIFGALSAGATLVLPDEARRR 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 265 EIY---KNIEMHNVTHMCCVPTVFNILLKGNSLDLSHRSGPVHVLTGGSPPPAALVKKVQRL--GFQVMHAYGLTEATGP 339
Cdd:cd12114 205 DPAhwaELIERHGVTLWNSVPALLEMLLDVLEAAQALLPSLRLVLLSGDWIPLDLPARLRALapDARLISLGGATEASIW 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 340 VLFCEWQD---EWNRLP-----ENQQMELKARQGlsilgltevdvrnketqESVPrDGkTMGEIVMKGSSIMKGYLKNPK 411
Cdd:cd12114 285 SIYHPIDEvppDWRSIPygrplANQRYRVLDPRG-----------------RDCP-DW-VPGELWIGGRGVALGYLGDPE 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 412 ATYEAFKH-----GWLNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPTwGETPC 486
Cdd:cd12114 346 LTAARFVThpdgeRLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDPG-GKRLA 424
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 15218840 487 AFVVlekgetnnEDREDKLVTKErDLIEYCRENLPHFMCPRKVVFLDELPKNGNGKILK 545
Cdd:cd12114 425 AFVV--------PDNDGTPIAPD-ALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDR 474
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
187-543 |
1.88e-25 |
|
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: 107.11 E-value: 1.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 187 DPISLNYTSGTTADPKGVVISHR-----------GAYLSTLSAII--GWEMGTCPVY-----LWTlpmfhcngwtftwgt 248
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERswiesfvcnedLFNISGEDAILapGPLSHSLFLYgaisaLYL--------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 249 aarGGTSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSHRSgpvhVLTGGSPPPAALVKKVQRlgfQVM 328
Cdd:cd17633 66 ---GGTFIGQRKFNPKSWIRKINQYNATVIYLVPTMLQALARTLEPESKIKS----IFSSGQKLFESTKKKLKN---IFP 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 329 HA-----YGLTEATgpvlFCEWQdewnrlpENQQMELKARQGLSILGLtEVDVRNKetqesvprDGKTMGEIVMKGSSIM 403
Cdd:cd17633 136 KAnliefYGTSELS----FITYN-------FNQESRPPNSVGRPFPNV-EIEIRNA--------DGGEIGKIFVKSEMVF 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 404 KGYLKNPKATyeafKHGWLNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPTWGE 483
Cdd:cd17633 196 SGYVRGGFSN----PDGWMSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGE 271
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 484 TPCAFVVLEKgetnnedredklVTKeRDLIEYCRENLPHFMCPRKVVFLDELPKNGNGKI 543
Cdd:cd17633 272 IAVALYSGDK------------LTY-KQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKI 318
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
180-549 |
2.87e-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: 2.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 180 FCIQDE----HDPISLNYTSGTTADPKGVVISHRG---AYLSTLSAI------IGWEMGTcpvylwtlPMFHCNGWTFTW 246
Cdd:cd05974 75 YAAVDEnthaDDPMLLYFTSGTTSKPKLVEHTHRSypvGHLSTMYWIglkpgdVHWNISS--------PGWAKHAWSCFF 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 247 GTAARGGTSVCMRHV--TAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLdlSHRSGPVHVLTGGSPPPAALVKKVQRL- 323
Cdd:cd05974 147 APWNAGATVFLFNYArfDAKRVLAALVRYGVTTLCAPPTVWRMLIQQDLA--SFDVKLREVVGAGEPLNPEVIEQVRRAw 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 324 GFQVMHAYGLTEATGPVLFCEWQDewnrlpenqqmeLKARQGLSILGLTEVDVRNKETQESvprdgkTMGEIVMKGSS-- 401
Cdd:cd05974 225 GLTIRDGYGQTETTALVGNSPGQP------------VKAGSMGRPLPGYRVALLDPDGAPA------TEGEVALDLGDtr 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 402 ---IMKGYLKNPKATYEAFKHGWLNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPH 478
Cdd:cd05974 287 pvgLMKGYAGDPDKTAHAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPD 366
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15218840 479 PTWGETPCAFVVLEKGetNNEDREDKLvtkerDLIEYCRENLPHFMCPRKVVFLdELPKNGNGKILKPKLR 549
Cdd:cd05974 367 PVRLSVPKAFIVLRAG--YEPSPETAL-----EIFRFSRERLAPYKRIRRLEFA-ELPKTISGKIRRVELR 429
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
27-543 |
5.08e-24 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 105.34 E-value: 5.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 27 YPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAI 106
Cdd:PRK09029 16 RPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLLEEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 107 LRHakpkilfiyrsfepLAREILQLLSSEDSNLNLPVIfiheidfpkRVSSEESDYECLIQrgeptPLLLArmfciqdeh 186
Cdd:PRK09029 96 LPS--------------LTLDFALVLEGENTFSALTSL---------HLQLVEGAHAVAWQ-----PQRLA--------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 187 dpiSLNYTSGTTADPKGVVISHRgAYLStlSAIigwemGTCPV--------YLWTLPMFHCNGWTFTWGTAARGGTSVcm 258
Cdd:PRK09029 139 ---TMTLTSGSTGLPKAAVHTAQ-AHLA--SAE-----GVLSLmpftaqdsWLLSLPLFHVSGQGIVWRWLYAGATLV-- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 259 rhVTAPE-IYKNIEMhnVTHMCCVPTVFNILLKGNSLDLSHRsgpvHVLTGGSPPPAALVKKVQRLGFQVMHAYGLTEAT 337
Cdd:PRK09029 206 --VRDKQpLEQALAG--CTHASLVPTQLWRLLDNRSEPLSLK----AVLLGGAAIPVELTEQAEQQGIRCWCGYGLTEMA 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 338 GPVlfCEwqdewnrlpenqqmelKARQGLSILGLT----EVDVRNketqesvprdgktmGEIVMKGSSIMKGYLKNPKAT 413
Cdd:PRK09029 278 STV--CA----------------KRADGLAGVGSPlpgrEVKLVD--------------GEIWLRGASLALGYWRQGQLV 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 414 YEAFKHGWLNSGDVGVIHpDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPTWGETPCAFVVLEK 493
Cdd:PRK09029 326 PLVNDEGWFATRDRGEWQ-NGELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVADAEFGQRPVAVVESDS 404
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 15218840 494 GETNNEDRE---DKLVTKERDlIEYCRenLPHfmcprkvvfldELpKNGNGKI 543
Cdd:PRK09029 405 EAAVVNLAEwlqDKLARFQQP-VAYYL--LPP-----------EL-KNGGIKI 442
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
36-550 |
3.88e-23 |
|
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: 102.51 E-value: 3.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 36 GKTrFTWPQTYDRCCRLAASLIS-LNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSiaailrhakpki 114
Cdd:cd05937 3 GKT-WTYSETYDLVLRYAHWLHDdLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDP------------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 115 lfiyrsfeplareilqllssedsnlnlpviFIHEIdfpkRVSSeesdyecliqrgeptplllARmFCIQDEHDPISLNYT 194
Cdd:cd05937 70 ------------------------------LIHCL----KLSG-------------------SR-FVIVDPDDPAILIYT 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 195 SGTTADPKGVVISHRGAYLSTLSaiIGWEMGTCPVYLW--TLPMFHCNGWTFTWGTAARGGTSVCMRH-VTAPEIYKNIE 271
Cdd:cd05937 96 SGTTGLPKAAAISWRRTLVTSNL--LSHDLNLKNGDRTytCMPLYHGTAAFLGACNCLMSGGTLALSRkFSASQFWKDVR 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 272 MHNVTHMCCVPTVFNILLKG--NSLDLSHRsgpVHVLTGGSPPPAALVKKVQRLGFQVMHA-YGLTEATGPVlfcewqde 348
Cdd:cd05937 174 DSGATIIQYVGELCRYLLSTppSPYDRDHK---VRVAWGNGLRPDIWERFRERFNVPEIGEfYAATEGVFAL-------- 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 349 WNRLPENQQMELKARQGL---SILGLTEVDVRNKETQESVPRDGKT----------MGEIVM----KGSSIMKGYLKNPK 411
Cdd:cd05937 243 TNHNVGDFGAGAIGHHGLirrWKFENQVVLVKMDPETDDPIRDPKTgfcvrapvgePGEMLGrvpfKNREAFQGYLHNED 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 412 ATY-----EAFKHG--WLNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPTW-GE 483
Cdd:cd05937 323 ATEsklvrDVFRKGdiYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVKVPGHdGR 402
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15218840 484 TPCAFVVLEKgETNNEDREDKLVtkerdLIEYCRENLPHFMCPRKVVFLDELPKNGNGKILKPKLRD 550
Cdd:cd05937 403 AGCAAITLEE-SSAVPTEFTKSL-----LASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLRD 463
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
187-542 |
6.16e-23 |
|
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: 100.53 E-value: 6.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 187 DPISLNYTSGTTADPKGVVISH--------------RGAYLSTLSAIIGWEMGTCPVYLWTLPMFHCNGWtFTWGTAARG 252
Cdd:cd05924 4 DDLYILYTGGTTGMPKGVMWRQedifrmlmggadfgTGEFTPSEDAHKAAAAAAGTVMFPAPPLMHGTGS-WTAFGGLLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 253 GTSVCMRHV--TAPEIYKNIEMHNVTHMCCVPTVF-----NILLKGNSLDLShrsGPVHVLTGGspppAALVKKVQRLGF 325
Cdd:cd05924 83 GQTVVLPDDrfDPEEVWRTIEKHKVTSMTIVGDAMarpliDALRDAGPYDLS---SLFAISSGG----ALLSPEVKQGLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 326 QVMHAYGLTEATGPVLFCEWQDEWNRLPENQQMELKARQGLSILglteVDVRNKEtqesVPRDGKTMGEIVMKGSsIMKG 405
Cdd:cd05924 156 ELVPNITLVDAFGSSETGFTGSGHSAGSGPETGPFTRANPDTVV----LDDDGRV----VPPGSGGVGWIARRGH-IPLG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 406 YLKNPKATYEAFKH----GWLNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPTW 481
Cdd:cd05924 227 YYGDEAKTAETFPEvdgvRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERW 306
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15218840 482 GETPCAFVVLEKGETNNEDredklvtkerDLIEYCRENLPHFMCPRKVVFLDELPKNGNGK 542
Cdd:cd05924 307 GQEVVAVVQLREGAGVDLE----------ELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
20-551 |
1.12e-22 |
|
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: 101.98 E-value: 1.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 20 LKRASECYPNRTsIIY-----GKTRFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPI 94
Cdd:cd05906 16 LLRAAERGPTKG-ITYidadgSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 95 NTRLDATSIAAILRHAK--------PKILFIYRSFEPLAReilqlLSSEDSNLNLPVIFIHEidfpkrVSSEESDYECLI 166
Cdd:cd05906 95 TVPPTYDEPNARLRKLRhiwqllgsPVVLTDAELVAEFAG-----LETLSGLPGIRVLSIEE------LLDTAADHDLPQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 167 QRGEptplllarmfciqdehDPISLNYTSGTTADPKGVVISHRgaylSTLSAIIG--WEMGTCP--VYLWTLPMFHCNGW 242
Cdd:cd05906 164 SRPD----------------DLALLMLTSGSTGFPKAVPLTHR----NILARSAGkiQHNGLTPqdVFLNWVPLDHVGGL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 243 TFTWGTAARGGTSvcMRHVTAPEIYKN-------IEMHNVTHMCCVPTVFNILL------KGNSLDLSH-R---SG--PV 303
Cdd:cd05906 224 VELHLRAVYLGCQ--QVHVPTEEILADplrwldlIDRYRVTITWAPNFAFALLNdlleeiEDGTWDLSSlRylvNAgeAV 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 304 HVLTGgspppAALVKKVQRLGFQ--VMH-AYGLTEATGPVLFCEWQDEWNRLPENQQMELkarqGLSILGlteVDVR-NK 379
Cdd:cd05906 302 VAKTI-----RRLLRLLEPYGLPpdAIRpAFGMTETCSGVIYSRSFPTYDHSQALEFVSL----GRPIPG---VSMRiVD 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 380 ETQESVPRDgkTMGEIVMKGSSIMKGYLKNPKATYEAF-KHGWLNSGDVGVIHpDGHVEIKDRSKDIIISGGENISSVEV 458
Cdd:cd05906 370 DEGQLLPEG--EVGRLQVRGPVVTKGYYNNPEANAEAFtEDGWFRTGDLGFLD-NGNLTITGRTKDTIIVNGVNYYSHEI 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 459 ENIIYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETNNEDREDKLVTKERDlieycrenlpHFM-----CPRKVVFL- 532
Cdd:cd05906 447 EAAVEEVPGVEPSFTAAFAVRDPGAETEELAIFFVPEYDLQDALSETLRAIRS----------VVSrevgvSPAYLIPLp 516
|
570 580
....*....|....*....|
gi 15218840 533 -DELPKNGNGKILKPKLRDI 551
Cdd:cd05906 517 kEEIPKTSLGKIQRSKLKAA 536
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
28-543 |
3.53e-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: 3.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 28 PNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAIL 107
Cdd:cd17650 1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 108 RHAKPKILFIyrsfeplareilqllssedsnlnlpvifiheidfpkrvsseesdyecliqrgEPTplllarmfciqdehD 187
Cdd:cd17650 81 EDSGAKLLLT----------------------------------------------------QPE--------------D 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 188 PISLNYTSGTTADPKGVVISHRgaylSTLSAIIGW----EMGTCPVYLWTLPMFHCNGWTftwGTAAR----GGTSV-CM 258
Cdd:cd17650 95 LAYVIYTSGTTGKPKGVMVEHR----NVAHAAHAWrreyELDSFPVRLLQMASFSFDVFA---GDFARsllnGGTLViCP 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 259 RHVTA--PEIYKNIEMHNVTHMCCVPTVFNILLK---GNSLDLSHrsgpVHVLTGGSPPPAALVKK--VQRLG--FQVMH 329
Cdd:cd17650 168 DEVKLdpAALYDLILKSRITLMESTPALIRPVMAyvyRNGLDLSA----MRLLIVGSDGCKAQDFKtlAARFGqgMRIIN 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 330 AYGLTEATGPVLFCEWQDEwnRLPENQQMELKarqglSILGLTEVDVRNKETQesvPRDGKTMGEIVMKGSSIMKGYLKN 409
Cdd:cd17650 244 SYGVTEATIDSTYYEEGRD--PLGDSANVPIG-----RPLPNTAMYVLDERLQ---PQPVGVAGELYIGGAGVARGYLNR 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 410 PKATYEAFKHGWLNS-------GDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLEtAVVAMPHPTWG 482
Cdd:cd17650 314 PELTAERFVENPFAPgermyrtGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDE-AVVAVREDKGG 392
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15218840 483 ETP-CAFVVlekgetnnedREDKLVTKErdLIEYCRENLPHFMCPRKVVFLDELPKNGNGKI 543
Cdd:cd17650 393 EARlCAYVV----------AAATLNTAE--LRAFLAKELPSYMIPSYYVQLDALPLTPNGKV 442
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
39-549 |
3.58e-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: 99.35 E-value: 3.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 39 RFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFIY 118
Cdd:cd05940 3 ALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLVVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 119 RSFeplareilqllssedsnlnlpvifiheidfpkrvsseesdyecLIqrgeptplllarmfciqdehdpislnYTSGTT 198
Cdd:cd05940 83 AAL-------------------------------------------YI--------------------------YTSGTT 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 199 ADPKGVVISHRGAYLST-LSAIIGWEMGTCPVYLwTLPMFHCNGWTFTWGTAARGGTSVCMRH-VTAPEIYKNIEMHNVT 276
Cdd:cd05940 94 GLPKAAIISHRRAWRGGaFFAGSGGALPSDVLYT-CLPLYHSTALIVGWSACLASGATLVIRKkFSASNFWDDIRKYQAT 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 277 hmcCVPTVFNIL-----LKGNSLDLSHRsgpVHVLTGGSPPPAALVKKVQRLGF-QVMHAYGLTEatGPVLFcewqdeWN 350
Cdd:cd05940 173 ---IFQYIGELCryllnQPPKPTERKHK---VRMIFGNGLRPDIWEEFKERFGVpRIAEFYAATE--GNSGF------IN 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 351 RlpENQQMELKARQGLSILG----LTEVDV------RNKETQ-ESVPRD--GKTMGEIVMKGSsiMKGYLKNPKAT---- 413
Cdd:cd05940 239 F--FGKPGAIGRNPSLLRKVaplaLVKYDLesgepiRDAEGRcIKVPRGepGLLISRINPLEP--FDGYTDPAATEkkil 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 414 YEAFKHG--WLNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHP-TWGETPCAFVV 490
Cdd:cd05940 315 RDVFKKGdaWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQVPgTDGRAGMAAIV 394
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 15218840 491 LEKGEtnNEDREdklvtkerDLIEYCRENLPHFMCPRKVVFLDELPKNGNGKILKPKLR 549
Cdd:cd05940 395 LQPNE--EFDLS--------ALAAHLEKNLPGYARPLFLRLQPEMEITGTFKQQKVDLR 443
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
28-571 |
4.92e-22 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 101.57 E-value: 4.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 28 PNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAIL 107
Cdd:PRK12316 4565 PDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMM 4644
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 108 RHAKPKILFIYRSFEPlareilqllssedsnlNLPVifiheidfPKRVSS----EESDYEcliQRGEPTPLLLArmfciq 183
Cdd:PRK12316 4645 EDSGAALLLTQSHLLQ----------------RLPI--------PDGLASlaldRDEDWE---GFPAHDPAVRL------ 4691
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 184 dehDPISLNY---TSGTTADPKGVVISHRGayLSTLSAIIGWEMGTCP---VYLWTLPMFHCNGWTFTWGTAArgGTSVC 257
Cdd:PRK12316 4692 ---HPDNLAYviyTSGSTGRPKGVAVSHGS--LVNHLHATGERYELTPddrVLQFMSFSFDGSHEGLYHPLIN--GASVV 4764
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 258 MRHVTA--PE-IYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSHRSGPVHVLTGGSPPPAALvkkvqRLGFQVMHAYGLT 334
Cdd:PRK12316 4765 IRDDSLwdPErLYAEIHEHRVTVLVFPPVYLQQLAEHAERDGEPPSLRVYCFGGEAVAQASY-----DLAWRALKPVYLF 4839
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 335 EATGPVLFCEWQDEWNRLPENQQMELKARQGlSILGLTEVDVRNKETQesvPRDGKTMGEIVMKGSSIMKGYLKNPKATY 414
Cdd:PRK12316 4840 NGYGPTETTVTVLLWKARDGDACGAAYMPIG-TPLGNRSGYVLDGQLN---PLPVGVAGELYLGGEGVARGYLERPALTA 4915
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 415 EAF------KHG--WLNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPTwGETPC 486
Cdd:PRK12316 4916 ERFvpdpfgAPGgrLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAV-GKQLV 4994
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 487 AFVVLEKGETNNED-REDKLVTKERDLIeycRENLPHFMCPRKVVFLDELPKNGNGKILKPKLRDIAKGLVAEDEVNVRS 565
Cdd:PRK12316 4995 GYVVPQDPALADADeAQAELRDELKAAL---RERLPEYMVPAHLVFLARMPLTPNGKLDRKALPQPDASLLQQAYVAPRS 5071
|
....*.
gi 15218840 566 KVQRPV 571
Cdd:PRK12316 5072 ELEQQV 5077
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
28-548 |
2.70e-21 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 99.26 E-value: 2.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 28 PNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAIL 107
Cdd:PRK12316 2017 PEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYML 2096
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 108 RHAKPKILFIYRSFE---PLAREILQLLSSEDSNLNlpvifiheiDFPKrvsseesdyecliqrGEPTPLLlarmfciqD 184
Cdd:PRK12316 2097 EDSGAALLLTQRHLLerlPLPAGVARLPLDRDAEWA---------DYPD---------------TAPAVQL--------A 2144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 185 EHDPISLNYTSGTTADPKGVVISHrGAYLSTLSAI-IGWEMGTCPVYLWTLPmFHCNGWTFTWGTAARGGTSVCMR---H 260
Cdd:PRK12316 2145 GENLAYVIYTSGSTGLPKGVAVSH-GALVAHCQAAgERYELSPADCELQFMS-FSFDGAHEQWFHPLLNGARVLIRddeL 2222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 261 VTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDlsHRSGPVHVLT-GGSPPPAALVKKVQRL--GFQVMHAYGLTEAT 337
Cdd:PRK12316 2223 WDPEQLYDEMERHGVTILDFPPVYLQQLAEHAERD--GRPPAVRVYCfGGEAVPAASLRLAWEAlrPVYLFNGYGPTEAV 2300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 338 GPVLF--CEWQDewnrlPENQQM----ELKARQGLSILGltevdvrnkETQESVPRDGktMGEIVMKGSSIMKGYLKNPK 411
Cdd:PRK12316 2301 VTPLLwkCRPQD-----PCGAAYvpigRALGNRRAYILD---------ADLNLLAPGM--AGELYLGGEGLARGYLNRPG 2364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 412 ATYEAF-------KHGWL-NSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPTwGE 483
Cdd:PRK12316 2365 LTAERFvpdpfsaSGERLyRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQDGAS-GK 2443
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15218840 484 TPCAFVVLEKGETNNEDredklvtkerDLIEYCRENLPHFMCPRKVVFLDELPKNGNGKILKPKL 548
Cdd:PRK12316 2444 QLVAYVVPDDAAEDLLA----------ELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKAL 2498
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
28-578 |
3.85e-21 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 98.69 E-value: 3.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 28 PNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAIL 107
Cdd:PRK12467 1588 PEAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMI 1667
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 108 RHAKPKILFIYRsfeplarEILQLLSSEDSnlnLPVIFIHEIDfpkrvsseesdyECLIQRGEPTPLLLArmfciqdehD 187
Cdd:PRK12467 1668 EDSGIELLLTQS-------HLQARLPLPDG---LRSLVLDQED------------DWLEGYSDSNPAVNL---------A 1716
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 188 PISLNY---TSGTTADPKGVVISHrGAYLSTLSAIIGWeMGTCPVYLWTLPM---FHCNGWTFTWgtAARGGTSVCMR-- 259
Cdd:PRK12467 1717 PQNLAYviyTSGSTGRPKGAGNRH-GALVNRLCATQEA-YQLSAADVVLQFTsfaFDVSVWELFW--PLINGARLVIApp 1792
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 260 --HVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSHRSGPVHVLTGGSPPPAALVKKVQRLGF-QVMHAYGLTEA 336
Cdd:PRK12467 1793 gaHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQMDEQVEHPLSLRRVVCGGEALEVEALRPWLERLPDtGLFNLYGPTET 1872
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 337 TGPVLF--CEWQDEWNR--LPENQQMelkARQGLSILgltevdvrnKETQESVPRdgKTMGEIVMKGSSIMKGYLKNPKA 412
Cdd:PRK12467 1873 AVDVTHwtCRRKDLEGRdsVPIGQPI---ANLSTYIL---------DASLNPVPI--GVAGELYLGGVGLARGYLNRPAL 1938
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 413 TYEAF------KHG--WLNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPTwGET 484
Cdd:PRK12467 1939 TAERFvadpfgTVGsrLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQDGAN-GKQ 2017
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 485 PCAFVVLEKGETNNEDreDKLVTKERDLIEYCRENLPHFMCPRKVVFLDELPKNGNGKILKpklrdiaKGLVAEDEVNVR 564
Cdd:PRK12467 2018 LVAYVVPTDPGLVDDD--EAQVALRAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDR-------KALPAPDASELQ 2088
|
570
....*....|....
gi 15218840 565 SKVQRPVEHFTSRL 578
Cdd:PRK12467 2089 QAYVAPQSELEQRL 2102
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
20-479 |
6.95e-21 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 96.63 E-value: 6.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 20 LKRASECYPN-----RTSIIYGKT-RFTWP---QTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAV 90
Cdd:PLN02614 51 FRMSVEKYPNnpmlgRREIVDGKPgKYVWQtyqEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLY 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 91 LNPINTRLDATSIAAILRHAKPKILFIYRSFEPlarEILQLLSSEDSNLNLPVIFiheiDFPKRVSSEESD--------Y 162
Cdd:PLN02614 131 CVPLYDTLGAGAVEFIISHSEVSIVFVEEKKIS---ELFKTCPNSTEYMKTVVSF----GGVSREQKEEAEtfglviyaW 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 163 ECLIQRGEPTPLLLArmfcIQDEHDPISLNYTSGTTADPKGVVISHRGAYLSTLSAI-----IGWEMGTCPVYLWTLPMF 237
Cdd:PLN02614 204 DEFLKLGEGKQYDLP----IKKKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIrllksANAALTVKDVYLSYLPLA 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 238 HCNGWTFTWGTAARGGtSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLS-------------------- 297
Cdd:PLN02614 280 HIFDRVIEECFIQHGA-AIGFWRGDVKLLIEDLGELKPTIFCAVPRVLDRVYSGLQKKLSdggflkkfvfdsafsykfgn 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 298 ------HRS------------------GPVHVLTGGSPPPAALVKKVQRL--GFQVMHAYGLTEATGPVlFCEWQDEWNR 351
Cdd:PLN02614 359 mkkgqsHVEasplcdklvfnkvkqglgGNVRIILSGAAPLASHVESFLRVvaCCHVLQGYGLTESCAGT-FVSLPDELDM 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 352 L----PENQQMELKarqglsilgLTEVDVRNKETQESVPRdgktmGEIVMKGSSIMKGYLKNPKATYEAFKHGWLNSGDV 427
Cdd:PLN02614 438 LgtvgPPVPNVDIR---------LESVPEMEYDALASTPR-----GEICIRGKTLFSGYYKREDLTKEVLIDGWLHTGDV 503
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15218840 428 GVIHPDGHVEIKDRSKDII-ISGGENISSVEVENI---------IYKYPKVLETAVVAMPHP 479
Cdd:PLN02614 504 GEWQPNGSMKIIDRKKNIFkLSQGEYVAVENIENIygevqavdsVWVYGNSFESFLVAIANP 565
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
193-543 |
9.04e-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: 95.01 E-value: 9.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 193 YTSGTTADPKGVVISHRGayLSTLSAIIGWEMGTCP---VYLWTLPMFHCNGWTFtWGTAARGGTSVCM-RHVTAP--EI 266
Cdd:cd17652 100 YTSGSTGRPKGVVVTHRG--LANLAAAQIAAFDVGPgsrVLQFASPSFDASVWEL-LMALLAGATLVLApAEELLPgePL 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 267 YKNIEMHNVTHMCCVPTVFNILLKGNSLDLshrsgpVHVLTGGSPPPAALVKKVQRlGFQVMHAYGLTEATGPVLFCEWQ 346
Cdd:cd17652 177 ADLLREHRITHVTLPPAALAALPPDDLPDL------RTLVVAGEACPAELVDRWAP-GRRMINAYGPTETTVCATMAGPL 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 347 DEWNRLPenqqmelkarQGLSILGlTEVDVRNkETQESVPrDGKTmGEIVMKGSSIMKGYLKNPKATYEAF---KHGWLN 423
Cdd:cd17652 250 PGGGVPP----------IGRPVPG-TRVYVLD-ARLRPVP-PGVP-GELYIAGAGLARGYLNRPGLTAERFvadPFGAPG 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 424 S-----GDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETnn 498
Cdd:cd17652 316 SrmyrtGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPGAA-- 393
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 15218840 499 edredklVTKERdLIEYCRENLPHFMCPRKVVFLDELPKNGNGKI 543
Cdd:cd17652 394 -------PTAAE-LRAHLAERLPGYMVPAAFVVLDALPLTPNGKL 430
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
193-555 |
1.07e-20 |
|
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: 95.30 E-value: 1.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 193 YTSGTTADPKGVVISHRgAYLSTLSAII-GWEMGTCPVYLWtlpmFhcNGWTF------TWGTAARGGTsVCmrhVTAPE 265
Cdd:cd05918 113 FTSGSTGKPKGVVIEHR-ALSTSALAHGrALGLTSESRVLQ----F--ASYTFdvsileIFTTLAAGGC-LC---IPSEE 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 266 IYKN-----IEMHNVTHMCCVPTVFNILLKGNSLDLSHrsgpvhVLTGGSPPPAALVKK-VQRLgfQVMHAYGLTEATGP 339
Cdd:cd05918 182 DRLNdlagfINRLRVTWAFLTPSVARLLDPEDVPSLRT------LVLGGEALTQSDVDTwADRV--RLINAYGPAECTIA 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 340 VLFCEWQDEWNRlpenqqmelkarqglSILGLTeVDVR----NKETQES-VPRDGktMGEIVMKGSSIMKGYLKNPKATY 414
Cdd:cd05918 254 ATVSPVVPSTDP---------------RNIGRP-LGATcwvvDPDNHDRlVPIGA--VGELLIEGPILARGYLNDPEKTA 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 415 EAFKHG--WL------------NSGDVGVIHPDGHVEIKDRsKD--IIISG-----GEnissveVENIIYKYPKVLETAV 473
Cdd:cd05918 316 AAFIEDpaWLkqegsgrgrrlyRTGDLVRYNPDGSLEYVGR-KDtqVKIRGqrvelGE------IEHHLRQSLPGAKEVV 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 474 VAMPHPTWGETP---CAFVVLEKGETNNEDRE-------DKLVTKERDLIEYCRENLPHFMCPRKVVFLDELPKNGNGKI 543
Cdd:cd05918 389 VEVVKPKDGSSSpqlVAFVVLDGSSSGSGDGDslflepsDEFRALVAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKI 468
|
410
....*....|..
gi 15218840 544 LKPKLRDIAKGL 555
Cdd:cd05918 469 DRRALRELAESL 480
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
27-563 |
1.21e-20 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 95.35 E-value: 1.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 27 YPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMyemhfAVPMAGAVLN-----PINTRLDAT 101
Cdd:PRK04813 15 QPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEM-----LATFLGAVKAghayiPVDVSSPAE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 102 SIAAILRHAKPKiLFIYRSFEPLAREILQLLSSEDsnlnLPVIFIH--EIDFPKRVSSEESDYecLIqrgeptplllarm 179
Cdd:PRK04813 90 RIEMIIEVAKPS-LIIATEELPLEILGIPVITLDE----LKDIFATgnPYDFDHAVKGDDNYY--II------------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 180 fciqdehdpislnYTSGTTADPKGVVISHrgaylSTLSAIIGWE-----MGTCPVYLWTLPmfhcngWTF-----TWG-T 248
Cdd:PRK04813 150 -------------FTSGTTGKPKGVQISH-----DNLVSFTNWMledfaLPEGPQFLNQAP------YSFdlsvmDLYpT 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 249 AARGGTSVCMRH-VTA--PEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSHRSGPVHVLTGGSPPPAALVKK-VQRlg 324
Cdd:PRK04813 206 LASGGTLVALPKdMTAnfKQLFETLPQLPINVWVSTPSFADMCLLDPSFNEEHLPNLTHFLFCGEELPHKTAKKlLER-- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 325 F---QVMHAYGLTEATGPVLFCEWQDE----WNRLPenqqmelkarqglsiLGLTEVDVR---NKETQESVPRDGKtmGE 394
Cdd:PRK04813 284 FpsaTIYNTYGPTEATVAVTSIEITDEmldqYKRLP---------------IGYAKPDSPlliIDEEGTKLPDGEQ--GE 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 395 IVMKGSSIMKGYLKNPKATYEAF----KHGWLNSGDVGVIhPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVlE 470
Cdd:PRK04813 347 IVISGPSVSKGYLNNPEKTAEAFftfdGQPAYHTGDAGYL-EDGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYV-E 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 471 TAVVAmphPTWGETPC----AFVVLEKGEtnnedredklVTKERDLIEYCRENL----PHFMCPRKVVFLDELPKNGNGK 542
Cdd:PRK04813 425 SAVVV---PYNKDHKVqyliAYVVPKEED----------FEREFELTKAIKKELkerlMEYMIPRKFIYRDSLPLTPNGK 491
|
570 580
....*....|....*....|.
gi 15218840 543 IlkpklrDIaKGLVAedEVNV 563
Cdd:PRK04813 492 I------DR-KALIE--EVNK 503
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
41-464 |
1.36e-20 |
|
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: 95.50 E-value: 1.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 41 TWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFIYRs 120
Cdd:cd05933 10 TYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEANILVVEN- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 121 feplAREILQLLSSEDSnlnLP----VIFIHEIDFPKR-------------VSSEESDYECLIQRGEPTPlllarmfCIq 183
Cdd:cd05933 89 ----QKQLQKILQIQDK---LPhlkaIIQYKEPLKEKEpnlyswdefmelgRSIPDEQLDAIISSQKPNQ-------CC- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 184 dehdpiSLNYTSGTTADPKGVVISHRGAYLSTLSAIIGWEMGTCPV-------YL------------WTlPMFHCNGWTF 244
Cdd:cd05933 154 ------TLIYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLRPATVgqesvvsYLplshiaaqildiWL-PIKVGGQVYF 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 245 TWGTAARGGTSVCMRHVTApeiykniemhnvTHMCCVPTVF--------------------------NILLKGNSLDLSH 298
Cdd:cd05933 227 AQPDALKGTLVKTLREVRP------------TAFMGVPRVWekiqekmkavgaksgtlkrkiaswakGVGLETNLKLMGG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 299 RSGP-----------------------VHVL-TGGSPPPAALVKKVQRLGFQVMHAYGLTEATGPVLFCewqdewnrLPE 354
Cdd:cd05933 295 ESPSplfyrlakklvfkkvrkalgldrCQKFfTGAAPISRETLEFFLSLNIPIMELYGMSETSGPHTIS--------NPQ 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 355 NQQMelkarqgLSIlGLTEVDVRNKETQEsvprDGKTMGEIVMKGSSIMKGYLKNPKATYEAFK-HGWLNSGDVGVIHPD 433
Cdd:cd05933 367 AYRL-------LSC-GKALPGCKTKIHNP----DADGIGEICFWGRHVFMGYLNMEDKTEEAIDeDGWLHSGDLGKLDED 434
|
490 500 510
....*....|....*....|....*....|..
gi 15218840 434 GHVEIKDRSKDIII-SGGENISSVEVENIIYK 464
Cdd:cd05933 435 GFLYITGRIKELIItAGGENVPPVPIEDAVKK 466
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
43-558 |
1.42e-20 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 96.19 E-value: 1.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 43 PQTYDRCCRLAASL---ISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFIYR 119
Cdd:PRK06814 658 PLTYRKLLTGAFVLgrkLKKNTPPGENVGVMLPNANGAAVTFFALQSAGRVPAMINFSAGIANILSACKAAQVKTVLTSR 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 120 SFEPLAReilqlLSSEDSNLNLPVIFIHEIDFPKRVSSEESdyecliQRGEPTPLLLARMFCIQDEHDPISLNYTSGTTA 199
Cdd:PRK06814 738 AFIEKAR-----LGPLIEALEFGIRIIYLEDVRAQIGLADK------IKGLLAGRFPLVYFCNRDPDDPAVILFTSGSEG 806
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 200 DPKGVVISHRG--AYLSTLSAIIgwEMGTCPVYLWTLPMFHCNGWTftwgtaarGGTSVCM------------RHV-TAP 264
Cdd:PRK06814 807 TPKGVVLSHRNllANRAQVAARI--DFSPEDKVFNALPVFHSFGLT--------GGLVLPLlsgvkvflypspLHYrIIP 876
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 265 E-IYKNiemhNVTHMCCVPTvfniLLKG-----NSLDLshRSgpVHVLTGGSPPPAALVKKV--QRLGFQVMHAYGLTEa 336
Cdd:PRK06814 877 ElIYDT----NATILFGTDT----FLNGyaryaHPYDF--RS--LRYVFAGAEKVKEETRQTwmEKFGIRILEGYGVTE- 943
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 337 TGPVLFCewqdewnrlpeNQQMELKARQGLSILGLTEVDVrnketqESVP--RDGktmGEIVMKGSSIMKGYLK--NPkA 412
Cdd:PRK06814 944 TAPVIAL-----------NTPMHNKAGTVGRLLPGIEYRL------EPVPgiDEG---GRLFVRGPNVMLGYLRaeNP-G 1002
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 413 TYEAFKHGWLNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPTWGETpcaFVVLE 492
Cdd:PRK06814 1003 VLEPPADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELWPDALHAAVSIPDARKGER---IILLT 1079
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15218840 493 KGETNNEDredklvtkerDLIEYCREN-LPHFMCPRKVVFLDELPKNGNGKILKPKLRDIAKGLVAE 558
Cdd:PRK06814 1080 TASDATRA----------AFLAHAKAAgASELMVPAEIITIDEIPLLGTGKIDYVAVTKLAEEAAAK 1136
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
193-479 |
1.55e-20 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 95.65 E-value: 1.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 193 YTSGTTADPKGVVISHRGAYLSTLSAIIGWE-----MGTCPVYLWTLPMFHC-----NGWTFtwgtaaRGGTSVCMRHVT 262
Cdd:PLN02430 227 YTSGTSGDPKGVVLTHEAVATFVRGVDLFMEqfedkMTHDDVYLSFLPLAHIldrmiEEYFF------RKGASVGYYHGD 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 263 APEIYKNIEMHNVTHMCCVPTVFNILLKG----------------NSL----------DLSHRS---------------- 300
Cdd:PLN02430 301 LNALRDDLMELKPTLLAGVPRVFERIHEGiqkalqelnprrrlifNALykyklawmnrGYSHKKaspmadflafrkvkak 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 301 --GPVHVLTGGSPPPAALVKKVQRL---GFqVMHAYGLTEATGPVLFCeWQDEwnrlpenqqmelkarqgLSILG-LTEV 374
Cdd:PLN02430 381 lgGRLRLLISGGAPLSTEIEEFLRVtscAF-VVQGYGLTETLGPTTLG-FPDE-----------------MCMLGtVGAP 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 375 DVRNKETQESVPRDG------KTMGEIVMKGSSIMKGYLKNPKATYEAFKHGWLNSGDVGVIHPDGHVEIKDRSKDII-I 447
Cdd:PLN02430 442 AVYNELRLEEVPEMGydplgePPRGEICVRGKCLFSGYYKNPELTEEVMKDGWFHTGDIGEILPNGVLKIIDRKKNLIkL 521
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 15218840 448 SGGENISSVEVENiIYKYPKVLE-------------TAVVAmPHP 479
Cdd:PLN02430 522 SQGEYVALEYLEN-VYGQNPIVEdiwvygdsfksmlVAVVV-PNE 564
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
28-543 |
3.02e-20 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 95.61 E-value: 3.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 28 PNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAIL 107
Cdd:PRK12467 526 PERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYML 605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 108 RHAKPKILfIYRSfeplarEILQLLSSEDSnlnLPVIFIHEIDFPKRVSSEESdyecliqrgEPTPLllarmfciqdehD 187
Cdd:PRK12467 606 DDSGVRLL-LTQS------HLLAQLPVPAG---LRSLCLDEPADLLCGYSGHN---------PEVAL------------D 654
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 188 PISLNY---TSGTTADPKGVVISHRGayLSTLSAIIGWEMGTCP---VYLWTLPMFHCNGWTFTWGTAArgGTSVCMR-- 259
Cdd:PRK12467 655 PDNLAYviyTSGSTGQPKGVAISHGA--LANYVCVIAERLQLAAddsMLMVSTFAFDLGVTELFGALAS--GATLHLLpp 730
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 260 --HVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSHRSGPVHVltGGSPPPAALVKKVQRLGFQ--VMHAYGLTE 335
Cdd:PRK12467 731 dcARDAEAFAALMADQGVTVLKIVPSHLQALLQASRVALPRPQRALVC--GGEALQVDLLARVRALGPGarLINHYGPTE 808
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 336 ATGPVLFCEWQDEwNRLPENQQMElkarQGLSILGLTEVDvrnketQESVPRDGKTMGEIVMKGSSIMKGYLKNPKATYE 415
Cdd:PRK12467 809 TTVGVSTYELSDE-ERDFGNVPIG----QPLANLGLYILD------HYLNPVPVGVVGELYIGGAGLARGYHRRPALTAE 877
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 416 AF-------KHGWL-NSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPTwGETPCA 487
Cdd:PRK12467 878 RFvpdpfgaDGGRLyRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDA-GLQLVA 956
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 15218840 488 FVVLEKGETNNEDREdklvtKERDLIEYCRENLPHFMCPRKVVFLDELPKNGNGKI 543
Cdd:PRK12467 957 YLVPAAVADGAEHQA-----TRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKL 1007
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
27-549 |
4.00e-20 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 94.17 E-value: 4.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 27 YPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAI 106
Cdd:PRK08279 50 HPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQRGAVLAHS 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 107 LRHAKPKILFIyrsfeplAREILQLLSSEDSNLNLPVIFIHEIDFPKRVSSEESDYECLIQRGEPTPL-----LLARmfc 181
Cdd:PRK08279 130 LNLVDAKHLIV-------GEELVEAFEEARADLARPPRLWVAGGDTLDDPEGYEDLAAAAAGAPTTNPasrsgVTAK--- 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 182 iqdehDPISLNYTSGTTADPKGVVISHRgAYLSTLSAIIG-WEMGTCPVYLWTLPMFHCNGWTFTWGTA-ARGGTSVCMR 259
Cdd:PRK08279 200 -----DTAFYIYTSGTTGLPKAAVMSHM-RWLKAMGGFGGlLRLTPDDVLYCCLPLYHNTGGTVAWSSVlAAGATLALRR 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 260 HVTAPEIYKNIEMHNVTHMCCVPTVFNILLKG--NSLDLSHRsgpVHVLTGGSPPPAALVKKVQRLG-FQVMHAYGLTEA 336
Cdd:PRK08279 274 KFSASRFWDDVRRYRATAFQYIGELCRYLLNQppKPTDRDHR---LRLMIGNGLRPDIWDEFQQRFGiPRILEFYAASEG 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 337 T----------GPVLFCEwqdEWNRLPenqqmelkarqglsiLGLTEVDVrnkETQESVpRD-------------GKTMG 393
Cdd:PRK08279 351 NvgfinvfnfdGTVGRVP---LWLAHP---------------YAIVKYDV---DTGEPV-RDadgrcikvkpgevGLLIG 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 394 EIVMKGSsiMKGYLkNPKAT-----YEAFKHG--WLNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYP 466
Cdd:PRK08279 409 RITDRGP--FDGYT-DPEASekkilRDVFKKGdaWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENALSGFP 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 467 KVLETAV--VAMPHpTWGETPCAFVVLEKGETNNEDRedklvtkerdLIEYCRENLPHFMCPrkvVFL---DELPKNGNG 541
Cdd:PRK08279 486 GVEEAVVygVEVPG-TDGRAGMAAIVLADGAEFDLAA----------LAAHLYERLPAYAVP---LFVrlvPELETTGTF 551
|
....*...
gi 15218840 542 KILKPKLR 549
Cdd:PRK08279 552 KYRKVDLR 559
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
28-571 |
5.47e-20 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 95.02 E-value: 5.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 28 PNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAIL 107
Cdd:PRK12316 525 PEAPALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYML 604
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 108 RHAKPKILFIYR---SFEPLAREIlQLLSSEDSNLNLPVifiheidfpkrvSSEESDYECLiqrgepTPLLLARMFciqd 184
Cdd:PRK12316 605 EDSGVQLLLSQShlgRKLPLAAGV-QVLDLDRPAAWLEG------------YSEENPGTEL------NPENLAYVI---- 661
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 185 ehdpislnYTSGTTADPKGVVISHRGaylstLSAIIGW-----EMGTCPVYLWTLPM-FHCNGWTFtWGTAARGGTsvcm 258
Cdd:PRK12316 662 --------YTSGSTGKPKGAGNRHRA-----LSNRLCWmqqayGLGVGDTVLQKTPFsFDVSVWEF-FWPLMSGAR---- 723
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 259 RHVTAPEIYKN-------IEMHNVTHMCCVPTVFNILLKGNSLD--LSHRSgpvhVLTGGSPPPAALVKKVQRLGFQ--V 327
Cdd:PRK12316 724 LVVAAPGDHRDpaklvelINREGVDTLHFVPSMLQAFLQDEDVAscTSLRR----IVCSGEALPADAQEQVFAKLPQagL 799
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 328 MHAYGLTEATGPVLFCEWQDEWNRlpenqqmELKARQGLSILGLTEVDVrnkeTQESVPRdgKTMGEIVMKGSSIMKGYL 407
Cdd:PRK12316 800 YNLYGPTEAAIDVTHWTCVEEGGD-------SVPIGRPIANLACYILDA----NLEPVPV--GVLGELYLAGRGLARGYH 866
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 408 KNPKATYEAF-------KHGWLNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPhpt 480
Cdd:PRK12316 867 GRPGLTAERFvpspfvaGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD--- 943
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 481 wGETPCAFVVLEkgETNNEDREDklvtkerdLIEYCRENLPHFMCPRKVVFLDELPKNGNGKILKPKLRDIAKGLVAEDE 560
Cdd:PRK12316 944 -GKQLVGYVVLE--SEGGDWREA--------LKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKALPAPEASVAQQGY 1012
|
570
....*....|.
gi 15218840 561 VNVRSKVQRPV 571
Cdd:PRK12316 1013 VAPRNALERTL 1023
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
193-543 |
1.11e-19 |
|
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: 92.11 E-value: 1.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 193 YTSGTTADPKGVVISHRgaylstlsAIIGWEMGTCPVYLWTLPMFHCNGWTFTWGTAAR-------GGTSVCMR----HV 261
Cdd:cd17644 113 YTSGSTGKPKGVMIEHQ--------SLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEeiyvtllSGATLVLRpeemRS 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 262 TAPEIYKNIEMHNVTHMCCVPTVFNILLkgNSLDLSHRSGPVH---VLTGGS---PPPAALVKKVQRLGFQVMHAYGLTE 335
Cdd:cd17644 185 SLEDFVQYIQQWQLTVLSLPPAYWHLLV--LELLLSTIDLPSSlrlVIVGGEavqPELVRQWQKNVGNFIQLINVYGPTE 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 336 ATGPVLFCEWQDewnrlpenqqmeLKARQGLSI-----LGLTEVDVRNkETQESVPRDgkTMGEIVMKGSSIMKGYLKNP 410
Cdd:cd17644 263 ATIAATVCRLTQ------------LTERNITSVpigrpIANTQVYILD-ENLQPVPVG--VPGELHIGGVGLARGYLNRP 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 411 KATYEAF-KHGWLNS--------GDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPTW 481
Cdd:cd17644 328 ELTAEKFiSHPFNSSeserlyktGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPG 407
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15218840 482 GETPCAFVVLEKGETNNedredklVTKERdliEYCRENLPHFMCPRKVVFLDELPKNGNGKI 543
Cdd:cd17644 408 NKRLVAYIVPHYEESPS-------TVELR---QFLKAKLPDYMIPSAFVVLEELPLTPNGKI 459
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
38-543 |
1.68e-19 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 91.98 E-value: 1.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 38 TRFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINT---RLD----ATSIAAILRHA 110
Cdd:PRK07768 28 VRHTWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTMLHQptpRTDlavwAEDTLRVIGMI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 111 KPKILFIYRSFEPLAreilQLLSSEDsnlnLPVIFIHEidfpkrvsseesdyecLIQRGEPTPLLLarmfciqDEHDPIS 190
Cdd:PRK07768 108 GAKAVVVGEPFLAAA----PVLEEKG----IRVLTVAD----------------LLAADPIDPVET-------GEDDLAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 191 LNYTSGTTADPKGVVISHRGAYlSTLSAI---IGWEMGTCPVYLWtLPMFHCNGWT-FTWGTAARGGTSVC---MRHVTA 263
Cdd:PRK07768 157 MQLTSGSTGSPKAVQITHGNLY-ANAEAMfvaAEFDVETDVMVSW-LPLFHDMGMVgFLTVPMYFGAELVKvtpMDFLRD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 264 PEIY-KNIEMHNVThMCCVP----TVFNILL----KGNSLDLSH-RsgpvHVLTGGSP-PPAA---LVKKVQRLGFQ--- 326
Cdd:PRK07768 235 PLLWaELISKYRGT-MTAAPnfayALLARRLrrqaKPGAFDLSSlR----FALNGAEPiDPADvedLLDAGARFGLRpea 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 327 VMHAYGLTEATGPVLFCEWQ-----DEWNR-LPENQQMELKARQG----LSILG--LTEVDVRnketqeSVPRDGKTM-- 392
Cdd:PRK07768 310 ILPAYGMAEATLAVSFSPCGaglvvDEVDAdLLAALRRAVPATKGntrrLATLGppLPGLEVR------VVDEDGQVLpp 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 393 ---GEIVMKGSSIMKGYLK--NPKATYEAfkHGWLNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPK 467
Cdd:PRK07768 384 rgvGVIELRGESVTPGYLTmdGFIPAQDA--DGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEG 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 468 VLETAVVA--MPHPTWGETpcaFVVLekGETNNEDREDKLVTKERDLIEYCRENLPhfMCPRKVVFLD--ELPKNGNGKI 543
Cdd:PRK07768 462 VRPGNAVAvrLDAGHSREG---FAVA--VESNAFEDPAEVRRIRHQVAHEVVAEVG--VRPRNVVVLGpgSIPKTPSGKL 534
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
9-543 |
1.96e-19 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 92.80 E-value: 1.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 9 ANNVPLTPIT-FLKRASECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMA 87
Cdd:PRK10252 452 AVEIPETTLSaLVAQQAAKTPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEA 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 88 GAVLNPINTRLDATSIAAILRHAKPKILFIYRSFEPLareilqllssedsnlnlpvifiheidFPKRVSSEESDYECLIQ 167
Cdd:PRK10252 532 GAAWLPLDTGYPDDRLKMMLEDARPSLLITTADQLPR--------------------------FADVPDLTSLCYNAPLA 585
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 168 RGEPTPLLLARmfciqdEHDPISLNYTSGTTADPKGVVISHRgaylstlsAIIG---W-----EMGTCPVYLWTLPM-FH 238
Cdd:PRK10252 586 PQGAAPLQLSQ------PHHTAYIIFTSGSTGRPKGVMVGQT--------AIVNrllWmqnhyPLTADDVVLQKTPCsFD 651
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 239 CNGWTFTWGTAArGGTSVcmrhVTAPEIYKN-------IEMHNVTHMCCVPTVFNILLKGNSLDLSHRSGPV--HVLTGG 309
Cdd:PRK10252 652 VSVWEFFWPFIA-GAKLV----MAEPEAHRDplamqqfFAEYGVTTTHFVPSMLAAFVASLTPEGARQSCASlrQVFCSG 726
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 310 SPPPAALVKKVQRLGFQVMH-AYGLTEATGPVLFcewqdeWNRLPEnqqmELKARQGLSI--------LGLTEVDVRNKE 380
Cdd:PRK10252 727 EALPADLCREWQQLTGAPLHnLYGPTEAAVDVSW------YPAFGE----ELAAVRGSSVpigypvwnTGLRILDARMRP 796
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 381 TQESVPrdgktmGEIVMKGSSIMKGYLKNPKATYEAFKHG-------WLNSGDVGVIHPDGHVEIKDRSKDIIISGGENI 453
Cdd:PRK10252 797 VPPGVA------GDLYLTGIQLAQGYLGRPDLTASRFIADpfapgerMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRI 870
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 454 SSVEVENIIYKYPKVlETAVV-------AMPHPTWGETPCAFVVLEKGETNNEDredklvtkerDLIEYCRENLPHFMCP 526
Cdd:PRK10252 871 ELGEIDRAMQALPDV-EQAVThacvinqAAATGGDARQLVGYLVSQSGLPLDTS----------ALQAQLRERLPPHMVP 939
|
570
....*....|....*..
gi 15218840 527 RKVVFLDELPKNGNGKI 543
Cdd:PRK10252 940 VVLLQLDQLPLSANGKL 956
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
40-474 |
2.72e-19 |
|
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: 91.33 E-value: 2.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 40 FTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKilFIYR 119
Cdd:cd17641 12 FTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGAR--VVIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 120 SFEPLAREILQLLSSedsnlnlpvifIHEIDF-----PK--------RVSSEESDYECLIQRGEPTPLLLARMFCIQDEH 186
Cdd:cd17641 90 EDEEQVDKLLEIADR-----------IPSVRYviycdPRgmrkyddpRLISFEDVVALGRALDRRDPGLYEREVAAGKGE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 187 DPISLNYTSGTTADPKGVVISHRgAYLSTLSAIIGW-EMGTCPVYLWTLPMFHCNGWTFTWGTAARGGTSVC-------- 257
Cdd:cd17641 159 DVAVLCTTSGTTGKPKLAMLSHG-NFLGHCAAYLAAdPLGPGDEYVSVLPLPWIGEQMYSVGQALVCGFIVNfpeepetm 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 258 ---MRHV------TAPEIYKNIEMHNVTHMCCVP----TVFNILLK-GN-SLDLSHRSGPVHVltgGSPPPAALVKKV-- 320
Cdd:cd17641 238 medLREIgptfvlLPPRVWEGIAADVRARMMDATpfkrFMFELGMKlGLrALDRGKRGRPVSL---WLRLASWLADALlf 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 321 ----QRLGF-QVMHAYGLTEATGPVLFCEWQdewnrlpenqQMELKARQglsILGLTEV----------DVRNKETqeSV 385
Cdd:cd17641 315 rplrDRLGFsRLRSAATGGAALGPDTFRFFH----------AIGVPLKQ---LYGQTELagaytvhrdgDVDPDTV--GV 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 386 PRDGKTM-----GEIVMKGSSIMKGYLKNPKATYEAF-KHGWLNSGDVGVIHPDGHVEIKDRSKDI-IISGGENISSVEV 458
Cdd:cd17641 380 PFPGTEVridevGEILVRSPGVFVGYYKNPEATAEDFdEDGWLHTGDAGYFKENGHLVVIDRAKDVgTTSDGTRFSPQFI 459
|
490
....*....|....*.
gi 15218840 459 ENIIYKYPKVLEtAVV 474
Cdd:cd17641 460 ENKLKFSPYIAE-AVV 474
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
281-552 |
2.97e-19 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 90.44 E-value: 2.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 281 VPTVFNILLKGNSLDLSHRSGpvhVLTGGSPPPAALVKKVQRLGFQVMHAYGLTEATGPVLFCEWQDEWNrlpenqqmel 360
Cdd:PRK07445 214 VPTQLQRLLQLRPQWLAQFRT---ILLGGAPAWPSLLEQARQLQLRLAPTYGMTETASQIATLKPDDFLA---------- 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 361 KARQGLSILGLTEVDVRNKETqesvprdgktmGEIVMKGSSIMKGYLKNPKATYEAFKhgwlnSGDVGVIHPDGHVEIKD 440
Cdd:PRK07445 281 GNNSSGQVLPHAQITIPANQT-----------GNITIQAQSLALGYYPQILDSQGIFE-----TDDLGYLDAQGYLHILG 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 441 RSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETNNEDREDKLVTKerdlieycrenL 520
Cdd:PRK07445 345 RNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVPKDPSISLEELKTAIKDQ-----------L 413
|
250 260 270
....*....|....*....|....*....|..
gi 15218840 521 PHFMCPRKVVFLDELPKNGNGKILKPKLRDIA 552
Cdd:PRK07445 414 SPFKQPKHWIPVPQLPRNPQGKINRQQLQQIA 445
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
193-459 |
1.14e-17 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 86.71 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 193 YTSGTTADPKGVVISHrGAYLSTLSAI--IGWEMGTCPVYLWTLPMFH-----CNGWTFTWGTAARGGTSVCMRHvTAPE 265
Cdd:PLN02387 257 YTSGSTGLPKGVMMTH-GNIVATVAGVmtVVPKLGKNDVYLAYLPLAHilelaAESVMAAVGAAIGYGSPLTLTD-TSNK 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 266 IYK----NIEMHNVTHMCCVPTVFNILLKG-------------NSLDLSHR----------------------------- 299
Cdd:PLN02387 335 IKKgtkgDASALKPTLMTAVPAILDRVRDGvrkkvdakgglakKLFDIAYKrrlaaiegswfgawglekllwdalvfkki 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 300 ----SGPVH-VLTGGSPppaaLVKKVQR-----LGFQVMHAYGLTEATGPVLFCEWQDE-----WNRLPenqqmelkarq 364
Cdd:PLN02387 415 ravlGGRIRfMLSGGAP----LSGDTQRfinicLGAPIGQGYGLTETCAGATFSEWDDTsvgrvGPPLP----------- 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 365 gLSILGLTEVDVRNKETQES-VPRdgktmGEIVMKGSSIMKGYLKNPKATYEAFK---HG--WLNSGDVGVIHPDGHVEI 438
Cdd:PLN02387 480 -CCYVKLVSWEEGGYLISDKpMPR-----GEIVIGGPSVTLGYFKNQEKTDEVYKvdeRGmrWFYTGDIGQFHPDGCLEI 553
|
330 340
....*....|....*....|..
gi 15218840 439 KDRSKDII-ISGGENISSVEVE 459
Cdd:PLN02387 554 IDRKKDIVkLQHGEYVSLGKVE 575
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
191-549 |
1.24e-17 |
|
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: 86.00 E-value: 1.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 191 LNYTSGTTADPKGVVISHRGAYLSTLSAIIGWEMGTCPVYLWTLPMFHCNGWTFTWGTAARGG-------TSVCMRHvta 263
Cdd:cd05908 111 IQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGmnqylmpTRLFIRR--- 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 264 PEIY-KNIEMHNVTHMCCVPTVFNILLK------GNSLDLSHrsgpVHVLTGGSPPPAA-----LVKKVQRLGFQ---VM 328
Cdd:cd05908 188 PILWlKKASEHKATIVSSPNFGYKYFLKtlkpekANDWDLSS----IRMILNGAEPIDYelcheFLDHMSKYGLKrnaIL 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 329 HAYGLTEAT-------------GPVLFCEWQDEWNRLPENQQMELKARQGLSI-LGLTEVDVRNKETQESVPRDGkTMGE 394
Cdd:cd05908 264 PVYGLAEASvgaslpkaqspfkTITLGRRHVTHGEPEPEVDKKDSECLTFVEVgKPIDETDIRICDEDNKILPDG-YIGH 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 395 IVMKGSSIMKGYLKNPKATYEAF-KHGWLNSGDVGVIHpDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAV 473
Cdd:cd05908 343 IQIRGKNVTPGYYNNPEATAKVFtDDGWLKTGDLGFIR-NGRLVITGREKDIIFVNGQNVYPHDIERIAEELEGVELGRV 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 474 VAMphptwgetpcafvvlekGETNNEDREDKLVT------KERDLIEYCRENLPHF-----MCPRKVVFLDELPKNGNGK 542
Cdd:cd05908 422 VAC-----------------GVNNSNTRNEEIFCfiehrkSEDDFYPLGKKIKKHLnkrggWQINEVLPIRRIPKTTSGK 484
|
....*..
gi 15218840 543 ILKPKLR 549
Cdd:cd05908 485 VKRYELA 491
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
52-513 |
1.65e-17 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 85.83 E-value: 1.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 52 LAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNP--INTRL---DA--TSIAAILRHAKPKILFIYRSFEPL 124
Cdd:PRK09192 62 GARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPlpLPMGFggrESyiAQLRGMLASAQPAAIITPDELLPW 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 125 AREILqllssedSNLNLPVIFIHEiDFPKRvssEESDyeclIQRGEPTPlllarmfciqdeHDPISLNYTSGTTADPKGV 204
Cdd:PRK09192 142 VNEAT-------HGNPLLHVLSHA-WFKAL---PEAD----VALPRPTP------------DDIAYLQYSSGSTRFPRGV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 205 VISHRgAYLSTLSAI-------------IGW-----EMG---------TCPV---YLWT----------LPMFHCNGWTF 244
Cdd:PRK09192 195 IITHR-ALMANLRAIshdglkvrpgdrcVSWlpfyhDMGlvgflltpvATQLsvdYLPTrdfarrplqwLDLISRNRGTI 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 245 TWgtAARGGTSVCMRHVTAPEIykniemhnvthmccvptvfnillkgNSLDLSH-RSGPVhvltGGSPPPA----ALVKK 319
Cdd:PRK09192 274 SY--SPPFGYELCARRVNSKDL-------------------------AELDLSCwRVAGI----GADMIRPdvlhQFAEA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 320 VQRLGFQ---VMHAYGLTEATGPVLFcewqdewnrLPENQ--QMELKARQGLSILGLT---------------------- 372
Cdd:PRK09192 323 FAPAGFDdkaFMPSYGLAEATLAVSF---------SPLGSgiVVEEVDRDRLEYQGKAvapgaetrrvrtfvncgkalpg 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 373 -EVDVRNkETQESVPRdgKTMGEIVMKGSSIMKGYLKNPKATYEAFKHGWLNSGDVGVIHpDGHVEIKDRSKDIIISGGE 451
Cdd:PRK09192 394 hEIEIRN-EAGMPLPE--RVVGHICVRGPSLMSGYFRDEESQDVLAADGWLDTGDLGYLL-DGYLYITGRAKDLIIINGR 469
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15218840 452 NISSVEVENIIYKYPKVL--ETAVVAMPHPTwGETPcafVVLEKGETNNEDREDKLVTKERDLI 513
Cdd:PRK09192 470 NIWPQDIEWIAEQEPELRsgDAAAFSIAQEN-GEKI---VLLVQCRISDEERRGQLIHALAALV 529
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
28-571 |
2.87e-17 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 86.16 E-value: 2.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 28 PNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAIL 107
Cdd:PRK12316 3071 PDAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYML 3150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 108 RHAKPKILFIYRSFEPLAREILQLLSSEDSNLNLPvifihEIDFPKRVSSEESDYecliqrgeptplllarmfciqdehd 187
Cdd:PRK12316 3151 EDSGAQLLLSQSHLRLPLAQGVQVLDLDRGDENYA-----EANPAIRTMPENLAY------------------------- 3200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 188 pisLNYTSGTTADPKGVVISHrGAYLSTLSAIIGWEMGTCPVYLWTLPMFHCNGWTFTWGTAARGGTSVCMRHV---TAP 264
Cdd:PRK12316 3201 ---VIYTSGSTGKPKGVGIRH-SALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPedwRDP 3276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 265 EIYknIEMHNVTHMCCVPTVFNILLKGNSLDLSHRSGPVH-VLTGGSPPPAALVKKVQrLGFQVMHAYGLTEATGPVLFC 343
Cdd:PRK12316 3277 ALL--VELINSEGVDVLHAYPSMLQAFLEEEDAHRCTSLKrIVCGGEALPADLQQQVF-AGLPLYNLYGPTEATITVTHW 3353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 344 EWQDEWNRLPENQQMELKARQGLSILGLTEVDVRNketqesvprdgktMGEIVMKGSSIMKGYLKNPKATYEAF------ 417
Cdd:PRK12316 3354 QCVEEGKDAVPIGRPIANRACYILDGSLEPVPVGA-------------LGELYLGGEGLARGYHNRPGLTAERFvpdpfv 3420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 418 -KHGWLNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPhptwGETPCAFVVLEKGET 496
Cdd:PRK12316 3421 pGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAVD----GRQLVAYVVPEDEAG 3496
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15218840 497 NnedredklvtKERDLIEYCRENLPHFMCPRKVVFLDELPKNGNGKILKPKLRDIAKGLVAEDEVNVRSKVQRPV 571
Cdd:PRK12316 3497 D----------LREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPRPDAALLQQDYVAPVNELERRL 3561
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
14-468 |
3.13e-17 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 85.28 E-value: 3.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 14 LTPITFLKRASECYPN-----RTSIIYGK----TRFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAV 84
Cdd:PLN02861 43 DSPWQFFSDAVKKYPNnqmlgRRQVTDSKvgpyVWLTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEAC 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 85 PMAGAVLNPINTRLDATSIAAILRHAKPKILFIYrsfEPLAREILQLLSSEDSNLNLPVIFiHEIDFPKRVSSEESDYEC 164
Cdd:PLN02861 123 NSQGITYVPLYDTLGANAVEFIINHAEVSIAFVQ---ESKISSILSCLPKCSSNLKTIVSF-GDVSSEQKEEAEELGVSC 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 165 LiqRGEPTPLLLARMFCIQDEH--DPISLNYTSGTTADPKGVVISHRGAYLSTLSA-----IIGWEMGTCPVYLWTLPMF 237
Cdd:PLN02861 199 F--SWEEFSLMGSLDCELPPKQktDICTIMYTSGTTGEPKGVILTNRAIIAEVLSTdhllkVTDRVATEEDSYFSYLPLA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 238 HCNGWTFTWGTAARGgTSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLS-------------------- 297
Cdd:PLN02861 277 HVYDQVIETYCISKG-ASIGFWQGDIRYLMEDVQALKPTIFCGVPRVYDRIYTGIMQKISsggmlrkklfdfaynyklgn 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 298 -------HRSGP-----------------VHVLTGGSPPPAALVKKVQRL--GFQVMHAYGLTEATGPVlFCEWQDEWnr 351
Cdd:PLN02861 356 lrkglkqEEASPrldrlvfdkikeglggrVRLLLSGAAPLPRHVEEFLRVtsCSVLSQGYGLTESCGGC-FTSIANVF-- 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 352 lpenqqmelkarqglSILGLTEVDVRNKETQ-ESVPRDGKTM------GEIVMKGSSIMKGYLKNPKATYEAFKHGWLNS 424
Cdd:PLN02861 433 ---------------SMVGTVGVPMTTIEARlESVPEMGYDAlsdvprGEICLRGNTLFSGYHKRQDLTEEVLIDGWFHT 497
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 15218840 425 GDVGVIHPDGHVEIKDRSKDII-ISGGENISSVEVENIIYKYPKV 468
Cdd:PLN02861 498 GDIGEWQPNGAMKIIDRKKNIFkLSQGEYVAVENLENTYSRCPLI 542
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
162-473 |
5.42e-17 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 84.38 E-value: 5.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 162 YECLIQRGEPTPlllaRMFCIQDEHDPISLNYTSGTTADPKGVVISHRGAYLSTLSAIIGWEMGTCPVYLWTLPMFHcng 241
Cdd:PLN02736 201 YSKLLAQGRSSP----QPFRPPKPEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKFYPSDVHISYLPLAH--- 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 242 wtftwgTAARGGTSVCMRHVTAPEIYK--------NIEMHNVTHMCCVPTVFN--------------------------- 286
Cdd:PLN02736 274 ------IYERVNQIVMLHYGVAVGFYQgdnlklmdDLAALRPTIFCSVPRLYNriydgitnavkesgglkerlfnaayna 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 287 ---ILLKGNSLD----------LSHR-SGPVHVLTGGSPPPAALVKKVQRLGF--QVMHAYGLTEATGPVLFCewqDEWN 350
Cdd:PLN02736 348 kkqALENGKNPSpmwdrlvfnkIKAKlGGRVRFMSSGASPLSPDVMEFLRICFggRVLEGYGMTETSCVISGM---DEGD 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 351 RL-----PENQQMELKarqglsilgLTEVDVRNKETQES-VPRdgktmGEIVMKGSSIMKGYLKNPKATYEAF-KHGWLN 423
Cdd:PLN02736 425 NLsghvgSPNPACEVK---------LVDVPEMNYTSEDQpYPR-----GEICVRGPIIFKGYYKDEVQTREVIdEDGWLH 490
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 15218840 424 SGDVGVIHPDGHVEIKDRSKDII-ISGGENISSVEVENIIYKYPKVLETAV 473
Cdd:PLN02736 491 TGDIGLWLPGGRLKIIDRKKNIFkLAQGEYIAPEKIENVYAKCKFVAQCFV 541
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
413-554 |
6.84e-17 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 84.04 E-value: 6.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 413 TY-EAFKHGWLnSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPTWGETPCAFVVL 491
Cdd:PRK00174 476 TYfSTFKGMYF-TGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTL 554
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15218840 492 EKGETNnedrEDKLVTkerDLIEYCRENLPHFMCPRKVVFLDELPKNGNGKILKPKLRDIAKG 554
Cdd:PRK00174 555 KGGEEP----SDELRK---ELRNWVRKEIGPIAKPDVIQFAPGLPKTRSGKIMRRILRKIAEG 610
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
28-551 |
1.82e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 83.67 E-value: 1.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 28 PNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAIL 107
Cdd:PRK12467 3109 PEAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMI 3188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 108 rhakpkilfiyrsfeplareilqllssEDSNLNLpviFIHEIDFPKRVSSEESDYECLIQRGEPTPLLLArmfCIQDEHD 187
Cdd:PRK12467 3189 ---------------------------EDSGVKL---LLTQAHLLEQLPAPAGDTALTLDRLDLNGYSEN---NPSTRVM 3235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 188 PISLNY---TSGTTADPKGVVISHrGAYLSTLSAIIG-WEMGTCPVYLWTLPM-FHCNGWTFTWgTAARGGTSVCM--RH 260
Cdd:PRK12467 3236 GENLAYviyTSGSTGKPKGVGVRH-GALANHLCWIAEaYELDANDRVLLFMSFsFDGAQERFLW-TLICGGCLVVRdnDL 3313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 261 VTAPEIYKNIEMHNVTHMCCVPTVFNILLKgnslDLSHRSGPV--HVLTGGSPPPAALVKKVQRLGFQV--MHAYGLTEA 336
Cdd:PRK12467 3314 WDPEELWQAIHAHRISIACFPPAYLQQFAE----DAGGADCASldIYVFGGEAVPPAAFEQVKRKLKPRglTNGYGPTEA 3389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 337 TGPVLFceWqdewnRLPENQQMELKARQ-GLSILGLTEVDVRNKetQESVPRDgkTMGEIVMKGSSIMKGYLKNPKATYE 415
Cdd:PRK12467 3390 VVTVTL--W-----KCGGDAVCEAPYAPiGRPVAGRSIYVLDGQ--LNPVPVG--VAGELYIGGVGLARGYHQRPSLTAE 3458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 416 AF-------KHGWL-NSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPhPTWGETPCA 487
Cdd:PRK12467 3459 RFvadpfsgSGGRLyRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLARD-GAGGKQLVA 3537
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15218840 488 FVVLekgETNNEDREDKLvtkERDLieycRENLPHFMCPRKVVFLDELPKNGNGKILKPKLRDI 551
Cdd:PRK12467 3538 YVVP---ADPQGDWRETL---RDHL----AASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDP 3591
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
39-552 |
3.59e-16 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 81.87 E-value: 3.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 39 RFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPntpamyeMHFAVPMA-------GAVLNPINTRLDATSIAAILRHAK 111
Cdd:PLN02654 120 SLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLP-------MLMELPIAmlacariGAVHSVVFAGFSAESLAQRIVDCK 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 112 PKILfiyrsfeplareilqlLSSEDSNLNLPVIFIHEIDFPKRVSSEESDYE---CL-------IQRgEPTPLLLARMFC 181
Cdd:PLN02654 193 PKVV----------------ITCNAVKRGPKTINLKDIVDAALDESAKNGVSvgiCLtyenqlaMKR-EDTKWQEGRDVW 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 182 IQD---------------EHDPISLNYTSGTTADPKGVVIShRGAYLSTLSAIIGWEMGTCP--VYLWTLPMFHCNGWTF 244
Cdd:PLN02654 256 WQDvvpnyptkcevewvdAEDPLFLLYTSGSTGKPKGVLHT-TGGYMVYTATTFKYAFDYKPtdVYWCTADCGWITGHSY 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 245 -TWGTAARGGTSVCMRHV----TAPEIYKNIEMHNVTHMCCVPTVFNILLK-GNSLDLSHRSGPVHVLTGGSPP--PAAL 316
Cdd:PLN02654 335 vTYGPMLNGATVLVFEGApnypDSGRCWDIVDKYKVTIFYTAPTLVRSLMRdGDEYVTRHSRKSLRVLGSVGEPinPSAW 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 317 vkkvqRLGFQVmhaygLTEATGPVLFCEWQDE------------WNRLPENQQMELKARQGLSilglteVDVRNKETqes 384
Cdd:PLN02654 415 -----RWFFNV-----VGDSRCPISDTWWQTEtggfmitplpgaWPQKPGSATFPFFGVQPVI------VDEKGKEI--- 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 385 vprDGKTMGEIVMKGS-----SIMKGYLKNPKATYEAFKHGWLNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVE 459
Cdd:PLN02654 476 ---EGECSGYLCVKKSwpgafRTLYGDHERYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVE 552
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 460 NIIYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETNNEDRedklvtkERDLIEYCRENLPHFMCPRKVVFLDELPKNG 539
Cdd:PLN02654 553 SALVSHPQCAEAAVVGIEHEVKGQGIYAFVTLVEGVPYSEEL-------RKSLILTVRNQIGAFAAPDKIHWAPGLPKTR 625
|
570
....*....|...
gi 15218840 540 NGKILKPKLRDIA 552
Cdd:PLN02654 626 SGKIMRRILRKIA 638
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
28-548 |
5.41e-16 |
|
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: 80.60 E-value: 5.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 28 PNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAIL 107
Cdd:cd17656 2 PDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 108 RHAKPKILFIyrsfeplAREILQLLSSEDSnlnlpvifIHEIDFPkrVSSEESDYECLIqrgeptplllarmfcIQDEHD 187
Cdd:cd17656 82 LDSGVRVVLT-------QRHLKSKLSFNKS--------TILLEDP--SISQEDTSNIDY---------------INNSDD 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 188 PISLNYTSGTTADPKGVVISHRgaylsTLSAIIGWEmgtcpvYLWTLPMFHCNGWTFT-----------WGTAARGGTSV 256
Cdd:cd17656 130 LLYIIYTSGTTGKPKGVQLEHK-----NMVNLLHFE------REKTNINFSDKVLQFAtcsfdvcyqeiFSTLLSGGTLY 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 257 CMRHVT---APEIYKNIEMHNvTHMCCVPTVF-NILLKGNSLDLSHRSGPVHVLTGGSPPPAA--LVKKVQRLGFQVMHA 330
Cdd:cd17656 199 IIREETkrdVEQLFDLVKRHN-IEVVFLPVAFlKFIFSEREFINRFPTCVKHIITAGEQLVITneFKEMLHEHNVHLHNH 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 331 YGLTEaTGPVLFCEW--QDEWNRLPEnqqmelkarQGLSIlGLTEVDVRNKETQesvPRDGKTMGEIVMKGSSIMKGYLK 408
Cdd:cd17656 278 YGPSE-THVVTTYTInpEAEIPELPP---------IGKPI-SNTWIYILDQEQQ---LQPQGIVGELYISGASVARGYLN 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 409 NPKATYEAFKHGWLNS-------GDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPTW 481
Cdd:cd17656 344 RQELTAEKFFPDPFDPnermyrtGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKG 423
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15218840 482 GETPCAFVVLEKgETNNEDredklvtkerdLIEYCRENLPHFMCPRKVVFLDELPKNGNGKILKPKL 548
Cdd:cd17656 424 EKYLCAYFVMEQ-ELNISQ-----------LREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
193-549 |
9.62e-16 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 80.46 E-value: 9.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 193 YTSGTTADPKGVVISHRGAYlSTLSAIIGWEMGTCP--VYLWTLPMFHCNGW-TFTWGTAARGGTSVCMRHVTAPEIYKN 269
Cdd:PRK06060 152 YTSGTTGPPKAAIHRHADPL-TFVDAMCRKALRLTPedTGLCSARMYFAYGLgNSVWFPLATGGSAVINSAPVTPEAAAI 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 270 IEMH-NVTHMCCVPTVFNILLKGNSLDlSHRSGPVhVLTGGSPPPAALVKKVQRL--GFQVMHAYGLTEaTGPVLFCEWQ 346
Cdd:PRK06060 231 LSARfGPSVLYGVPNFFARVIDSCSPD-SFRSLRC-VVSAGEALELGLAERLMEFfgGIPILDGIGSTE-VGQTFVSNRV 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 347 DEWnrlpenqqmelkaRQGL--SILGLTEVDVrnketqesVPRDGKTMG-----EIVMKGSSIMKGYLKNPKATYEafKH 419
Cdd:PRK06060 308 DEW-------------RLGTlgRVLPPYEIRV--------VAPDGTTAGpgvegDLWVRGPAIAKGYWNRPDSPVA--NE 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 420 GWLNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETNNE 499
Cdd:PRK06060 365 GWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGATIDG 444
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 15218840 500 dredklvTKERDLIEYCRENLPHFMCPRKVVFLDELPKNGNGKILKPKLR 549
Cdd:PRK06060 445 -------SVMRDLHRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALR 487
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
193-543 |
1.45e-15 |
|
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: 79.37 E-value: 1.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 193 YTSGTTADPKGVVISHRGAyLSTLSAIIGWEMGTCPVYLWTLPM------FHCNGWTFtwgtAARGGTSVC-----MRhV 261
Cdd:cd17648 101 YTSGTTGKPKGVLVEHGSV-VNLRTSLSERYFGRDNGDEAVLFFsnyvfdFFVEQMTL----ALLNGQKLVvppdeMR-F 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 262 TAPEIYKNIEMHNVTHMCCVPTVFNILlkgnslDLSHRSGPVHVLTGGSPPPAALVKKV-QRLGFQVMHAYGLTEATGPV 340
Cdd:cd17648 175 DPDRFYAYINREKVTYLSGTPSVLQQY------DLARLPHLKRVDAAGEEFTAPVFEKLrSRFAGLIINAYGPTETTVTN 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 341 LFcewqdewNRLPENQQMELKARQGLsilGLTEVDVRNKETQEsVPRDGktMGEIVMKGSSIMKGYLKNPKATYEAF--- 417
Cdd:cd17648 249 HK-------RFFPGDQRFDKSLGRPV---RNTKCYVLNDAMKR-VPVGA--VGELYLGGDGVARGYLNRPELTAERFlpn 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 418 -----------KHGWL-NSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPTWGETP 485
Cdd:cd17648 316 pfqteqerargRNARLyKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDASQAQSR 395
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15218840 486 -----CAFVVLEKGetnnedredklVTKERDLIEYCRENLPHFMCPRKVVFLDELPKNGNGKI 543
Cdd:cd17648 396 iqkylVGYYLPEPG-----------HVPESDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKL 447
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
183-476 |
2.51e-15 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 78.65 E-value: 2.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 183 QDEHDPISLNYTSGTTADPKGVVIShRGAYLSTLSAI---IGWEMGTCPVYLWtLPMFHCNGWTFTWgTAARGGTSVCMR 259
Cdd:PRK05851 149 PDSGGPAVLQGTAGSTGTPRTAILS-PGAVLSNLRGLnarVGLDAATDVGCSW-LPLYHDMGLAFLL-TAALAGAPLWLA 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 260 HVTA----PEIYKNIEMHNVTHMCCVPTV-FNILLKGNS----LDLshrsGPVHV-LTGGSPPPAALVKK----VQRLGF 325
Cdd:PRK05851 226 PTTAfsasPFRWLSWLSDSRATLTAAPNFaYNLIGKYARrvsdVDL----GALRVaLNGGEPVDCDGFERfataMAPFGF 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 326 Q---VMHAYGLTEATGPV---------LFCEWQDewnrlPENQQMELKARQGLSILGLtevDVRNKETQESVPRDGKTMG 393
Cdd:PRK05851 302 DagaAAPSYGLAESTCAVtvpvpgiglRVDEVTT-----DDGSGARRHAVLGNPIPGM---EVRISPGDGAAGVAGREIG 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 394 EIVMKGSSIMKGYLKNPKATYEafkhGWLNSGDVGVIHPDGHVeIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAV 473
Cdd:PRK05851 374 EIEIRGASMMSGYLGQAPIDPD----DWFPTGDLGYLVDGGLV-VCGRAKELITVAGRNIFPTEIERVAAQVRGVREGAV 448
|
...
gi 15218840 474 VAM 476
Cdd:PRK05851 449 VAV 451
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
28-451 |
1.15e-14 |
|
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: 77.11 E-value: 1.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 28 PNRTSIIYGktrftwpQTYDRCCRLAASLISLN-IGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAI 106
Cdd:cd17632 63 PRFETITYA-------ELWERVGAVAAAHDPEQpVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPI 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 107 LRHAKPKILFIYRSFEPLAREILqLLSSEDSNLnlpVIFIHEIDFPKRVSSEESDYECLIQRGEPTPLL----------- 175
Cdd:cd17632 136 LAETEPRLLAVSAEHLDLAVEAV-LEGGTPPRL---VVFDHRPEVDAHRAALESARERLAAVGIPVTTLtliavrgrdlp 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 176 LARMFCIQDEHDPIS-LNYTSGTTADPKGVVISHRGAYLSTLSAiIGWEMGTCP--VYLWTLPMFHCNGWTFTWGTAARG 252
Cdd:cd17632 212 PAPLFRPEPDDDPLAlLIYTSGSTGTPKGAMYTERLVATFWLKV-SSIQDIRPPasITLNFMPMSHIAGRISLYGTLARG 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 253 GTSVcmrHVTAPE---IYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSHRSGPVH----------------VLTG----- 308
Cdd:cd17632 291 GTAY---FAAASDmstLFDDLALVRPTELFLVPRVCDMLFQRYQAELDRRSVAGAdaetlaervkaelrerVLGGrllaa 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 309 --GSPPPAALVKKV--QRLGFQVMHAYGLTEATGPVLfcewQDEWNRLPenqqmelkarqglsILGLTEVDVrnKE---- 380
Cdd:cd17632 368 vcGSAPLSAEMKAFmeSLLDLDLHDGYGSTEAGAVIL----DGVIVRPP--------------VLDYKLVDV--PElgyf 427
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15218840 381 -TQESVPRdgktmGEIVMKGSSIMKGYLKNPKATYEAF-KHGWLNSGDV-GVIHPDGHVEIKDRSKDIIISGGE 451
Cdd:cd17632 428 rTDRPHPR-----GELLVKTDTLFPGYYKRPEVTAEVFdEDGFYRTGDVmAELGPDRLVYVDRRNNVLKLSQGE 496
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
18-499 |
1.26e-14 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 76.86 E-value: 1.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 18 TFLKRASECYPNRTSIIYGKTRFTWPQ-TYD---------RCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMA 87
Cdd:PRK09274 10 RHLPRAAQERPDQLAVAVPGGRGADGKlAYDelsfaeldaRSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 88 GAVLNPINTRLDATSIAAILRHAKPKIlFIYRSFEPLAREILqlLSSEDSnlnlpviFIHEIDFPKRVSSEESDYECLIQ 167
Cdd:PRK09274 90 GAVPVLVDPGMGIKNLKQCLAEAQPDA-FIGIPKAHLARRLF--GWGKPS-------VRRLVTVGGRLLWGGTTLATLLR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 168 RGEPTPLLLARMfciqDEHDPISLNYTSGTTADPKGVVISHRG--AYLSTLSAIIGWEMGTcpVYLWTLPMFHCNGwtft 245
Cdd:PRK09274 160 DGAAAPFPMADL----APDDMAAILFTSGSTGTPKGVVYTHGMfeAQIEALREDYGIEPGE--IDLPTFPLFALFG---- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 246 wgtAARGGTSV--CM---RHVTA-PE-IYKNIEMHNVTHMCCVPTVFNILL---KGNSLDL-SHRSgpvhVLTGGSPPPA 314
Cdd:PRK09274 230 ---PALGMTSVipDMdptRPATVdPAkLFAAIERYGVTNLFGSPALLERLGrygEANGIKLpSLRR----VISAGAPVPI 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 315 ALVKKVQRL---GFQVMHAYGLTEATgPVLFCEWQDEwnrLPENQQMelkARQG-------------LSILGLTEVDVRN 378
Cdd:PRK09274 303 AVIERFRAMlppDAEILTPYGATEAL-PISSIESREI---LFATRAA---TDNGagicvgrpvdgveVRIIAISDAPIPE 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 379 KETQESVPRDGktMGEIVMKGSSIMKGYLKNPKATYEA--------FKHgwlNSGDVGVIHPDGHVEIKDRSKDIIISGG 450
Cdd:PRK09274 376 WDDALRLATGE--IGEIVVAGPMVTRSYYNRPEATRLAkipdgqgdVWH---RMGDLGYLDAQGRLWFCGRKAHRVETAG 450
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 15218840 451 ENISSVEVENIIYKYPKVLETAVVAMPHPTwGETPCAFVVLEKGETNNE 499
Cdd:PRK09274 451 GTLYTIPCERIFNTHPGVKRSALVGVGVPG-AQRPVLCVELEPGVACSK 498
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
305-543 |
1.27e-14 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 75.47 E-value: 1.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 305 VLTGGSPPPAALVKKVQRLGFQVMHAYGLTEATGPVLFcewqdewnrlpenqqmelkarqglsilgltevdvrnketqES 384
Cdd:PRK07824 156 VLVGGGPAPAPVLDAAAAAGINVVRTYGMSETSGGCVY----------------------------------------DG 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 385 VPRDGKTM----GEIVMKGSSIMKGYlKNPkATYEAF-KHGWLNSGDVGVIHpDGHVEIKDRSKDIIISGGENISSVEVE 459
Cdd:PRK07824 196 VPLDGVRVrvedGRIALGGPTLAKGY-RNP-VDPDPFaEPGWFRTDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVE 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 460 NIIYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETNNEDredklvtkerDLIEYCRENLPHFMCPRKVVFLDELPKNG 539
Cdd:PRK07824 273 AALATHPAVADCAVFGLPDDRLGQRVVAAVVGDGGPAPTLE----------ALRAHVARTLDRTAAPRELHVVDELPRRG 342
|
....
gi 15218840 540 NGKI 543
Cdd:PRK07824 343 IGKV 346
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
182-548 |
2.31e-14 |
|
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: 75.28 E-value: 2.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 182 IQDEHDPISLNYTSGTTADPKGVVISHRgaylsTLSAIIGWEMGTCPV------YLWTLPMFHCNGW-TFTWGTAargGT 254
Cdd:cd17645 100 LTNPDDLAYVIYTSGSTGLPKGVMIEHH-----NLVNLCEWHRPYFGVtpadksLVYASFSFDASAWeIFPHLTA---GA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 255 SVcmrHVTAPEIYKNI-------EMHNVThMCCVPTVfnilLKGNSLDLSHRSGPVhVLTGGSpppaaLVKKVQRLGFQV 327
Cdd:cd17645 172 AL---HVVPSERRLDLdalndyfNQEGIT-ISFLPTG----AAEQFMQLDNQSLRV-LLTGGD-----KLKKIERKGYKL 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 328 MHAYGLTEATGPVLFCEWQDEWNRLPENQQMelkARQGLSILGltevdvrnkETQESVPRDgkTMGEIVMKGSSIMKGYL 407
Cdd:cd17645 238 VNNYGPTENTVVATSFEIDKPYANIPIGKPI---DNTRVYILD---------EALQLQPIG--VAGELCIAGEGLARGYL 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 408 KNPKATYEAF-------KHGWLNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPT 480
Cdd:cd17645 304 NRPELTAEKFivhpfvpGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDAD 383
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15218840 481 WGETPCAFVVLEKGETNNEDRedklvtkerdliEYCRENLPHFMCPRKVVFLDELPKNGNGKILKPKL 548
Cdd:cd17645 384 GRKYLVAYVTAPEEIPHEELR------------EWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
183-543 |
2.83e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 75.07 E-value: 2.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 183 QDEHDPISLNYTSGTTADPKGV------VISHRGAYLSTLSAiigwEMGTCPVYLwtLPMFHCNGwtFTWGTAA---RGG 253
Cdd:PRK08308 98 YLAEEPSLLQYSSGTTGEPKLIrrswteIDREIEAYNEALNC----EQDETPIVA--CPVTHSYG--LICGVLAaltRGS 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 254 TSVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKgnsldLSHRSGPVH-VLTGGSPPPAALVKKVQRLGFQVMHAYG 332
Cdd:PRK08308 170 KPVIITNKNPKFALNILRNTPQHILYAVPLMLHILGR-----LLPGTFQFHaVMTSGTPLPEAWFYKLRERTTYMMQQYG 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 333 LTEAtGPVLFCewqdewnrlpenqqMELKARQGLSILgLTEVDVRNKETQESvPRdgktmgEIV--MKGSSImkgylknp 410
Cdd:PRK08308 245 CSEA-GCVSIC--------------PDMKSHLDLGNP-LPHVSVSAGSDENA-PE------EIVvkMGDKEI-------- 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 411 katyeafkhgwlNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPTWGETPCAFVV 490
Cdd:PRK08308 294 ------------FTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVI 361
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 15218840 491 LEKGETNNEDRedklvtkerdliEYCRENLPHFMCPRKVVFLDELPKNGNGKI 543
Cdd:PRK08308 362 SHEEIDPVQLR------------EWCIQHLAPYQVPHEIESVTEIPKNANGKV 402
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
32-546 |
5.78e-14 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 74.78 E-value: 5.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 32 SIIY-----GKT-RFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNT--P--AMyemhFAVPMAGAVLNPINTRLDAT 101
Cdd:PTZ00237 79 ALIYecpylKKTiKLTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTlePliAM----LSCARIGATHCVLFDGYSVK 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 102 SIAAILRHAKPKiLFIYRSFEPLAREILQLLSSEDSNLNLPViFI--HEIDFPKRVSSEESDYEcLIQRGEPTPLLLARM 179
Cdd:PTZ00237 155 SLIDRIETITPK-LIITTNYGILNDEIITFTPNLKEAIELST-FKpsNVITLFRNDITSESDLK-KIETIPTIPNTLSWY 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 180 FCIQ----------------DEHDPISLNYTSGTTADPKGVVISHrGAYLstlsaiigwemgTCPVYLWTLPM------- 236
Cdd:PTZ00237 232 DEIKkikennqspfyeyvpvESSHPLYILYTSGTTGNSKAVVRSN-GPHL------------VGLKYYWRSIIekdiptv 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 237 FHCN---GWT----FTWGTAARGGTSVCMR-HVTAPE-----IYKNIEMHNVTHMCCVPTVFNILLK----GNSL----D 295
Cdd:PTZ00237 299 VFSHssiGWVsfhgFLYGSLSLGNTFVMFEgGIIKNKhieddLWNTIEKHKVTHTLTLPKTIRYLIKtdpeATIIrskyD 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 296 LSHRsgpVHVLTGGSPPPAALVKKV-QRLGFQVMHAYGLTEATGPVLFCEwqdewnrlpENQQMELKArqglsiLGLTEV 374
Cdd:PTZ00237 379 LSNL---KEIWCGGEVIEESIPEYIeNKLKIKSSRGYGQTEIGITYLYCY---------GHINIPYNA------TGVPSI 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 375 DVRNKETQEsvprDGKTM-----GEIVMK---GSSIMKGYLKNP---KATYEAFKhGWLNSGDVGVIHPDGHVEIKDRSK 443
Cdd:PTZ00237 441 FIKPSILSE----DGKELnvneiGEVAFKlpmPPSFATTFYKNDekfKQLFSKFP-GYYNSGDLGFKDENGYYTIVSRSD 515
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 444 DIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETNNEDREDKLVTKERDLIEycrENLPHF 523
Cdd:PTZ00237 516 DQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGLLVLKQDQSNQSIDLNKLKNEINNIIT---QDIESL 592
|
570 580
....*....|....*....|...
gi 15218840 524 MCPRKVVFLDELPKNGNGKILKP 546
Cdd:PTZ00237 593 AVLRKIIIVNQLPKTKTGKIPRQ 615
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
35-548 |
2.11e-13 |
|
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: 72.71 E-value: 2.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 35 YGKTRFTWPQTYDRCCRLAASLIS-LNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPK 113
Cdd:cd05938 1 FEGETYTYRDVDRRSNQAARALLAhAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 114 ILFIYRSFEPLAREILQLLSSEdsnlNLPVIFIHEIDFPKRVSS------EESDyecliqrgEPTPlllarmfciQDEHD 187
Cdd:cd05938 81 VLVVAPELQEAVEEVLPALRAD----GVSVWYLSHTSNTEGVISlldkvdAASD--------EPVP---------ASLRA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 188 PISLN------YTSGTTADPKGVVISHRGAYLSTLsaiIGWEMGTCP---VYLwTLPMFHCNGWTFTW-GTAARGGTSVC 257
Cdd:cd05938 140 HVTIKspalyiYTSGTTGLPKAARISHLRVLQCSG---FLSLCGVTAddvIYI-TLPLYHSSGFLLGIgGCIELGATCVL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 258 MRHVTAPEIYKNIEMHNVT----------HMCCVPTVFNillkgnslDLSHRsgpVHVLTGGSPPPAALVKKVQRLG-FQ 326
Cdd:cd05938 216 KPKFSASQFWDDCRKHNVTviqyigellrYLCNQPQSPN--------DRDHK---VRLAIGNGLRADVWREFLRRFGpIR 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 327 VMHAYGLTEatGPVLFCEWQDEW---NRLPENQQMelkarqgLSILGLTEVDVrnkETQESVpRDGKTMGEIVMKG---- 399
Cdd:cd05938 285 IREFYGSTE--GNIGFFNYTGKIgavGRVSYLYKL-------LFPFELIKFDV---EKEEPV-RDAQGFCIPVAKGepgl 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 400 --SSIMK-----GYLKNPKAT-----YEAFKHG--WLNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKY 465
Cdd:cd05938 352 lvAKITQqspflGYAGDKEQTekkllRDVFKKGdvYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLL 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 466 PKVLETAVVAMPHPTW-GETPCAFVVLEKGETNNEDRedklvtkerdLIEYCRENLPHFMCPRKVVFLDELPKNGNGKIL 544
Cdd:cd05938 432 DFLQEVNVYGVTVPGHeGRIGMAAVKLKPGHEFDGKK----------LYQHVREYLPAYARPRFLRIQDSLEITGTFKQQ 501
|
....
gi 15218840 545 KPKL 548
Cdd:cd05938 502 KVRL 505
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
38-554 |
2.53e-13 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 72.67 E-value: 2.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 38 TRFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTP-AMYEMhFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILF 116
Cdd:PRK10524 83 RTYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAeAAFAM-LACARIGAIHSVVFGGFASHSLAARIDDAKPVLIV 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 117 IYRS---------FEPLAREILQLLSSEDSNLnlpVIFIHEIDFPKRVSSEESDYECLIQRgeptpLLLARMFCIQ-DEH 186
Cdd:PRK10524 162 SADAgsrggkvvpYKPLLDEAIALAQHKPRHV---LLVDRGLAPMARVAGRDVDYATLRAQ-----HLGARVPVEWlESN 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 187 DPISLNYTSGTTADPKGVvisHR--GAYLSTLSAI------------------IGWEMG-TCPVY------LWTLpMFHc 239
Cdd:PRK10524 234 EPSYILYTSGTTGKPKGV---QRdtGGYAVALATSmdtifggkagetffcasdIGWVVGhSYIVYapllagMATI-MYE- 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 240 ngwtftwGTAARGGTSVCMRHVtapeiykniEMHNVTHMCCVPTVFNILlKGNSLDLSHR---SGPVHVLTGGSP---PP 313
Cdd:PRK10524 309 -------GLPTRPDAGIWWRIV---------EKYKVNRMFSAPTAIRVL-KKQDPALLRKhdlSSLRALFLAGEPldePT 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 314 AALVkkvqrlgfqvmhayglTEATG-PVLFCEWQDE--WNRLPENQQMELKARQ----GLSILGLtEVDVRNKETQESVP 386
Cdd:PRK10524 372 ASWI----------------SEALGvPVIDNYWQTEtgWPILAIARGVEDRPTRlgspGVPMYGY-NVKLLNEVTGEPCG 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 387 RDGKtmGEIVMKG-------SSI-------MKGYlknpkatYEAFKHGWLNSGDVGVIHPDGHVEIKDRSKDIIISGGEN 452
Cdd:PRK10524 435 PNEK--GVLVIEGplppgcmQTVwgdddrfVKTY-------WSLFGRQVYSTFDWGIRDADGYYFILGRTDDVINVAGHR 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 453 ISSVEVENIIYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETnNEDREDKLvTKERDLIEYCRENLPHFMCPRKVVFL 532
Cdd:PRK10524 506 LGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSDS-LADREARL-ALEKEIMALVDSQLGAVARPARVWFV 583
|
570 580
....*....|....*....|..
gi 15218840 533 DELPKNGNGKILKPKLRDIAKG 554
Cdd:PRK10524 584 SALPKTRSGKLLRRAIQAIAEG 605
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
193-549 |
3.10e-13 |
|
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: 72.07 E-value: 3.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 193 YTSGTTADPKGVVISHRGAYlsTLSAIIGWEMGTCP---VYLwTLPMFHCNGWTFTWGTAARGGTSVCMRH-VTAPEIYK 268
Cdd:cd05939 111 YTSGTTGLPKAAVIVHSRYY--RIAAGAYYAFGMRPedvVYD-CLPLYHSAGGIMGVGQALLHGSTVVIRKkFSASNFWD 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 269 NIEMHNVTHMCCVPTVFNILLKGNSLDlSHRSGPVHVLTGGSPPPAALVKKVQRLGF-QVMHAYGLTEATGPVLfcewqd 347
Cdd:cd05939 188 DCVKYNCTIVQYIGEICRYLLAQPPSE-EEQKHNVRLAVGNGLRPQIWEQFVRRFGIpQIGEFYGATEGNSSLV------ 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 348 ewnrlpeNQQMELKARQGLSILGLTEVDVR----NKETQESVpRD-------------GKTMGEIVMKG-SSIMKGYLK- 408
Cdd:cd05939 261 -------NIDNHVGACGFNSRILPSVYPIRlikvDEDTGELI-RDsdglcipcqpgepGLLVGKIIQNDpLRRFDGYVNe 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 409 ---NPKATYEAFKHG--WLNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAV--VAMPHpTW 481
Cdd:cd05939 333 gatNKKIARDVFKKGdsAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVygVEVPG-VE 411
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15218840 482 GETPCAFVVLEKGETNNEdredklvtkerDLIEYCRENLPHFMCPRKVVFLDELPKNGNGKILKPKLR 549
Cdd:cd05939 412 GRAGMAAIVDPERKVDLD-----------RFSAVLAKSLPPYARPQFIRLLPEVDKTGTFKLQKTDLQ 468
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
48-552 |
2.38e-12 |
|
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: 69.03 E-value: 2.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 48 RCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKIlfiyrsfeplare 127
Cdd:cd05910 11 RSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAEPDA------------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 128 ilqllssedsnlnlpviFIheidfpkrvsseesdyecliqrGEPTPLllarmfciqdehDPISLNYTSGTTADPKGVVIS 207
Cdd:cd05910 78 -----------------FI----------------------GIPKAD------------EPAAILFTSGSTGTPKGVVYR 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 208 HR--GAYLSTLSAIIGWEMGTcpVYLWTLPMFHCNGwtftwgtAARGGTSVC--MRHvTAP------EIYKNIEMHNVTH 277
Cdd:cd05910 107 HGtfAAQIDALRQLYGIRPGE--VDLATFPLFALFG-------PALGLTSVIpdMDP-TRParadpqKLVGAIRQYGVSI 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 278 MCCVPTVfnillkgnsLDLSHRSGPVH---------VLTGGSPPPAALVKKVQRL---GFQVMHAYGLTEATgPVLFCEW 345
Cdd:cd05910 177 VFGSPAL---------LERVARYCAQHgitlpslrrVLSAGAPVPIALAARLRKMlsdEAEILTPYGATEAL-PVSSIGS 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 346 QD---EWNRLPENQQMELKARQ----GLSILGLTEVDVRNKETQESVPRDGktMGEIVMKGSSIMKGYLKNPKATYEA-- 416
Cdd:cd05910 247 REllaTTTAATSGGAGTCVGRPipgvRVRIIEIDDEPIAEWDDTLELPRGE--IGEITVTGPTVTPTYVNRPVATALAki 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 417 --FKHG-WLNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPTwGETPcafVVLEK 493
Cdd:cd05910 325 ddNSEGfWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGVGKPG-CQLP---VLCVE 400
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15218840 494 GETNNEDREDKLvtkERDLIEYCRENlPHFMCPRKVVFLDELPKN--GNGKILKPKLRDIA 552
Cdd:cd05910 401 PLPGTITPRARL---EQELRALAKDY-PHTQRIGRFLIHPSFPVDirHNAKIFREKLAVWA 457
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
37-554 |
1.74e-11 |
|
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: 66.91 E-value: 1.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 37 KTRFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILF 116
Cdd:cd05943 96 RTEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFGVPGVLDRFGQIEPKVLF 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 117 -----IYRSFE-PLAREILQLLSSEDSNLNLPVIFI----HEIDFPKrvSSEESDYECLIQRGEPTPLLLARM-FciqdE 185
Cdd:cd05943 176 avdayTYNGKRhDVREKVAELVKGLPSLLAVVVVPYtvaaGQPDLSK--IAKALTLEDFLATGAAGELEFEPLpF----D 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 186 HdPISLNYTSGTTADPKGVVISHRGAYLSTLSA-IIGWEMGTCPVYLWtlpmFHCNGWtFTWGTAARG---GTSVCMR-- 259
Cdd:cd05943 250 H-PLYILYSSGTTGLPKCIVHGAGGTLLQHLKEhILHCDLRPGDRLFY----YTTCGW-MMWNWLVSGlavGATIVLYdg 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 260 ---HVTAPEIYKNIEMHNVTHMCCVPTVFNILLK-----GNSLDLS--HrsgpvHVLTGGSPPPAALVKKVQRlgfQVMH 329
Cdd:cd05943 324 spfYPDTNALWDLADEEGITVFGTSAKYLDALEKaglkpAETHDLSslR-----TILSTGSPLKPESFDYVYD---HIKP 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 330 AYGLTEATGPVLFCewqdewnrlpenqqmelkarqGLSILGLTEVDVRNKETQ--------ESVPRDGKT----MGEIVM 397
Cdd:cd05943 396 DVLLASISGGTDII---------------------SCFVGGNPLLPVYRGEIQcrglgmavEAFDEEGKPvwgeKGELVC 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 398 KGS--SIMKGYLKNP------KATYEAFKHGWLNsGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVL 469
Cdd:cd05943 455 TKPfpSMPVGFWNDPdgsryrAAYFAKYPGVWAH-GDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVE 533
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 470 ETAVVAMPHPTWGETPCAFVVLEKGETNNEDREDKLvtkeRDLIeycRENL-PHFMcPRKVVFLDELPKNGNGKILKPKL 548
Cdd:cd05943 534 DSLVVGQEWKDGDERVILFVKLREGVELDDELRKRI----RSTI---RSALsPRHV-PAKIIAVPDIPRTLSGKKVEVAV 605
|
....*.
gi 15218840 549 RDIAKG 554
Cdd:cd05943 606 KKIIAG 611
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
180-453 |
3.03e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 63.20 E-value: 3.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 180 FCIQDEhDP---ISLNYTSGTTADPKGVVISHRGAY-----LSTLSAIIGWEMGTcpvYLWTLPMFHCNGWTFTWGTAAR 251
Cdd:PTZ00342 296 YKIQNE-DPdfiTSIVYTSGTSGKPKGVMLSNKNLYntvvpLCKHSIFKKYNPKT---HLSYLPISHIYERVIAYLSFML 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 252 GGTSvcmrHVTAPEI---YKNIEMHNVTHMCCVPTVFN-------------------ILLKGNSLDLSHRSGP------- 302
Cdd:PTZ00342 372 GGTI----NIWSKDInyfSKDIYNSKGNILAGVPKVFNriytnimteinnlpplkrfLVKKILSLRKSNNNGGfskfleg 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 303 -VHV---------------LTGGspppAALVKKVQR-----LGFQVMHAYGLTEATGPvLFCEWQDEWNrlPENQqmelk 361
Cdd:PTZ00342 448 iTHIsskikdkvnpnleviLNGG----GKLSPKIAEelsvlLNVNYYQGYGLTETTGP-IFVQHADDNN--TESI----- 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 362 arqGLSILGLTEVDVRNKET---QESVPRdgktmGEIVMKGSSIMKGYLKNPKATYEAFKH-GWLNSGDVGVIHPDGHVE 437
Cdd:PTZ00342 516 ---GGPISPNTKYKVRTWETykaTDTLPK-----GELLIKSDSIFSGYFLEKEQTKNAFTEdGYFKTGDIVQINKNGSLT 587
|
330
....*....|....*..
gi 15218840 438 IKDRSKDII-ISGGENI 453
Cdd:PTZ00342 588 FLDRSKGLVkLSQGEYI 604
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
392-548 |
4.20e-10 |
|
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: 62.77 E-value: 4.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 392 MGEIVMKGSSIMKGYLKNPKATYEAFKHGWL-----------------------------NSGDVGVIHPDGHVEIKDRS 442
Cdd:TIGR03443 621 VGEIYVRAGGLAEGYLGLPELNAEKFVNNWFvdpshwidldkennkperefwlgprdrlyRTGDLGRYLPDGNVECCGRA 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 443 KDIIISGGENISSVEVENIIYKYPKVLE-------------TAVVAM-PHPTWGEtpcafvvLE--KGETNNEDREDKLV 506
Cdd:TIGR03443 701 DDQVKIRGFRIELGEIDTHLSQHPLVREnvtlvrrdkdeepTLVSYIvPQDKSDE-------LEefKSEVDDEESSDPVV 773
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15218840 507 ---TKERDLI----EYCRENLPHFMCPRKVVFLDELPKNGNGKILKPKL 548
Cdd:TIGR03443 774 kglIKYRKLIkdirEYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKPAL 822
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
116-548 |
1.13e-09 |
|
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: 60.56 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 116 FIYRSFEPLAREI-LQLLSSEDSNLN-LPVIFIHEIDFPKRVSSEESD---------YECLIQRGEPTplLLARMFCIQD 184
Cdd:cd17654 32 FLRKKFQTEERAIgLRCDRGTESPVAiLAILFLGAAYAPIDPASPEQRsltvmkkchVSYLLQNKELD--NAPLSFTPEH 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 185 EHDPISLNY-------TSGTTADPKGVVISHRgaylSTLSAIIG----WEMGTCPVYLWTLPMFHCNGWTFTWGTAARGG 253
Cdd:cd17654 110 RHFNIRTDEclayvihTSGTTGTPKIVAVPHK----CILPNIQHfrslFNITSEDILFLTSPLTFDPSVVEIFLSLSSGA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 254 TSVCMRHVTAPEIYK----NIEMHNVTHMCCVPTVFNILLKGNSLD--LSHRSGPVHVLTGGSPPPAALVKKVQR---LG 324
Cdd:cd17654 186 TLLIVPTSVKVLPSKladiLFKRHRITVLQATPTLFRRFGSQSIKStvLSATSSLRVLALGGEPFPSLVILSSWRgkgNR 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 325 FQVMHAYGLTEAtgpvlfCEWQdEWNRLPENQQMElkarQGLSILGLTEVDVRNKETQESvprdgktMGEIVMKGSS--- 401
Cdd:cd17654 266 TRIFNIYGITEV------SCWA-LAYKVPEEDSPV----QLGSPLLGTVIEVRDQNGSEG-------TGQVFLGGLNrvc 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 402 IMKGYLKNPKATYEAfkhgwlnSGDVgVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVvamphpTW 481
Cdd:cd17654 328 ILDDEVTVPKGTMRA-------TGDF-VTVKDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAV------TL 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15218840 482 --GETPCAFVVLEKgetnnedrEDKLVTKERDLieycrENLPHFMCPRKVVFLDELPKNGNGKILKPKL 548
Cdd:cd17654 394 sdQQRLIAFIVGES--------SSSRIHKELQL-----TLLSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
171-462 |
1.84e-09 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 60.21 E-value: 1.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 171 PTPLLLaRMFCI--QDEHDPISLNYTSGTTADPKGVVISHRGAYLSTLSAIIGWEMGTCPVYLWTLPMFHCNGWTFTWGT 248
Cdd:PRK06334 167 PFEWLM-RWFGVsdKDPEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLPPFHAYGFNSCTLF 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 249 AARGGTSVCMRH--VTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSHRSGPVHVLTGGSPPPAALVKKVQRL--G 324
Cdd:PRK06334 246 PLLSGVPVVFAYnpLYPKKIVEMIDEAKVTFLGSTPVFFDYILKTAKKQESCLPSLRFVVIGGDAFKDSLYQEALKTfpH 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 325 FQVMHAYGLTEATgPVLFCEWQDEwnrlPENQQMelkarQGLSILGLtEVDVRNKETQesVPRDGKTMGEIVMKGSSIMK 404
Cdd:PRK06334 326 IQLRQGYGTTECS-PVITINTVNS----PKHESC-----VGMPIRGM-DVLIVSEETK--VPVSSGETGLVLTRGTSLFS 392
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15218840 405 GYLKNPkatyeaFKHG--------WLNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENII 462
Cdd:PRK06334 393 GYLGED------FGQGfvelggetWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESIL 452
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
392-548 |
2.79e-09 |
|
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: 59.84 E-value: 2.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 392 MGEIVMKGSSIMKGYLKNPKATYEAFKHGWL-----------------------------NSGDVGVIHPDGHVEIKDRS 442
Cdd:cd17647 315 VGEIYVRAGGLAEGYRGLPELNKEKFVNNWFvepdhwnyldkdnnepwrqfwlgprdrlyRTGDLGRYLPNGDCECCGRA 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 443 KDIIISGGENISSVEVENIIYKYPKVLETavVAMPHPTWGETPC--AFVV--LEKGETNNEDREDKLVTKERDLI----- 513
Cdd:cd17647 395 DDQVKIRGFRIELGEIDTHISQHPLVREN--ITLVRRDKDEEPTlvSYIVprFDKPDDESFAQEDVPKEVSTDPIvkgli 472
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15218840 514 ----------EYCRENLPHFMCPRKVVFLDELPKNGNGKILKPKL 548
Cdd:cd17647 473 gyrklikdirEFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKL 517
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
185-470 |
9.28e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 58.20 E-value: 9.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 185 EHDPIS-LNYTSGTTADPKGVVISHRGAYLSTLSAI--IGWEMGTCPVYlWtLPMFHCNGWTFTWGTAARGGTSVCMR-- 259
Cdd:PRK07769 178 NEDTIAyLQYTSGSTRIPAGVQITHLNLPTNVLQVIdaLEGQEGDRGVS-W-LPFFHDMGLITVLLPALLGHYITFMSpa 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 260 -HVTAPeiYKNI-EMHNVTHMccVPTVFNIL---------LKG------NSLDLSHRSGpvhVLTGGSPPPAALVKKVQR 322
Cdd:PRK07769 256 aFVRRP--GRWIrELARKPGG--TGGTFSAApnfafehaaARGlpkdgePPLDLSNVKG---LLNGSEPVSPASMRKFNE 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 323 ----LGFQ---VMHAYGLTEATGPVLFCEWQDE-------WNRLPENQQMELKARQGLSI-------LGLTE----VDvr 377
Cdd:PRK07769 329 afapYGLPptaIKPSYGMAEATLFVSTTPMDEEptviyvdRDELNAGRFVEVPADAPNAVaqvsagkVGVSEwaviVD-- 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 378 nKETQESVPrDGKtMGEIVMKGSSIMKGYLKNPKATYEAFK----------HG--------WLNSGDVGVIHpDGHVEIK 439
Cdd:PRK07769 407 -PETASELP-DGQ-IGEIWLHGNNIGTGYWGKPEETAATFQnilksrlsesHAegapddalWVRTGDYGVYF-DGELYIT 482
|
330 340 350
....*....|....*....|....*....|.
gi 15218840 440 DRSKDIIISGGENissveveniiyKYPKVLE 470
Cdd:PRK07769 483 GRVKDLVIIDGRN-----------HYPQDLE 502
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
193-443 |
9.79e-09 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 58.06 E-value: 9.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 193 YTSGTTADPKGVVISHrGAYLSTLSAIIGW------EMGTCPVYLWTLPMFHCNGWTFTWGTAARG-----GTSVCMRHV 261
Cdd:PTZ00216 271 YTSGTTGDPKGVMHTH-GSLTAGILALEDRlndligPPEEDETYCSYLPLAHIMEFGVTNIFLARGaligfGSPRTLTDT 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 262 TA-PeiYKNIEMHNVTHMCCVPTVFNILLKG--------NSL-----DLSHRS--------------------------- 300
Cdd:PTZ00216 350 FArP--HGDLTEFRPVFLIGVPRIFDTIKKAveaklppvGSLkrrvfDHAYQSrlralkegkdtpywnekvfsapravlg 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 301 GPVH-VLTGG---SPPPAALVKKVqrLGfQVMHAYGLTE--ATGPVLFC-EWQDEWNRLPENQQmELKarqglsilgLTE 373
Cdd:PTZ00216 428 GRVRaMLSGGgplSAATQEFVNVV--FG-MVIQGWGLTEtvCCGGIQRTgDLEPNAVGQLLKGV-EMK---------LLD 494
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15218840 374 VDvRNKETQESVPRdgktmGEIVMKGSSIMKGYLKNPKATYEAF-KHGWLNSGDVGVIHPDGHVEIKDRSK 443
Cdd:PTZ00216 495 TE-EYKHTDTPEPR-----GEILLRGPFLFKGYYKQEELTREVLdEDGWFHTGDVGSIAANGTLRIIGRVK 559
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
191-543 |
1.55e-08 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 57.87 E-value: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 191 LNYTSGTTADPKGVVISHrGAYLSTLSAII---GWEMGTCPVYLWTLpmfHCNGWTFTWGTAARGGTSVCMR---HVTAP 264
Cdd:PRK05691 2338 LIYTSGSTGKPKGVVVSH-GEIAMHCQAVIerfGMRADDCELHFYSI---NFDAASERLLVPLLCGARVVLRaqgQWGAE 2413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 265 EIYKNIEMHNVTHMCCVPTVFNILlkGNSLDLSHRSGPVH-VLTGGSpppAALVKKVQRL--GFQ---VMHAYGLTEATG 338
Cdd:PRK05691 2414 EICQLIREQQVSILGFTPSYGSQL--AQWLAGQGEQLPVRmCITGGE---ALTGEHLQRIrqAFApqlFFNAYGPTETVV 2488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 339 PVLFCEWQDewnRLPENQ-QMELKARQGLSILGLTEVDVrnketqESVPRDGktMGEIVMKGSSIMKGYLKNPKATYEAF 417
Cdd:PRK05691 2489 MPLACLAPE---QLEEGAaSVPIGRVVGARVAYILDADL------ALVPQGA--TGELYVGGAGLAQGYHDRPGLTAERF 2557
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 418 -------KHGWL-NSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPTwGETPCAFV 489
Cdd:PRK05691 2558 vadpfaaDGGRLyRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLALDTPS-GKQLAGYL 2636
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 15218840 490 VlekGETNNEDREDKLVTKERdLIEYCRENLPHFMCPRKVVFLDELPKNGNGKI 543
Cdd:PRK05691 2637 V---SAVAGQDDEAQAALREA-LKAHLKQQLPDYMVPAHLILLDSLPLTANGKL 2686
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
392-543 |
1.86e-08 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 57.87 E-value: 1.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 392 MGEIVMKGSSIMKGYLKNPKATYEAF-KHG---WLNSGDVGVIHpDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPK 467
Cdd:PRK05691 397 VGEIWASGPSIAHGYWRNPEASAKTFvEHDgrtWLRTGDLGFLR-DGELFVTGRLKDMLIVRGHNLYPQDIEKTVEREVE 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 468 VLETAVVAmphptwgetpcAFVVLEKGE------TNNEDREDKLVTKErDLIEYCRENLP--HFMCPRKVVFLD--ELPK 537
Cdd:PRK05691 476 VVRKGRVA-----------AFAVNHQGEegigiaAEISRSVQKILPPQ-ALIKSIRQAVAeaCQEAPSVVLLLNpgALPK 543
|
....*.
gi 15218840 538 NGNGKI 543
Cdd:PRK05691 544 TSSGKL 549
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
393-573 |
5.35e-08 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 55.87 E-value: 5.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 393 GEIVMKGSSIMKGYLK-------------NPKATYEAfkhGWLNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVE 459
Cdd:PRK08043 554 GRLQLKGPNIMNGYLRvekpgvlevptaeNARGEMER---GWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVE 630
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 460 NIIYKYPKVLETAVVAMPHPTWGETPCAFVVlekgetnnedreDKLVTKERdLIEYCREN-LPHFMCPRKVVFLDELPKN 538
Cdd:PRK08043 631 QLALGVSPDKQHATAIKSDASKGEALVLFTT------------DSELTREK-LQQYAREHgVPELAVPRDIRYLKQLPLL 697
|
170 180 190
....*....|....*....|....*....|....*
gi 15218840 539 GNGKilkpklrdiakglvaEDEVNVRSKVQRPVEH 573
Cdd:PRK08043 698 GSGK---------------PDFVTLKSMVDEPEQH 717
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
193-543 |
1.08e-07 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 55.17 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 193 YTSGTTADPKGVVISHRGAYLSTLSAIIGWEMGTCPVYLWTLPM-FHCNGWTFTwgTAARGGTSVcmrhvtapEIYKNIE 271
Cdd:PRK05691 3876 YTSGSTGLPKGVMVEQRGMLNNQLSKVPYLALSEADVIAQTASQsFDISVWQFL--AAPLFGARV--------EIVPNAI 3945
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 272 MHN------------VTHMCCVPTVFNILLKGNSLDLShrsGPVHVL-TGGSPPPAALVKKVQRL-GFQVMHAYGLTEAT 337
Cdd:PRK05691 3946 AHDpqgllahvqaqgITVLESVPSLIQGMLAEDRQALD---GLRWMLpTGEAMPPELARQWLQRYpQIGLVNAYGPAECS 4022
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 338 GPVLFCEWQDEWNR---LP-----ENQQmelkarqgLSILGltevdvrnkETQESVPRDGktMGEIVMKGSSIMKGYLKN 409
Cdd:PRK05691 4023 DDVAFFRVDLASTRgsyLPigsptDNNR--------LYLLD---------EALELVPLGA--VGELCVAGTGVGRGYVGD 4083
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 410 PKATYEAF---KHG-----WLNSGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPKVLETAVVAMPHPTw 481
Cdd:PRK05691 4084 PLRTALAFvphPFGapgerLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAVQEGVN- 4162
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15218840 482 GETPCAFVVLEKGETNNEDREDKLvtKERdlieyCRENLPHFMCPRKVVFLDELPKNGNGKI 543
Cdd:PRK05691 4163 GKHLVGYLVPHQTVLAQGALLERI--KQR-----LRAELPDYMVPLHWLWLDRLPLNANGKL 4217
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
41-473 |
4.62e-07 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 52.82 E-value: 4.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 41 TWPQTYDRCCRLAASLISLnIGKNDVVSVVAPNTPAMYEMHFAVPMAGAVLNPI--------NTRLDAtsiaaILRHAKP 112
Cdd:PRK12476 70 TWTQLGVRLRAVGARLQQV-AGPGDRVAILAPQGIDYVAGFFAAIKAGTIAVPLfapelpghAERLDT-----ALRDAEP 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 113 KILFIYRSFEPLAREILQLLSSEDSNLnlpVIFIHEIdfPKRVSSeesDYEcliqrgePTPLllarmfciqDEHDPISLN 192
Cdd:PRK12476 144 TVVLTTTAAAEAVEGFLRNLPRLRRPR---VIAIDAI--PDSAGE---SFV-------PVEL---------DTDDVSHLQ 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 193 YTSGTTADPKGVVISHRGAYLSTLSAIIG---WEMGTCPVYlWtLPMFHCNGWTFTWGTAARGGTSVCM----------- 258
Cdd:PRK12476 200 YTSGSTRPPVGVEITHRAVGTNLVQMILSidlLDRNTHGVS-W-LPLYHDMGLSMIGFPAVYGGHSTLMsptafvrrpqr 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 259 ------------RHVTAPEIYKniemHNVTHMCCVPTvfnillKGNSLDLSHRsgpvhVLTGGSPP-------------- 312
Cdd:PRK12476 278 wikalsegsrtgRVVTAAPNFA----YEWAAQRGLPA------EGDDIDLSNV-----VLIIGSEPvsidavttfnkafa 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 313 ----PAALVKKvqrlgfqvmhAYGLTEATgpvLFCEWQDewnrlpenQQMELKA----RQGLSILGLTEVD--------- 375
Cdd:PRK12476 343 pyglPRTAFKP----------SYGIAEAT---LFVATIA--------PDAEPSVvyldREQLGAGRAVRVAadapnavah 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 376 -------------VRNKETQESVPrDGkTMGEIVMKGSSIMKGYLKNPKATYEAFK-----------HG--------WLN 423
Cdd:PRK12476 402 vscgqvarsqwavIVDPDTGAELP-DG-EVGEIWLHGDNIGRGYWGRPEETERTFGaklqsrlaegsHAdgaaddgtWLR 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 15218840 424 SGDVGViHPDGHVEIKDRSKDIIISGGENissveveniiyKYPKVLETAV 473
Cdd:PRK12476 480 TGDLGV-YLDGELYITGRIADLIVIDGRN-----------HYPQDIEATV 517
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
72-567 |
5.52e-07 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 52.51 E-value: 5.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 72 PNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFIY-------RSFePL---------AREILQLLSSE 135
Cdd:PLN03051 2 PMTVDAVIIYLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFTQdvvlrggRAL-PLyskvveaapAKAIVLPAAGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 136 DSNLNLPVIFIHEIDFPKRVSSEESDYEcliqrGEPTPLllarmfcIQDEHDPISLNYTSGTTADPKGVVISHrgayLST 215
Cdd:PLN03051 81 PVAVPLREQDLSWCDFLGVAAAQGSVGG-----NEYSPV-------YAPVESVTNILFSSGTTGEPKAIPWTH----LSP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 216 L-SAIIGW-EMGTCP--VYLWTLPMFHCNGWTFTWGTAARGGTsVCMRH--VTAPEIYKNIEMHNVTHMCCVPTVFNILL 289
Cdd:PLN03051 145 LrCASDGWaHMDIQPgdVVCWPTNLGWMMGPWLLYSAFLNGAT-LALYGgaPLGRGFGKFVQDAGVTVLGLVPSIVKAWR 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 290 KGNS-----LDLSHRSgpVHVLTG-GSPPPAALVKKVQRLGFQ-VMHAYGLTE-ATGPVLFCEWQdewnrlPENQQMELK 361
Cdd:PLN03051 224 HTGAfamegLDWSKLR--VFASTGeASAVDDVLWLSSVRGYYKpVIEYCGGTElASGYISSTLLQ------PQAPGAFST 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 362 ARQGLSILGLTEVDvrnketqESVPRDGKTMGEI----VMKGSSIMKGYLKNPKATYEAFKHGWLNS------GDVGVIH 431
Cdd:PLN03051 296 ASLGTRFVLLNDNG-------VPYPDDQPCVGEValapPMLGASDRLLNADHDKVYYKGMPMYGSKGmplrrhGDIMKRT 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 432 PDGHVEIKDRSKDIIISGGENISSVEVENIIYKYPK-VLETAVVAMPHPTWGETPCAFVVLEK--GETNNEDREDKLVTK 508
Cdd:PLN03051 369 PGGYFCVQGRADDTMNLGGIKTSSVEIERACDRAVAgIAETAAVGVAPPDGGPELLVIFLVLGeeKKGFDQARPEALQKK 448
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 509 ERDLIeycRENL-PHFMCPRkVVFLDELPKNGNGKILKPKLRDIAKglvaeDEVNVRSKV 567
Cdd:PLN03051 449 FQEAI---QTNLnPLFKVSR-VKIVPELPRNASNKLLRRVLRDQLK-----KELSGRSKL 499
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
28-213 |
1.97e-06 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 50.56 E-value: 1.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 28 PNRTSIIY-----GKTRFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTP----AMyemhfavpmagavlnpintrL 98
Cdd:PRK03584 98 DDRPAIIFrgedgPRRELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPetvvAM--------------------L 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 99 DATSIAAI----------------LRHAKPKILFI---YR----SFEPLArEILQLLSSEDSNLNLPVI-FIHEIDFPKR 154
Cdd:PRK03584 158 ATASLGAIwsscspdfgvqgvldrFGQIEPKVLIAvdgYRyggkAFDRRA-KVAELRAALPSLEHVVVVpYLGPAAAAAA 236
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 155 VSSeESDYECLIQRGEPTPLLLARM-FciqdEHdPISLNYTSGTTADPKGVVISHRGAYL 213
Cdd:PRK03584 237 LPG-ALLWEDFLAPAEAAELEFEPVpF----DH-PLWILYSSGTTGLPKCIVHGHGGILL 290
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
39-426 |
7.84e-06 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 48.72 E-value: 7.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 39 RFTWPQTYDRCCRLAASLISLNIGKNDVVSVVAPNTP-----AMYEMHFAVPMAgaVLNPINTRL--DATSIAAILRHAK 111
Cdd:PRK08180 69 RLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIehallALAAMYAGVPYA--PVSPAYSLVsqDFGKLRHVLELLT 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 112 PKILFIyRSFEPLAREILQLLSSEdsnlnLPVIFIHEIDFPKRVSSeesdYECLIQRgEPTPLLLARMFCIqDEHDPISL 191
Cdd:PRK08180 147 PGLVFA-DDGAAFARALAAVVPAD-----VEVVAVRGAVPGRAATP----FAALLAT-PPTAAVDAAHAAV-GPDTIAKF 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 192 NYTSGTTADPKGVVISHR------GAYLSTLSaiigwEMGTC-PVYL-WtLP---MF---HCNGWTFTWG---------- 247
Cdd:PRK08180 215 LFTSGSTGLPKAVINTHRmlcanqQMLAQTFP-----FLAEEpPVLVdW-LPwnhTFggnHNLGIVLYNGgtlyiddgkp 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 248 TAARGGTSV-CMRHVtAPEIYKNiemhnvthmccVPTVFNIL---LKGNSlDLSHRS-GPVHVLT-GGSPPPAALVKKVQ 321
Cdd:PRK08180 289 TPGGFDETLrNLREI-SPTVYFN-----------VPKGWEMLvpaLERDA-ALRRRFfSRLKLLFyAGAALSQDVWDRLD 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 322 RLGFQV-------MHAYGLTEATGPVLFCEWQDEwnrlpenqqmelkaRQGlsILGL----TEVDVrnketqesVPRDGK 390
Cdd:PRK08180 356 RVAEATcgerirmMTGLGMTETAPSATFTTGPLS--------------RAG--NIGLpapgCEVKL--------VPVGGK 411
|
410 420 430
....*....|....*....|....*....|....*..
gi 15218840 391 TmgEIVMKGSSIMKGYLKNPKATYEAF-KHGWLNSGD 426
Cdd:PRK08180 412 L--EVRVKGPNVTPGYWRAPELTAEAFdEEGYYRSGD 446
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
193-426 |
8.66e-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: 48.58 E-value: 8.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 193 YTSGTTADPKGVVISHR--GAYLSTLSAIIGWEMGTCPVYLWTLPmfhcngWTFTWGTAA-------RGGTSVCMRHVTA 263
Cdd:cd05921 172 FTSGSTGLPKAVINTQRmlCANQAMLEQTYPFFGEEPPVLVDWLP------WNHTFGGNHnfnlvlyNGGTLYIDDGKPM 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 264 P----EIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSHRS---GPVHVLT-GGSPPPAALVKKVQRLGFQ-------VM 328
Cdd:cd05921 246 PggfeETLRNLREISPTVYFNVPAGWEMLVAALEKDEALRRrffKRLKLMFyAGAGLSQDVWDRLQALAVAtvgeripMM 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 329 HAYGLTEATGPVLFCEWqdewnrlpenqqmeLKARQGLSILGLTEVDVRnketqeSVPRDGKTmgEIVMKGSSIMKGYLK 408
Cdd:cd05921 326 AGLGATETAPTATFTHW--------------PTERSGLIGLPAPGTELK------LVPSGGKY--EVRVKGPNVTPGYWR 383
|
250
....*....|....*....
gi 15218840 409 NPKATYEAF-KHGWLNSGD 426
Cdd:cd05921 384 QPELTAQAFdEEGFYCLGD 402
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
425-550 |
6.25e-05 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 45.84 E-value: 6.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 425 GDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENIIYK-YPKVLETAVVAMPHPTWG-ETPCAFVVLeKGETNNEDRE 502
Cdd:PLN03052 594 GDIFERTSGGYYRAHGRADDTMNLGGIKVSSVEIERVCNAaDESVLETAAIGVPPPGGGpEQLVIAAVL-KDPPGSNPDL 672
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 15218840 503 DKLVTKERDLIEycrENL-PHFMCpRKVVFLDELPKNGNGKILKPKLRD 550
Cdd:PLN03052 673 NELKKIFNSAIQ---KKLnPLFKV-SAVVIVPSFPRTASNKVMRRVLRQ 717
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
191-462 |
2.17e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 44.16 E-value: 2.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 191 LNYTSGTTADPKGVVISHR-----------------GAYLSTLSAIIGW-----EMGT-----------CPVYLwTLPM- 236
Cdd:PRK05850 165 LQYTSGSTRTPAGVMVSHRnvianfeqlmsdyfgdtGGVPPPDTTVVSWlpfyhDMGLvlgvcapilggCPAVL-TSPVa 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 237 F-------------HCNGWT----FTWGTAARGGTSVCMrhvtapeiykniemhnvthmccvptvfnillkgNSLDLSHr 299
Cdd:PRK05850 244 FlqrparwmqllasNPHAFSaapnFAFELAVRKTSDDDM---------------------------------AGLDLGG- 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 300 sgpVHVLTGGSP--PPAALVKKVQRL---GFQ---VMHAYGLTEATGPVLFCEWQD-------EWNRLPENQQMELKARQ 364
Cdd:PRK05850 290 ---VLGIISGSErvHPATLKRFADRFapfNLRetaIRPSYGLAEATVYVATREPGQppesvrfDYEKLSAGHAKRCETGG 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218840 365 GLSILGL-----TEVDVRNKETQESVPrDGkTMGEIVMKGSSIMKGYLKNPKATYEAFkHG-------------WLNSGD 426
Cdd:PRK05850 367 GTPLVSYgsprsPTVRIVDPDTCIECP-AG-TVGEIWVHGDNVAAGYWQKPEETERTF-GAtlvdpspgtpegpWLRTGD 443
|
330 340 350
....*....|....*....|....*....|....*.
gi 15218840 427 VGVIHpDGHVEIKDRSKDIIISGGENISSVEVENII 462
Cdd:PRK05850 444 LGFIS-EGELFIVGRIKDLLIVDGRNHYPDDIEATI 478
|
|
| |
