|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
71-738 |
0e+00 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 1436.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 71 VLGEPLPALDDPglLVHPSADFAAQALVSSTQQYREMYQKSIDDPAGFWSEIADEFYWKQKWSPDEVCAENLDVTKGPIK 150
Cdd:PLN02654 1 VLGESLASEEND--LVFPSKDFSAQALVSSPQQYMEMYKRSVDDPAGFWSDIASQFYWKQKWEGDEVCSENLDVRKGPIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 151 IEWFKGGKTNICYNAVDRHVEAGNGDKIAMYWEGNEPSQDGKLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMEL 230
Cdd:PLN02654 79 IEWFKGGKTNICYNCLDRNVEAGNGDKIAIYWEGNEPGFDASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMEL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 231 PIAMLACARIGAVHSVVFAGFSAEALAQRVIDCKPKVVITCNAVKRGLKIIFLKDIVDASLDESAKNGVDVGICLTYENQ 310
Cdd:PLN02654 159 PIAMLACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVITCNAVKRGPKTINLKDIVDAALDESAKNGVSVGICLTYENQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 311 SALNKVDTRWTTGRDVWWQDVVPDFPTKCDVEWVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMVYSATTFKHAFDYKPTD 390
Cdd:PLN02654 239 LAMKREDTKWQEGRDVWWQDVVPNYPTKCEVEWVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMVYTATTFKYAFDYKPTD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 391 IYWCTADCGWITGHSYVTYGPLLNGATVLVFEGAPNYPDPGRCWDIVDKYGVTIFYTAPTLIRSLMRDGTEYVARYSRKS 470
Cdd:PLN02654 319 VYWCTADCGWITGHSYVTYGPMLNGATVLVFEGAPNYPDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGDEYVTRHSRKS 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 471 LRVLGSVGEPINPTAWRWFYDVIGDSRCPISDTWWQTETGGFMITPLPGAWPQKPGSATFPFFGVQPVIVDEKGREMEGE 550
Cdd:PLN02654 399 LRVLGSVGEPINPSAWRWFFNVVGDSRCPISDTWWQTETGGFMITPLPGAWPQKPGSATFPFFGVQPVIVDEKGKEIEGE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 551 CSGYLCIKKSWPGAFRTLYGDKERYETTYFKPFAGYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSH 630
Cdd:PLN02654 479 CSGYLCVKKSWPGAFRTLYGDHERYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSH 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 631 PKCAEAAVVGIDHEVKGQGIYAFVTLVDGVPYSDDLRKSLVMTVRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKIA 710
Cdd:PLN02654 559 PQCAEAAVVGIEHEVKGQGIYAFVTLVEGVPYSEELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKIA 638
|
650 660
....*....|....*....|....*...
gi 1205963319 711 SRQLDELGDTSTLADPGVVDQLIVLSDS 738
Cdd:PLN02654 639 SRQLDELGDTSTLADPGVVDQLIALADS 666
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
102-725 |
0e+00 |
|
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: 1149.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 102 QQYREMYQKSIDDPAGFWSEIADEFYWKQKWspDEVcaenLDVTKGPIKIEWFKGGKTNICYNAVDRHVEAgNGDKIAMY 181
Cdd:cd05966 1 EQYKELYKQSIEDPEEFWGEIAKELDWFKPW--DKV----LDWSKGPPFIKWFEGGKLNISYNCLDRHLKE-RGDKVAII 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 182 WEGNEPSQDGKLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAEALAQRVI 261
Cdd:cd05966 74 WEGDEPDQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFAGFSAESLADRIN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 262 DCKPKVVITCNAVKRGLKIIFLKDIVDASLdesaKNGVDVGICLTYENqsalNKVDTRWTTGRDVWWQDVVPDFPTKCDV 341
Cdd:cd05966 154 DAQCKLVITADGGYRGGKVIPLKEIVDEAL----EKCPSVEKVLVVKR----TGGEVPMTEGRDLWWHDLMAKQSPECEP 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 342 EWVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMVYSATTFKHAFDYKPTDIYWCTADCGWITGHSYVTYGPLLNGATVLVF 421
Cdd:cd05966 226 EWMDSEDPLFILYTSGSTGKPKGVVHTTGGYLLYAATTFKYVFDYHPDDIYWCTADIGWITGHSYIVYGPLANGATTVMF 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 422 EGAPNYPDPGRCWDIVDKYGVTIFYTAPTLIRSLMRDGTEYVARYSRKSLRVLGSVGEPINPTAWRWFYDVIGDSRCPIS 501
Cdd:cd05966 306 EGTPTYPDPGRYWDIVEKHKVTIFYTAPTAIRALMKFGDEWVKKHDLSSLRVLGSVGEPINPEAWMWYYEVIGKERCPIV 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 502 DTWWQTETGGFMITPLPGAWPQKPGSATFPFFGVQPVIVDEKGREMEGECSGYLCIKKSWPGAFRTLYGDKERYETTYFK 581
Cdd:cd05966 386 DTWWQTETGGIMITPLPGATPLKPGSATRPFFGIEPAILDEEGNEVEGEVEGYLVIKRPWPGMARTIYGDHERYEDTYFS 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 582 PFAGYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAVVGIDHEVKGQGIYAFVTLVDGVP 661
Cdd:cd05966 466 KFPGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEE 545
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1205963319 662 YSDDLRKSLVMTVRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKIASRQlDELGDTSTLAD 725
Cdd:cd05966 546 PSDELRKELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMRRILRKIAAGE-EELGDTSTLAD 608
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
85-733 |
0e+00 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 1127.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 85 LVHPSADFAAQALVSsTQQYREMYQKSIDDPAGFWSEIADEFYWKQKWSpdevcaENLDvtKGPIKIEWFKGGKTNICYN 164
Cdd:PRK00174 1 VFPPPAEFAANALID-MEQYKALYQESVEDPEGFWAEQAKRLDWFKPFD------TVLD--WNAPFIKWFEDGELNVSYN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 165 AVDRHVEAGnGDKIAMYWEGNEPSQDGKLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVH 244
Cdd:PRK00174 72 CLDRHLKTR-GDKVAIIWEGDDPGDSRKITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVH 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 245 SVVFAGFSAEALAQRVIDCKPKVVITCNAVKRGLKIIFLKDIVDASLdesakngvdvgicltyENQSALNKV-------- 316
Cdd:PRK00174 151 SVVFGGFSAEALADRIIDAGAKLVITADEGVRGGKPIPLKANVDEAL----------------ANCPSVEKVivvrrtgg 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 317 DTRWTTGRDVWWQDVVPDFPTKCDVEWVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMVYSATTFKHAFDYKPTDIYWCTA 396
Cdd:PRK00174 215 DVDWVEGRDLWWHELVAGASDECEPEPMDAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAAMTMKYVFDYKDGDVYWCTA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 397 DCGWITGHSYVTYGPLLNGATVLVFEGAPNYPDPGRCWDIVDKYGVTIFYTAPTLIRSLMRDGTEYVARYSRKSLRVLGS 476
Cdd:PRK00174 295 DVGWVTGHSYIVYGPLANGATTLMFEGVPNYPDPGRFWEVIDKHKVTIFYTAPTAIRALMKEGDEHPKKYDLSSLRLLGS 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 477 VGEPINPTAWRWFYDVIGDSRCPISDTWWQTETGGFMITPLPGAWPQKPGSATFPFFGVQPVIVDEKGREMEGECSGYLC 556
Cdd:PRK00174 375 VGEPINPEAWEWYYKVVGGERCPIVDTWWQTETGGIMITPLPGATPLKPGSATRPLPGIQPAVVDEEGNPLEGGEGGNLV 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 557 IKKSWPGAFRTLYGDKERYETTYFKPFAGYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEA 636
Cdd:PRK00174 455 IKDPWPGMMRTIYGDHERFVKTYFSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEA 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 637 AVVGIDHEVKGQGIYAFVTLVDGVPYSDDLRKSLVMTVRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKIASRQLdE 716
Cdd:PRK00174 535 AVVGRPDDIKGQGIYAFVTLKGGEEPSDELRKELRNWVRKEIGPIAKPDVIQFAPGLPKTRSGKIMRRILRKIAEGEE-I 613
|
650
....*....|....*..
gi 1205963319 717 LGDTSTLADPGVVDQLI 733
Cdd:PRK00174 614 LGDTSTLADPSVVEKLI 630
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
98-733 |
0e+00 |
|
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called acetyl-CoA synthetase and acetyl-activating enzyme. It catalyzes the reaction ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA and belongs to the family of AMP-binding enzymes described by pfam00501.
Pssm-ID: 274022 [Multi-domain] Cd Length: 626 Bit Score: 1058.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 98 VSSTQQYREMYQKSIDDPAGFWSEIADE-FYWKQKWSpdEVCAENLdvtkgPIKIEWFKGGKTNICYNAVDRHVEAgNGD 176
Cdd:TIGR02188 1 IANLEQYKELYEESIEDPDKFWAKLARElLDWFKPFT--KVLDWSF-----PPFYKWFVGGELNVSYNCVDRHLEA-RPD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 177 KIAMYWEGNEPSQDGKLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAEAL 256
Cdd:TIGR02188 73 KVAIIWEGDEPGEVRKITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIHSVVFGGFSAEAL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 257 AQRVIDCKPKVVITCNAVKRGLKIIFLKDIVDASLdesAKNGVDVGICLTYenQSALNKVDTrWTTGRDVWWQDVVPDFP 336
Cdd:TIGR02188 153 ADRINDAGAKLVITADEGLRGGKVIPLKAIVDEAL---EKCPVSVEHVLVV--RRTGNPVVP-WVEGRDVWWHDLMAKAS 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 337 TKCDVEWVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMVYSATTFKHAFDYKPTDIYWCTADCGWITGHSYVTYGPLLNGA 416
Cdd:TIGR02188 227 AYCEPEPMDSEDPLFILYTSGSTGKPKGVLHTTGGYLLYAAMTMKYVFDIKDGDIFWCTADVGWITGHSYIVYGPLANGA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 417 TVLVFEGAPNYPDPGRCWDIVDKYGVTIFYTAPTLIRSLMRDGTEYVARYSRKSLRVLGSVGEPINPTAWRWFYDVIGDS 496
Cdd:TIGR02188 307 TTVMFEGVPTYPDPGRFWEIIEKHKVTIFYTAPTAIRALMRLGDEWVKKHDLSSLRLLGSVGEPINPEAWMWYYKVVGKE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 497 RCPISDTWWQTETGGFMITPLPGAWPQKPGSATFPFFGVQPVIVDEKGREMEG-ECSGYLCIKKSWPGAFRTLYGDKERY 575
Cdd:TIGR02188 387 RCPIVDTWWQTETGGIMITPLPGATPTKPGSATLPFFGIEPAVVDEEGNPVEGpGEGGYLVIKQPWPGMLRTIYGDHERF 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 576 ETTYFKPFAGYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAVVGIDHEVKGQGIYAFVT 655
Cdd:TIGR02188 467 VDTYFSPFPGYYFTGDGARRDKDGYIWITGRVDDVINVSGHRLGTAEIESALVSHPAVAEAAVVGIPDDIKGQAIYAFVT 546
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1205963319 656 LVDGVPYSDDLRKSLVMTVRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKIASRQLDELGDTSTLADPGVVDQLI 733
Cdd:TIGR02188 547 LKDGYEPDDELRKELRKHVRKEIGPIAKPDKIRFVPGLPKTRSGKIMRRLLRKIAAGEAEILGDTSTLEDPSVVEELI 624
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
152-733 |
0e+00 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 873.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 152 EWFKGGKTNICYNAVDRHVEaGNGDKIAMYWEGnEPSQDGKLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELP 231
Cdd:COG0365 1 RWFVGGRLNIAYNCLDRHAE-GRGDKVALIWEG-EDGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 232 IAMLACARIGAVHSVVFAGFSAEALAQRVIDCKPKVVITCNAVKRGLKIIFLKDIVDASLDESAKngVDVGICLTYENQS 311
Cdd:COG0365 79 IAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGGLRGGKVIDLKEKVDEALEELPS--LEHVIVVGRTGAD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 312 AlnkvdtrwTTGRDVWWQDVVPDFPTKCDVEWVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMVYSATTFKHAFDYKPTDI 391
Cdd:COG0365 157 V--------PMEGDLDWDELLAAASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYVLDLKPGDV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 392 YWCTADCGWITGHSYVTYGPLLNGATVLVFEGAPNYPDPGRCWDIVDKYGVTIFYTAPTLIRSLMRDGTEYVARYSRKSL 471
Cdd:COG0365 229 FWCTADIGWATGHSYIVYGPLLNGATVVLYEGRPDFPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEPLKKYDLSSL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 472 RVLGSVGEPINPTAWRWFYDVIGdsrCPISDTWWQTETGGFMITPLPGaWPQKPGSATFPFFGVQPVIVDEKGREMEGEC 551
Cdd:COG0365 309 RLLGSAGEPLNPEVWEWWYEAVG---VPIVDGWGQTETGGIFISNLPG-LPVKPGSMGKPVPGYDVAVVDEDGNPVPPGE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 552 SGYLCIKKSWPGAFRTLYGDKERYETTYFKPFAGYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHP 631
Cdd:COG0365 385 EGELVIKGPWPGMFRGYWNDPERYRETYFGRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHP 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 632 KCAEAAVVGIDHEVKGQGIYAFVTLVDGVPYSDDLRKSLVMTVRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKIAS 711
Cdd:COG0365 465 AVAEAAVVGVPDEIRGQVVKAFVVLKPGVEPSDELAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKIAE 544
|
570 580
....*....|....*....|..
gi 1205963319 712 RQldELGDTSTLADPGVVDQLI 733
Cdd:COG0365 545 GR--PLGDTSTLEDPEALDEIK 564
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
104-702 |
0e+00 |
|
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: 718.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 104 YREMYQKSIDDPAGFWSEIADEFYWKqkWSPDEVcaENLDVTKGPIKIEWFKGGKTNICYNAVDRHVEaGNGDKIAMYWE 183
Cdd:cd17634 1 YETKYRQSINDPDTFWGEAGKILDWI--TPYQKV--KNTSFAPGAPSIKWFEDATLNLAANALDRHLR-ENGDRTAIIYE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 184 GNEPSQDGKLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAEALAQRVIDC 263
Cdd:cd17634 76 GDDTSQSRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 264 KPKVVITCNAVKRGLKIIFLKDIVDASLDESAKNGVDVgICLTYENqsalnkVDTRWTTGRDVWWQDVVPDFPTKCDVEW 343
Cdd:cd17634 156 SSRLLITADGGVRAGRSVPLKKNVDDALNPNVTSVEHV-IVLKRTG------SDIDWQEGRDLWWRDLIAKASPEHQPEA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 344 VDAEDPLFLLYTSGSTGKPKGVLHTTGGYMVYSATTFKHAFDYKPTDIYWCTADCGWITGHSYVTYGPLLNGATVLVFEG 423
Cdd:cd17634 229 MNAEDPLFILYTSGTTGKPKGVLHTTGGYLVYAATTMKYVFDYGPGDIYWCTADVGWVTGHSYLLYGPLACGATTLLYEG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 424 APNYPDPGRCWDIVDKYGVTIFYTAPTLIRSLMRDGTEYVARYSRKSLRVLGSVGEPINPTAWRWFYDVIGDSRCPISDT 503
Cdd:cd17634 309 VPNWPTPARMWQVVDKHGVNILYTAPTAIRALMAAGDDAIEGTDRSSLRILGSVGEPINPEAYEWYWKKIGKEKCPVVDT 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 504 WWQTETGGFMITPLPGAWPQKPGSATFPFFGVQPVIVDEKGREMEGECSGYLCIKKSWPGAFRTLYGDKERYETTYFKPF 583
Cdd:cd17634 389 WWQTETGGFMITPLPGAIELKAGSATRPVFGVQPAVVDNEGHPQPGGTEGNLVITDPWPGQTRTLFGDHERFEQTYFSTF 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 584 AGYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAVVGIDHEVKGQGIYAFVTLVDGVPYS 663
Cdd:cd17634 469 KGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNHGVEPS 548
|
570 580 590
....*....|....*....|....*....|....*....
gi 1205963319 664 DDLRKSLVMTVRSQIGAFAAPDKIHWAPGLPKTRSGKIM 702
Cdd:cd17634 549 PELYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKIM 587
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
104-732 |
0e+00 |
|
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: 635.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 104 YREMYQKSIDDPAGFWSEIADEFYWKQKWspdevcAENLDVTKGPIKiEWFKGGKTNICYNAVDRHVEAGNGDKIAMYWE 183
Cdd:cd05967 1 YEEVYARSIAEPEAFWAEQARLIDWFKPP------EKILDNSNPPFT-RWFVGGRLNTCYNALDRHVEAGRGDQIALIYD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 184 GNEPSQDGKLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAEALAQRVIDC 263
Cdd:cd05967 74 SPVTGTERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAKELASRIDDA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 264 KPKVVITCNAVKRGLKIIFLKDIVDASLDESaknGVDVGICLTYenQSALNKVDTRwTTGRDVWWQDVVPDfPTKCDVEW 343
Cdd:cd05967 154 KPKLIVTASCGIEPGKVVPYKPLLDKALELS---GHKPHHVLVL--NRPQVPADLT-KPGRDLDWSELLAK-AEPVDCVP 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 344 VDAEDPLFLLYTSGSTGKPKGVLHTTGGYMVYSATTFKHAFDYKPTDIYWCTADCGWITGHSYVTYGPLLNGATVLVFEG 423
Cdd:cd05967 227 VAATDPLYILYTSGTTGKPKGVVRDNGGHAVALNWSMRNIYGIKPGDVWWAASDVGWVVGHSYIVYGPLLHGATTVLYEG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 424 AP-NYPDPGRCWDIVDKYGVTIFYTAPTLIRSLMRDGT--EYVARYSRKSLRVLGSVGEPINPTAWRWFYDVIGdsrCPI 500
Cdd:cd05967 307 KPvGTPDPGAFWRVIEKYQVNALFTAPTAIRAIRKEDPdgKYIKKYDLSSLRTLFLAGERLDPPTLEWAENTLG---VPV 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 501 SDTWWQTETGGFMITPLPG--AWPQKPGSATFPFFGVQPVIVDEKGREMEGECSGYLCIKKSW-PGAFRTLYGDKERYET 577
Cdd:cd05967 384 IDHWWQTETGWPITANPVGlePLPIKAGSPGKPVPGYQVQVLDEDGEPVGPNELGNIVIKLPLpPGCLLTLWKNDERFKK 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 578 TYFKPFAGYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAVVGIDHEVKGQGIYAFVTLV 657
Cdd:cd05967 464 LYLSKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVVLK 543
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1205963319 658 DGVPYS-DDLRKSLVMTVRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKIAsrQLDELGDTSTLADPGVVDQL 732
Cdd:cd05967 544 EGVKITaEELEKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRKIA--DGEDYTIPSTIEDPSVLDEI 617
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
101-732 |
0e+00 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 585.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 101 TQQYREMYQKSIDDPAGFWSEIADEFYWKQKwsPDEVCaenlDVTKGPIKiEWFKGGKTNICYNAVDRHVEAgNGDKIAM 180
Cdd:PRK10524 1 MMSYSEFYQRSIDDPEAFWAEQARRIDWQTP--FTQVL----DYSNPPFA-RWFVGGRTNLCHNAVDRHLAK-RPEQLAL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 181 YWEGNEPSQDGKLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAEALAQRV 260
Cdd:PRK10524 73 IAVSTETDEERTYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIHSVVFGGFASHSLAARI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 261 IDCKPKVVITCNAVKRGLKIIFLKDIVDASLDESAKNG-----VDVGIcltyenqsalnkVDTRWTTGRDVWWQD----- 330
Cdd:PRK10524 153 DDAKPVLIVSADAGSRGGKVVPYKPLLDEAIALAQHKPrhvllVDRGL------------APMARVAGRDVDYATlraqh 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 331 ---VVPdfptkcdVEWVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMVYSATTFKHAFDYKPTDIYWCTADCGWITGHSYV 407
Cdd:PRK10524 221 lgaRVP-------VEWLESNEPSYILYTSGTTGKPKGVQRDTGGYAVALATSMDTIFGGKAGETFFCASDIGWVVGHSYI 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 408 TYGPLLNGATVLVFEGAPNYPDPGRCWDIVDKYGVTIFYTAPTLIRSLMRDGTEYVARYSRKSLRVLGSVGEPIN-PTAw 486
Cdd:PRK10524 294 VYAPLLAGMATIMYEGLPTRPDAGIWWRIVEKYKVNRMFSAPTAIRVLKKQDPALLRKHDLSSLRALFLAGEPLDePTA- 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 487 RWFYDVIGdsrCPISDTWWQTETGGFMITPLPG--AWPQKPGSATFPFFGVQPVIVDEK-GREMEGECSGYLCIKKSW-P 562
Cdd:PRK10524 373 SWISEALG---VPVIDNYWQTETGWPILAIARGveDRPTRLGSPGVPMYGYNVKLLNEVtGEPCGPNEKGVLVIEGPLpP 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 563 GAFRTLYGDKERYETTYFKPFAG-YYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAVVGI 641
Cdd:PRK10524 450 GCMQTVWGDDDRFVKTYWSLFGRqVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGV 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 642 DHEVKGQGIYAFVTLVDGVPYSDD-----LRKSLVMTVRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKIASRQldE 716
Cdd:PRK10524 530 KDALKGQVAVAFVVPKDSDSLADRearlaLEKEIMALVDSQLGAVARPARVWFVSALPKTRSGKLLRRAIQAIAEGR--D 607
|
650
....*....|....*.
gi 1205963319 717 LGDTSTLADPGVVDQL 732
Cdd:PRK10524 608 PGDLTTIEDPAALQQI 623
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
151-725 |
0e+00 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 528.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 151 IEWFKGGKTNICYNAVDRHVEAGNGDKIAMYWEGnePSQDGKLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMEL 230
Cdd:PRK04319 34 FSWLETGKVNIAYEAIDRHADGGRKDKVALRYLD--ASRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPEL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 231 PIAMLACARIGAVHSVVFAGFSAEALAQRVIDCKPKVVITCNAVKR--------GLKIIFLkdiVDASLDESAKngvdvg 302
Cdd:PRK04319 112 YFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLITTPALLErkpaddlpSLKHVLL---VGEDVEEGPG------ 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 303 iclTYENQSALNKVDTRwttgrdvwwqdvvpdfptkCDVEWVDAEDPLFLLYTSGSTGKPKGVLHTTGGyMVYSATTFKH 382
Cdd:PRK04319 183 ---TLDFNALMEQASDE-------------------FDIEWTDREDGAILHYTSGSTGKPKGVLHVHNA-MLQHYQTGKY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 383 AFDYKPTDIYWCTADCGWITGHSYVTYGPLLNGATVLVFEGApnyPDPGRCWDIVDKYGVTIFYTAPTLIRSLMRDGTEY 462
Cdd:PRK04319 240 VLDLHEDDVYWCTADPGWVTGTSYGIFAPWLNGATNVIDGGR---FSPERWYRILEDYKVTVWYTAPTAIRMLMGAGDDL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 463 VARYSRKSLRVLGSVGEPINPTAWRWFYDVIGdsrCPISDTWWQTETGGFMITPLPgAWPQKPGSATFPFFGVQPVIVDE 542
Cdd:PRK04319 317 VKKYDLSSLRHILSVGEPLNPEVVRWGMKVFG---LPIHDNWWMTETGGIMIANYP-AMDIKPGSMGKPLPGIEAAIVDD 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 543 KGREMEGECSGYLCIKKSWPGAFRTLYGDKERYEtTYFKPfaGYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAE 622
Cdd:PRK04319 393 QGNELPPNRMGNLAIKKGWPSMMRGIWNNPEKYE-SYFAG--DWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFE 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 623 VESALVSHPKCAEAAVVGIDHEVKGQGIYAFVTLVDGVPYSDDLRKSLVMTVRSQIGAFAAPDKIHWAPGLPKTRSGKIM 702
Cdd:PRK04319 470 VESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVALRPGYEPSEELKEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIM 549
|
570 580
....*....|....*....|....
gi 1205963319 703 RRILRkiaSRQLD-ELGDTSTLAD 725
Cdd:PRK04319 550 RRVLK---AWELGlPEGDLSTMED 570
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
102-726 |
9.10e-170 |
|
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: 501.25 E-value: 9.10e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 102 QQYREMYQKSIDDPAGFWSEIADEF-YWKQKwSPDEVcaenLDVTKGPIKIEWFKGGKTNICYNAVDRHVeAGNGDKIAM 180
Cdd:cd05968 7 PDLEAFLERSAEDNAWFWGEFVKDVgIEWYE-PPYQT----LDLSGGKPWAAWFVGGRMNIVEQLLDKWL-ADTRTRPAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 181 YWEGnEPSQDGKLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAEALAQRV 260
Cdd:cd05968 81 RWEG-EDGTSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 261 IDCKPKVVITCNAVKRGLKIIFLKDIVDASLDEsakngvdvgiCLTYENQSALN--KVDTRWTTGRDVWWQDVVPDFPTK 338
Cdd:cd05968 160 QDAEAKALITADGFTRRGREVNLKEEADKACAQ----------CPTVEKVVVVRhlGNDFTPAKGRDLSYDEEKETAGDG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 339 cdVEWVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMVYSATTFKHAFDYKPTD-IYWCTaDCGWITGhSYVTYGPLLNGAT 417
Cdd:cd05968 230 --AERTESEDPLMIIYTSGTTGKPKGTVHVHAGFPLKAAQDMYFQFDLKPGDlLTWFT-DLGWMMG-PWLIFGGLILGAT 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 418 VLVFEGAPNYPDPGRCWDIVDKYGVTIFYTAPTLIRSLMRDGTEYVARYSRKSLRVLGSVGEPINPTAWRWFYDVIGDSR 497
Cdd:cd05968 306 MVLYDGAPDHPKADRLWRMVEDHEITHLGLSPTLIRALKPRGDAPVNAHDLSSLRVLGSTGEPWNPEPWNWLFETVGKGR 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 498 CPISDTWWQTET-----GGFMITPLpgawpqKPGSATFPFFGVQPVIVDEKGREMEGEcSGYLCIKKSWPGAFRTLYGDK 572
Cdd:cd05968 386 NPIINYSGGTEIsggilGNVLIKPI------KPSSFNGPVPGMKADVLDESGKPARPE-VGELVLLAPWPGMTRGFWRDE 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 573 ERYETTYFKPFAGYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAVVGIDHEVKGQGIYA 652
Cdd:cd05968 459 DRYLETYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVC 538
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1205963319 653 FVTLVDGVPYSDDLRKSLVMTVRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKIASRQldELGDTSTLADP 726
Cdd:cd05968 539 FVVLKPGVTPTEALAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIRAAYLGK--ELGDLSSLENP 610
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
193-711 |
3.18e-143 |
|
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: 426.92 E-value: 3.18e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 193 LTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAEALAQRVIDCKPKVVITCN 272
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 273 AVKrglkiiflkdivdasldesakngvdvgicltyenqsalnkvdtrwttgrdvwwqdvvpdfptkcdvEWVDAEDPLFL 352
Cdd:cd05969 81 ELY------------------------------------------------------------------ERTDPEDPTLL 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 353 LYTSGSTGKPKGVLHTTGGyMVYSATTFKHAFDYKPTDIYWCTADCGWITGHSYVTYGPLLNGATVLVFEGAPnypDPGR 432
Cdd:cd05969 95 HYTSGTTGTPKGVLHVHDA-MIFYYFTGKYVLDLHPDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVVYEGRF---DAES 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 433 CWDIVDKYGVTIFYTAPTLIRSLMRDGTEYVARYSRKSLRVLGSVGEPINPTAWRWFYDVIGdsrCPISDTWWQTETGGF 512
Cdd:cd05969 171 WYGIIERVKVTVWYTAPTAIRMLMKEGDELARKYDLSSLRFIHSVGEPLNPEAIRWGMEVFG---VPIHDTWWQTETGSI 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 513 MITPLPGAwPQKPGSATFPFFGVQPVIVDEKGREMEGECSGYLCIKKSWPGAFRTLYGDKERYETtYFKpfAGYYFSGDG 592
Cdd:cd05969 248 MIANYPCM-PIKPGSMGKPLPGVKAAVVDENGNELPPGTKGILALKPGWPSMFRGIWNDEERYKN-SFI--DGWYLTGDL 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 593 CSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAVVGIDHEVKGQGIYAFVTLVDGVPYSDDLRKSLVM 672
Cdd:cd05969 324 AYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSDELKEEIIN 403
|
490 500 510
....*....|....*....|....*....|....*....
gi 1205963319 673 TVRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKIAS 711
Cdd:cd05969 404 FVRQKLGAHVAPREIEFVDNLPKTRSGKIMRRVLKAKEL 442
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
193-708 |
4.77e-118 |
|
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: 361.65 E-value: 4.77e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 193 LTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAEALAQRVIDCKPKVVITcn 272
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 273 avkrglkiiflkdivdasldesakngvdvgicltyenqsalnkvdtrwttgrdvwwqdvvpdfptkcdvewvDAEDPLFL 352
Cdd:cd05972 79 ------------------------------------------------------------------------DAEDPALI 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 353 LYTSGSTGKPKGVLHTTGgYMVYSATTFKHAFDYKPTDIYWCTADCGWITGHSYVTYGPLLNGATVLVFEGAPNypDPGR 432
Cdd:cd05972 87 YFTSGTTGLPKGVLHTHS-YPLGHIPTAAYWLGLRPDDIHWNIADPGWAKGAWSSFFGPWLLGATVFVYEGPRF--DAER 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 433 CWDIVDKYGVTIFYTAPTLIRSLMRDGTEyvaRYSRKSLRVLGSVGEPINPTAWRWFYDVIGdsrCPISDTWWQTETGgF 512
Cdd:cd05972 164 ILELLERYGVTSFCGPPTAYRMLIKQDLS---SYKFSHLRLVVSAGEPLNPEVIEWWRAATG---LPIRDGYGQTETG-L 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 513 MITPLPGAwPQKPGSATFPFFGVQPVIVDEKGREMEGECSGYLCIKKSWPGAFRTLYGDKERYETTYFkpfAGYYFSGDG 592
Cdd:cd05972 237 TVGNFPDM-PVKPGSMGRPTPGYDVAIIDDDGRELPPGEEGDIAIKLPPPGLFLGYVGDPEKTEASIR---GDYYLTGDR 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 593 CSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAVVGIDHEVKGQGIYAFVTLVDGVPYSDDLRKSLVM 672
Cdd:cd05972 313 AYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPSEELAEELQG 392
|
490 500 510
....*....|....*....|....*....|....*.
gi 1205963319 673 TVRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRK 708
Cdd:cd05972 393 HVKKVLAPYKYPREIEFVEELPKTISGKIRRVELRD 428
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
172-614 |
2.88e-112 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 346.22 E-value: 2.88e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 172 AGNGDKIAMywegnEPSQDGKLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGF 251
Cdd:pfam00501 6 ARTPDKTAL-----EVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 252 SAEALAQRVIDCKPKVVITCNAVKrglkiiflkdivDASLDESAKNGVDVGICLTYENQSALNKvdtrwttgrDVWWQDV 331
Cdd:pfam00501 81 PAEELAYILEDSGAKVLITDDALK------------LEELLEALGKLEVVKLVLVLDRDPVLKE---------EPLPEEA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 332 VPDFPTKCDVEWVDAEDPLFLLYTSGSTGKPKGVLHTTgGYMVYSATTFK----HAFDYKPTDIYWCTADCGWITGHSYV 407
Cdd:pfam00501 140 KPADVPPPPPPPPDPDDLAYIIYTSGTTGKPKGVMLTH-RNLVANVLSIKrvrpRGFGLGPDDRVLSTLPLFHDFGLSLG 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 408 TYGPLLNGATVLVFEGAPNyPDPGRCWDIVDKYGVTIFYTAPTLIRSLMRDGTEYVARYSrkSLRVLGSVGEPINPTAWR 487
Cdd:pfam00501 219 LLGPLLAGATVVLPPGFPA-LDPAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLS--SLRLVLSGGAPLPPELAR 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 488 WFYDVIGdsrCPISDTWWQTETGGFMITPLPGAWPQ-KPGSATFPFFGVQPVIVDEK-GREMEGECSGYLCIKKswPGAF 565
Cdd:pfam00501 296 RFRELFG---GALVNGYGLTETTGVVTTPLPLDEDLrSLGSVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRG--PGVM 370
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1205963319 566 RTLYGDKERYETTYFKPfaGYYFSGDGCSRDKDGYHWLTGRVDDVINVS 614
Cdd:pfam00501 371 KGYLNDPELTAEAFDED--GWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
104-730 |
3.44e-94 |
|
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: 305.73 E-value: 3.44e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 104 YREMYQKSIDDPAGFWSEIADefYWKQKWSPDEvcaENLDVTKGPIKI-EWFKGGKTNICYNAVdRHveAGNGDKIAMYW 182
Cdd:cd05943 19 YAALHRWSVDDPGAFWAAVWD--FSGVRGSKPY---DVVVVSGRIMPGaRWFPGARLNYAENLL-RH--ADADDPAAIYA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 183 EGNEPSQdgKLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAEALAQRVID 262
Cdd:cd05943 91 AEDGERT--EVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFGVPGVLDRFGQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 263 CKPKVVITCNAVKRGLKIIFLKDIVDASLDE--SAKNGVDVGICLTYENQSALNkvdtrwtTGRDVWWQDVVPDFPT-KC 339
Cdd:cd05943 169 IEPKVLFAVDAYTYNGKRHDVREKVAELVKGlpSLLAVVVVPYTVAAGQPDLSK-------IAKALTLEDFLATGAAgEL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 340 DVEWVDAEDPLFLLYTSGSTGKPKGVLHTTGGymvysaTTFKH------AFDYKPTDIYWCTADCGWITGHSYVTYgpLL 413
Cdd:cd05943 242 EFEPLPFDHPLYILYSSGTTGLPKCIVHGAGG------TLLQHlkehilHCDLRPGDRLFYYTTCGWMMWNWLVSG--LA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 414 NGATVLVFEGAPNYPDPGRCWDIVDKYGVTIFYTAPTLIRSLMRDGTEYVARYSRKSLRVLGSVGEPINPTAWRWFYDVI 493
Cdd:cd05943 314 VGATIVLYDGSPFYPDTNALWDLADEEGITVFGTSAKYLDALEKAGLKPAETHDLSSLRTILSTGSPLKPESFDYVYDHI 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 494 GdsrcpiSDTWWQTETGG------FMIT-PLpgaWPQKPGSATFPFFGVQPVIVDEKGREMEGEcSGYLCIKKSWPGAFR 566
Cdd:cd05943 394 K------PDVLLASISGGtdiiscFVGGnPL---LPVYRGEIQCRGLGMAVEAFDEEGKPVWGE-KGELVCTKPFPSMPV 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 567 TLYGDKE--RYETTYFKPFAGYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAVVGIDHE 644
Cdd:cd05943 464 GFWNDPDgsRYRAAYFAKYPGVWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWK 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 645 VKGQGIYAFVTLVDGVPYSDDLRKSLVMTVRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKIASRQldELGDTSTLA 724
Cdd:cd05943 544 DGDERVILFVKLREGVELDDELRKRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGKKVEVAVKKIIAGR--PVKNAGALA 621
|
....*.
gi 1205963319 725 DPGVVD 730
Cdd:cd05943 622 NPESLD 627
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
165-716 |
6.23e-93 |
|
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: 297.11 E-value: 6.23e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 165 AVDRHVEAgNGDKIAMYWEGNEpsqdgkLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVH 244
Cdd:COG0318 4 LLRRAAAR-HPDRPALVFGGRR------LTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 245 SVVFAGFSAEALAQRVIDCKPKVVITCnavkrglkiiflkdivdasldesakngvdvgicltyenqsalnkvdtrwttgr 324
Cdd:COG0318 77 VPLNPRLTAEELAYILEDSGARALVTA----------------------------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 325 dvwwqdvvpdfptkcdvewvdaedplFLLYTSGSTGKPKGVLHTTGGyMVYSATTFKHAFDYKPTDIYWCTADCGWITGH 404
Cdd:COG0318 104 --------------------------LILYTSGTTGRPKGVMLTHRN-LLANAAAIAAALGLTPGDVVLVALPLFHVFGL 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 405 SYVTYGPLLNGATVLVFEGapnyPDPGRCWDIVDKYGVTIFYTAPTLIRSLMRDGTeyVARYSRKSLRVLGSVGEPINPT 484
Cdd:COG0318 157 TVGLLAPLLAGATLVLLPR----FDPERVLELIERERVTVLFGVPTMLARLLRHPE--FARYDLSSLRLVVSGGAPLPPE 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 485 AWRWFYDVIGdsrCPISDTWWQTETGGFMITPLPGAWPQKPGSATFPFFGVQPVIVDEKGREM----EGEcsgyLCIKKs 560
Cdd:COG0318 231 LLERFEERFG---VRIVEGYGLTETSPVVTVNPEDPGERRPGSVGRPLPGVEVRIVDEDGRELppgeVGE----IVVRG- 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 561 wPGAFRTLYGDKEryETTyfKPFA-GYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAVV 639
Cdd:COG0318 303 -PNVMKGYWNDPE--ATA--EAFRdGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVV 377
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1205963319 640 GIDHEVKGQGIYAFVTLVDGVPYS-DDLRKSLvmtvRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKIASRQLDE 716
Cdd:COG0318 378 GVPDEKWGERVVAFVVLRPGAELDaEELRAFL----RERLARYKVPRRVEFVDELPRTASGKIDRRALRERYAAGALE 451
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
348-702 |
3.61e-88 |
|
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: 280.33 E-value: 3.61e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 348 DPLFLLYTSGSTGKPKGVLHTTGGYMVYSATTFkHAFDYKPTDIYWCTADCGWItGHSYVTYGPLLNGATVLVFEGapny 427
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALA-ASGGLTEGDVFLSTLPLFHI-GGLFGLLGALLAGGTVVLLPK---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 428 PDPGRCWDIVDKYGVTIFYTAPTLIRSLMRdgTEYVARYSRKSLRVLGSVGEPINPTAWRWFYDVIGdsrCPISDTWWQT 507
Cdd:cd04433 75 FDPEAALELIEREKVTILLGVPTLLARLLK--APESAGYDLSSLRALVSGGAPLPPELLERFEEAPG---IKLVNGYGLT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 508 ETGGFMITPLPGAWPQKPGSATFPFFGVQPVIVDEKGREMEGECSGYLCIKKSWPGAFRTLygdkeRYETTYFKPFAGYY 587
Cdd:cd04433 150 ETGGTVATGPPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWN-----NPEATAAVDEDGWY 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 588 FSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAVVGIDHEVKGQGIYAFVTLVDGV-PYSDDL 666
Cdd:cd04433 225 RTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGAdLDAEEL 304
|
330 340 350
....*....|....*....|....*....|....*.
gi 1205963319 667 RKslvmTVRSQIGAFAAPDKIHWAPGLPKTRSGKIM 702
Cdd:cd04433 305 RA----HVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
193-708 |
1.01e-84 |
|
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: 275.17 E-value: 1.01e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 193 LTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAEALAQRVIDCKPKVVItCN 272
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVV-TD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 273 AVKRglkiiflkdivdasldesakngvdvgicltyenqsalNKVDtrwttgrdvwwqdvvpdfptkcdvewvdaEDPLFL 352
Cdd:cd05973 80 AANR-------------------------------------HKLD-----------------------------SDPFVM 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 353 LYTSGSTGKPKGVLHTTGGYMVYSATtFKHAFDYKPTDIYWCTADCGWITGHSYVTYGPLLNGATVLVFEGAPNYPDpgr 432
Cdd:cd05973 94 MFTSGTTGLPKGVPVPLRALAAFGAY-LRDAVDLRPEDSFWNAADPGWAYGLYYAITGPLALGHPTILLEGGFSVES--- 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 433 CWDIVDKYGVTIFYTAPTLIRSLMRDGTEyVARYSRKSLRVLGSVGEPINPTAWRWFYDVIGdsrCPISDTWWQTETGGF 512
Cdd:cd05973 170 TWRVIERLGVTNLAGSPTAYRLLMAAGAE-VPARPKGRLRRVSSAGEPLTPEVIRWFDAALG---VPIHDHYGQTELGMV 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 513 MITPLPGAWPQKPGSATFPFFGVQPVIVDEKGREMEGECSGYLCIKKS-----WPGAFrTLYGDKEryettyfkPFAGYY 587
Cdd:cd05973 246 LANHHALEHPVHAGSAGRAMPGWRVAVLDDDGDELGPGEPGRLAIDIAnsplmWFRGY-QLPDTPA--------IDGGYY 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 588 FSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAVVGIDHEVKGQGIYAFVTLVDGVPYSDDLR 667
Cdd:cd05973 317 LTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGTPALA 396
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1205963319 668 KSLVMTVRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRK 708
Cdd:cd05973 397 DELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQRFLLRR 437
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
88-731 |
6.68e-84 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 279.37 E-value: 6.68e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 88 PSADFAAQALVSSTQQ------------YREMYQKSIDDPAGFWSEIADEFywKQKWSPDEVCAENLDVTKGPikiEWFK 155
Cdd:PRK03584 8 PSAERIAASRMTAFIRwlaarrglsfddYAALWRWSVEDLEAFWQSVWDFF--GVIGSTPYTVVLAGRRMPGA---RWFP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 156 GGKTNICYNAVdRHveaGNGDKIAMYWEGnEPSQDGKLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAML 235
Cdd:PRK03584 83 GARLNYAENLL-RH---RRDDRPAIIFRG-EDGPRRELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAML 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 236 ACARIGAVHSVVFAGFSAEALAQRVIDCKPKVVITCNAVKRGLKIIFLKDIVDASLDE--SAKNGVDVgiclTYENQSAL 313
Cdd:PRK03584 158 ATASLGAIWSSCSPDFGVQGVLDRFGQIEPKVLIAVDGYRYGGKAFDRRAKVAELRAAlpSLEHVVVV----PYLGPAAA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 314 NKVDTRWTTgrdvwWQDVVPDFPTK-CDVEWVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMVysaTTFK-HAF--DYKPT 389
Cdd:PRK03584 234 AAALPGALL-----WEDFLAPAEAAeLEFEPVPFDHPLWILYSSGTTGLPKCIVHGHGGILL---EHLKeLGLhcDLGPG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 390 D-IYWCTAdCGWITGHSYVtyGPLLNGATVLVFEGAPNYPDPGRCWDIVDKYGVTIFYTAPTLIRSLMRDGTEYVARYSR 468
Cdd:PRK03584 306 DrFFWYTT-CGWMMWNWLV--SGLLVGATLVLYDGSPFYPDPNVLWDLAAEEGVTVFGTSAKYLDACEKAGLVPGETHDL 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 469 KSLRVLGSVGEPINPTAWRWFYDVIGdsrcpiSDTWWQTETGGfmiTPLPGAW-------PQKPGSATFPFFGVQPVIVD 541
Cdd:PRK03584 383 SALRTIGSTGSPLPPEGFDWVYEHVK------ADVWLASISGG---TDICSCFvggnpllPVYRGEIQCRGLGMAVEAWD 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 542 EKGREMEGEcSGYLCIKKSWPGafRTLY----GDKERYETTYFKPFAGYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHR 617
Cdd:PRK03584 454 EDGRPVVGE-VGELVCTKPFPS--MPLGfwndPDGSRYRDAYFDTFPGVWRHGDWIEITEHGGVVIYGRSDATLNRGGVR 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 618 IGTAEVESALVSHPKCAEAAVVGIDHEVKGQGIYAFVTLVDGVPYSDDLRKSLVMTVRSQIGAFAAPDKIHWAPGLPKTR 697
Cdd:PRK03584 531 IGTAEIYRQVEALPEVLDSLVIGQEWPDGDVRMPLFVVLAEGVTLDDALRARIRTTIRTNLSPRHVPDKIIAVPDIPRTL 610
|
650 660 670
....*....|....*....|....*....|....*...
gi 1205963319 698 SGKIM----RRILRKiasRQLDELGDTSTLADPGVVDQ 731
Cdd:PRK03584 611 SGKKVelpvKKLLHG---RPVKKAVNRDALANPEALDW 645
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
104-708 |
1.11e-79 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 267.76 E-value: 1.11e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 104 YREMYQKSIDDPAGFWSEIADEF-YWKQKW----SPDEvcaenldvtkgpIKIEWFKGGKTNICYNAVDRHVE-AGNGDK 177
Cdd:PTZ00237 10 YENDSNYANSNPESFWDEVAKKYvHWDKMYdkvySGDE------------IYPDWFKGGELNTCYNVLDIHVKnPLKRDQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 178 IAMYWEGNEPSQDGKLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAEALA 257
Cdd:PTZ00237 78 DALIYECPYLKKTIKLTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVKSLI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 258 QRVIDCKPKVVITCNAVKRGLKII-FLKDIVDA-SLDESAKNGVDVGICLTYENQSALNKVDTRWTTGRDVWWQDVVPDF 335
Cdd:PTZ00237 158 DRIETITPKLIITTNYGILNDEIItFTPNLKEAiELSTFKPSNVITLFRNDITSESDLKKIETIPTIPNTLSWYDEIKKI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 336 P---TKCDVEWVDAED--PLFLLYTSGSTGKPKGVLHTTGGYMV---YSATTFKHAfdyKPTDIYWCTADCGWITGHSYV 407
Cdd:PTZ00237 238 KennQSPFYEYVPVESshPLYILYTSGTTGNSKAVVRSNGPHLVglkYYWRSIIEK---DIPTVVFSHSSIGWVSFHGFL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 408 tYGPLLNGATVLVFEGA----PNYPDpgRCWDIVDKYGVTIFYTAPTLIRSLMR---DGTEYVARYSRKSLRVLGSVGEP 480
Cdd:PTZ00237 315 -YGSLSLGNTFVMFEGGiiknKHIED--DLWNTIEKHKVTHTLTLPKTIRYLIKtdpEATIIRSKYDLSNLKEIWCGGEV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 481 INPTAWRWFYDVIgdsRCPISDTWWQTETGgfmITPLPG-AWPQKPGSAT-FPFFGVQPVIVDEKGREMEGECSGYLCIK 558
Cdd:PTZ00237 392 IEESIPEYIENKL---KIKSSRGYGQTEIG---ITYLYCyGHINIPYNATgVPSIFIKPSILSEDGKELNVNEIGEVAFK 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 559 KSWPGAF-RTLYGDKERYETTYFKpFAGYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAA 637
Cdd:PTZ00237 466 LPMPPSFaTTFYKNDEKFKQLFSK-FPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECC 544
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1205963319 638 VVGIDHEVKGQGIYAFVTL--VDGVPYSD--DLRKSLVMTVRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRK 708
Cdd:PTZ00237 545 SIGIYDPDCYNVPIGLLVLkqDQSNQSIDlnKLKNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPRQIISK 619
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
192-707 |
1.08e-76 |
|
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: 253.89 E-value: 1.08e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 192 KLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAEALAQRVIDCKPKVVITc 271
Cdd:cd05971 6 KVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVT- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 272 navkrglkiiflkdivdaslDESakngvdvgicltyenqsalnkvdtrwttgrdvwwqdvvpdfptkcdvewvdaEDPLF 351
Cdd:cd05971 85 --------------------DGS----------------------------------------------------DDPAL 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 352 LLYTSGSTGKPKGVLHT----TGGYMVYSattFKHAFDYKPTDIYWCTADCGWITGHSYVTYGPLLNGATVLVFEGAPNy 427
Cdd:cd05971 93 IIYTSGTTGPPKGALHAhrvlLGHLPGVQ---FPFNLFPRDGDLYWTPADWAWIGGLLDVLLPSLYFGVPVLAHRMTKF- 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 428 pDPGRCWDIVDKYGVTIFYTAPTLIRsLMRDGTEYVARYSRKsLRVLGSVGEPINPTAWRWFYDVIGDsrcPISDTWWQT 507
Cdd:cd05971 169 -DPKAALDLMSRYGVTTAFLPPTALK-MMRQQGEQLKHAQVK-LRAIATGGESLGEELLGWAREQFGV---EVNEFYGQT 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 508 EtGGFMITPLPGAWPQKPGSATFPFFGVQPVIVDEKGREMEGECSGYLCIKKSWPGAFRTLYGDKERYEttyfKPFAGYY 587
Cdd:cd05971 243 E-CNLVIGNCSALFPIKPGSMGKPIPGHRVAIVDDNGTPLPPGEVGEIAVELPDPVAFLGYWNNPSATE----KKMAGDW 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 588 F-SGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAVVGIDHEVKGQGIYAFVTLVDGVPYSDDL 666
Cdd:cd05971 318 LlTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETPSDAL 397
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1205963319 667 RKSLVMTVRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRILR 707
Cdd:cd05971 398 AREIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRRELR 438
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
160-707 |
4.72e-70 |
|
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: 238.93 E-value: 4.72e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 160 NICYNAVDRHVEAgNGDKIAMYWeGNEPSQDGKLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACAR 239
Cdd:cd05970 17 NFAYDVVDAMAKE-YPDKLALVW-CDDAGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 240 IGAVHSVVFAGFSAEALAQRVIDCKPKVVItCNAVKRglkiifLKDIVDASLDE--SAKNGVDVGicltyenqsalNKVD 317
Cdd:cd05970 95 LGAIAIPATHQLTAKDIVYRIESADIKMIV-AIAEDN------IPEEIEKAAPEcpSKPKLVWVG-----------DPVP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 318 TRWTTGRDVWwQDVVPDFPTKCDVEWVDAEDPLFLLYTSGSTGKPKGVLHTTGgYMVYSATTFKHAFDYKPTDIYWCTAD 397
Cdd:cd05970 157 EGWIDFRKLI-KNASPDFERPTANSYPCGEDILLVYFSSGTTGMPKMVEHDFT-YPLGHIVTAKYWQNVREGGLHLTVAD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 398 CGWITGHSYVTYGPLLNGATVLVFEGapNYPDPGRCWDIVDKYGVTIFYTAPTLIRSLMRdgtEYVARYSRKSLRVLGSV 477
Cdd:cd05970 235 TGWGKAVWGKIYGQWIAGAAVFVYDY--DKFDPKALLEKLSKYGVTTFCAPPTIYRFLIR---EDLSRYDLSSLRYCTTA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 478 GEPINPTAWRWFYDVIGDSrcpISDTWWQTETGgFMITPLPGAWPqKPGSATFPFFGVQPVIVDEKGREMEGECSGYLCI 557
Cdd:cd05970 310 GEALNPEVFNTFKEKTGIK---LMEGFGQTETT-LTIATFPWMEP-KPGSMGKPAPGYEIDLIDREGRSCEAGEEGEIVI 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 558 K--KSWP-GAFRTLYGDKERYETTYFKpfaGYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCA 634
Cdd:cd05970 385 RtsKGKPvGLFGGYYKDAEKTAEVWHD---GYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVL 461
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1205963319 635 EAAVVGIDHEVKGQGIYAFVTLVDGVPYSDDLRKSLVMTVRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRILR 707
Cdd:cd05970 462 ECAVTGVPDPIRGQVVKATIVLAKGYEPSEELKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEIR 534
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
163-707 |
4.49e-63 |
|
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: 219.16 E-value: 4.49e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 163 YNA---VDRHVEAGNGDKIAMYwegnepSQDGKLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACAR 239
Cdd:cd05959 3 YNAatlVDLNLNEGRGDKTAFI------DDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 240 IGAVHSVVFAGFSAEALAQRVIDCKPKVVITCNAvkrglkiifLKDIVDASLDESAKNGVDVGICLTYENQSAlnkvdtr 319
Cdd:cd05959 77 AGIVPVPVNTLLTPDDYAYYLEDSRARVVVVSGE---------LAPVLAAALTKSEHTLVVLIVSGGAGPEAG------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 320 wttgrDVWWQDVVPDFPTKCDVEWVDAEDPLFLLYTSGSTGKPKGVLHTTGGyMVYSATTF-KHAFDYKPTDIYWCTADC 398
Cdd:cd05959 141 -----ALLLAELVAAEAEQLKPAATHADDPAFWLYSSGSTGRPKGVVHLHAD-IYWTAELYaRNVLGIREDDVCFSAAKL 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 399 GWITGHSYVTYGPLLNGATVLVFegaPNYPDPGRCWDIVDKYGVTIFYTAPTLIRSLMRDgtEYVARYSRKSLRVLGSVG 478
Cdd:cd05959 215 FFAYGLGNSLTFPLSVGATTVLM---PERPTPAAVFKRIRRYRPTVFFGVPTLYAAMLAA--PNLPSRDLSSLRLCVSAG 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 479 EPINPTAWRWFYDVIGdsrCPISDTWWQTETGGFMITPLPGAwpQKPGSATFPFFGVQPVIVDEKGREMEGECSGYLCIK 558
Cdd:cd05959 290 EALPAEVGERWKARFG---LDILDGIGSTEMLHIFLSNRPGR--VRYGTTGKPVPGYEVELRDEDGGDVADGEPGELYVR 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 559 KswpGAFRTLYGDkeRYETTYfKPFAGYYF-SGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAA 637
Cdd:cd05959 365 G---PSSATMYWN--NRDKTR-DTFQGEWTrTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAA 438
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 638 VVGIDHEVKGQGIYAFVTLVDGVPYSDDLRKSLVMTVRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRILR 707
Cdd:cd05959 439 VVGVEDEDGLTKPKAFVVLRPGYEDSEALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
190-707 |
1.03e-59 |
|
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: 208.08 E-value: 1.03e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 190 DGKLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAEALAQRVIDCKPKVVI 269
Cdd:cd05919 8 DRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 270 TcnavkrglkiiflkdivdasldesakngvdvgicltyenqsalnkvdtrwttgrdvwwqdvvpdfptkcdvewvDAEDP 349
Cdd:cd05919 88 T--------------------------------------------------------------------------SADDI 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 350 LFLLYTSGSTGKPKGVLHTTGGYMVYSATTFKHAFDYKPTDIYWCTADC--GWITGHSyvTYGPLLNGATVLVFEGAPny 427
Cdd:cd05919 94 AYLLYSSGTTGPPKGVMHAHRDPLLFADAMAREALGLTPGDRVFSSAKMffGYGLGNS--LWFPLAVGASAVLNPGWP-- 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 428 pDPGRCWDIVDKYGVTIFYTAPTLIRSLMRDGTeyVARYSRKSLRVLGSVGEPINPTAWRWFYDVIGdsrCPISDTWWQT 507
Cdd:cd05919 170 -TAERVLATLARFRPTVLYGVPTFYANLLDSCA--GSPDALRSLRLCVSAGEALPRGLGERWMEHFG---GPILDGIGAT 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 508 ETGGFMITPLPGAWpqKPGSATFPFFGVQPVIVDEKGREMEGECSGYLCIKKswPGAFRTLYGDKERYETTYFkpfAGYY 587
Cdd:cd05919 244 EVGHIFLSNRPGAW--RLGSTGRPVPGYEIRLVDEEGHTIPPGEEGDLLVRG--PSAAVGYWNNPEKSRATFN---GGWY 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 588 FSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAVVGIDHEVKGQGIYAFVTLVDGVPYSDDLR 667
Cdd:cd05919 317 RTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQESLA 396
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1205963319 668 KSLVMTVRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRILR 707
Cdd:cd05919 397 RDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
172-707 |
1.32e-59 |
|
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: 208.57 E-value: 1.32e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 172 AGNGDKIAMYWegnepsQDGKLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVhsVVFAG- 250
Cdd:cd05936 10 RRFPDKTALIF------MGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAV--VVPLNp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 251 -FSAEALAQRVIDCKPKVVITcnavkrglkiiflkdivdasldesakngvdvgicltyenqsalnkvdtrwttgrDVWWQ 329
Cdd:cd05936 82 lYTPRELEHILNDSGAKALIV------------------------------------------------------AVSFT 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 330 DVVPDFPTKCDVEWVDAEDPLFLLYTSGSTGKPKGVLHTTGGyMVYSATTFKHAF--DYKPTDIYWCTADCgwitghsYV 407
Cdd:cd05936 108 DLLAAGAPLGERVALTPEDVAVLQYTSGTTGVPKGAMLTHRN-LVANALQIKAWLedLLEGDDVVLAALPL-------FH 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 408 TYG-------PLLNGATVLVFegaPNyPDPGRCWDIVDKYGVTIFYTAPTLIRSLMrdGTEYVARYSRKSLRVLGSVGEP 480
Cdd:cd05936 180 VFGltvalllPLALGATIVLI---PR-FRPIGVLKEIRKHRVTIFPGVPTMYIALL--NAPEFKKRDFSSLRLCISGGAP 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 481 INPTAWRWFYDVIGdsrCPISDTWWQTETGgfmitPL----PGAWPQKPGSATFPFFGVQPVIVDEKGREME-GEcSGYL 555
Cdd:cd05936 254 LPVEVAERFEELTG---VPIVEGYGLTETS-----PVvavnPLDGPRKPGSIGIPLPGTEVKIVDDDGEELPpGE-VGEL 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 556 CIKKswPGAFRTLYGDKERYETTyFKpfAGYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAE 635
Cdd:cd05936 325 WVRG--PQVMKGYWNRPEETAEA-FV--DGWLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAE 399
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1205963319 636 AAVVGIDHEVKGQGIYAFVTLVDGVPYS-DDLRKSLvmtvRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRILR 707
Cdd:cd05936 400 AAVVGVPDPYSGEAVKAFVVLKEGASLTeEEIIAFC----REQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
174-707 |
1.27e-58 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 207.35 E-value: 1.27e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 174 NGDKIAMYWEGnepsqdGKLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYL---PMLMElpiAMLACARIGAV-HSV-VF 248
Cdd:PRK06187 19 HPDKEAVYFDG------RRTTYAELDERVNRLANALRALGVKKGDRVAVFDwnsHEYLE---AYFAVPKIGAVlHPInIR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 249 agFSAEALAQRVIDCKPKVVItcnavkrglkiiflkdiVDASLdesakngvdvgicltyenQSALNKVDTRWTTGRDVWW 328
Cdd:PRK06187 90 --LKPEEIAYILNDAEDRVVL-----------------VDSEF------------------VPLLAAILPQLPTVRTVIV 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 329 QDVVPDFPTKCDV----EWVDAEDPLF------------LLYTSGSTGKPKGVLHTtggymvySATTFKH------AFDY 386
Cdd:PRK06187 133 EGDGPAAPLAPEVgeyeELLAAASDTFdfpdidendaaaMLYTSGTTGHPKGVVLS-------HRNLFLHslavcaWLKL 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 387 KPTDIY-----------WctadcGWitghsyvTYGPLLNGATVLvfegapnYP---DPGRCWDIVDKYGVTIFYTAPTLI 452
Cdd:PRK06187 206 SRDDVYlvivpmfhvhaW-----GL-------PYLALMAGAKQV-------IPrrfDPENLLDLIETERVTFFFAVPTIW 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 453 RSLMRDGTEYVARYSrkSLRVLGSVGEPINPTAWRWFYDVIGdsrCPISDTWWQTETGGFM-ITPL----PGAWPqKPGS 527
Cdd:PRK06187 267 QMLLKAPRAYFVDFS--SLRLVIYGGAALPPALLREFKEKFG---IDLVQGYGMTETSPVVsVLPPedqlPGQWT-KRRS 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 528 ATFPFFGVQPVIVDEKGREME--GECSGYLCIKKSWpgafRTL--YGDKERYETTYFKpfaGYYFSGDGCSRDKDGYHWL 603
Cdd:PRK06187 341 AGRPLPGVEARIVDDDGDELPpdGGEVGEIIVRGPW----LMQgyWNRPEATAETIDG---GWLHTGDVGYIDEDGYLYI 413
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 604 TGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAVVGIDHEVKGQGIYAFVTLVDGVPYS-DDLRKSLvmtvRSQIGAFA 682
Cdd:PRK06187 414 TDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLKPGATLDaKELRAFL----RGRLAKFK 489
|
570 580
....*....|....*....|....*
gi 1205963319 683 APDKIHWAPGLPKTRSGKIMRRILR 707
Cdd:PRK06187 490 LPKRIAFVDELPRTSVGKILKRVLR 514
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
174-703 |
7.30e-58 |
|
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: 202.84 E-value: 7.30e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 174 NGDKIAMYWEGNEpsqdgkLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSA 253
Cdd:cd17631 8 HPDRTALVFGGRS------LTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 254 EALAQRVIDCKPKVVItcnavkrglkiiflkdivdasldesakngvdvgicltyenqsalnkvdtrwttgrdvwwqdvvp 333
Cdd:cd17631 82 PEVAYILADSGAKVLF---------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 334 dfptkcdvewvdaEDPLFLLYTSGSTGKPKGVLHTTG--GYMVYSATTfkhAFDYKPTDIYWCTADCGWITGHSYVTYGP 411
Cdd:cd17631 98 -------------DDLALLMYTSGTTGRPKGAMLTHRnlLWNAVNALA---ALDLGPDDVLLVVAPLFHIGGLGVFTLPT 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 412 LLNGATVLVFEGapnyPDPGRCWDIVDKYGVTIFYTAPTLIRSLMRdgTEYVARYSRKSLRVLGSVGEPInPTAWRWFYD 491
Cdd:cd17631 162 LLRGGTVVILRK----FDPETVLDLIERHRVTSFFLVPTMIQALLQ--HPRFATTDLSSLRAVIYGGAPM-PERLLRALQ 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 492 VIGdsrCPISDTWWQTETGGfMITPLPGAWPQ-KPGSATFPFFGVQPVIVDEKGREMEGECSGYLCIKKswPGAFRTLYG 570
Cdd:cd17631 235 ARG---VKFVQGYGMTETSP-GVTFLSPEDHRrKLGSAGRPVFFVEVRIVDPDGREVPPGEVGEIVVRG--PHVMAGYWN 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 571 DKERYETTYFKpfaGYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAVVGIDHEVKGQGI 650
Cdd:cd17631 309 RPEATAAAFRD---GWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAV 385
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1205963319 651 YAFVTLVDGVPYSDDlrkSLVMTVRSQIGAFAAPDKIHWAPGLPKTRSGKIMR 703
Cdd:cd17631 386 VAVVVPRPGAELDED---ELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
181-708 |
2.85e-57 |
|
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: 203.85 E-value: 2.85e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 181 YWEGNEPSQDGKLTYSELLEKVCQLSNYL-KSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAEALAQR 259
Cdd:cd05928 30 LWWVNGKGDEVKWSFRELGSLSRKAANVLsGACGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 260 VIDCKPKVVITcnavkrglkiiflKDIVDASLDESAKNGVDVGICLTYENQSalnkvdtrwttgRDVW--WQDVVPDFPT 337
Cdd:cd05928 110 LQASKAKCIVT-------------SDELAPEVDSVASECPSLKTKLLVSEKS------------RDGWlnFKELLNEAST 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 338 KCDVEWVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMVYSATTFKHAFDYKPTDIYWCTADCGWITGHSYVTYGPLLNGAT 417
Cdd:cd05928 165 EHHCVETGSQEPMAIYFTSGTTGSPKMAEHSHSSLGLGLKVNGRYWLDLTASDIMWNTSDTGWIKSAWSSLFEPWIQGAC 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 418 VLVFEgAPNYpDPGRCWDIVDKYGVTIFYTAPTLIRSLMRDGteyVARYSRKSLRVLGSVGEPINPTA---WRwfydviG 494
Cdd:cd05928 245 VFVHH-LPRF-DPLVILKTLSSYPITTFCGAPTVYRMLVQQD---LSSYKFPSLQHCVTGGEPLNPEVlekWK------A 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 495 DSRCPISDTWWQTETGgfMITPLPGAWPQKPGS--ATFPFFGVQpvIVDEKGREM----EGECSgyLCIKKSWPGAFRTL 568
Cdd:cd05928 314 QTGLDIYEGYGQTETG--LICANFKGMKIKPGSmgKASPPYDVQ--IIDDNGNVLppgtEGDIG--IRVKPIRPFGLFSG 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 569 Y-GDKERYETTYFKPFagyYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAVVGIDHEVKG 647
Cdd:cd05928 388 YvDNPEKTAATIRGDF---YLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRG 464
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1205963319 648 QGIYAFVTLVdgVPYS----DDLRKSLVMTVRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRK 708
Cdd:cd05928 465 EVVKAFVVLA--PQFLshdpEQLTKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRD 527
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
187-708 |
3.17e-52 |
|
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: 189.06 E-value: 3.17e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 187 PSQDGKLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAEALAQRVIDCKPK 266
Cdd:cd05926 9 PGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 267 VVITC---------NAVKRGLKIIFLkdivdasldesaknGVDVGICLTYENQSALNKVDTrwttgrdvwwQDVVPDFPT 337
Cdd:cd05926 89 LVLTPkgelgpasrAASKLGLAILEL--------------ALDVGVLIRAPSAESLSNLLA----------DKKNAKSEG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 338 KcdvewVDAEDPLFLLYTSGSTGKPKGVLHTTGGyMVYSATTFKHAFDYKPTDIYWCTADCGWITGHSYVTYGPLLNGAT 417
Cdd:cd05926 145 V-----PLPDDLALILHTSGTTGRPKGVPLTHRN-LAASATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGS 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 418 VLVfegaPNYPDPGRCWDIVDKYGVTiFYTA-PTLIRS-LMRDGTEYVARYSrkSLRVLGSVGEPINPTAWRWFYDVIGd 495
Cdd:cd05926 219 VVL----PPRFSASTFWPDVRDYNAT-WYTAvPTIHQIlLNRPEPNPESPPP--KLRFIRSCSASLPPAVLEALEATFG- 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 496 srCPISDTWWQTETGGFMIT-PLPGAwPQKPGSATFPFfGVQPVIVDEKGREMEGECSGYLCIKKswPGAFRTLYGDKER 574
Cdd:cd05926 291 --APVLEAYGMTEAAHQMTSnPLPPG-PRKPGSVGKPV-GVEVRILDEDGEILPPGVVGEICLRG--PNVTRGYLNNPEA 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 575 YETTYFKpfAGYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAVVGIDHEVKGQGIYAFV 654
Cdd:cd05926 365 NAEAAFK--DGWFRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAV 442
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1205963319 655 TLVDGVPYS-DDLRKSLvmtvRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRK 708
Cdd:cd05926 443 VLREGASVTeEELRAFC----RKHLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
176-708 |
4.11e-52 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 189.37 E-value: 4.11e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 176 DKIAMYWEgnepsqDGKLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAEA 255
Cdd:PRK08316 26 DKTALVFG------DRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 256 LAQRVIDCKPKVVITCNAvkrglkiifLKDIVDASLDESAKNGVDVgicltyENQSALNKVDTRWTTGRDvwWQDVVPDF 335
Cdd:PRK08316 100 LAYILDHSGARAFLVDPA---------LAPTAEAALALLPVDTLIL------SLVLGGREAPGGWLDFAD--WAEAGSVA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 336 PTkcDVEwVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMV-YSATTfkHAFDYKPTDI-------YWCTAdcgwitghSYV 407
Cdd:PRK08316 163 EP--DVE-LADDDLAQILYTSGTESLPKGAMLTHRALIAeYVSCI--VAGDMSADDIplhalplYHCAQ--------LDV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 408 TYGP-LLNGATVLVFEGapnyPDPGRCWDIVDKYGVTIFYTAPTLIRSLMRDgteyvARYSRKSLRVL--GSVGEPINPT 484
Cdd:PRK08316 230 FLGPyLYVGATNVILDA----PDPELILRTIEAERITSFFAPPTVWISLLRH-----PDFDTRDLSSLrkGYYGASIMPV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 485 AwrwfydVIGD--SRCPISDTW---WQTEtggfmITPL-----PGAWPQKPGSATFPFFGVQPVIVDEKGREM-EGE--- 550
Cdd:PRK08316 301 E------VLKElrERLPGLRFYncyGQTE-----IAPLatvlgPEEHLRRPGSAGRPVLNVETRVVDDDGNDVaPGEvge 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 551 --------CSGYlcikkswpgafrtlYGDKERYETTyfkpFAGYYF-SGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTA 621
Cdd:PRK08316 370 ivhrspqlMLGY--------------WDDPEKTAEA----FRGGWFhSGDLGVMDEEGYITVVDRKKDMIKTGGENVASR 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 622 EVESALVSHPKCAEAAVVGIDHEVKGQGIYAFVTLVDGVPYSDDlrkSLVMTVRSQIGAFAAPDKIHWAPGLPKTRSGKI 701
Cdd:PRK08316 432 EVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAGATVTED---ELIAHCRARLAGFKVPKRVIFVDELPRNPSGKI 508
|
....*..
gi 1205963319 702 MRRILRK 708
Cdd:PRK08316 509 LKRELRE 515
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
192-702 |
7.65e-52 |
|
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: 187.81 E-value: 7.65e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 192 KLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAEALAQRVIDCKPKVVITC 271
Cdd:cd05911 10 ELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 272 NA----VKRGLKIIFLKDIVdasldesakngvdvgICLTYENQSALNKVD-TRWTTGRDVWWQDVVPDfptkcdvewVDA 346
Cdd:cd05911 90 PDglekVKEAAKELGPKDKI---------------IVLDDKPDGVLSIEDlLSPTLGEEDEDLPPPLK---------DGK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 347 EDPLFLLYTSGSTGKPKGVL--HTTGGYMVYSA-TTFKHAFDYKPTDIYWCTADcgWITG-HSYVTYgpLLNGATVLVFe 422
Cdd:cd05911 146 DDTAAILYSSGTTGLPKGVClsHRNLIANLSQVqTFLYGNDGSNDVILGFLPLY--HIYGlFTTLAS--LLNGATVIIM- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 423 gapNYPDPGRCWDIVDKYGVTIFYTAPTLIRSLMRDGTeyVARYSRKSLRVLGSVGEPInptaWRWFYDVIG--DSRCPI 500
Cdd:cd05911 221 ---PKFDSELFLDLIEKYKITFLYLVPPIAAALAKSPL--LDKYDLSSLRVILSGGAPL----SKELQELLAkrFPNATI 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 501 SDTWWQTETGGfMITPLPGaWPQKPGSATFPFFGVQPVIVDEKGRE-----MEGEcsgyLCIKKswPGAFRTLYGDKERY 575
Cdd:cd05911 292 KQGYGMTETGG-ILTVNPD-GDDKPGSVGRLLPNVEAKIVDDDGKDslgpnEPGE----ICVRG--PQVMKGYYNNPEAT 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 576 ETTYFKpfAGYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAVVGIDHEVKGQGIYAFVT 655
Cdd:cd05911 364 KETFDE--DGWLHTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVV 441
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1205963319 656 LVDGvpySDDLRKSLVMTVRSQIGAFAAPDK-IHWAPGLPKTRSGKIM 702
Cdd:cd05911 442 RKPG---EKLTEKEVKDYVAKKVASYKQLRGgVVFVDEIPKSASGKIL 486
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
190-707 |
4.06e-51 |
|
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: 184.03 E-value: 4.06e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 190 DGKLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAEALAQRVIDCKPKVVI 269
Cdd:cd05934 1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 270 TcnavkrglkiiflkdivdasldesakngvdvgicltyenqsalnkvdtrwttgrdvwwqdvvpdfptkcdvewvdaeDP 349
Cdd:cd05934 81 V-----------------------------------------------------------------------------DP 83
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 350 LFLLYTSGSTGKPKGVLhTTGGYMVYSATTFKHAFDYKPTDIYWCTADCGWITGHSYVTYGPLLNGATVLVfegAPNYpD 429
Cdd:cd05934 84 ASILYTSGTTGPPKGVV-ITHANLTFAGYYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVL---LPRF-S 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 430 PGRCWDIVDKYGVTIFYTAPTLIRSLMRdgTEYVARYSRKSLRVLGsvGEPINPTAWRWFYDVIGdsrCPISDTWWQTET 509
Cdd:cd05934 159 ASRFWSDVRRYGATVTNYLGAMLSYLLA--QPPSPDDRAHRLRAAY--GAPNPPELHEEFEERFG---VRLLEGYGMTET 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 510 GGFMITPLPGawPQKPGSATFPFFGVQPVIVDEKGREMEGECSGYLCIKKSWP-GAFRTLYGDKERYEttyfKPFA-GYY 587
Cdd:cd05934 232 IVGVIGPRDE--PRRPGSIGRPAPGYEVRIVDDDGQELPAGEPGELVIRGLRGwGFFKGYYNMPEATA----EAMRnGWF 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 588 FSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAVVGIDHEVKGQGIYAFVTLVDGVPYSDDlr 667
Cdd:cd05934 306 HTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDPE-- 383
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1205963319 668 kSLVMTVRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRILR 707
Cdd:cd05934 384 -ELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
193-710 |
1.26e-50 |
|
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: 182.77 E-value: 1.26e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 193 LTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAEALAQRVidckpkvvitcn 272
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRV------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 273 avKRGLKIIflkdivdASLDESAKngvdvgicltyenqsalnkvdtrwttgrdvwwqdvvpdfptkcdvewvdAEDPLFL 352
Cdd:cd05974 69 --DRGGAVY-------AAVDENTH-------------------------------------------------ADDPMLL 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 353 LYTSGSTGKPKGVLHTTGGYMVYSATTFkHAFDYKPTDIYWCTADCGWiTGHSYVT-YGPLLNGATVLVFegapNYP--D 429
Cdd:cd05974 91 YFTSGTTSKPKLVEHTHRSYPVGHLSTM-YWIGLKPGDVHWNISSPGW-AKHAWSCfFAPWNAGATVFLF----NYArfD 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 430 PGRCWDIVDKYGVTIFYTAPTLIRSLMRdgtEYVARYSRKSLRVLGSvGEPINPtawrwfyDVIGDSR----CPISDTWW 505
Cdd:cd05974 165 AKRVLAALVRYGVTTLCAPPTVWRMLIQ---QDLASFDVKLREVVGA-GEPLNP-------EVIEQVRrawgLTIRDGYG 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 506 QTETGGfMITPLPGAwPQKPGSATFPFFGVQPVIVDEKGREM-EGECSgyLCIKKSWPGAFRTLY-GDKERyetTYFKPF 583
Cdd:cd05974 234 QTETTA-LVGNSPGQ-PVKAGSMGRPLPGYRVALLDPDGAPAtEGEVA--LDLGDTRPVGLMKGYaGDPDK---TAHAMR 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 584 AGYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAVVGIDHEVKGQGIYAFVTLVDGVPYS 663
Cdd:cd05974 307 GGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGYEPS 386
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1205963319 664 DDLRKSLVMTVRSQIGAFAAPDKIHWAPgLPKTRSGKIMRRILRKIA 710
Cdd:cd05974 387 PETALEIFRFSRERLAPYKRIRRLEFAE-LPKTISGKIRRVELRRRE 432
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
190-704 |
4.99e-48 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341253 [Multi-domain] Cd Length: 444 Bit Score: 175.79 E-value: 4.99e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 190 DGKLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAEALAQRVIDCKPKVVI 269
Cdd:cd05930 10 DQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYILEDSGAKLVL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 270 TcnavkrglkiiflkdivdasldesakngvdvgicltyenqsalnkvdtrwttgrdvwwqdvvpdfptkcdvewvDAEDP 349
Cdd:cd05930 90 T--------------------------------------------------------------------------DPDDL 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 350 LFLLYTSGSTGKPKGVLHTTGGYMVYsATTFKHAFDYKPTDIYWCTADCGWItGHSYVTYGPLLNGATVLVfegAPN--Y 427
Cdd:cd05930 96 AYVIYTSGSTGKPKGVMVEHRGLVNL-LLWMQEAYPLTPGDRVLQFTSFSFD-VSVWEIFGALLAGATLVV---LPEevR 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 428 PDPGRCWDIVDKYGVTIFYTAPTLIRSLMRDGTEYVArysrKSLRVLGSVGEPINPTAWRWFYDVIGDSR---------C 498
Cdd:cd05930 171 KDPEALADLLAEEGITVLHLTPSLLRLLLQELELAAL----PSLRLVLVGGEALPPDLVRRWRELLPGARlvnlygpteA 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 499 PISDTWWQTETGGFMITPLP-GAwpqkpgsatfPFFGVQPVIVDEKGRE----MEGEcsgyLCIkkSWPGAFRTLYGDKE 573
Cdd:cd05930 247 TVDATYYRVPPDDEEDGRVPiGR----------PIPNTRVYVLDENLRPvppgVPGE----LYI--GGAGLARGYLNRPE 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 574 RyetTYFK----PFAG---YYFSGDGCSRDKDG---YHwltGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAVVGIDH 643
Cdd:cd05930 311 L---TAERfvpnPFGPgerMYRTGDLVRWLPDGnleFL---GRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVARED 384
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1205963319 644 EVKGQGIYAFVTLVDGVPYS-DDLRKSLvmtvRSQIGAFAAPDKIHWAPGLPKTRSGKIMRR 704
Cdd:cd05930 385 GDGEKRLVAYVVPDEGGELDeEELRAHL----AERLPDYMVPSAFVVLDALPLTPNGKVDRK 442
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
193-708 |
5.13e-47 |
|
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: 172.95 E-value: 5.13e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 193 LTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAEALAQRVIDCKPKVVITCN 272
Cdd:cd05903 2 LTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 273 AVKRglkiiflKDIVDasldesakngvdvgicltyenqsalnkvdtrwttgrdvwwqdvVPDfptkcdvewvdaeDPLFL 352
Cdd:cd05903 82 RFRQ-------FDPAA-------------------------------------------MPD-------------AVALL 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 353 LYTSGSTGKPKGVLHTTGGyMVYSATTFKHAFDYKPTDIYWCTADCGWITGHSYVTYGPLLNGATVLVFEGApnypDPGR 432
Cdd:cd05903 99 LFTSGTTGEPKGVMHSHNT-LSASIRQYAERLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIW----DPDK 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 433 CWDIVDKYGVTIFYTAPTLIRSLMRDGTEYVARYSRksLRVLGSVGEPINPTAWRWFYDVIGDSRCPIsdtWWQTETGGF 512
Cdd:cd05903 174 ALALMREHGVTFMMGATPFLTDLLNAVEEAGEPLSR--LRTFVCGGATVPRSLARRAAELLGAKVCSA---YGSTECPGA 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 513 MITPLPGAWPQKPGSATFPFFGVQPVIVDEKGREMEGECSGYLCIKKswPGAFrtlYGDKERYETTYFKPFAGYYFSGDG 592
Cdd:cd05903 249 VTSITPAPEDRRLYTDGRPLPGVEIKVVDDTGATLAPGVEGELLSRG--PSVF---LGYLDRPDLTADAAPEGWFRTGDL 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 593 CSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAVVGIDHEVKGQGIYAFVTLVDG-VPYSDDLRKSLv 671
Cdd:cd05903 324 ARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGaLLTFDELVAYL- 402
|
490 500 510
....*....|....*....|....*....|....*..
gi 1205963319 672 mtVRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRK 708
Cdd:cd05903 403 --DRQGVAKQYWPERLVHVDDLPRTPSGKVQKFRLRE 437
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
163-708 |
8.45e-46 |
|
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ligase, 4-hydroxybenzoate-CoA ligase, 2-aminobenzoate-CoA ligase, etc. Members are related to fatty acid and acetate CoA ligases.
Pssm-ID: 274059 [Multi-domain] Cd Length: 505 Bit Score: 171.18 E-value: 8.45e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 163 YNA----VDRHVEAGNGDKIAMYwegnepSQDGKLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACA 238
Cdd:TIGR02262 3 YNAaedlLDRNVVEGRGGKTAFI------DDISSLSYGELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLGAI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 239 RIGAVHSVVFAGFSAEALAQRVIDCKPKVVITCNAVkrglkIIFLKDIVDASLDESAKngVDVGICLTYENQSAlNKVDT 318
Cdd:TIGR02262 77 RAGIVPVALNTLLTADDYAYMLEDSRARVVFVSGAL-----LPVIKAALGKSPHLEHR--VVVGRPEAGEVQLA-ELLAT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 319 RwttgrdvwwQDVVPDFPTKCDvewvdaeDPLFLLYTSGSTGKPKGVLHTTGGYMVYSATTFKHAFDYKPTDIYWCTADC 398
Cdd:TIGR02262 149 E---------SEQFKPAATQAD-------DPAFWLYSSGSTGMPKGVVHTHSNPYWTAELYARNTLGIREDDVCFSAAKL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 399 GWITGHSYVTYGPLLNGATVLVFegaPNYPDPGRCWDIVDKYGVTIFYTAPTLIRSLMRDgtEYVARYSRKSLRVLGSVG 478
Cdd:TIGR02262 213 FFAYGLGNALTFPMSVGATTVLM---GERPTPDAVFDRLRRHQPTIFYGVPTLYAAMLAD--PNLPSEDQVRLRLCTSAG 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 479 EPINPTAWRWFYDVIGdsrCPISDTWWQTETGGFMITPLPGAwpQKPGSATFPFFGVQPVIVDEKGREMEGECSGYLCIk 558
Cdd:TIGR02262 288 EALPAEVGQRWQARFG---VDIVDGIGSTEMLHIFLSNLPGD--VRYGTSGKPVPGYRLRLVGDGGQDVADGEPGELLI- 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 559 kSWPGAFRTLYGDKERYETTYFKPFAGyyfSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAV 638
Cdd:TIGR02262 362 -SGPSSATMYWNNRAKSRDTFQGEWTR---SGDKYVRNDDGSYTYAGRTDDMLKVSGIYVSPFEIESALIQHPAVLEAAV 437
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1205963319 639 VGI---DHEVKGQgiyAFVTLVDGvpySDDLRKSLVMTVRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRK 708
Cdd:TIGR02262 438 VGVadeDGLIKPK---AFVVLRPG---QTALETELKEHVKDRLAPYKYPRWIVFVDDLPKTATGKIQRFKLRE 504
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
339-707 |
7.47e-45 |
|
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: 166.88 E-value: 7.47e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 339 CDVEWVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMVYSATTFKHAFDYKPTDIYWCTADCGWITGHSYVTYGPLLNGATV 418
Cdd:cd05958 89 CAHALTASDDICILAFTSGTTGAPKATMHFHRDPLASADRYAVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASG 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 419 LVFEGApnypDPGRCWDIVDKYGVTIFYTAPTLIRSLMRDGTEyvARYSRKSLRVLGSVGEPINPTAWRWFYDVIGdsrC 498
Cdd:cd05958 169 VLLEEA----TPDLLLSAIARYKPTVLFTAPTAYRAMLAHPDA--AGPDLSSLRKCVSAGEALPAALHRAWKEATG---I 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 499 PISDTWWQTETGGFMITPLPGAwpQKPGSATFPFFGVQPVIVDEKGREMEGECSGYLCIKKswPGAFRtlyGDKERYETT 578
Cdd:cd05958 240 PIIDGIGSTEMFHIFISARPGD--ARPGATGKPVPGYEAKVVDDEGNPVPDGTIGRLAVRG--PTGCR---YLADKRQRT 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 579 YFKpfAGYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAVVGIDHEVKGQGIYAFVTLVD 658
Cdd:cd05958 313 YVQ--GGWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRP 390
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1205963319 659 GVPYSDDLRKSLVMTVRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRILR 707
Cdd:cd05958 391 GVIPGPVLARELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFALR 439
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
193-730 |
2.73e-41 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 160.12 E-value: 2.73e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 193 LTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLAcariGAVHSVVFA---GFSAEALAQRVIDCKPKVVI 269
Cdd:PRK07529 59 WTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWG----GEAAGIANPinpLLEPEQIAELLRAAGAKVLV 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 270 TcnavkrglkiifLKDIVDASLDESAKNGVDVGICLTYENQSALNKVDTRWTTGRDVWWQ----DVVPDFPTKCDVEWVD 345
Cdd:PRK07529 135 T------------LGPFPGTDIWQKVAEVLAALPELRTVVEVDLARYLPGPKRLAVPLIRrkahARILDFDAELARQPGD 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 346 ---------AEDPLFLLYTSGSTGKPKGVLHTTGGyMVYSATTFKHAFDYKPTDiywcTADCGWITGH---SYVT-YGPL 412
Cdd:PRK07529 203 rlfsgrpigPDDVAAYFHTGGTTGMPKLAQHTHGN-EVANAWLGALLLGLGPGD----TVFCGLPLFHvnaLLVTgLAPL 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 413 LNGATVlVFEGAPNYPDPG---RCWDIVDKYGVTIFYTAPTLIRSLMRdgtEYVARYSRKSLRVLGSVGEPINPTAWRWF 489
Cdd:PRK07529 278 ARGAHV-VLATPQGYRGPGviaNFWKIVERYRINFLSGVPTVYAALLQ---VPVDGHDISSLRYALCGAAPLPVEVFRRF 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 490 YDVIGdsrCPISDTWWQTE-TGGFMITPLPGawPQKPGSA--TFPFFGVQPVIVDEKGREMEgECS----GYLCIkkSWP 562
Cdd:PRK07529 354 EAATG---VRIVEGYGLTEaTCVSSVNPPDG--ERRIGSVglRLPYQRVRVVILDDAGRYLR-DCAvdevGVLCI--AGP 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 563 GAFRT-LYGDKER---YETTYFKpfagyyfSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAV 638
Cdd:PRK07529 426 NVFSGyLEAAHNKglwLEDGWLN-------TGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAA 498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 639 VGIDHEVKGQGIYAFVTLVDGVPYSDDlrkSLVMTVRSQIGAFAA-PDKIHWAPGLPKTRSGKIMRRILRKIASRQ---- 713
Cdd:PRK07529 499 VGRPDAHAGELPVAYVQLKPGASATEA---ELLAFARDHIAERAAvPKHVRILDALPKTAVGKIFKPALRRDAIRRvlra 575
|
570
....*....|....*...
gi 1205963319 714 -LDELGdtstlADPGVVD 730
Cdd:PRK07529 576 aLRDAG-----VEAEVVD 588
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
194-638 |
3.09e-41 |
|
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: 155.89 E-value: 3.09e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 194 TYSELLEKVCQLSNYLKS-VGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAEALAQRVIDCKPKVVITcn 272
Cdd:TIGR01733 1 TYRELDERANRLARHLRAaGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 273 avkrglkiiflkdivDASLDESAKNGVDVGICLTyenqsalnkvdtrwttgrDVWWQDVVPDFPTKCDVEWVDAEDPLFL 352
Cdd:TIGR01733 79 ---------------DSALASRLAGLVLPVILLD------------------PLELAALDDAPAPPPPDAPSGPDDLAYV 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 353 LYTSGSTGKPKGVLHTTGGyMVYSATTFKHAFDYKPTDIywctadcgWITGHSYV-------TYGPLLNGATVLVFEGAP 425
Cdd:TIGR01733 126 IYTSGSTGRPKGVVVTHRS-LVNLLAWLARRYGLDPDDR--------VLQFASLSfdasveeIFGALLAGATLVVPPEDE 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 426 NYPDPGRCWDIVDKYGVTIFYTAPTLIRSLMrdgteYVARYSRKSLRVLGSVGEPINPTAWRWFYDVIGDSRcpisdtWW 505
Cdd:TIGR01733 197 ERDDAALLAALIAEHPVTVLNLTPSLLALLA-----AALPPALASLRLVILGGEALTPALVDRWRARGPGAR------LI 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 506 Q----TE-TGGFMITPLPGAWPQKPGSATF--PFFGVQPVIVDEKGREMEGECSGYLCIkkSWPGAFRTLYGDKERYETT 578
Cdd:TIGR01733 266 NlygpTEtTVWSTATLVDPDDAPRESPVPIgrPLANTRLYVLDDDLRPVPVGVVGELYI--GGPGVARGYLNRPELTAER 343
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1205963319 579 YFK-PFAG-----YYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAV 638
Cdd:TIGR01733 344 FVPdPFAGgdgarLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
189-708 |
1.41e-40 |
|
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.
Pssm-ID: 211788 [Multi-domain] Cd Length: 517 Bit Score: 156.48 E-value: 1.41e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 189 QDGKLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAEALAQRVIDCKPKVV 268
Cdd:TIGR03098 22 HDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQVAHILADCNVRLL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 269 ITCNAvkrglKIIFLKDiVDAS---------LDESAKNGVDvgicLTYENQSALNKVDTRWTTGRDVwwqDVVPDfptkc 339
Cdd:TIGR03098 102 VTSSE-----RLDLLHP-ALPGchdlrtliiVGDPAHASEG----HPGEEPASWPKLLALGDADPPH---PVIDS----- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 340 dvewvdaeDPLFLLYTSGSTGKPKGVL--HTTggyMVYSATTFKHAFDYKPTDIYWCTADCGWITGHSYVTYGpLLNGAT 417
Cdd:TIGR03098 164 --------DMAAILYTSGSTGRPKGVVlsHRN---LVAGAQSVATYLENRPDDRLLAVLPLSFDYGFNQLTTA-FYVGAT 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 418 VLVFegapNYPDPGRCWDIVDKYGVTIFYTAPTLIRSLMR-DGTEYVARysrkSLRVLGSVGEPINPTAWRWFYDVIGDS 496
Cdd:TIGR03098 232 VVLH----DYLLPRDVLKALEKHGITGLAAVPPLWAQLAQlDWPESAAP----SLRYLTNSGGAMPRATLSRLRSFLPNA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 497 RcpISDTWWQTEtgGFMITPL-PGAWPQKPGS--ATFPFFGVQpvIVDEKGREM----EGEC--SGYLCIKKSWPGAFRT 567
Cdd:TIGR03098 304 R--LFLMYGLTE--AFRSTYLpPEEVDRRPDSigKAIPNAEVL--VLREDGSECapgeEGELvhRGALVAMGYWNDPEKT 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 568 lygdKERyettyFKPFAGYY----------FSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAA 637
Cdd:TIGR03098 378 ----AER-----FRPLPPFPgelhlpelavWSGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAV 448
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1205963319 638 VVGIDHEVKGQGIYAFVTLVDGVPYSddlRKSLVMTVRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRK 708
Cdd:TIGR03098 449 AFGVPDPTLGQAIVLVVTPPGGEELD---RAALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKALAK 516
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
165-708 |
1.47e-39 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 153.14 E-value: 1.47e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 165 AVDRHveagnGDKIAmYWEGnepsqDGKLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVH 244
Cdd:PRK07656 14 AARRF-----GDKEA-YVFG-----DQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 245 SVVFAGFSAEALAQRVIDCKPKVVITCNAvkrglkiiFLKdivdasLDESAKNGVD----VGICLTYENQSALNKVDTrw 320
Cdd:PRK07656 83 VPLNTRYTADEAAYILARGDAKALFVLGL--------FLG------VDYSATTRLPalehVVICETEEDDPHTEKMKT-- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 321 ttgrdvwWQDVVPDFPTKCDVEWVDAEDPLFLLYTSGSTGKPKGVLHT-----------------TGGYMVYSATTFKHA 383
Cdd:PRK07656 147 -------FTDFLAAGDPAERAPEVDPDDVADILFTSGTTGRPKGAMLThrqllsnaadwaeylglTEGDRYLAANPFFHV 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 384 FDYKptdiywctadCGWITghsyvtygPLLNGATVL---VFegapnypDPGRCWDIVDKYGVTIFYTAPTLIRSLMRdgT 460
Cdd:PRK07656 220 FGYK----------AGVNA--------PLMRGATILplpVF-------DPDEVFRLIETERITVLPGPPTMYNSLLQ--H 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 461 EYVARYSRKSLRVLGSVGEPINPTAWRWFYDVIGDSRcpISDTWWQTETGGFM-ITPLPGAWPQKPGSATFPFFGVQPVI 539
Cdd:PRK07656 273 PDRSAEDLSSLRLAVTGAASMPVALLERFESELGVDI--VLTGYGLSEASGVTtFNRLDDDRKTVAGTIGTAIAGVENKI 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 540 VDEKGREMEGECSGYLCIKKswPGAFRTLYGDKEryETTYFKPFAGYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIG 619
Cdd:PRK07656 351 VNELGEEVPVGEVGELLVRG--PNVMKGYYDDPE--ATAAAIDADGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVY 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 620 TAEVESALVSHPKCAEAAVVGIDHEVKGQGIYAFVTLVDGVPYSDDlrkSLVMTVRSQIGAFAAPDKIHWAPGLPKTRSG 699
Cdd:PRK07656 427 PAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLKPGAELTEE---ELIAYCREHLAKYKVPRSIEFLDELPKNATG 503
|
....*....
gi 1205963319 700 KIMRRILRK 708
Cdd:PRK07656 504 KVLKRALRE 512
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
168-707 |
5.79e-39 |
|
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: 150.96 E-value: 5.79e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 168 RHVEAgNGDKIAMYWEGnepsqdGKLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVV 247
Cdd:cd17651 3 RQAAR-TPDAPALVAEG------RRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 248 FAGFSAEALAQRVIDCKPKVVITCNAVKRGLkiiflkdivdasldesaknGVDVGICLTYENQSALNKVDTRwttgrdvw 327
Cdd:cd17651 76 DPAYPAERLAFMLADAGPVLVLTHPALAGEL-------------------AVELVAVTLLDQPGAAAGADAE-------- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 328 wqdvvPDFPTkcdvewvDAEDPLFLLYTSGSTGKPKGVL------------HTTGGYMVYSATTFKHA---FDYKPTDIY 392
Cdd:cd17651 129 -----PDPAL-------DADDLAYVIYTSGSTGRPKGVVmphrslanlvawQARASSLGPGARTLQFAglgFDVSVQEIF 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 393 wctadcgwitghsyvtyGPLLNGATvLVFEGAPNYPDPGRCWDIVDKYGVTIFYTAPTLIRSLMRDGTEYVARYSrkSLR 472
Cdd:cd17651 197 -----------------STLCAGAT-LVLPPEEVRTDPPALAAWLDEQRISRVFLPTVALRALAEHGRPLGVRLA--ALR 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 473 VLGSVGEPIN-------PTAWRWFYDVIgdsrcpisDTWWQTET---GGFMITPLPGAWPQKPGSATfPFFGVQPVIVDE 542
Cdd:cd17651 257 YLLTGGEQLVltedlreFCAGLPGLRLH--------NHYGPTEThvvTALSLPGDPAAWPAPPPIGR-PIDNTRVYVLDA 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 543 KGREMEGECSGYLCIkkSWPGAFRTLYGD----KERYETTYFKPFAGYYFSGDGCSRDKDG-YHWLtGRVDDVINVSGHR 617
Cdd:cd17651 328 ALRPVPPGVPGELYI--GGAGLARGYLNRpeltAERFVPDPFVPGARMYRTGDLARWLPDGeLEFL-GRADDQVKIRGFR 404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 618 IGTAEVESALVSHPKCAEAAVVGIDHEVKGQGIYAFVTLVDGVPYS-DDLRKSLvmtvRSQIGAFAAPDKIHWAPGLPKT 696
Cdd:cd17651 405 IELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEAPVDaAELRAAL----ATHLPEYMVPSAFVLLDALPLT 480
|
570
....*....|.
gi 1205963319 697 RSGKIMRRILR 707
Cdd:cd17651 481 PNGKLDRRALP 491
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
193-706 |
6.44e-38 |
|
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: 148.15 E-value: 6.44e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 193 LTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAEALAQRVIDCKPKVVITCN 272
Cdd:cd05904 33 LTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFTTA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 273 AVkrglkiiflkdivdasLDESAKNGVDVGICLTYENQSALNKVDTRWTTgrdvwwqdvvpdfPTKCDVEWVDAEDPLFL 352
Cdd:cd05904 113 EL----------------AEKLASLALPVVLLDSAEFDSLSFSDLLFEAD-------------EAEPPVVVIKQDDVAAL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 353 LYTSGSTGKPKGVLHTTGGY--MVySATTFKHAFDYKPTDIYWCTADCGWITGHSYVTYGPLLNGATVLVFEGApnypDP 430
Cdd:cd05904 164 LYSSGTTGRSKGVMLTHRNLiaMV-AQFVAGEGSNSDSEDVFLCVLPMFHIYGLSSFALGLLRLGATVVVMPRF----DL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 431 GRCWDIVDKYGVTIFYTAPTLIRSLMRDGTeyVARYSRKSLRVLGSVGEPINPTAWRWFYDVIGDsrCPISDTWWQTE-T 509
Cdd:cd05904 239 EELLAAIERYKVTHLPVVPPIVLALVKSPI--VDKYDLSSLRQIMSGAAPLGKELIEAFRAKFPN--VDLGQGYGMTEsT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 510 GGFMITPLPGAWPQKPGSATFPFFGVQPVIVD-EKGREMEGECSGYLCIKKswPGAFRTLYGDKERYETTYFKpfAGYYF 588
Cdd:cd05904 315 GVVAMCFAPEKDRAKYGSVGRLVPNVEAKIVDpETGESLPPNQTGELWIRG--PSIMKGYLNNPEATAATIDK--EGWLH 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 589 SGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAVVGIDHEVKGQGIYAFVTLVDGvpysDDLRK 668
Cdd:cd05904 391 TGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPG----SSLTE 466
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1205963319 669 SLVMT-VRSQIgafaAPDK----IHWAPGLPKTRSGKIMRRIL 706
Cdd:cd05904 467 DEIMDfVAKQV----APYKkvrkVAFVDAIPKSPSGKILRKEL 505
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
187-707 |
7.58e-38 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 148.30 E-value: 7.58e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 187 PSQDGKLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAEALAQRVIDCKPK 266
Cdd:PRK13391 19 ASTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAYIVDDSGAR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 267 VVITCNAvKRglkiiflkDIVDASLDESAKngvdVGICLTYENQSALNKVDTrwttgrdvwWQDVVPDFP-TKCDVEWVD 345
Cdd:PRK13391 99 ALITSAA-KL--------DVARALLKQCPG----VRHRLVLDGDGELEGFVG---------YAEAVAGLPaTPIADESLG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 346 AEdplfLLYTSGSTGKPKGVL---------HTTGGYMVysattFKHAFDYKPTDIYWCTADCGWITGHSYVTYGPLLnGA 416
Cdd:PRK13391 157 TD----MLYSSGTTGRPKGIKrplpeqppdTPLPLTAF-----LQRLWGFRSDMVYLSPAPLYHSAPQRAVMLVIRL-GG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 417 TVLVFEgapnYPDPGRCWDIVDKYGVTIFYTAPTLIRSLMRDGTEYVARYSRKSLRVLGSVGEPINPTAWRWFYDVIGds 496
Cdd:PRK13391 227 TVIVME----HFDAEQYLALIEEYGVTHTQLVPTMFSRMLKLPEEVRDKYDLSSLEVAIHAAAPCPPQVKEQMIDWWG-- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 497 rcPISDTWW-QTETGGFMITPlPGAWPQKPGSATFPFFGVqPVIVDEKGREMEGECSGYLCIKKSWPgaFRTLYGDKERY 575
Cdd:PRK13391 301 --PIIHEYYaATEGLGFTACD-SEEWLAHPGTVGRAMFGD-LHILDDDGAELPPGEPGTIWFEGGRP--FEYLNDPAKTA 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 576 ETTYfkPFAGYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAVVGIDHEVKGQGIYAFVT 655
Cdd:PRK13391 375 EARH--PDGTWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQ 452
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1205963319 656 LVDGVPYSDDLRKSLVMTVRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRILR 707
Cdd:PRK13391 453 PVDGVDPGPALAAELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLR 504
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
190-706 |
1.04e-37 |
|
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: 147.05 E-value: 1.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 190 DGKLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAEALAQRVIDCKPKVVI 269
Cdd:cd12116 10 DRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALVL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 270 TcnavkrglkiiflkdivDASLDESAKNGVDVgICLTyeNQSALNKVDTRWTTgrdvwwqdVVPDfptkcdvewvdaeDP 349
Cdd:cd12116 90 T-----------------DDALPDRLPAGLPV-LLLA--LAAAAAAPAAPRTP--------VSPD-------------DL 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 350 LFLLYTSGSTGKPKGV-----------------LHTTGGYMVYSATTFkhAFDYKPTDIYWctadcgwitghsyvtygPL 412
Cdd:cd12116 129 AYVIYTSGSTGRPKGVvvshrnlvnflhsmrerLGLGPGDRLLAVTTY--AFDISLLELLL-----------------PL 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 413 LNGATVLVFEGAPNYpDPGRCWDIVDKYGVTIFYTAPTLIRSLMRDGTEyvarySRKSLRVL-GsvGEPINPTAWRWF-- 489
Cdd:cd12116 190 LAGARVVIAPRETQR-DPEALARLIEAHSITVMQATPATWRMLLDAGWQ-----GRAGLTALcG--GEALPPDLAARLls 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 490 -----YDVIGdsrcPISDTWWQTetggfmITPLPGAWPQKPgsATFPFFGVQPVIVDEKGREM-EGECsGYLCIkkSWPG 563
Cdd:cd12116 262 rvgslWNLYG----PTETTIWST------AARVTAAAGPIP--IGRPLANTQVYVLDAALRPVpPGVP-GELYI--GGDG 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 564 AFRTLYGDKERYETTYFK-PFAG----YYFSGDGCSRDKDG---YHwltGRVDDVINVSGHRIGTAEVESALVSHPKCAE 635
Cdd:cd12116 327 VAQGYLGRPALTAERFVPdPFAGpgsrLYRTGDLVRRRADGrleYL---GRADGQVKIRGHRIELGEIEAALAAHPGVAQ 403
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1205963319 636 AAVVgIDHEVKGQGIYAFVTLVDGVPYS-DDLRKSLvmtvRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRIL 706
Cdd:cd12116 404 AAVV-VREDGGDRRLVAYVVLKAGAAPDaAALRAHL----RATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
166-710 |
1.85e-37 |
|
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: 147.60 E-value: 1.85e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 166 VDRHVEAgNGDKIAMYwegnepSQDGKLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVhs 245
Cdd:COG1021 31 LRRRAER-HPDRIAVV------DGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAI-- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 246 VVFAGFS-----AEALAQRVidcKPKVVITCnAVKRGlkiiF-LKDIVDASLDEsakngvdvgicltyenQSALNKVDTR 319
Cdd:COG1021 102 PVFALPAhrraeISHFAEQS---EAVAYIIP-DRHRG----FdYRALARELQAE----------------VPSLRHVLVV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 320 WTTGRDVWWQDVVPDfPTKCDVEWVDAEDPLFLLYTSGSTGKPKGVLHTTGGYmVYSATTFKHAFDYKPTDIYWCTADcg 399
Cdd:COG1021 158 GDAGEFTSLDALLAA-PADLSEPRPDPDDVAFFQLSGGTTGLPKLIPRTHDDY-LYSVRASAEICGLDADTVYLAALP-- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 400 wiTGHSY-----VTYGPLLNGATVlVFegAPNyPDPGRCWDIVDKYGVTIfyTA--PTLIRSLMRDGTEYvaRYSRKSLR 472
Cdd:COG1021 234 --AAHNFplsspGVLGVLYAGGTV-VL--APD-PSPDTAFPLIERERVTV--TAlvPPLALLWLDAAERS--RYDLSSLR 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 473 VLGSVGEPINPTAWRWFYDVIG--------------------DSR--------CPIS--DTWWqtetggfmitplpgawp 522
Cdd:COG1021 304 VLQVGGAKLSPELARRVRPALGctlqqvfgmaeglvnytrldDPEevilttqgRPISpdDEVR----------------- 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 523 qkpgsatfpffgvqpvIVDEKGRE-MEGECsGYLCIKKswPGAFRTLYGDKErYETTYFKPfAGYYFSGDGCSRDKDGYH 601
Cdd:COG1021 367 ----------------IVDEDGNPvPPGEV-GELLTRG--PYTIRGYYRAPE-HNARAFTP-DGFYRTGDLVRRTPDGYL 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 602 WLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAVVGIDHEVKGQGIYAFVTLVDGVPYSDDLRKSLvmtvRSQ-IGA 680
Cdd:COG1021 426 VVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFVVPRGEPLTLAELRRFL----RERgLAA 501
|
570 580 590
....*....|....*....|....*....|
gi 1205963319 681 FAAPDKIHWAPGLPKTRSGKIMRRILRKIA 710
Cdd:COG1021 502 FKLPDRLEFVDALPLTAVGKIDKKALRAAL 531
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
190-706 |
3.78e-37 |
|
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: 145.55 E-value: 3.78e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 190 DGKLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVhsVVFAGFSaealaqrvidckpkvvi 269
Cdd:cd05920 38 DRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAV--PVLALPS----------------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 270 tcnavKRGLKIIFLKDIVDASLdesakngvdvgicltYENQSALNKVDTRWTTgrdvwwQDVVPDFPtkcdvewvdaeDP 349
Cdd:cd05920 99 -----HRRSELSAFCAHAEAVA---------------YIVPDRHAGFDHRALA------RELAESIP-----------EV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 350 LFLLYTSGSTGKPKGVLHTTGGYmVYSATTFKHAFDYKPTDIYWCTADcgwiTGHSYVTYGP-----LLNGATVLVfegA 424
Cdd:cd05920 142 ALFLLSGGTTGTPKLIPRTHNDY-AYNVRASAEVCGLDQDTVYLAVLP----AAHNFPLACPgvlgtLLAGGRVVL---A 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 425 PNyPDPGRCWDIVDKYGVTifytAPTLIRSLMRDGTEYVARYSR--KSLRVL---GS---------VGEPINPTAWRWF- 489
Cdd:cd05920 214 PD-PSPDAAFPLIEREGVT----VTALVPALVSLWLDAAASRRAdlSSLRLLqvgGArlspalarrVPPVLGCTLQQVFg 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 490 -------YDVIGDSRCPIsdtwwqTETGGFMITPLPGAWpqkpgsatfpffgvqpvIVDEKGREM-EGEcSGYLCIKKsw 561
Cdd:cd05920 289 maegllnYTRLDDPDEVI------IHTQGRPMSPDDEIR-----------------VVDEEGNPVpPGE-EGELLTRG-- 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 562 PGAFRTLYgDKERYETTYFKPfAGYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAVVGI 641
Cdd:cd05920 343 PYTIRGYY-RAPEHNARAFTP-DGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAM 420
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1205963319 642 DHEVKGQGIYAFVTLVDGVPYSDDLRKSLvmtVRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRIL 706
Cdd:cd05920 421 PDELLGERSCAFVVLRDPPPSAAQLRRFL---RERGLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
190-700 |
2.15e-35 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 141.18 E-value: 2.15e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 190 DGKLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVV------------FAGFSAEAL- 256
Cdd:PRK07798 26 DRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVnyryvedelrylLDDSDAVALv 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 257 -----AQRVIDCKPKVvitcnavkRGLKIIFLkdIVDASLDESAKNGVDvgicltYEnqSALNKVDTRwttgrdvwwqdv 331
Cdd:PRK07798 106 yerefAPRVAEVLPRL--------PKLRTLVV--VEDGSGNDLLPGAVD------YE--DALAAGSPE------------ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 332 vPDFPTKCdvewvdaEDPLFLLYTSGSTGKPKGVLHTTGGYMVYSATTFKHAFDYKPTDIYWCTADCGWITG-------- 403
Cdd:PRK07798 156 -RDFGERS-------PDDLYLLYTGGTTGMPKGVMWRQEDIFRVLLGGRDFATGEPIEDEEELAKRAAAGPGmrrfpapp 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 404 --H---SYVTYGPLLNGATVlVFEGAPNYpDPGRCWDIVDKYGVT-IFYT----APTLIRSLMRDGteyvaRYSRKSLRV 473
Cdd:PRK07798 228 lmHgagQWAAFAALFSGQTV-VLLPDVRF-DADEVWRTIEREKVNvITIVgdamARPLLDALEARG-----PYDLSSLFA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 474 LGSVGEPINPTAWRWFYDVIgdsrcP---ISDTWWQTETGgFMITPLPGAWPQKPGSATFPFfGVQPVIVDEKGREME-- 548
Cdd:PRK07798 301 IASGGALFSPSVKEALLELL-----PnvvLTDSIGSSETG-FGGSGTVAKGAVHTGGPRFTI-GPRTVVLDEDGNPVEpg 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 549 GECSGYLCIKKSWPGAFrtlYGDKERYETTyFKPFAG--YYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESA 626
Cdd:PRK07798 374 SGEIGWIARRGHIPLGY---YKDPEKTAET-FPTIDGvrYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEA 449
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1205963319 627 LVSHPKCAEAAVVGIDHEVKGQGIYAFVTLVDGVPYSDDlrkSLVMTVRSQIGAFAAPDKIHWAPGLPKTRSGK 700
Cdd:PRK07798 450 LKAHPDVADALVVGVPDERWGQEVVAVVQLREGARPDLA---ELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
190-706 |
3.16e-35 |
|
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: 140.03 E-value: 3.16e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 190 DGKLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAEALAQRVIDCKPKVVI 269
Cdd:cd12117 20 DRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAERLAFMLADAGAKVLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 270 TCNAVKRGLKIIFLKDIVDASLDESAKNGVDVGicltyenqsalnkvdtrwttgrdvwwqdvvpdfptkcdvewVDAEDP 349
Cdd:cd12117 100 TDRSLAGRAGGLEVAVVIDEALDAGPAGNPAVP-----------------------------------------VSPDDL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 350 LFLLYTSGSTGKPKGV---------LHTTGGYMVYSA-TTF----KHAFDYKPTDIYwctadcgwitghsyvtyGPLLNG 415
Cdd:cd12117 139 AYVMYTSGSTGRPKGVavthrgvvrLVKNTNYVTLGPdDRVlqtsPLAFDASTFEIW-----------------GALLNG 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 416 AT-VLVFEGAPnyPDPGRCWDIVDKYGVT-IFYTAPtLIRSLMRDGTEYVArysrkSLRVLGSVGEPINPTAWRWFYDVI 493
Cdd:cd12117 202 ARlVLAPKGTL--LDPDALGALIAEEGVTvLWLTAA-LFNQLADEDPECFA-----GLRELLTGGEVVSPPHVRRVLAAC 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 494 GDSRcpISDTWWQTETGGF----MITPLPGAWPQKP-GSatfPFFGVQPVIVDEKGREMEGECSGYLCIkkSWPGAFRTL 568
Cdd:cd12117 274 PGLR--LVNGYGPTENTTFttshVVTELDEVAGSIPiGR---PIANTRVYVLDEDGRPVPPGVPGELYV--GGDGLALGY 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 569 YGD----KERYETTYFKPFAGYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAVVGIDHE 644
Cdd:cd12117 347 LNRpaltAERFVADPFGPGERLYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDA 426
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1205963319 645 VKGQGIYAFVTLVDGVPySDDLRKSLvmtvRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRIL 706
Cdd:cd12117 427 GGDKRLVAYVVAEGALD-AAELRAFL----RERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
176-706 |
4.91e-35 |
|
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: 138.60 E-value: 4.91e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 176 DKIAMYwegnepSQDGKLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAEA 255
Cdd:cd12115 14 DAIALV------CGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPER 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 256 LAQRVIDCKPKVVITcnavkrglkiiflkdivdasldesakngvdvgicltyenqsalnkvdtrwttgrdvwwqdvvpdf 335
Cdd:cd12115 88 LRFILEDAQARLVLT----------------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 336 ptkcdvewvDAEDPLFLLYTSGSTGKPKGVLHTTGgymvySATTFkhafdykptdIYWCTADCG--WITGHSYVT----- 408
Cdd:cd12115 103 ---------DPDDLAYVIYTSGSTGRPKGVAIEHR-----NAAAF----------LQWAAAAFSaeELAGVLASTsicfd 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 409 ------YGPLLNGATVLVFEGAPNYPD-PGRCwdivdkyGVTIFYTAPTLIRSLMRdgteyvARYSRKSLRVLGSVGEPI 481
Cdd:cd12115 159 lsvfelFGPLATGGKVVLADNVLALPDlPAAA-------EVTLINTVPSAAAELLR------HDALPASVRVVNLAGEPL 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 482 NPTAWRWFYDVIGDSRC-----PISDTWWQTetgGFMITPLPGAWPqkpgSATFPFFGVQPVIVDEKGREMEGECSGYLC 556
Cdd:cd12115 226 PRDLVQRLYARLQVERVvnlygPSEDTTYST---VAPVPPGASGEV----SIGRPLANTQAYVLDRALQPVPLGVPGELY 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 557 IkkSWPGAFRTLYGD----KERYETTYFKPFAGYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPK 632
Cdd:cd12115 299 I--GGAGVARGYLGRpgltAERFLPDPFGPGARLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPG 376
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1205963319 633 CAEAAVVGIDHEVKGQGIYAFVTLVDGV-PYSDDLRKSLvmtvRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRIL 706
Cdd:cd12115 377 VREAVVVAIGDAAGERRLVAYIVAEPGAaGLVEDLRRHL----GTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
168-708 |
3.12e-34 |
|
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: 137.76 E-value: 3.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 168 RHVEAGNGDKIAMYWEGNEPsqDGKLTYSELLEKVCQLSNYLKSVGVGKGDAVVIylpML------MELpiaMLACARIG 241
Cdd:cd12119 3 EHAARLHGDREIVSRTHEGE--VHRYTYAEVAERARRLANALRRLGVKPGDRVAT---LAwnthrhLEL---YYAVPGMG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 242 AVHSVVFAGFSAEALAQRVIDCKPKVVITCNAvkrglkiiFLKdIVDASLDESAKngVDVGICLTYENQSALnkvdtrwT 321
Cdd:cd12119 75 AVLHTINPRLFPEQIAYIINHAEDRVVFVDRD--------FLP-LLEAIAPRLPT--VEHVVVMTDDAAMPE-------P 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 322 TGRDVW-WQDVVPDFPTKCDVEWVDAEDPLFLLYTSGSTGKPKGVlhttggymVYS-ATTFKHAFDYKPTD-IYWCTADC 398
Cdd:cd12119 137 AGVGVLaYEELLAAESPEYDWPDFDENTAAAICYTSGTTGNPKGV--------VYShRSLVLHAMAALLTDgLGLSESDV 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 399 -----------GWITGHSYVTYGpllngaTVLVFEGApnYPDPGRCWDIVDKYGVTIFYTAPTLIRSLMrdgtEYVAR-- 465
Cdd:cd12119 209 vlpvvpmfhvnAWGLPYAAAMVG------AKLVLPGP--YLDPASLAELIEREGVTFAAGVPTVWQGLL----DHLEAng 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 466 YSRKSLRVLGSVGEPINPTAWRWFYDVIgdsrCPISDTWWQTETG--GFMITPLPG----------AWPQKPGsatFPFF 533
Cdd:cd12119 277 RDLSSLRRVVIGGSAVPRSLIEAFEERG----VRVIHAWGMTETSplGTVARPPSEhsnlsedeqlALRAKQG---RPVP 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 534 GVQPVIVDEKGREME--GECSGYLCIKKSW-PGAFrtlYGDKERYEttyfKPFAGYYF-SGDGCSRDKDGYHWLTGRVDD 609
Cdd:cd12119 350 GVELRIVDDDGRELPwdGKAVGELQVRGPWvTKSY---YKNDEESE----ALTEDGWLrTGDVATIDEDGYLTITDRSKD 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 610 VINVSGHRIGTAEVESALVSHPKCAEAAVVGIDHEVKGQGIYAFVTLVDGV-PYSDDLRKSLvmtvRSQIGAFAAPDKIH 688
Cdd:cd12119 423 VIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEGAtVTAEELLEFL----ADKVAKWWLPDDVV 498
|
570 580
....*....|....*....|
gi 1205963319 689 WAPGLPKTRSGKIMRRILRK 708
Cdd:cd12119 499 FVDEIPKTSTGKIDKKALRE 518
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
348-708 |
3.13e-34 |
|
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: 136.27 E-value: 3.13e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 348 DPLFLLYTSGSTGKPKGVLHTTGGymVYS-ATTFKHAFDYKPTD-IYWCTAdcgWITGHSYVT--YGPLLNGATVLVFeg 423
Cdd:cd05941 90 DPALILYTSGTTGRPKGVVLTHAN--LAAnVRALVDAWRWTEDDvLLHVLP---LHHVHGLVNalLCPLFAGASVEFL-- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 424 aPNYpDPGRCWDIVDKYGVTIFYTAPT----LIRS--LMRDGTEYVARYSRKSLR--VLGSVGEPInPTAWRWfydvigd 495
Cdd:cd05941 163 -PKF-DPKEVAISRLMPSITVFMGVPTiytrLLQYyeAHFTDPQFARAAAAERLRlmVSGSAALPV-PTLEEW------- 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 496 srCPIS-----DTWWQTETGGFMITPLPGawPQKPGSATFPFFGVQPVIVD-EKGREMEGECSGYLCIKKswPGAFRTLY 569
Cdd:cd05941 233 --EAITghtllERYGMTEIGMALSNPLDG--ERRPGTVGMPLPGVQARIVDeETGEPLPRGEVGEIQVRG--PSVFKEYW 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 570 GDKERYEttyfKPFA--GYYFSGDGCSRDKDGYHWLTGRV-DDVINVSGHRIGTAEVESALVSHPKCAEAAVVGIDHEVK 646
Cdd:cd05941 307 NKPEATK----EEFTddGWFKTGDLGVVDEDGYYWILGRSsVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDW 382
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1205963319 647 GQGIYAFVTLVDGVP--YSDDLRKSLvmtvRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRK 708
Cdd:cd05941 383 GERVVAVVVLRAGAAalSLEELKEWA----KQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
84-723 |
4.00e-34 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 139.44 E-value: 4.00e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 84 LLVHPSADFAAQALVSSTQQYREMYQKSIDDPAGFWSEIADEFYWKQKWSPDEVCAENLDVTKGPikiEWFKGGKTNI-- 161
Cdd:PLN03052 102 LLEARGKELLGSKYKDPISSFSEFQRFSVENPEVYWSIVLDELSLVFSVPPRCILDTSDESNPGG---QWLPGAVLNVae 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 162 -CYNAVDRHveagNGDKIAMYW--EGNEPSQDGKLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACA 238
Cdd:PLN03052 179 cCLTPKPSK----TDDSIAIIWrdEGSDDLPVNRMTLSELRSQVSRVANALDALGFEKGDAIAIDMPMNVHAVIIYLAII 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 239 RIGAVHSVVFAGFSAEALAQRVIDCKPKVVITCNAVKRGLKIIFL-KDIVDAsldESAKNGV----DVGICLTYENQsal 313
Cdd:PLN03052 255 LAGCVVVSIADSFAPSEIATRLKISKAKAIFTQDVIVRGGKSIPLySRVVEA---KAPKAIVlpadGKSVRVKLREG--- 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 314 nkvdtrwttgrDVWWQDVVPDF-PTKCDVEWVDAEDPL----FLLYTSGSTGKPKGVLHTTGGYMVYSATTFKHaFDYKP 388
Cdd:PLN03052 329 -----------DMSWDDFLARAnGLRRPDEYKAVEQPVeaftNILFSSGTTGEPKAIPWTQLTPLRAAADAWAH-LDIRK 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 389 TDIY-WCTaDCGWITGHsYVTYGPLLNGATVLVFEGAPNYPDPGRcwdIVDKYGVTIFYTAPTLIRSLMRdgTEYVARYS 467
Cdd:PLN03052 397 GDIVcWPT-NLGWMMGP-WLVYASLLNGATLALYNGSPLGRGFAK---FVQDAKVTMLGTVPSIVKTWKN--TNCMAGLD 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 468 RKSLRVLGSVGEPINPTAWRWFYdvigdSRC---PISDTWWQTETGGFMITplpGAWPQKPGSATF--PFFGVQPVIVDE 542
Cdd:PLN03052 470 WSSIRCFGSTGEASSVDDYLWLM-----SRAgykPIIEYCGGTELGGGFVT---GSLLQPQAFAAFstPAMGCKLFILDD 541
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 543 KGREM--EGECSGYLCIKKSWPGAFRTLYgDKERYETtYFK--P-FAGYYFS--GDGCSRDKDGYHWLTGRVDDVINVSG 615
Cdd:PLN03052 542 SGNPYpdDAPCTGELALFPLMFGASSTLL-NADHYKV-YFKgmPvFNGKILRrhGDIFERTSGGYYRAHGRADDTMNLGG 619
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 616 HRIGTAEVESAL-VSHPKCAEAAVVGIdhEVKGQGIYAFVTLV------DGVPYSDDLRKSLVMTVRSQIGAFAAPDKIH 688
Cdd:PLN03052 620 IKVSSVEIERVCnAADESVLETAAIGV--PPPGGGPEQLVIAAvlkdppGSNPDLNELKKIFNSAIQKKLNPLFKVSAVV 697
|
650 660 670
....*....|....*....|....*....|....*
gi 1205963319 689 WAPGLPKTRSGKIMRRILRKiasrQLDELGDTSTL 723
Cdd:PLN03052 698 IVPSFPRTASNKVMRRVLRQ----QLAQELSRSKL 728
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
224-707 |
5.92e-34 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 136.48 E-value: 5.92e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 224 LPMLMELPIAMLACARIGAVHSVVFAGFSAEALAQRVIDCKPKVVITCNAVKRGLKIIFLKDIVDASLDESA----KNGV 299
Cdd:PLN03051 1 MPMTVDAVIIYLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFTQDVVLRGGRALPLYSKVVEAAPAKAivlpAAGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 300 DVGICLTYENQS--ALNKVDTRWTTGRDVWWQDVVpdfptkcdvewVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMVYSA 377
Cdd:PLN03051 81 PVAVPLREQDLSwcDFLGVAAAQGSVGGNEYSPVY-----------APVESVTNILFSSGTTGEPKAIPWTHLSPLRCAS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 378 TTFKHaFDYKPTDIYWCTADCGWITGhSYVTYGPLLNGATVLVFEGAPNYPDPGrcwDIVDKYGVTIFYTAPTLIRSLMR 457
Cdd:PLN03051 150 DGWAH-MDIQPGDVVCWPTNLGWMMG-PWLLYSAFLNGATLALYGGAPLGRGFG---KFVQDAGVTVLGLVPSIVKAWRH 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 458 DGTEYVARYSRKSLRVLGSVGEPINPTAWRWFYDVIGDSRcPISDTWWQTETGGFMI--TPLPgawPQKPGSATFPFFGV 535
Cdd:PLN03051 225 TGAFAMEGLDWSKLRVFASTGEASAVDDVLWLSSVRGYYK-PVIEYCGGTELASGYIssTLLQ---PQAPGAFSTASLGT 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 536 QPVIVDEKGREM--EGECSGYLCIKKSWPGAF-RTLYGDkerYETTYFKPFAGYYFS-------GDGCSRDKDGYHWLTG 605
Cdd:PLN03051 301 RFVLLNDNGVPYpdDQPCVGEVALAPPMLGASdRLLNAD---HDKVYYKGMPMYGSKgmplrrhGDIMKRTPGGYFCVQG 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 606 RVDDVINVSGHRIGTAEVESALVSHPKC-AEAAVVGIDHEVKG-QGIYAFVTLVD-----GVPYSDDLRKSLVMTVRSQI 678
Cdd:PLN03051 378 RADDTMNLGGIKTSSVEIERACDRAVAGiAETAAVGVAPPDGGpELLVIFLVLGEekkgfDQARPEALQKKFQEAIQTNL 457
|
490 500
....*....|....*....|....*....
gi 1205963319 679 GAFAAPDKIHWAPGLPKTRSGKIMRRILR 707
Cdd:PLN03051 458 NPLFKVSRVKIVPELPRNASNKLLRRVLR 486
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
167-710 |
1.41e-33 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 135.95 E-value: 1.41e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 167 DRHVEAgNGDKIAMYWEGNEPSQDGKLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAV--- 243
Cdd:PRK13295 31 DACVAS-CPDKTAVTAVRLGTGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVlnp 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 244 -------HSV----------------VFAGFSAEALAQRVIDCKPKvvitcnavkrgLKIIFlkdIVDASLDESakngvd 300
Cdd:PRK13295 110 lmpifreRELsfmlkhaeskvlvvpkTFRGFDHAAMARRLRPELPA-----------LRHVV---VVGGDGADS------ 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 301 vgicltyenqsalnkVDTRWTTGRdvWWQDvvPDFPTKCDVEWVDAEDPLFLLYTSGSTGKPKGVLHTT----GGYMVYS 376
Cdd:PRK13295 170 ---------------FEALLITPA--WEQE--PDAPAILARLRPGPDDVTQLIYTSGTTGEPKGVMHTAntlmANIVPYA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 377 AttfkhAFDYKPTDIYWCTADCGWITGHSYVTYGPLLNGATVLVFEgapnYPDPGRCWDIVDKYGVTiFYTAPTlirSLM 456
Cdd:PRK13295 231 E-----RLGLGADDVILMASPMAHQTGFMYGLMMPVMLGATAVLQD----IWDPARAAELIRTEGVT-FTMAST---PFL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 457 RDGTEYVA--RYSRKSLRVLGSVGEPINPTAWRWFYDVIGDSRCPisdTWWQTETGGFMITpLPGAWPQKpGSAT--FPF 532
Cdd:PRK13295 298 TDLTRAVKesGRPVSSLRTFLCAGAPIPGALVERARAALGAKIVS---AWGMTENGAVTLT-KLDDPDER-ASTTdgCPL 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 533 FGVQPVIVDEKGREMEGECSGYLCIKKswPGAFRTLYGDKERYETTyfkpFAGYYFSGDGCSRDKDGYHWLTGRVDDVIN 612
Cdd:PRK13295 373 PGVEVRVVDADGAPLPAGQIGRLQVRG--CSNFGGYLKRPQLNGTD----ADGWFDTGDLARIDADGYIRISGRSKDVII 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 613 VSGHRIGTAEVESALVSHPKCAEAAVVGIDHEVKGQGIYAFVTLVDGVPYsdDLRkSLVMTVRSQIGAFA-APDKIHWAP 691
Cdd:PRK13295 447 RGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPGQSL--DFE-EMVEFLKAQKVAKQyIPERLVVRD 523
|
570
....*....|....*....
gi 1205963319 692 GLPKTRSGKIMRRILRKIA 710
Cdd:PRK13295 524 ALPRTPSGKIQKFRLREML 542
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
193-706 |
1.66e-33 |
|
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: 133.76 E-value: 1.66e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 193 LTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAEALAQRVIDCKPKVVItcn 272
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAV--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 273 avkrglkiiflkdiVDASLDESAkngvdvgicltyenqsalnkvdtrwttgrdvwwqdVVPdfptkcdvewvdaedplfl 352
Cdd:cd05935 79 --------------VGSELDDLA-----------------------------------LIP------------------- 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 353 lYTSGSTGKPKGVLHTTGGyMVYSATTFKHAFDYKPTDIYWCTADCGWITGHSYVTYGPLLNGATVLVF-----EGAPny 427
Cdd:cd05935 91 -YTSGTTGLPKGCMHTHFS-AAANALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMarwdrETAL-- 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 428 pdpgrcwDIVDKYGVTIFYTAPTLIRSLMrdGTEYVARYSRKSLRVLGSVGEPINPTAWRWFYDVIGdsrCPISDTWWQT 507
Cdd:cd05935 167 -------ELIEKYKVTFWTNIPTMLVDLL--ATPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTG---LRFVEGYGLT 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 508 ETggfmITPLPGAWPQKPGSATF--PFFGVQPVIVD-EKGREMEGECSGYLCIKKswPGAFRTlYGDKERYETTYFKPFA 584
Cdd:cd05935 235 ET----MSQTHTNPPLRPKLQCLgiP*FGVDARVIDiETGRELPPNEVGEIVVRG--PQIFKG-YWNRPEETEESFIEIK 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 585 G--YYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAVVGIDHEVKGQGIYAFVTLVDGVPY 662
Cdd:cd05935 308 GrrFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYRG 387
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1205963319 663 SDDlRKSLVMTVRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRIL 706
Cdd:cd05935 388 KVT-EEDIIEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
176-706 |
3.13e-33 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 135.09 E-value: 3.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 176 DKIAMYWEGNEpsqdgkLTYSELLEKVCQLSNYLKSV-GVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAE 254
Cdd:PRK08314 25 DKTAIVFYGRA------ISYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 255 ALAQRVIDCKPKVVIT----CNAVKRGLKIIFLKDIVDAS----LDESAKNGVDVGICLTYENQSALNkvdtrwttGRDV 326
Cdd:PRK08314 99 ELAHYVTDSGARVAIVgselAPKVAPAVGNLRLRHVIVAQysdyLPAEPEIAVPAWLRAEPPLQALAP--------GGVV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 327 WWQDVVPDFPTKCDVEwVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMVySATTFKHAFDYKPTDIYWCTADCGWITGHSY 406
Cdd:PRK08314 171 AWKEALAAGLAPPPHT-AGPDDLAVLPYTSGTTGVPKGCMHTHRTVMA-NAVGSVLWSNSTPESVVLAVLPLFHVTGMVH 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 407 VTYGPLLNGATVLVF-----EGAPnypdpgrcwDIVDKYGVTIFYTAPTLIRSLMrdGTEYVARYSRKSLRVLGSVGEPI 481
Cdd:PRK08314 249 SMNAPIYAGATVVLMprwdrEAAA---------RLIERYRVTHWTNIPTMVVDFL--ASPGLAERDLSSLRYIGGGGAAM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 482 nPTA-WRWFYDVIGdsrCPISDTWWQTETGGFMITPLPGAwpQKPGSATFPFFGVQPVIVD-EKGREM----EGEcsgyl 555
Cdd:PRK08314 318 -PEAvAERLKELTG---LDYVEGYGLTETMAQTHSNPPDR--PKLQCLGIPTFGVDARVIDpETLEELppgeVGE----- 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 556 cIKKSWPGAFRTLYGDKERYETTyFKPFAGYYF--SGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKC 633
Cdd:PRK08314 387 -IVVHGPQVFKGYWNRPEATAEA-FIEIDGKRFfrTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAI 464
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1205963319 634 AEAAVVGIDHEVKGQGIYAFVTLVD---GVPYSDDLRKslvmTVRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRIL 706
Cdd:PRK08314 465 QEACVIATPDPRRGETVKAVVVLRPearGKTTEEEIIA----WAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQL 536
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
189-706 |
3.73e-33 |
|
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: 133.14 E-value: 3.73e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 189 QDGKLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAEALAQRVIDCKPKVV 268
Cdd:cd05945 13 GGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIREILDAAKPALL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 269 ItcnavkrglkiiflkdivdasldesakngvdvgicltyenqsalnkvdtrwttgrdvwwqdvvpdfptkcdvewVDAED 348
Cdd:cd05945 93 I--------------------------------------------------------------------------ADGDD 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 349 PLFLLYTSGSTGKPKGVLHTTGGYMVYS---------------ATTFKHAFDYKPTDIYwctadCGWITGhsyvtygpll 413
Cdd:cd05945 99 NAYIIFTSGSTGRPKGVQISHDNLVSFTnwmlsdfplgpgdvfLNQAPFSFDLSVMDLY-----PALASG---------- 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 414 nGATVLVFEGApnYPDPGRCWDIVDKYGVTIFYTAPTLIRSLMRDGTEYVARYsrKSLRVLGSVGEPI-NPTAWRWFydv 492
Cdd:cd05945 164 -ATLVPVPRDA--TADPKQLFRFLAEHGITVWVSTPSFAAMCLLSPTFTPESL--PSLRHFLFCGEVLpHKTARALQ--- 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 493 igdSR---CPISDTWWQTETggfMITPLPGAWPQKPGSAT------FPFFGVQPVIVDEKGREMEGECSGYLCIkkSWPG 563
Cdd:cd05945 236 ---QRfpdARIYNTYGPTEA---TVAVTYIEVTPEVLDGYdrlpigYAKPGAKLVILDEDGRPVPPGEKGELVI--SGPS 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 564 AFRTLYGDKERYETTYFkPFAGY--YFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAVVGI 641
Cdd:cd05945 308 VSKGYLNNPEKTAAAFF-PDEGQraYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPK 386
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1205963319 642 DHEVKGQGIYAFVTLVDGVPY--SDDLRKSLvmtvRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRIL 706
Cdd:cd05945 387 YKGEKVTELIAFVVPKPGAEAglTKAIKAEL----AERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
191-707 |
1.52e-32 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 132.96 E-value: 1.52e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 191 GKLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAvHSVVF-AGFSAEALAQrvidckpkvVI 269
Cdd:PRK13382 67 GTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGA-DILLLnTSFAGPALAE---------VV 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 270 TcnavKRGLKIIF----LKDIVDASLDESAKngvdvgicltyenqsALNKVDtrWTTGRDVWWQDVVPDFPTKCDVEWVD 345
Cdd:PRK13382 137 T----REGVDTVIydeeFSATVDRALADCPQ---------------ATRIVA--WTDEDHDLTVEVLIAAHAGQRPEPTG 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 346 AEDPLFLLyTSGSTGKPKGVLHT-TGGYMVYSATtfkhaFDYKPtdiywctadcgWITGHSYVTYGPLLN--GATVLVFE 422
Cdd:PRK13382 196 RKGRVILL-TSGTTGTPKGARRSgPGGIGTLKAI-----LDRTP-----------WRAEEPTVIVAPMFHawGFSQLVLA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 423 GAPNYP-------DPGRCWDIVDKYGVTIFYTAPTLIRSLMRDGTEYVARYSRKSLRVLGSVGEPINPTAWRWFYDVIGD 495
Cdd:PRK13382 259 ASLACTivtrrrfDPEATLDLIDRHRATGLAVVPVMFDRIMDLPAEVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGD 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 496 SrcpISDTWWQTETGgfMI-TPLPGAWPQKPGSATFPFFGVQPVIVDEKGREM-EGECsGYLCIKKSwpgafrTLYgdkE 573
Cdd:PRK13382 339 V---IYNNYNATEAG--MIaTATPADLRAAPDTAGRPAEGTEIRILDQDFREVpTGEV-GTIFVRND------TQF---D 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 574 RYETTYFKPF-AGYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAVVGIDHEVKGQGIYA 652
Cdd:PRK13382 404 GYTSGSTKDFhDGFMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAA 483
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1205963319 653 FVTLVDGVPYSDDLRKSlvmTVRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRILR 707
Cdd:PRK13382 484 FVVLKPGASATPETLKQ---HVRDNLANYKVPRDIVVLDELPRGATGKILRRELQ 535
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
193-707 |
2.84e-32 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 131.56 E-value: 2.84e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 193 LTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAEALAQRVIDCKPKVVITCN 272
Cdd:PRK08276 12 VTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVLIVSA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 273 AVKRGLKIifLKDIVDASLDESAKNGVDVGICLTYENqsalnkvdtrwttgrdvwWQDVVPDFPTkcDVEWVDAEdplfL 352
Cdd:PRK08276 92 ALADTAAE--LAAELPAGVPLLLVVAGPVPGFRSYEE------------------ALAAQPDTPI--ADETAGAD----M 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 353 LYTSGSTGKPKGVL--------HTTGGYMVYSATTFkhaFDYKPTDIYWCTADcgwitghSYVTyGPLLNGATVLVFEGA 424
Cdd:PRK08276 146 LYSSGTTGRPKGIKrplpgldpDEAPGMMLALLGFG---MYGGPDSVYLSPAP-------LYHT-APLRFGMSALALGGT 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 425 ----PNYpDPGRCWDIVDKYGVTIFYTAPTLIRSLMRDGTEYVARYSRKSLRVLGSVGEPinptawrwfydvigdsrCPI 500
Cdd:PRK08276 215 vvvmEKF-DAEEALALIERYRVTHSQLVPTMFVRMLKLPEEVRARYDVSSLRVAIHAAAP-----------------CPV 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 501 S------DtWW---------QTETGGF-MITPlpGAWPQKPGSATFPFFGVQPvIVDEKGREM----EG----ECSGYlc 556
Cdd:PRK08276 277 EvkramiD-WWgpiiheyyaSSEGGGVtVITS--EDWLAHPGSVGKAVLGEVR-ILDEDGNELppgeIGtvyfEMDGY-- 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 557 ikkswpgAFrTLYGDKERYETTYFKpfAGYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEA 636
Cdd:PRK08276 351 -------PF-EYHNDPEKTAAARNP--HGWVTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADV 420
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1205963319 637 AVVGIDHEVKGQGIYAFVTLVDGVPYSDDLRKSLVMTVRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRILR 707
Cdd:PRK08276 421 AVFGVPDEEMGERVKAVVQPADGADAGDALAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLR 491
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
175-706 |
8.86e-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: 129.70 E-value: 8.86e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 175 GDKIAMYWEGnepsqdGKLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAE 254
Cdd:cd17646 12 PDAPAVVDEG------RTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPAD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 255 ALAQRVIDCKPKVVITcnavkrglkiiflkdivDASLDESAKNGVDVGICltyenqsalnkVDTRWTTGRD-VWWQDVVP 333
Cdd:cd17646 86 RLAYMLADAGPAVVLT-----------------TADLAARLPAGGDVALL-----------GDEALAAPPAtPPLVPPRP 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 334 DfptkcdvewvdaeDPLFLLYTSGSTGKPKGVLHTTGGyMVYSATTFKHAFDYKPTDIYWCTADCG-----WitghsyVT 408
Cdd:cd17646 138 D-------------NLAYVIYTSGSTGRPKGVMVTHAG-IVNRLLWMQDEYPLGPGDRVLQKTPLSfdvsvW------EL 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 409 YGPLLNGATVLVFEgAPNYPDPGRCWDIVDKYGVTIFYTAPTLIRSLMRDgteyVARYSRKSLRVLGSVGEPINPTAWRW 488
Cdd:cd17646 198 FWPLVAGARLVVAR-PGGHRDPAYLAALIREHGVTTCHFVPSMLRVFLAE----PAAGSCASLRRVFCSGEALPPELAAR 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 489 FYDVI--------GDSRCPISDTWWQTEtggfmitplpGAWPQKPGSATFPFFGVQPVIVDEKGREMEGECSGYLCIkks 560
Cdd:cd17646 273 FLALPgaelhnlyGPTEAAIDVTHWPVR----------GPAETPSVPIGRPVPNTRLYVLDDALRPVPVGVPGELYL--- 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 561 wpGAFRTLYG-------DKERYETTYFKPFAGYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKC 633
Cdd:cd17646 340 --GGVQLARGylgrpalTAERFVPDPFGPGSRMYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAV 417
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1205963319 634 AEAAVVGIDHEVKGQGIYAFVTLVDGVPYSDD--LRKSLvmtvRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRIL 706
Cdd:cd17646 418 THAVVVARAAPAGAARLVGYVVPAAGAAGPDTaaLRAHL----AERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
202-707 |
1.13e-31 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 129.10 E-value: 1.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 202 VCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVF----AGFSAEALAQRVIDCKPKVVItcnavkrg 277
Cdd:cd05922 3 VSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRLGLVFvplnPTLKESVLRYLVADAGGRIVL-------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 278 lkiiflkdivdasLDESAKNGVDVGICLTYENQSALNkVDTRWTTGRDVwwqdvvPDFPtkcdvewVDAEDPLFLLYTSG 357
Cdd:cd05922 75 -------------ADAGAADRLRDALPASPDPGTVLD-ADGIRAARASA------PAHE-------VSHEDLALLLYTSG 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 358 STGKPKGVL--HTTggyMVYSATTFKHAFDYKPTDIYWCTADCGWITGHSYVTYGpLLNGATVLVfegAPNYPDPGRCWD 435
Cdd:cd05922 128 STGSPKLVRlsHQN---LLANARSIAEYLGITADDRALTVLPLSYDYGLSVLNTH-LLRGATLVL---TNDGVLDDAFWE 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 436 IVDKYGVTIFYTAPT---LIRSLMRDGTEYvarysrKSLRVLGSVGEPINPTAWRWFYDVIGDSRcpISDTWWQTETGGF 512
Cdd:cd05922 201 DLREHGATGLAGVPStyaMLTRLGFDPAKL------PSLRYLTQAGGRLPQETIARLRELLPGAQ--VYVMYGQTEATRR 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 513 MITPLPGAWPQKPGSATFPFFGVQPVIVDEKG-REMEGECsGYLCIKkswpGAFRTL-YGDKERYETtyfKP--FAGYYF 588
Cdd:cd05922 273 MTYLPPERILEKPGSIGLAIPGGEFEILDDDGtPTPPGEP-GEIVHR----GPNVMKgYWNDPPYRR---KEgrGGGVLH 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 589 SGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAVVGIDHEVkGQGIYAFVTLVDGVPYSDDLRK 668
Cdd:cd05922 345 TGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPL-GEKLALFVTAPDKIDPKDVLRS 423
|
490 500 510
....*....|....*....|....*....|....*....
gi 1205963319 669 slvmtVRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRILR 707
Cdd:cd05922 424 -----LAERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
166-670 |
2.05e-31 |
|
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: 132.29 E-value: 2.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 166 VDRHVEAgNGDKIAMYWEgnepsqDGKLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHS 245
Cdd:COG1020 482 FEAQAAR-TPDAVAVVFG------DQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYV 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 246 VVFAGFSAEALAQRVIDCKPKVVITCNAVKRGLkiiflkdivdasldesAKNGVDVgICL---TYENQSALNkvdtrwtt 322
Cdd:COG1020 555 PLDPAYPAERLAYMLEDAGARLVLTQSALAARL----------------PELGVPV-LALdalALAAEPATN-------- 609
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 323 grdvwwqdvvPDFPtkcdvewVDAEDPLFLLYTSGSTGKPKGVLHTTGGyMVYSATTFKHAFDYKPTDIywctadCGWIT 402
Cdd:COG1020 610 ----------PPVP-------VTPDDLAYVIYTSGSTGRPKGVMVEHRA-LVNLLAWMQRRYGLGPGDR------VLQFA 665
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 403 GHS-----YVTYGPLLNGAT-VLVFEGAPnyPDPGRCWDIVDKYGVTIFYTAPTLIRSLMRDGTEyvarySRKSLRVLGS 476
Cdd:COG1020 666 SLSfdasvWEIFGALLSGATlVLAPPEAR--RDPAALAELLARHRVTVLNLTPSLLRALLDAAPE-----ALPSLRLVLV 738
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 477 VGEPINPTAWRWFYDVIGDSRC-----PisdtwwqTETG----GFMITPLPGAWPQKP-GSatfPFFGVQPVIVDEKGRE 546
Cdd:COG1020 739 GGEALPPELVRRWRARLPGARLvnlygP-------TETTvdstYYEVTPPDADGGSVPiGR---PIANTRVYVLDAHLQP 808
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 547 ----MEGEcsgyLCIkkswpGafrtlyGD-------------KERYETTYFkPFAG--YYFSGDGCSRDKDG---YHwlt 604
Cdd:COG1020 809 vpvgVPGE----LYI-----G------GAglargylnrpeltAERFVADPF-GFPGarLYRTGDLARWLPDGnleFL--- 869
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1205963319 605 GRVDDVINVSGHRIGTAEVESALVSHPKCAEAAVVGIDHEVKGQGIYAFVTLVDGVPYSDDLRKSL 670
Cdd:COG1020 870 GRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLA 935
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
168-719 |
3.06e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 125.92 E-value: 3.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 168 RHVEAGNGDKIAMYWegnepsQDGKLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAV---- 243
Cdd:PRK07470 14 RQAARRFPDRIALVW------GDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVwvpt 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 244 ------HSVVFAGFSAEALAQRVIDCKPKVVITCNAVKRGLKIIFLKDIVDASLDesakngvdvgicltYENQSALNkvd 317
Cdd:PRK07470 88 nfrqtpDEVAYLAEASGARAMICHADFPEHAAAVRAASPDLTHVVAIGGARAGLD--------------YEALVARH--- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 318 trwtTGRDVwwqdvvpdfptkcDVEWVDAEDPLFLLYTSGSTGKPK-GVLhtTGGYMVYSATTfkHAFDYKP--TDiywc 394
Cdd:PRK07470 151 ----LGARV-------------ANAAVDHDDPCWFFFTSGTTGRPKaAVL--THGQMAFVITN--HLADLMPgtTE---- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 395 tADCgwitghSYVTyGPLLNGATV----LVFEGA-----PNYP-DPGRCWDIVDKYGVTIFYTAPTLIRSLMRDgtEYVA 464
Cdd:PRK07470 206 -QDA------SLVV-APLSHGAGIhqlcQVARGAatvllPSERfDPAEVWALVERHRVTNLFTVPTILKMLVEH--PAVD 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 465 RYSRKSLRVLGSVGEPINPTAWRWFYDVIGDSrcpISDTWWQTETGGfMITPLPGAW------PQ-KPGSATFPFFGVQP 537
Cdd:PRK07470 276 RYDHSSLRYVIYAGAPMYRADQKRALAKLGKV---LVQYFGLGEVTG-NITVLPPALhdaedgPDaRIGTCGFERTGMEV 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 538 VIVDEKGREMEGECSGYLCIKKswPGAFRTLYGDKERYEttyfKPFAGYYF-SGDGCSRDKDGYHWLTGRVDDVINVSGH 616
Cdd:PRK07470 352 QIQDDEGRELPPGETGEICVIG--PAVFAGYYNNPEANA----KAFRDGWFrTGDLGHLDARGFLYITGRASDMYISGGS 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 617 RIGTAEVESALVSHPKCAEAAVVGIDHEVKGQGIYAFVTLVDGVPYSDDlrkSLVMTVRSQIGAFAAPDKIHWAPGLPKT 696
Cdd:PRK07470 426 NVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARDGAPVDEA---ELLAWLDGKVARYKLPKRFFFWDALPKS 502
|
570 580
....*....|....*....|...
gi 1205963319 697 RSGKIMRRILRKiasrQLDELGD 719
Cdd:PRK07470 503 GYGKITKKMVRE----ELEERGL 521
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
176-706 |
3.35e-30 |
|
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: 124.34 E-value: 3.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 176 DKIAMYWEGNEpsqdgkLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAEA 255
Cdd:cd17643 2 EAVAVVDEDRR------LTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 256 LAQRVIDCKPKVVITcnavkrglkiiflkdivdasldesakngvdvgicltyenqsalnkvdtrwttgrdvwwqdvvpdf 335
Cdd:cd17643 76 IAFILADSGPSLLLT----------------------------------------------------------------- 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 336 ptkcdvewvDAEDPLFLLYTSGSTGKPKGVLHTTGGYM-VYSATTfkHAFDYKPTDIywctadcgWITGHSYV------- 407
Cdd:cd17643 91 ---------DPDDLAYVIYTSGSTGRPKGVVVSHANVLaLFAATQ--RWFGFNEDDV--------WTLFHSYAfdfsvwe 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 408 TYGPLLNGATVLVfegAPNYP--DPGRCWDIVDKYGVTIFYTAPTLIRSLM----RDGTEyvarysRKSLR--VLGsvGE 479
Cdd:cd17643 152 IWGALLHGGRLVV---VPYEVarSPEDFARLLRDEGVTVLNQTPSAFYQLVeaadRDGRD------PLALRyvIFG--GE 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 480 PINPTAWRWFYDVIGDSRCPISDTWWQTETGGFM----ITP--LPGAWPQKPGsATFPFFGVQpvIVDEKGREMEGECSG 553
Cdd:cd17643 221 ALEAAMLRPWAGRFGLDRPQLVNMYGITETTVHVtfrpLDAadLPAAAASPIG-RPLPGLRVY--VLDADGRPVPPGVVG 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 554 YLCIkkSWPGAFRTlYGDKERYETTYF--KPFAG----YYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESAL 627
Cdd:cd17643 298 ELYV--SGAGVARG-YLGRPELTAERFvaNPFGGpgsrMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAAL 374
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1205963319 628 VSHPKCAEAAVVGIDHEVKGQGIYAFVTLVDGvpySDDLRKSLVMTVRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRIL 706
Cdd:cd17643 375 ATHPSVRDAAVIVREDEPGDTRLVAYVVADDG---AAADIAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
341-707 |
8.57e-30 |
|
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: 123.25 E-value: 8.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 341 VEWVDAEDP---LFLLYTSGSTGKPKGVLHTTGGYMVYSATTFKhAFDYKPTDIYWCTADCGWITGHSYVtYGPLLNGAT 417
Cdd:cd17649 85 AGLLLTHHPrqlAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAE-RYGLTPGDRELQFASFNFDGAHEQL-LPPLICGAC 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 418 VLVfEGAPNYPDPGRCWDIVDKYGVTIFYTAPTLIRSLMRDGTEYVARySRKSLRVLGSVGEPINP-TAWRWfydvigds 496
Cdd:cd17649 163 VVL-RPDELWASADELAEMVRELGVTVLDLPPAYLQQLAEEADRTGDG-RPPSLRLYIFGGEALSPeLLRRW-------- 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 497 rCPISDTWWQ----TETggfMITPLpgAWPQKPGSATF--------PFFGVQPVIVDEKGREMEGECSGYLCIkkSWPGA 564
Cdd:cd17649 233 -LKAPVRLFNaygpTEA---TVTPL--VWKCEAGAARAgasmpigrPLGGRSAYILDADLNPVPVGVTGELYI--GGEGL 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 565 FRtlyGDKERYETT--------YFKPFAGYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEA 636
Cdd:cd17649 305 AR---GYLGRPELTaerfvpdpFGAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREA 381
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1205963319 637 AVVGIDHEVKGQgIYAFVTLVDGVPYSDD---LRKSLvmtvRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRILR 707
Cdd:cd17649 382 AVVALDGAGGKQ-LVAYVVLRAAAAQPELraqLRTAL----RASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
354-713 |
1.24e-29 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 121.05 E-value: 1.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 354 YTSGSTGKPKGVLHTTGGyMVYSATTFKHAFDYKPTDIYWCTADCGWITGhSYVTYG-PLLNGATVlVFEGAPNYPDPG- 431
Cdd:cd05944 9 HTGGTTGTPKLAQHTHSN-EVYNAWMLALNSLFDPDDVLLCGLPLFHVNG-SVVTLLtPLASGAHV-VLAGPAGYRNPGl 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 432 --RCWDIVDKYGVTIFYTAPTLIRSLM-RDGTEYVArysrkSLRVLGSVGEPINPTAWRWFYDVIGdsrCPISDTWWQTE 508
Cdd:cd05944 86 fdNFWKLVERYRITSLSTVPTVYAALLqVPVNADIS-----SLRFAMSGAAPLPVELRARFEDATG---LPVVEGYGLTE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 509 TGGFMITPLPGAwPQKPGSA--TFPFFGVQPVIVDEKG---REMEGECSGYLCIKKswPGAFRtLYGDKERYETTYFKPf 583
Cdd:cd05944 158 ATCLVAVNPPDG-PKRPGSVglRLPYARVRIKVLDGVGrllRDCAPDEVGEICVAG--PGVFG-GYLYTEGNKNAFVAD- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 584 aGYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAVVGIDHEVKGQGIYAFVTLVDGVPYS 663
Cdd:cd05944 233 -GWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGAVVE 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1205963319 664 DDlrkSLVMTVRSQIGAFAA-PDKIHWAPGLPKTRSGKIMRRILRKIASRQ 713
Cdd:cd05944 312 EE---ELLAWARDHVPERAAvPKHIEVLEELPVTAVGKVFKPALRADAIHR 359
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
194-714 |
1.81e-29 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 123.70 E-value: 1.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 194 TYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAEALAQRVIDCKPKVVITCNA 273
Cdd:PRK06087 51 TYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFAPTL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 274 VKRG---LKIIFLKDIVDaSLDESAknGVDVgicLTYENQS-ALNKVDTRWTTgrdvwwqdvVPDFPTkcdvewVDAEDP 349
Cdd:PRK06087 131 FKQTrpvDLILPLQNQLP-QLQQIV--GVDK---LAPATSSlSLSQIIADYEP---------LTTAIT------THGDEL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 350 LFLLYTSGSTGKPKGVLHTTGGyMVYSATTFKHAFDYKPTDIYWCTADCGWITGHSYVTYGPLLNGATVLVFEgapnYPD 429
Cdd:PRK06087 190 AAVLFTSGTEGLPKGVMLTHNN-ILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLD----IFT 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 430 PGRCWDIVDKYGVTIFYTAPTLIRSLMRDGTEYVARYSrkSLRVLGSVGEPInPT-----AWRWfydviGDSRCPIsdtW 504
Cdd:PRK06087 265 PDACLALLEQQRCTCMLGATPFIYDLLNLLEKQPADLS--ALRFFLCGGTTI-PKkvareCQQR-----GIKLLSV---Y 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 505 WQTETGGFMITPLPGAWPQKPGSATFPFFGVQPVIVDEKGREMEGECSGYLCIKKswPGAFRTLYGDKERyeTTYFKPFA 584
Cdd:PRK06087 334 GSTESSPHAVVNLDDPLSRFMHTDGYAAAGVEIKVVDEARKTLPPGCEGEEASRG--PNVFMGYLDEPEL--TARALDEE 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 585 GYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAVVGIDHEVKGQGIYAFVTLVDGVpYSD 664
Cdd:PRK06087 410 GWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVLKAPH-HSL 488
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1205963319 665 DLRKSLVMTVRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKIASRQL 714
Cdd:PRK06087 489 TLEEVVAFFSRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRKDIMRRL 538
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
187-706 |
4.00e-29 |
|
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: 121.85 E-value: 4.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 187 PSQDGKLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAEALAQRVIDCKPK 266
Cdd:cd05923 23 PARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEMT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 267 VVITCNA-------VKRGLKIIFLKDIVDASLDESAKngvdvgicltyenqsalnkvdtrwttgrdvwwqDVVPDFPTKc 339
Cdd:cd05923 103 AAVIAVDaqvmdaiFQSGVRVLALSDLVGLGEPESAG---------------------------------PLIEDPPRE- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 340 dvewvdAEDPLFLLYTSGSTGKPKGVL---HTTGGYMVYSATTFKHAFDYKPTDIywctadcGWITGHSYVTYGPLLNGA 416
Cdd:cd05923 149 ------PEQPAFVFYTSGTTGLPKGAVipqRAAESRVLFMSTQAGLRHGRHNVVL-------GLMPLYHVIGFFAVLVAA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 417 tvLVFEG---APNYPDPGRCWDIVDKYGVTIFYTAPTLIRSLMrdGTEYVARYSRKSLRVLGSVGEPINPTAWRWFYDVI 493
Cdd:cd05923 216 --LALDGtyvVVEEFDPADALKLIEQERVTSLFATPTHLDALA--AAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQHL 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 494 GDsrcPISDTWWQTETGGFMITPLPgawpqKPGSATFPFFGVQPVIVDEKGREME----GEcSGYLCIKKSWPGAFRtly 569
Cdd:cd05923 292 PG---EKVNIYGTTEAMNSLYMRDA-----RTGTEMRPGFFSEVRIVRIGGSPDEalanGE-EGELIVAAAADAAFT--- 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 570 GDKERYETTYFKPFAGYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAVVGIDHEVKGQG 649
Cdd:cd05923 360 GYLNQPEATAKKLQDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQS 439
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1205963319 650 IYAFVTLVDGVPYSDDLRKslvMTVRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRIL 706
Cdd:cd05923 440 VTACVVPREGTLSADELDQ---FCRASELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
194-707 |
4.30e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 121.84 E-value: 4.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 194 TYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAEALAQRVIDCKPKVVITcna 273
Cdd:PRK09088 24 TYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLLLG--- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 274 vkrglkiiflkdivDASLDESAKNGVDVgicltyenqsalnkvdtrwttgrDVWWQDVvpDFPTKCDVEWVDAEDPLFLL 353
Cdd:PRK09088 101 --------------DDAVAAGRTDVEDL-----------------------AAFIASA--DALEPADTPSIPPERVSLIL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 354 YTSGSTGKPKGVlhttggyMVYSATTFKHAFDYKPT------DIYWCTADCGWITGHSYVTYGPLLNGATVLVFEGApny 427
Cdd:PRK09088 142 FTSGTSGQPKGV-------MLSERNLQQTAHNFGVLgrvdahSSFLCDAPMFHIIGLITSVRPVLAVGGSILVSNGF--- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 428 pDPGRC--WDIVDKYGVTIFYTAPTLIRSLmRDGTEYVARYSRkSLRVLGSVGEPINPTAWRWFYDvigdSRCPISDTWW 505
Cdd:PRK09088 212 -EPKRTlgRLGDPALGITHYFCVPQMAQAF-RAQPGFDAAALR-HLTALFTGGAPHAAEDILGWLD----DGIPMVDGFG 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 506 QTETGGFMITPL-PGAWPQKPGSATFPFFGVQPVIVDEKGREMEGECSGYLCIKKswPGAFRTLYGDKEryETTYFKPFA 584
Cdd:PRK09088 285 MSEAGTVFGMSVdCDVIRAKAGAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRG--PNLSPGYWRRPQ--ATARAFTGD 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 585 GYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAVVGIDHEVKGQGIYAFVTLVDGVPYS- 663
Cdd:PRK09088 361 GWFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAPLDl 440
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1205963319 664 DDLRKSLVmtvrSQIGAFAAPDKIHWAPGLPKTRSGKIMRRILR 707
Cdd:PRK09088 441 ERIRSHLS----TRLAKYKVPKHLRLVDALPRTASGKLQKARLR 480
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
190-709 |
5.95e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 121.96 E-value: 5.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 190 DGKLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAEALAqrviDCkpkvvi 269
Cdd:PRK07788 72 RGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQLA----EV------ 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 270 tcnAVKRGLKIIFLKDIVDASLDESAKngvDVGICLTyenqsalnkvdtrWTTGRDVWwQDVVPDFPTKCDVEWVDAEDP 349
Cdd:PRK07788 142 ---AAREGVKALVYDDEFTDLLSALPP---DLGRLRA-------------WGGNPDDD-EPSGSTDETLDDLIAGSSTAP 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 350 L--------FLLYTSGSTGKPKGVLHTT------------------GGYMVYSATTFkHAfdykptdiyWCTADCGWITG 403
Cdd:PRK07788 202 LpkppkpggIVILTSGTTGTPKGAPRPEpsplaplagllsrvpfraGETTLLPAPMF-HA---------TGWAHLTLAMA 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 404 HsyvtygpllnGATVLV---FegapnypDPGRCWDIVDKYGVTIFYTAPTLIRSLMRDGTEYVARYSRKSLRVLGSVGEP 480
Cdd:PRK07788 272 L----------GSTVVLrrrF-------DPEATLEDIAKHKATALVVVPVMLSRILDLGPEVLAKYDTSSLKIIFVSGSA 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 481 INPTAWRWFYDVIGDSRCpisDTWWQTETGgFMITPLPGAWPQKPGSATFPFFGVQPVIVDEKGREMEGECSGYLCIKKS 560
Cdd:PRK07788 335 LSPELATRALEAFGPVLY---NLYGSTEVA-FATIATPEDLAEAPGTVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNG 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 561 WPGAFRTLYGDKERYEttyfkpfaGYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAVVG 640
Cdd:PRK07788 411 FPFEGYTDGRDKQIID--------GLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIG 482
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 641 IDHEVKGQGIYAFVTLVDGVPY-SDDLRKSlvmtVRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKI 709
Cdd:PRK07788 483 VDDEEFGQRLRAFVVKAPGAALdEDAIKDY----VRDNLARYKVPRDVVFLDELPRNPTGKVLKRELREM 548
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
190-706 |
7.11e-29 |
|
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: 120.84 E-value: 7.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 190 DGKLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAEALAQRVIDCKPKVVI 269
Cdd:cd12114 10 DGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARLVL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 270 TCnavkrglkiiflkdivdaslDESAKNGVDVgICLTYENQSAlnkvdtrwttgrdvwwqDVVPDFPTKCDVewvDAEDP 349
Cdd:cd12114 90 TD--------------------GPDAQLDVAV-FDVLILDLDA-----------------LAAPAPPPPVDV---APDDL 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 350 LFLLYTSGSTGKPKGVLHTTGGYM-VYSATTFKHAFDykPTDIYWCTADCGwitgHSYVTY---GPLLNGATvLVFEGAP 425
Cdd:cd12114 129 AYVIFTSGSTGTPKGVMISHRAALnTILDINRRFAVG--PDDRVLALSSLS----FDLSVYdifGALSAGAT-LVLPDEA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 426 NYPDPGRCWDIVDKYGVTIFYTAPTLIRSLMRDGTEYVARYSrkSLR-VLGSvGEPIN---PTAWRwfyDVIGDSRcPIS 501
Cdd:cd12114 202 RRRDPAHWAELIERHGVTLWNSVPALLEMLLDVLEAAQALLP--SLRlVLLS-GDWIPldlPARLR---ALAPDAR-LIS 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 502 ------DTWWQTEtggFMITPLPGAWPQKP-GsatFPFFGVQPVIVDEKGREMEGECSGYLCIkkSWPGAFRTLYGDKER 574
Cdd:cd12114 275 lggateASIWSIY---HPIDEVPPDWRSIPyG---RPLANQRYRVLDPRGRDCPDWVPGELWI--GGRGVALGYLGDPEL 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 575 YETTYFKPFAG--YYFSGD-GCSRDkDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAVVGIDhEVKGQGIY 651
Cdd:cd12114 347 TAARFVTHPDGerLYRTGDlGRYRP-DGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLG-DPGGKRLA 424
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1205963319 652 AFVTLVDGVP--YSDDLRKSLVMTVRsqigAFAAPDKIHWAPGLPKTRSGKIMRRIL 706
Cdd:cd12114 425 AFVVPDNDGTpiAPDALRAFLAQTLP----AYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
622-700 |
1.56e-28 |
|
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: 108.79 E-value: 1.56e-28
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1205963319 622 EVESALVSHPKCAEAAVVGIDHEVKGQGIYAFVTLVDGVpysDDLRKSLVMTVRSQIGAFAAPDKIHWAPGLPKTRSGK 700
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGV---ELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
193-709 |
7.51e-28 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 118.71 E-value: 7.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 193 LTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAEALAQRVIDCKPKVVItcn 272
Cdd:PRK06155 47 WTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLV--- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 273 avkrglkiiflkdiVDASLDEsakngvdvgicltyenqsALNKVDTRWTTGRDVWWQDVVPDFPTkcDVEW--------- 343
Cdd:PRK06155 124 --------------VEAALLA------------------ALEAADPGDLPLPAVWLLDAPASVSV--PAGWstaplppld 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 344 -------VDAEDPLFLLYTSGSTGKPKGVLHTtggymvysattfkHAfdykptDIYW----CTADCGWITGHSYVTYGPL 412
Cdd:PRK06155 170 apapaaaVQPGDTAAILYTSGTTGPSKGVCCP-------------HA------QFYWwgrnSAEDLEIGADDVLYTTLPL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 413 -------------LNGATvLVFEgaPNYpDPGRCWDIVDKYGVTIFYTAPTLIRSLmrDGTEYVARYSRKSLRVLGSVGE 479
Cdd:PRK06155 231 fhtnalnaffqalLAGAT-YVLE--PRF-SASGFWPAVRRHGATVTYLLGAMVSIL--LSQPARESDRAHRVRVALGPGV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 480 PinPTAWRWFYDVIGdsrCPISDTWWQTETGGFMITPLPGawpQKPGSATFPFFGVQPVIVDEKGREMEGECSGYLCIKK 559
Cdd:PRK06155 305 P--AALHAAFRERFG---VDLLDGYGSTETNFVIAVTHGS---QRPGSMGRLAPGFEARVVDEHDQELPDGEPGELLLRA 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 560 SWPGAFRTLY-GDKEryETTyfKPFAGYYF-SGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAA 637
Cdd:PRK06155 377 DEPFAFATGYfGMPE--KTV--EAWRNLWFhTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAA 452
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1205963319 638 VVGIDHEVKGQGIYAFVTLVDGVPYSDDlrkSLVMTVRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKI 709
Cdd:PRK06155 453 VFPVPSELGEDEVMAAVVLRDGTALEPV---ALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLREQ 521
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
175-707 |
2.26e-27 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 116.71 E-value: 2.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 175 GDKIAMYWEgnepSQDGK---LTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGF 251
Cdd:PRK08008 21 GHKTALIFE----SSGGVvrrYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 252 SAEALAQRVIDCKPKVVITCNAvkrglkiiFLKdIVDASLDESAkNGVDvGICLTYENQSAlnkvdtrwTTGRDVWWQDV 331
Cdd:PRK08008 97 LREESAWILQNSQASLLVTSAQ--------FYP-MYRQIQQEDA-TPLR-HICLTRVALPA--------DDGVSSFTQLK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 332 VPDFPTKCDVEWVDAEDPLFLLYTSGSTGKPKGVLHTT-----GGYmvYSAttFKHAFDYKptDIYWCTADCGWITGHSY 406
Cdd:PRK08008 158 AQQPATLCYAPPLSTDDTAEILFTSGTTSRPKGVVITHynlrfAGY--YSA--WQCALRDD--DVYLTVMPAFHIDCQCT 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 407 VTYGPLLNGATVLVFEgapNYpDPGRCWDIVDKYGVTIFYTAPTLIRSLM-------------RD--------GTEYVAR 465
Cdd:PRK08008 232 AAMAAFSAGATFVLLE---KY-SARAFWGQVCKYRATITECIPMMIRTLMvqppsandrqhclREvmfylnlsDQEKDAF 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 466 YSRKSLRVLGSVGepinptawrwfydvigdsrcpisdtwwQTETGGFMITPLPGA---WPqkpgSATFPFFGVQPVIVDE 542
Cdd:PRK08008 308 EERFGVRLLTSYG---------------------------MTETIVGIIGDRPGDkrrWP----SIGRPGFCYEAEIRDD 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 543 KGREMEGECSGYLCIKkSWPGA--FRTLYGDKERYETTyFKPfAGYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGT 620
Cdd:PRK08008 357 HNRPLPAGEIGEICIK-GVPGKtiFKEYYLDPKATAKV-LEA-DGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSC 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 621 AEVESALVSHPKCAEAAVVGIDHEVKGQGIYAFVTLVDGVPYSDDlrkSLVMTVRSQIGAFAAPDKIHWAPGLPKTRSGK 700
Cdd:PRK08008 434 VELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEE---EFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGK 510
|
....*..
gi 1205963319 701 IMRRILR 707
Cdd:PRK08008 511 IIKKNLK 517
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
164-707 |
2.68e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 116.62 E-value: 2.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 164 NAVDRHveagnGDKIAMYWEgnepsqDGKLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAV 243
Cdd:PRK06188 20 SALKRY-----PDRPALVLG------DTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 244 HSVVFAGFSAEALAQRVIDCKPKVVITCNA--VKRGLkiiflkdivdaSLDESAkngvdvgicltyenqSALNKVDT--R 319
Cdd:PRK06188 89 RTALHPLGSLDDHAYVLEDAGISTLIVDPApfVERAL-----------ALLARV---------------PSLKHVLTlgP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 320 WTTGRDVWWQ-DVVPDFPTKCDVewvDAEDPLFLLYTSGSTGKPKGVLHTTGGyMVYSATtfkhafdykptdiyWCTADC 398
Cdd:PRK06188 143 VPDGVDLLAAaAKFGPAPLVAAA---LPPDIAGLAYTGGTTGKPKGVMGTHRS-IATMAQ--------------IQLAEW 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 399 GWITGHSYVTYGP------------LLNGATVLVFEGApnypDPGRCWDIVDKYGVTIFYTAPTLIRSLMRDGTEYVARY 466
Cdd:PRK06188 205 EWPADPRFLMCTPlshaggafflptLLRGGTVIVLAKF----DPAEVLRAIEEQRITATFLVPTMIYALLDHPDLRTRDL 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 467 SrkSLRVLGSVGEPINPTAWRWFYDVIGdsrcPI-SDTWWQTETGGFmITPLP-----GAWPQKPGSATFPFFGVQPVIV 540
Cdd:PRK06188 281 S--SLETVYYGASPMSPVRLAEAIERFG----PIfAQYYGQTEAPMV-ITYLRkrdhdPDDPKRLTSCGRPTPGLRVALL 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 541 DEKGREME-GEcSGYLCIKKswPGAFRTLYGDKERYETTyFKpfAGYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIG 619
Cdd:PRK06188 354 DEDGREVAqGE-VGEICVRG--PLVMDGYWNRPEETAEA-FR--DGWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVF 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 620 TAEVESALVSHPKCAEAAVVGIDHEVKGQGIYAFVTLVDGVPYSDDlrkSLVMTVRSQIGAFAAPDKIHWAPGLPKTRSG 699
Cdd:PRK06188 428 PREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPGAAVDAA---ELQAHVKERKGSVHAPKQVDFVDSLPLTALG 504
|
....*...
gi 1205963319 700 KIMRRILR 707
Cdd:PRK06188 505 KPDKKALR 512
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
168-701 |
5.15e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 116.29 E-value: 5.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 168 RHVEAGNGDKIAMYWEGNEpsqdgkLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVV 247
Cdd:PRK06178 40 RAWARERPQRPAIIFYGHV------ITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 248 FAGFSAEALAQRVIDCKPKVVITCNAvkrglkiifLKDIVDASLDESA-KNGVDVGICLTYENQSALNKVDT-RWTTGRD 325
Cdd:PRK06178 114 SPLFREHELSYELNDAGAEVLLALDQ---------LAPVVEQVRAETSlRHVIVTSLADVLPAEPTLPLPDSlRAPRLAA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 326 VWWQDVVP---DFPTKCDVEWVDAEDPLFLLYTSGSTGKPKGVLHTTGgYMVYSATTFKHAFDYKPTD--------IYWc 394
Cdd:PRK06178 185 AGAIDLLPalrACTAPVPLPPPALDALAALNYTGGTTGMPKGCEHTQR-DMVYTAAAAYAVAVVGGEDsvflsflpEFW- 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 395 tadcgwITGHSYVTYGPLLNGATVLVFegapNYPDPGRCWDIVDKYGVTIfyTAPTL--IRSLMRdgTEYVARYSRKSLR 472
Cdd:PRK06178 263 ------IAGENFGLLFPLFSGATLVLL----ARWDAVAFMAAVERYRVTR--TVMLVdnAVELMD--HPRFAEYDLSSLR 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 473 VLGSVG--EPINPTAWRwfydvigdsRcpisdtwWQTETGGFMITplpGAW--PQKPGSATF--------------PFFG 534
Cdd:PRK06178 329 QVRVVSfvKKLNPDYRQ---------R-------WRALTGSVLAE---AAWgmTETHTCDTFtagfqdddfdllsqPVFV 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 535 VQPV------IVD-EKGREM----EGEcsgyLCIKKswPGAFRTLYGdKERYETTYFKpfAGYYFSGDGCSRDKDGY-HW 602
Cdd:PRK06178 390 GLPVpgtefkICDfETGELLplgaEGE----IVVRT--PSLLKGYWN-KPEATAEALR--DGWLHTGDIGKIDEQGFlHY 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 603 LtGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAVVGIDHEVKGQGIYAFVTLVDGVPYSDDlrkSLVMTVRSQIGAFA 682
Cdd:PRK06178 461 L-GRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGADLTAA---ALQAWCRENMAVYK 536
|
570
....*....|....*....
gi 1205963319 683 APdKIHWAPGLPKTRSGKI 701
Cdd:PRK06178 537 VP-EIRIVDALPMTATGKV 554
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
164-708 |
7.60e-27 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 115.64 E-value: 7.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 164 NAVDRHVEAgNGDKIAMYWEGNEpsqdgkLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAV 243
Cdd:PRK07786 21 NQLARHALM-QPDAPALRFLGNT------TTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 244 HSVVFAGFSAEALAQRVIDCKPKVVITcNAVKRGLKIIFLKDIVDASLDESAKNGVDVGIcLTYENQSAlnkvdtrwTTG 323
Cdd:PRK07786 94 AVPVNFRLTPPEIAFLVSDCGAHVVVT-EAALAPVATAVRDIVPLLSTVVVAGGSSDDSV-LGYEDLLA--------EAG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 324 RDVWWQDVVPDFPTkcdvewvdaedplFLLYTSGSTGKPKG-VL-HTTggyMVYSATTFKHAFDY-KPTDIYWCTADCGW 400
Cdd:PRK07786 164 PAHAPVDIPNDSPA-------------LIMYTSGTTGRPKGaVLtHAN---LTGQAMTCLRTNGAdINSDVGFVGVPLFH 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 401 ITGHSYVTYGPLLNGATVLVFEGAPnypDPGRCWDIVDKYGVTIFYTAPTLIRSLMRDGTeyvARYSRKSLRVLGSVGEP 480
Cdd:PRK07786 228 IAGIGSMLPGLLLGAPTVIYPLGAF---DPGQLLDVLEAEKVTGIFLVPAQWQAVCAEQQ---ARPRDLALRVLSWGAAP 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 481 INPTAWRWFYDVIGDSRcpISDTWWQTETGGFMITPLPGAWPQKPGSATFPFFGVQPVIVDEkgrEMEGECSGYLC-IKK 559
Cdd:PRK07786 302 ASDTLLRQMAATFPEAQ--ILAAFGQTEMSPVTCMLLGEDAIRKLGSVGKVIPTVAARVVDE---NMNDVPVGEVGeIVY 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 560 SWPgafrTLYGDKERYETTYFKPFAGYYF-SGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAV 638
Cdd:PRK07786 377 RAP----TLMSGYWNNPEATAEAFAGGWFhSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAV 452
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1205963319 639 VGIDHEVKGQGIYAFVTLVDGvpySDDLR-KSLVMTVRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRK 708
Cdd:PRK07786 453 IGRADEKWGEVPVAVAAVRND---DAALTlEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTELRE 520
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
176-713 |
1.68e-26 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 113.90 E-value: 1.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 176 DKIAMYWEgnepsqDGKLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVhsVVFAG--FSA 253
Cdd:PRK03640 17 DRTAIEFE------EKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAV--AVLLNtrLSR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 254 EALAQRVIDCKPKVVITcnavkrglkiiflkdivdaslDESAKNGVDVGICLTYENQSALNKVDTRWttgrdvwwqdvvp 333
Cdd:PRK03640 89 EELLWQLDDAEVKCLIT---------------------DDDFEAKLIPGISVKFAELMNGPKEEAEI------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 334 dfptkcdVEWVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMvYSATTfkHAFDYKPTDiywctADCgW--------ITGHS 405
Cdd:PRK03640 135 -------QEEFDLDEVATIMYTSGTTGKPKGVIQTYGNHW-WSAVG--SALNLGLTE-----DDC-WlaavpifhISGLS 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 406 YVTYGpLLNGATVLVFEGApnypDPGRCWDIVDKYGVTIFYTAPTLIRSLMRDGTEyvARYSrKSLR--VLGsvGEPINP 483
Cdd:PRK03640 199 ILMRS-VIYGMRVVLVEKF----DAEKINKLLQTGGVTIISVVSTMLQRLLERLGE--GTYP-SSFRcmLLG--GGPAPK 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 484 TawrwFYDVIGDSRCPISDTWWQTETGGFMITPLPGAWPQKPGSATFPFFGVQPVIVDEkGREM----EGE--------C 551
Cdd:PRK03640 269 P----LLEQCKEKGIPVYQSYGMTETASQIVTLSPEDALTKLGSAGKPLFPCELKIEKD-GVVVppfeEGEivvkgpnvT 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 552 SGYLCIKKSWPGAFRTlygdkeryettyfkpfaGYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHP 631
Cdd:PRK03640 344 KGYLNREDATRETFQD-----------------GWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHP 406
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 632 KCAEAAVVGIDHEVKGQGIYAFVtlVDGVPYSDDlrkSLVMTVRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKIAS 711
Cdd:PRK03640 407 GVAEAGVVGVPDDKWGQVPVAFV--VKSGEVTEE---ELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQLVE 481
|
..
gi 1205963319 712 RQ 713
Cdd:PRK03640 482 EM 483
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
188-707 |
3.59e-26 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 113.25 E-value: 3.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 188 SQDGKLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAEALAQRVIDCKPKV 267
Cdd:PRK12406 7 SGDRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 268 VI--------TCNAVKRGLKIIflkdiVDASLDESAKN-GVDVGICLTYENqsalnkvdtrwTTGRDVWWQDVVP-DFPT 337
Cdd:PRK12406 87 LIahadllhgLASALPAGVTVL-----SVPTPPEIAAAyRISPALLTPPAG-----------AIDWEGWLAQQEPyDGPP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 338 KcdvewvdaEDPLFLLYTSGSTGKPKGVLHT--TGGYMVYSATTFKHAFDYKPTDIYWCTadcgwitghsyvtyGPLLNG 415
Cdd:PRK12406 151 V--------PQPQSMIYTSGTTGHPKGVRRAapTPEQAAAAEQMRALIYGLKPGIRALLT--------------GPLYHS 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 416 A------------TVLVFEgaPNYpDPGRCWDIVDKYGVTIFYTAPTLIRSLMRDGTEYVARYSRKSLRVLGSVGEPINP 483
Cdd:PRK12406 209 ApnayglragrlgGVLVLQ--PRF-DPEELLQLIERHRITHMHMVPTMFIRLLKLPEEVRAKYDVSSLRHVIHAAAPCPA 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 484 TAWR----WFYDVIgdsrcpiSDTWWQTETGGfMITPLPGAWPQKPGSATFPFFGVQPVIVDEKGREME-GECSGYLCIK 558
Cdd:PRK12406 286 DVKRamieWWGPVI-------YEYYGSTESGA-VTFATSEDALSHPGTVGKAAPGAELRFVDEDGRPLPqGEIGEIYSRI 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 559 KSWPGaFRTLYGDKERYETTYfkpfAGYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAV 638
Cdd:PRK12406 358 AGNPD-FTYHNKPEKRAEIDR----GGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAV 432
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 639 VGIDHEVKGQGIYAFVTLVDGVPYS-DDLRKSLvmtvRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRILR 707
Cdd:PRK12406 433 FGIPDAEFGEALMAVVEPQPGATLDeADIRAQL----KARLAGYKVPKHIEIMAELPREDSGKIFKRRLR 498
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
190-714 |
8.12e-26 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 114.67 E-value: 8.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 190 DGKLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAEALAQRVIDCKPKVVI 269
Cdd:PRK12316 2026 DQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLL 2105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 270 TCNAVKRGLKIiflkdivdasldesaKNGVdvgICLTYEnqsalnkvdtrwttgRDVWWqdvvPDFPTKCDVEWVDAEDP 349
Cdd:PRK12316 2106 TQRHLLERLPL---------------PAGV---ARLPLD---------------RDAEW----ADYPDTAPAVQLAGENL 2148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 350 LFLLYTSGSTGKPKGV----------LHTTGGYMVYSAT-------TFkhAFDYKPTDIYWctadcgwitghsyvtygPL 412
Cdd:PRK12316 2149 AYVIYTSGSTGLPKGVavshgalvahCQAAGERYELSPAdcelqfmSF--SFDGAHEQWFH-----------------PL 2209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 413 LNGATVLVFEGApnYPDPGRCWDIVDKYGVTIFYTAPT----LIRSLMRDGteyvarySRKSLRVLGSVGEPINPTAWRW 488
Cdd:PRK12316 2210 LNGARVLIRDDE--LWDPEQLYDEMERHGVTILDFPPVylqqLAEHAERDG-------RPPAVRVYCFGGEAVPAASLRL 2280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 489 FYDVIGDSRcpISDTWWQTETggfMITPLpgAW---PQKPGSATFPFFGvQPV------IVDEKGREMEGECSGYLCIKK 559
Cdd:PRK12316 2281 AWEALRPVY--LFNGYGPTEA---VVTPL--LWkcrPQDPCGAAYVPIG-RALgnrrayILDADLNLLAPGMAGELYLGG 2352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 560 SwpGAFRTlYGDKERYETTYF--KPFAG----YYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKC 633
Cdd:PRK12316 2353 E--GLARG-YLNRPGLTAERFvpDPFSAsgerLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAV 2429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 634 AEAAVVGIDhEVKGQGIYAFVTLVDGvpySDDLRKSLVMTVRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKIASRQ 713
Cdd:PRK12316 2430 REAVVVAQD-GASGKQLVAYVVPDDA---AEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPKPDVSQ 2505
|
.
gi 1205963319 714 L 714
Cdd:PRK12316 2506 L 2506
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
352-707 |
1.06e-25 |
|
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: 111.32 E-value: 1.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 352 LLYTSGSTGKPKGVLHTTGGYMVYSATTFKHAFDYKPT--DIYWCTADCGWITGHSyVTYGPLLNGATVLVFEGApnypD 429
Cdd:cd05929 130 MLYSGGTTGRPKGIKRGLPGGPPDNDTLMAAALGFGPGadSVYLSPAPLYHAAPFR-WSMTALFMGGTLVLMEKF----D 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 430 PGRCWDIVDKYGVTIFYTAPTLIRSLMRDGTEYVARYSRKSLRVLGSVGEPINPtawrWFYDVIGDSRCPISDTWWQ-TE 508
Cdd:cd05929 205 PEEFLRLIERYRVTFAQFVPTMFVRLLKLPEAVRNAYDLSSLKRVIHAAAPCPP----WVKEQWIDWGGPIIWEYYGgTE 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 509 TGGFmiTPLPGA-WPQKPGSATFPFFGVQPvIVDEKGREM----EGEcsgylcIKKSWPGAFRTLYgdkeRYETTYFKPF 583
Cdd:cd05929 281 GQGL--TIINGEeWLTHPGSVGRAVLGKVH-ILDEDGNEVppgeIGE------VYFANGPGFEYTN----DPEKTAAARN 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 584 AGYYFS-GDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAVVGIDHEVKGQGIYAFVTLVDGVPY 662
Cdd:cd05929 348 EGGWSTlGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQPAPGADA 427
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1205963319 663 SDDLRKSLVMTVRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRILR 707
Cdd:cd05929 428 GTALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLR 472
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
346-707 |
1.81e-25 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 110.87 E-value: 1.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 346 AEDPL--FLLYTSGSTGKPKGV--------LHTTGGYMVYSATTFkhaFDYKPTDIYWCTADCGWITGHSYVTYGPLLNG 415
Cdd:PRK13390 145 TEQPCgaVMLYSSGTTGFPKGIqpdlpgrdVDAPGDPIVAIARAF---YDISESDIYYSSAPIYHAAPLRWCSMVHALGG 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 416 ATVLvfegAPNYpDPGRCWDIVDKYGVTIFYTAPTLIRSLMRDGTEYVARYSRKSLRVLGSVGEPINPTAWRWFYDVIGd 495
Cdd:PRK13390 222 TVVL----AKRF-DAQATLGHVERYRITVTQMVPTMFVRLLKLDADVRTRYDVSSLRAVIHAAAPCPVDVKHAMIDWLG- 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 496 srcPISDTWWQ-TETGGFMITPLPgAWPQKPGSATFPFFGVQPvIVDEKGREMEGecsgylcikkswpGAFRTLYGDKER 574
Cdd:PRK13390 296 ---PIVYEYYSsTEAHGMTFIDSP-DWLAHPGSVGRSVLGDLH-ICDDDGNELPA-------------GRIGTVYFERDR 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 575 YETTYFK-------------PFagYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAVVGI 641
Cdd:PRK13390 358 LPFRYLNdpektaaaqhpahPF--WTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGV 435
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1205963319 642 DHEVKGQGIYAFVTLVDGVPYSDDLRKSLVMTVRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRILR 707
Cdd:PRK13390 436 PDPEMGEQVKAVIQLVEGIRGSDELARELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
189-716 |
6.31e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 109.45 E-value: 6.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 189 QDGKLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAEALAQRVIDCKPKVV 268
Cdd:PRK06164 32 EDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARWL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 269 itcnAVKRGLKIIFLKDIVDAsLDESAKNGVDVGICLTYENQSALNKVDTRWTtgrdvwwqdVVPDFPTKCDV----EWV 344
Cdd:PRK06164 112 ----VVWPGFKGIDFAAILAA-VPPDALPPLRAIAVVDDAADATPAPAPGARV---------QLFALPDPAPPaaagERA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 345 DAEDPLFLLY-TSGSTGKPKGVLHTTGGyMVYSATTFKHAFDYKPTDIYWCTAD-CGwITGHSYVTyGPLLNGATVL--- 419
Cdd:PRK06164 178 ADPDAGALLFtTSGTTSGPKLVLHRQAT-LLRHARAIARAYGYDPGAVLLAALPfCG-VFGFSTLL-GALAGGAPLVcep 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 420 VFEGApnypdpgRCWDIVDKYGVTIFYTAPTLIRSLMRDGTEyvaRYSRKSLRVLGsvgepinptawrwFYDVIGDSRcp 499
Cdd:PRK06164 255 VFDAA-------RTARALRRHRVTHTFGNDEMLRRILDTAGE---RADFPSARLFG-------------FASFAPALG-- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 500 isDTWWQTETGGFMITPLPGAwpqkpgSATFPFFGVQPVIVDEK------GREMEGEC--------SGYLC-------IK 558
Cdd:PRK06164 310 --ELAALARARGVPLTGLYGS------SEVQALVALQPATDPVSvrieggGRPASPEArvrardpqDGALLpdgesgeIE 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 559 KSWPGAFRTLYGDKERYETTyFKPfAGYYFSGD-GCSRDKDGYHWLTgRVDDVINVSGHRIGTAEVESALVSHPKCAEAA 637
Cdd:PRK06164 382 IRAPSLMRGYLDNPDATARA-LTD-DGYFRTGDlGYTRGDGQFVYQT-RMGDSLRLGGFLVNPAEIEHALEALPGVAAAQ 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 638 VVGIDHEVKGQgIYAFVTLVDGVPYSDdlrKSLVMTVRSQIGAFAAPDKIHWAPGLPKTRSG---KIMRRILRKIASRQL 714
Cdd:PRK06164 459 VVGATRDGKTV-PVAFVIPTDGASPDE---AGLMAACREALAGFKVPARVQVVEAFPVTESAngaKIQKHRLREMAQARL 534
|
..
gi 1205963319 715 DE 716
Cdd:PRK06164 535 AA 536
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
192-706 |
7.71e-25 |
|
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: 108.32 E-value: 7.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 192 KLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAEALAQRVIDCKPKVVITc 271
Cdd:cd17650 12 QLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLEDSGAKLLLT- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 272 navkrglkiiflkdivdasldesakngvdvgicltyenqsalnkvdtrwttgrdvwwqdvvpdfptkcdvewvDAEDPLF 351
Cdd:cd17650 91 -------------------------------------------------------------------------QPEDLAY 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 352 LLYTSGSTGKPKGVLHTTGGYM-VYSATTFKHAFDYKPTDIYWctadcgwITGHSY-VTYG----PLLNGATVLVfegAP 425
Cdd:cd17650 98 VIYTSGTTGKPKGVMVEHRNVAhAAHAWRREYELDSFPVRLLQ-------MASFSFdVFAGdfarSLLNGGTLVI---CP 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 426 N--YPDPGRCWDIVDKYGVTIFYTAPTLIRSLMrdgtEYVARYSRK--SLRVLgSVGEPINPTAW-RWFYDVIGdSRCPI 500
Cdd:cd17650 168 DevKLDPAALYDLILKSRITLMESTPALIRPVM----AYVYRNGLDlsAMRLL-IVGSDGCKAQDfKTLAARFG-QGMRI 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 501 SDTWWQTET---GGFMITPLPGAwpqkPGSATFP----FFGVQPVIVDEKGREMEGECSGYLCIKKSwpGAFRTLYGD-- 571
Cdd:cd17650 242 INSYGVTEAtidSTYYEEGRDPL----GDSANVPigrpLPNTAMYVLDERLQPQPVGVAGELYIGGA--GVARGYLNRpe 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 572 --KERYETTYFKPFAGYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAVVgIDHEVKGQG 649
Cdd:cd17650 316 ltAERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVA-VREDKGGEA 394
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1205963319 650 IYAFVTLVDGVPYSDDLRKSLVmtvrSQIGAFAAPDKIHWAPGLPKTRSGKIMRRIL 706
Cdd:cd17650 395 RLCAYVVAAATLNTAELRAFLA----KELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
344-708 |
8.50e-25 |
|
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: 107.43 E-value: 8.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 344 VDAEDPLFLLYTSGSTGKPKGVLHTTGGYMvYSATTFKHAFDYKPTDIYWCTADCGWITGHSYVTYGpLLNGATVLVFEG 423
Cdd:cd05912 74 VKLDDIATIMYTSGTTGKPKGVQQTFGNHW-WSAIGSALNLGLTEDDNWLCALPLFHISGLSILMRS-VIYGMTVYLVDK 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 424 ApnypDPGRCWDIVDKYGVTIFYTAPTLIRSLMRDGTEyvaRYSrKSLR--VLGsvGEPINPTAWRwfydvigdsRC--- 498
Cdd:cd05912 152 F----DAEQVLHLINSGKVTIISVVPTMLQRLLEILGE---GYP-NNLRciLLG--GGPAPKPLLE---------QCkek 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 499 --PISDTWWQTETGGFMITPLPGAWPQKPGSATFPFFGVQPVIVDEKGREME-GEcsgyLCIKKS--WPGAFRTLYGDKE 573
Cdd:cd05912 213 giPVYQSYGMTETCSQIVTLSPEDALNKIGSAGKPLFPVELKIEDDGQPPYEvGE----ILLKGPnvTKGYLNRPDATEE 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 574 RYETTYFKpfagyyfSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAVVGIDHEVKGQGIYAF 653
Cdd:cd05912 289 SFENGWFK-------TGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAF 361
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1205963319 654 VtlVDGVPYSDDlrkSLVMTVRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRK 708
Cdd:cd05912 362 V--VSERPISEE---ELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHELKQ 411
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
176-709 |
1.31e-24 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 108.02 E-value: 1.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 176 DKIAMYweGNEPSqdgkLTYSELLEKVCQLSNYLK-SVGVGKGDAVVIYLPMLMELPIAMLACARIGAVhsvvfagfsae 254
Cdd:PRK06839 17 DRIAII--TEEEE----MTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECI----------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 255 alaqrvidckpkvvitcnAVKRGLKIiflkdiVDASLDESAKNGVDVGICLTYENQSALNKVDTRWTTGRDVWwqdvVPD 334
Cdd:PRK06839 80 ------------------AVPLNIRL------TENELIFQLKDSGTTVLFVEKTFQNMALSMQKVSYVQRVIS----ITS 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 335 FPTKCDVEWVDAED-----PLFLLYTSGSTGKPKGVLHTTGGyMVYSATTFKHAFDYKPTDIYWCTADCGWITGHSYVTY 409
Cdd:PRK06839 132 LKEIEDRKIDNFVEknesaSFIICYTSGTTGKPKGAVLTQEN-MFWNALNNTFAIDLTMHDRSIVLLPLFHIGGIGLFAF 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 410 GPLLNGATVLVfegaPNYPDPGRCWDIVDKYGVTIFYTAPT----LIRSLMRDGTEyvarysrkslrvLGSVgepinpta 485
Cdd:PRK06839 211 PTLFAGGVIIV----PRKFEPTKALSMIEKHKVTVVMGVPTihqaLINCSKFETTN------------LQSV-------- 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 486 wRWFYDviGDSRCPI-------------SDTWWQTETGG--FMITPLPGAwpQKPGSATFPFFGVQPVIVDEKGREMEGE 550
Cdd:PRK06839 267 -RWFYN--GGAPCPEelmrefidrgflfGQGFGMTETSPtvFMLSEEDAR--RKVGSIGKPVLFCDYELIDENKNKVEVG 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 551 CSGYLCIKKswPGAFRTLYGDKERYETTYFKpfaGYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSH 630
Cdd:PRK06839 342 EVGELLIRG--PNVMKEYWNRPDATEETIQD---GWLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKL 416
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1205963319 631 PKCAEAAVVGIDHEVKGQGIYAFVTLVDGVPYSDdlrKSLVMTVRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKI 709
Cdd:PRK06839 417 SDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIE---KDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVNQ 492
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
176-714 |
2.31e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 107.17 E-value: 2.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 176 DKIAMYWEgnepsqDGKLTYSELLEKVCQLSNYLKSVGvGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAEA 255
Cdd:PRK07638 16 NKIAIKEN------DRVLTYKDWFESVCKVANWLNEKE-SKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 256 LAQRVIDCKPKVVITcnavkrglKIIFLKDIVDA-----SLDEsakngvdvgicltyenqsalnkvdtrwttgrdvWWQD 330
Cdd:PRK07638 89 LKERLAISNADMIVT--------ERYKLNDLPDEegrviEIDE---------------------------------WKRM 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 331 V---VPDFPTKCDVEwvdaEDPLFLLYTSGSTGKPKGVLHTTGGYMvYSATTFKHAFDYKPTDIYWctadcgwITG---H 404
Cdd:PRK07638 128 IekyLPTYAPIENVQ----NAPFYMGFTSGSTGKPKAFLRAQQSWL-HSFDCNVHDFHMKREDSVL-------IAGtlvH 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 405 SYVTYGP---LLNGATVLVFegaPNYpDPGRCWDIVDKYGVTIFYTAPTLIRSLMRdgteyVARYSRKSLRVLGSVGE-- 479
Cdd:PRK07638 196 SLFLYGAistLYVGQTVHLM---RKF-IPNQVLDKLETENISVMYTVPTMLESLYK-----ENRVIENKMKIISSGAKwe 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 480 --------PINPTAWRwfYDVIGDSRCpisdtwwqtetgGFMITPLPGAWPQKPGSATFPFFGVQPVIVDEKGREMEGEC 551
Cdd:PRK07638 267 aeakekikNIFPYAKL--YEFYGASEL------------SFVTALVDEESERRPNSVGRPFHNVQVRICNEAGEEVQKGE 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 552 SGYLCIKKswPGAFRTLYGDKERYETTyfkPFAGYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHP 631
Cdd:PRK07638 333 IGTVYVKS--PQFFMGYIIGGVLAREL---NADGWMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHP 407
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 632 KCAEAAVVGIDHEVKGQgiyAFVTLVDGVPYSDDLRKSLvmtvRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKIAS 711
Cdd:PRK07638 408 AVDEIVVIGVPDSYWGE---KPVAIIKGSATKQQLKSFC----LQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAKSWIE 480
|
...
gi 1205963319 712 RQL 714
Cdd:PRK07638 481 NQE 483
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
189-714 |
4.88e-24 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 107.17 E-value: 4.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 189 QDGKLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAEALAQRVIDCKPKVV 268
Cdd:PRK12583 42 QALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 269 ITCNAVKRGLKIiflkDIVDASLDESAKNGVDVGICLTYENQSALNKVDTRWTTGRDVWwQDVV--PDFPTKCDVEWV-- 344
Cdd:PRK12583 122 ICADAFKTSDYH----AMLQELLPGLAEGQPGALACERLPELRGVVSLAPAPPPGFLAW-HELQarGETVSREALAERqa 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 345 --DAEDPLFLLYTSGSTGKPKGVLHT-----TGGYMVYSATTF-KHAFDYKPTDIYWCTadcgwitGHSYVTYGPLLNGA 416
Cdd:PRK12583 197 slDRDDPINIQYTSGTTGFPKGATLShhnilNNGYFVAESLGLtEHDRLCVPVPLYHCF-------GMVLANLGCMTVGA 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 417 TVLVfegaPN-YPDPGRCWDIVDKYGVTIFYTAPTLIRSLMrDGTEYvARYSRKSLRVLGSVGEPINPTAWRwfyDVIGD 495
Cdd:PRK12583 270 CLVY----PNeAFDPLATLQAVEEERCTALYGVPTMFIAEL-DHPQR-GNFDLSSLRTGIMAGAPCPIEVMR---RVMDE 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 496 SRCP-ISDTWWQTETGGfmITPLPGAWPQKPGSATfPFFGVQP----VIVDEKG----REMEGE-CS-GYLCIKKSWPGA 564
Cdd:PRK12583 341 MHMAeVQIAYGMTETSP--VSLQTTAADDLERRVE-TVGRTQPhlevKVVDPDGatvpRGEIGElCTrGYSVMKGYWNNP 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 565 FRTLYG-DKEryettyfkpfaGYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAVVGIDH 643
Cdd:PRK12583 418 EATAESiDED-----------GWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPD 486
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1205963319 644 EVKGQGIYAFVTLVDGVPYS-DDLRKslvmTVRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKIASRQL 714
Cdd:PRK12583 487 EKYGEEIVAWVRLHPGHAASeEELRE----FCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMREISIEEL 554
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
348-710 |
1.05e-23 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 102.79 E-value: 1.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 348 DPLFLLYTSGSTGKPKGVLHTTGGyMVYSATTFKHAFDYKPTDIYWCTADCGWITGHSYVTYGPLLNGATVLVFEGAPNY 427
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAAN-LLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLAILVRSLLAGAELVLLERNQALA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 428 PDPGRcwdivdkYGVTIFYTAPTLIRSLMRDGTeyvARYSRKSLRVLGSVGEPINPTAwrwfYDVIGDSRCPISDTWWQT 507
Cdd:cd17630 80 EDLAP-------PGVTHVSLVPTQLQRLLDSGQ---GPAALKSLRAVLLGGAPIPPEL----LERAADRGIPLYTTYGMT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 508 ETGGfMITPLPGAWPQKPGSATfPFFGVQPVIVDEkgremegecsGYLCIKkswpGAfrTLYGDKERYETTYFKPFAGYY 587
Cdd:cd17630 146 ETAS-QVATKRPDGFGRGGVGV-LLPGRELRIVED----------GEIWVG----GA--SLAMGYLRGQLVPEFNEDGWF 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 588 FSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAVVGIDHEVKGQGIYAFVTLVDGVPYSDdlr 667
Cdd:cd17630 208 TTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGPADPAE--- 284
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1205963319 668 ksLVMTVRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKIA 710
Cdd:cd17630 285 --LRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRAWL 325
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
348-703 |
1.12e-23 |
|
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: 102.48 E-value: 1.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 348 DPLFLLYTSGSTGKPKGVLHTTGGYMvysattfkHAFDYKPTDIYWCTADCGWITG---HSYVTYG---PLLNGATVLVF 421
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERSWI--------ESFVCNEDLFNISGEDAILAPGplsHSLFLYGaisALYLGGTFIGQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 422 EGApnypDPGRCWDIVDKYGVTIFYTAPTLIRSLMRDGTeyvarySRKSLRVLGSVGEPINPTAWRWFYDVIGDSRcpIS 501
Cdd:cd17633 73 RKF----NPKSWIRKINQYNATVIYLVPTMLQALARTLE------PESKIKSIFSSGQKLFESTKKKLKNIFPKAN--LI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 502 DTWWQTETGgfMITPLPGAWPQKPGSATFPFFGVQPVIVDEKGREMegecsGYLCIKKswPGAFrTLYGDKERYETTyfk 581
Cdd:cd17633 141 EFYGTSELS--FITYNFNQESRPPNSVGRPFPNVEIEIRNADGGEI-----GKIFVKS--EMVF-SGYVRGGFSNPD--- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 582 pfaGYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAVVGIDHEVKGQgIYAFVTLVDGVP 661
Cdd:cd17633 208 ---GWMSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGE-IAVALYSGDKLT 283
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1205963319 662 YSDDLRKslvmtVRSQIGAFAAPDKIHWAPGLPKTRSGKIMR 703
Cdd:cd17633 284 YKQLKRF-----LKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
347-700 |
1.26e-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: 103.23 E-value: 1.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 347 EDPLFLLYTSGSTGKPKGVLHTTGGYMVYSATTFKHAFDyKPTDIYWCTADCGWITGHSYVTYGPLLNGATVLVFEGAPN 426
Cdd:cd05924 3 ADDLYILYTGGTTGMPKGVMWRQEDIFRMLMGGADFGTG-EFTPSEDAHKAAAAAAGTVMFPAPPLMHGTGSWTAFGGLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 427 YP----------DPGRCWDIVDKYGVTIF------YTAPtLIRSLMRDGTeyvarYSRKSLRVLGSVGEPINPTAWRWFY 490
Cdd:cd05924 82 GGqtvvlpddrfDPEEVWRTIEKHKVTSMtivgdaMARP-LIDALRDAGP-----YDLSSLFAISSGGALLSPEVKQGLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 491 DVIGDSRcpISDTWWQTETGgFMITPLPGawPQKPGSATFPFFGVQPVIVDEKGREME--GECSGYLCIKKSWPGAFrtl 568
Cdd:cd05924 156 ELVPNIT--LVDAFGSSETG-FTGSGHSA--GSGPETGPFTRANPDTVVLDDDGRVVPpgSGGVGWIARRGHIPLGY--- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 569 YGDKERYETTyFKPFAG--YYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAVVGIDHEVK 646
Cdd:cd05924 228 YGDEAKTAET-FPEVDGvrYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERW 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1205963319 647 GQGIYAFVTLVDGVPYSDDlrkSLVMTVRSQIGAFAAPDKIHWAPGLPKTRSGK 700
Cdd:cd05924 307 GQEVVAVVQLREGAGVDLE---ELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
174-707 |
2.20e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 104.58 E-value: 2.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 174 NGDKIAMYWEGNEpsqdgkLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSA 253
Cdd:PRK06145 15 TPDRAALVYRDQE------ISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 254 EALAqrvidckpkvVITCNAvkrGLKIIFlkdiVDASLDESAKNGVDVGICLTYENQSAlnkvdTRWTTGRDvwwqdvvp 333
Cdd:PRK06145 89 DEVA----------YILGDA---GAKLLL----VDEEFDAIVALETPKIVIDAAAQADS-----RRLAQGGL-------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 334 dfptKCDVEWVDAEDPLF-LLYTSGSTGKPKGVLHTTGgymvysattfkhafdykptDIYWCTAD----CGWITGHSYVT 408
Cdd:PRK06145 139 ----EIPPQAAVAPTDLVrLMYTSGTTDRPKGVMHSYG-------------------NLHWKSIDhviaLGLTASERLLV 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 409 YGPL-------LNGATVLVFEGA----PNYpDPGRCWDIVDKYGVTIFYTAPTLIRSLMRDGTEYvaRYSRKSLRVLGSV 477
Cdd:PRK06145 196 VGPLyhvgafdLPGIAVLWVGGTlrihREF-DPEAVLAAIERHRLTCAWMAPVMLSRVLTVPDRD--RFDLDSLAWCIGG 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 478 GEPINPTAWRWFYDVIGDSRcpISDTWWQTETGGFMITPLPGAWPQKPGSATFPFFGVQPVIVDEKGREMEGECSGYLCI 557
Cdd:PRK06145 273 GEKTPESRIRDFTRVFTRAR--YIDAYGLTETCSGDTLMEAGREIEKIGSTGRALAHVEIRIADGAGRWLPPNMKGEICM 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 558 KKswPGAFRTLYGDKERYETTYFkpfAGYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAA 637
Cdd:PRK06145 351 RG--PKVTKGYWKDPEKTAEAFY---GDWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAA 425
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 638 VVGIDHEVKGQGIYAFVTLVDGVPYSDDlrkSLVMTVRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRILR 707
Cdd:PRK06145 426 VIGVHDDRWGERITAVVVLNPGATLTLE---ALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLR 492
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
193-706 |
2.27e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 105.12 E-value: 2.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 193 LTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAEALAQRVIDCKPKVVITCN 272
Cdd:PRK06710 50 ITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCLD 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 273 -------AVKRGLKI--IFLKDIVDasLDESAKNgvdvgICLTYENQSALNKVDTRWTTGRDVWWQDVVPDFPTKCDVEw 343
Cdd:PRK06710 130 lvfprvtNVQSATKIehVIVTRIAD--FLPFPKN-----LLYPFVQKKQSNLVVKVSESETIHLWNSVEKEVNTGVEVP- 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 344 VDAEDPLFLL-YTSGSTGKPKGVLHTTGGYMVYSATTFKHAFDYKP-TDIYWCTADCGWITGHSYVTYGPLLNGATVLVF 421
Cdd:PRK06710 202 CDPENDLALLqYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYNCKEgEEVVLGVLPFFHVYGMTAVMNLSIMQGYKMVLI 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 422 egaPNYpDPGRCWDIVDKYGVTIFYTAPTLIRSLMRdgTEYVARYSRKSLRVLGSVGEPINPTAWRWFYDVIGDSrcpIS 501
Cdd:PRK06710 282 ---PKF-DMKMVFEAIKKHKVTLFPGAPTIYIALLN--SPLLKEYDISSIRACISGSAPLPVEVQEKFETVTGGK---LV 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 502 DTWWQTETGGfmITPLPGAWPQK-PGSATFPFFGVQPVIVD-EKGREMEGECSGYLCIKKSwpgafRTLYGDKERYETTY 579
Cdd:PRK06710 353 EGYGLTESSP--VTHSNFLWEKRvPGSIGVPWPDTEAMIMSlETGEALPPGEIGEIVVKGP-----QIMKGYWNKPEETA 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 580 FKPFAGYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAVVGIDHEVKGQGIYAFVTLVDG 659
Cdd:PRK06710 426 AVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKEG 505
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1205963319 660 VPYSDDlrkSLVMTVRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRIL 706
Cdd:PRK06710 506 TECSEE---ELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
190-716 |
2.58e-23 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 106.78 E-value: 2.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 190 DGKLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAEALAQRVIDCKPKVVI 269
Cdd:PRK12467 3118 DQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLL 3197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 270 TcnavkrglkiiflkdivDASLDEsakngvdvgicltyenQSALNKVDTRWTTGRDVWWQdvvpdFPTKCDVEWVDAEDP 349
Cdd:PRK12467 3198 T-----------------QAHLLE----------------QLPAPAGDTALTLDRLDLNG-----YSENNPSTRVMGENL 3239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 350 LFLLYTSGSTGKPKGV--------LHT---------TGGYMVYSATTFkhAFDYKPTDIYWctadcgwitghsyvtygPL 412
Cdd:PRK12467 3240 AYVIYTSGSTGKPKGVgvrhgalaNHLcwiaeayelDANDRVLLFMSF--SFDGAQERFLW-----------------TL 3300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 413 LNGATVLVfegAPNYP-DPGRCWDIVDKYGVTIFYTAPTLIRSLMRDGTeyVARYSRKSLRVLGsvGEPINPTAW----- 486
Cdd:PRK12467 3301 ICGGCLVV---RDNDLwDPEELWQAIHAHRISIACFPPAYLQQFAEDAG--GADCASLDIYVFG--GEAVPPAAFeqvkr 3373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 487 ----RWFYDVIGDSRCPISDTWWQTETGGfmiTPLPGAWP---QKPGSATFPFFG-VQPVIVDEKGR-EMEGECSGYlci 557
Cdd:PRK12467 3374 klkpRGLTNGYGPTEAVVTVTLWKCGGDA---VCEAPYAPigrPVAGRSIYVLDGqLNPVPVGVAGElYIGGVGLAR--- 3447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 558 kkswpGAFRTLYGDKERYETTyfkPFAG----YYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKC 633
Cdd:PRK12467 3448 -----GYHQRPSLTAERFVAD---PFSGsggrLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSV 3519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 634 AEAAVVGIDHEvKGQGIYAFVTLVDgvpYSDDLRKSLVMTVRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKIASRQ 713
Cdd:PRK12467 3520 REAVVLARDGA-GGKQLVAYVVPAD---PQGDWRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDPDAKG 3595
|
...
gi 1205963319 714 LDE 716
Cdd:PRK12467 3596 SRE 3598
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
175-708 |
6.27e-23 |
|
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: 103.47 E-value: 6.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 175 GDKIAMYWEGNEPSQDGKLTYSELLEKVCQLSNYLKSVGvGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFA---GF 251
Cdd:cd05931 7 PDRPAYTFLDDEGGREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPptpGR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 252 SAEALAQRVIDCKPKVVITCNAVKRGlkiiflkdiVDASLDESAKNGVDVGICltyenqsalnkVDTRWTTGRDVWwqdv 331
Cdd:cd05931 86 HAERLAAILADAGPRVVLTTAAALAA---------VRAFAASRPAAGTPRLLV-----------VDLLPDTSAADW---- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 332 vpdfptkcDVEWVDAEDPLFLLYTSGSTGKPKGVLHTTGGyMVYSATTFKHAFDYKPTDIY--W--CTADCGWITGhsyv 407
Cdd:cd05931 142 --------PPPSPDPDDIAYLQYTSGSTGTPKGVVVTHRN-LLANVRQIRRAYGLDPGDVVvsWlpLYHDMGLIGG---- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 408 TYGPLLNGATVLVFegAPNY--PDPGRcW-DIVDKYGVTIFYtAPTLirslmrdGTEYVARYSRK---------SLRVLG 475
Cdd:cd05931 209 LLTPLYSGGPSVLM--SPAAflRRPLR-WlRLISRYRATISA-APNF-------AYDLCVRRVRDedlegldlsSWRVAL 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 476 SVGEPINPTAWRWFYD--------------------------VIGDSRCPISDTWWQTETGGfmitPLPGAWPQKPGSAT 529
Cdd:cd05931 278 NGAEPVRPATLRRFAEafapfgfrpeafrpsyglaeatlfvsGGPPGTGPVVLRVDRDALAG----RAVAVAADDPAARE 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 530 F-----PFFGVQPVIVD-EKGREME----GE--------CSGYLCIKKSWPGAFRTLYGDKERyettyfkpfaGYYFSGD 591
Cdd:cd05931 354 LvscgrPLPDQEVRIVDpETGRELPdgevGEiwvrgpsvASGYWGRPEATAETFGALAATDEG----------GWLRTGD 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 592 -GCSRdkDGYHWLTGRVDDVINVSGHRIGTAEVE-SALVSHP--KCAEAAVVGIDHEVKGQGIyaFVTLVDGVPYSDD-- 665
Cdd:cd05931 424 lGFLH--DGELYITGRLKDLIIVRGRNHYPQDIEaTAEEAHPalRPGCVAAFSVPDDGEERLV--VVAEVERGADPADla 499
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 1205963319 666 -LRKSLVMTVRSQIGafAAPDKIHWAP--GLPKTRSGKIMRRILRK 708
Cdd:cd05931 500 aIAAAIRAAVAREHG--VAPADVVLVRpgSIPRTSSGKIQRRACRA 543
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
191-710 |
7.22e-23 |
|
C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.
Pssm-ID: 341235 [Multi-domain] Cd Length: 490 Bit Score: 102.79 E-value: 7.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 191 GKLTYSELLEKVCQLSNYLKSVGVGkGDAVVIYLPMLMELPIAMLACARIGAVhsVVFAGFSAEALAQR--VIDCKPKVV 268
Cdd:cd05909 6 TSLTYRKLLTGAIALARKLAKMTKE-GENVGVMLPPSAGGALANFALALSGKV--PVMLNYTAGLRELRacIKLAGIKTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 269 ITCNA------------VKRGLKIIFLKDiVDASLdeSAKNGVDVGICLTYenqsalnkvdtrwttgRDVWWQDVVPDFP 336
Cdd:cd05909 83 LTSKQfieklklhhlfdVEYDARIVYLED-LRAKI--SKADKCKAFLAGKF----------------PPKWLLRIFGVAP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 337 tkcdvewVDAEDPLFLLYTSGSTGKPKGVLHTTGGYM--VYSATTFkhaFDYKPTDIYwctadCGWITG-HSY----VTY 409
Cdd:cd05909 144 -------VQPDDPAVILFTSGSEGLPKGVVLSHKNLLanVEQITAI---FDPNPEDVV-----FGALPFfHSFgltgCLW 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 410 GPLLNGATVlVFegAPNYPDPGRCWDIVDKYGVTIFYTAPTLIRSLMRdgteYVARYSRKSLRVLGSVGEPINPTAWRWF 489
Cdd:cd05909 209 LPLLSGIKV-VF--HPNPLDYKKIPELIYDKKATILLGTPTFLRGYAR----AAHPEDFSSLRLVVAGAEKLKDTLRQEF 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 490 YDVIGdsrCPISDTWWQTETGGFMITPLPGAwPQKPGSATFPFFGVQPVIVDEKGRE--MEGEcSGYLCIKKswPGAFRT 567
Cdd:cd05909 282 QEKFG---IRILEGYGTTECSPVISVNTPQS-PNKEGTVGRPLPGMEVKIVSVETHEevPIGE-GGLLLVRG--PNVMLG 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 568 LYGDKERyetTYFKPFAGYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSH-PKCAEAAVVGIDHEVK 646
Cdd:cd05909 355 YLNEPEL---TSFAFGDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDGRK 431
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1205963319 647 GQGIYAFVTLVDGVPysDDLRKSLvmtVRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKIA 710
Cdd:cd05909 432 GEKIVLLTTTTDTDP--SSLNDIL---KNAGISNLAKPSYIHQVEEIPLLGTGKPDYVTLKALA 490
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
193-706 |
9.57e-23 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 104.65 E-value: 9.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 193 LTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAEALAQRVIDCKPKVVITCN 272
Cdd:PRK12316 537 LDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQS 616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 273 AVKRGLKIiflkdivdasldesaKNGVDVgICLtyeNQSALnkvdtrwttgrdvwWqdvVPDFPTKCDVEWVDAEDPLFL 352
Cdd:PRK12316 617 HLGRKLPL---------------AAGVQV-LDL---DRPAA--------------W---LEGYSEENPGTELNPENLAYV 660
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 353 LYTSGSTGKPKGVLHTTG-----------------GYMVYSATTFkhAFDYKPTDIYWctadcgwitghsyvtygPLLNG 415
Cdd:PRK12316 661 IYTSGSTGKPKGAGNRHRalsnrlcwmqqayglgvGDTVLQKTPF--SFDVSVWEFFW-----------------PLMSG 721
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 416 ATvLVFEGAPNYPDPGRCWDIVDKYGVTIFYTAPTLIRSLMRDGteyvARYSRKSLRVLGSVGEPINPTAW------RW- 488
Cdd:PRK12316 722 AR-LVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDE----DVASCTSLRRIVCSGEALPADAQeqvfakLPq 796
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 489 --FYDVIGDSRCPISDTWWQTETGGFMITPLpGAwpqkpgsatfPFFGVQPVIVDEKGREMEGECSGYLCIKKSwpGAFR 566
Cdd:PRK12316 797 agLYNLYGPTEAAIDVTHWTCVEEGGDSVPI-GR----------PIANLACYILDANLEPVPVGVLGELYLAGR--GLAR 863
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 567 TLYG----DKERYETTYFKPFAGYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAVVGID 642
Cdd:PRK12316 864 GYHGrpglTAERFVPSPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD 943
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1205963319 643 hevkGQGIYAFVTLVDGvpySDDLRKSLVMTVRSQIGAFAAPDkiHWAP--GLPKTRSGKIMRRIL 706
Cdd:PRK12316 944 ----GKQLVGYVVLESE---GGDWREALKAHLAASLPEYMVPA--QWLAleRLPLTPNGKLDRKAL 1000
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
193-708 |
1.18e-22 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 102.37 E-value: 1.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 193 LTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAEALAQRVIDCKPKVVIT-- 270
Cdd:PLN02246 51 YTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLIITqs 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 271 CNAVK-------RGLKIIFLKDIVDASLDESAkngvdvgicLTYENQSALNKVDtrwttgrdvwwqdvvpdfptkcdvew 343
Cdd:PLN02246 131 CYVDKlkglaedDGVTVVTIDDPPEGCLHFSE---------LTQADENELPEVE-------------------------- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 344 VDAEDPLFLLYTSGSTGKPKGVLHTTGGYMvysaTTFKHAFDYKPTDIYWCTAD---CGWITGHSYVTYGPLLN----GA 416
Cdd:PLN02246 176 ISPDDVVALPYSSGTTGLPKGVMLTHKGLV----TSVAQQVDGENPNLYFHSDDvilCVLPMFHIYSLNSVLLCglrvGA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 417 TVLVFegaPNYpDPGRCWDIVDKYGVTIFYTAPTLIRSLMRdgTEYVARYSRKSLRVLGSVGEPINptawRWFYDVIGdS 496
Cdd:PLN02246 252 AILIM---PKF-EIGALLELIQRHKVTIAPFVPPIVLAIAK--SPVVEKYDLSSIRMVLSGAAPLG----KELEDAFR-A 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 497 RCP---ISDTWWQTETG-------GFMITPLPgawpQKPGSATFPFFGVQPVIVD-EKGREMEGECSGYLCIKKswPGAF 565
Cdd:PLN02246 321 KLPnavLGQGYGMTEAGpvlamclAFAKEPFP----VKSGSCGTVVRNAELKIVDpETGASLPRNQPGEICIRG--PQIM 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 566 RTLYGDKERYETTYFKpfAGYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAVVGIDHEV 645
Cdd:PLN02246 395 KGYLNDPEATANTIDK--DGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEV 472
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1205963319 646 KGQGIYAFVTLVDGVPYSDDLRKSLvmtVRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRK 708
Cdd:PLN02246 473 AGEVPVAFVVRSNGSEITEDEIKQF---VAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDLRA 532
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
192-708 |
1.39e-22 |
|
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: 101.99 E-value: 1.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 192 KLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAEALAQRVIDCKPKVVItc 271
Cdd:cd12118 29 RYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVLF-- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 272 navkrglkiiflkdiVDASLDesakngvdvgicltYENQSALNKVDTRWttgrdVWWQDvvpdfptkcdvEWvdaeDPLF 351
Cdd:cd12118 107 ---------------VDREFE--------------YEDLLAEGDPDFEW-----IPPAD-----------EW----DPIA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 352 LLYTSGSTGKPKGVLHTTGGYMVySATTFKHAFDYKPTDIYWCTAD----CGWItghsyVTYGPLLNGATVLVFEGApny 427
Cdd:cd12118 138 LNYTSGTTGRPKGVVYHHRGAYL-NALANILEWEMKQHPVYLWTLPmfhcNGWC-----FPWTVAAVGGTNVCLRKV--- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 428 pDPGRCWDIVDKYGVTIFYTAPTLIrSLMRDGTEYVARysrkslrvlgsvgepinPTAWRWFYDVIGDSrcPISDTWWQT 507
Cdd:cd12118 209 -DAKAIYDLIEKHKVTHFCGAPTVL-NMLANAPPSDAR-----------------PLPHRVHVMTAGAP--PPAAVLAKM 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 508 ETGGFMITPLPG-----------AWpqKPGSATFP--------------FFGVQPVIVDEK---------GREMeGEC-- 551
Cdd:cd12118 268 EELGFDVTHVYGltetygpatvcAW--KPEWDELPteerarlkarqgvrYVGLEEVDVLDPetmkpvprdGKTI-GEIvf 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 552 ------SGYLCIKKSWPGAFRtlygdkeryettyfkpfAGYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVES 625
Cdd:cd12118 345 rgnivmKGYLKNPEATAEAFR-----------------GGWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEG 407
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 626 ALVSHPKCAEAAVVGIDHEVKGQGIYAFVTLVDGVpysdDLRKSLVMT-VRSQIGAFAAPDKIHWAPgLPKTRSGKIMRR 704
Cdd:cd12118 408 VLYKHPAVLEAAVVARPDEKWGEVPCAFVELKEGA----KVTEEEIIAfCREHLAGFMVPKTVVFGE-LPKTSTGKIQKF 482
|
....
gi 1205963319 705 ILRK 708
Cdd:cd12118 483 VLRD 486
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
176-706 |
1.66e-22 |
|
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: 101.64 E-value: 1.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 176 DKIAMYWEgnepsqDGKLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAEA 255
Cdd:cd17655 12 DHTAVVFE------DQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEER 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 256 LAQRVIDCKPKVVITCNAVKrgLKIIFLKDIvDASLDESAKNGVDvgicltyENQSALNKvdtrwttgrdvwwqdvvpdf 335
Cdd:cd17655 86 IQYILEDSGADILLTQSHLQ--PPIAFIGLI-DLLDEDTIYHEES-------ENLEPVSK-------------------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 336 ptkcdvewvdAEDPLFLLYTSGSTGKPKGVLHTTGG-----------YMVYSATTF----KHAFDYKPTDIYwctadcgw 400
Cdd:cd17655 136 ----------SDDLAYVIYTSGSTGKPKGVMIEHRGvvnlvewankvIYQGEHLRValfaSISFDASVTEIF-------- 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 401 itghsyvtyGPLLNGATVLVFEGAPNYPDPGRCwDIVDKYGVTIFYTAPTLIRSL--MRDGTEYvarysrkSLRVLGSVG 478
Cdd:cd17655 198 ---------ASLLSGNTLYIVRKETVLDGQALT-QYIRQNRITIIDLTPAHLKLLdaADDSEGL-------SLKHLIVGG 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 479 EPINPTAWRWFYDVIGDSrCPISDTWWQTETG-GFMITPLPGAWPQKP----GSatfPFFGVQPVIVDEKGREMEGECSG 553
Cdd:cd17655 261 EALSTELAKKIIELFGTN-PTITNAYGPTETTvDASIYQYEPETDQQVsvpiGK---PLGNTRIYILDQYGRPQPVGVAG 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 554 YLCIkkSWPGAFRtlyGDKERYETTYFK----PFAgyyfSGDGCSRDKDGYHWLT-------GRVDDVINVSGHRIGTAE 622
Cdd:cd17655 337 ELYI--GGEGVAR---GYLNRPELTAEKfvddPFV----PGERMYRTGDLARWLPdgnieflGRIDHQVKIRGYRIELGE 407
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 623 VESALVSHPKCAEAAVVGIDHEVKGQGIYAFVTLVDGVPYSdDLRKSLVMTVRS-QIGA-FAAPDKIhwapglPKTRSGK 700
Cdd:cd17655 408 IEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEKELPVA-QLREFLARELPDyMIPSyFIKLDEI------PLTPNGK 480
|
....*.
gi 1205963319 701 IMRRIL 706
Cdd:cd17655 481 VDRKAL 486
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
193-709 |
1.89e-22 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 102.23 E-value: 1.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 193 LTYSELLEKVCQLSNYLKSV-GVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAEALAQRVIDCKPKVVITc 271
Cdd:PLN02574 67 ISYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFT- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 272 navkrglkiiflkdivdaSLDESAKNG-VDVGICLTYENQSaLNKVDTRWTTGRDVWWQDvvPDFptkCDVEWVDAEDPL 350
Cdd:PLN02574 146 ------------------SPENVEKLSpLGVPVIGVPENYD-FDSKRIEFPKFYELIKED--FDF---VPKPVIKQDDVA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 351 FLLYTSGSTGKPKGVLHTTGGY--MVYSATTFKHA-FDYKPTD-IYWCTADCGWITGHSYVTYGPLLNGATVLVFEGApn 426
Cdd:PLN02574 202 AIMYSSGTTGASKGVVLTHRNLiaMVELFVRFEASqYEYPGSDnVYLAALPMFHIYGLSLFVVGLLSLGSTIVVMRRF-- 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 427 ypDPGRCWDIVDKYGVTIFYTAPTLIRSLMRdGTEYVARYSRKSLRVLGSVGEPINPTAWRWFYDVIgdSRCPISDTWWQ 506
Cdd:PLN02574 280 --DASDMVKVIDRFKVTHFPVVPPILMALTK-KAKGVCGEVLKSLKQVSCGAAPLSGKFIQDFVQTL--PHVDFIQGYGM 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 507 TE-----TGGFMITPLpgawpQKPGSATFPFFGVQPVIVD-EKGREMEGECSGYLCIKKswPGAFRTLYGDKERYETTYF 580
Cdd:PLN02574 355 TEstavgTRGFNTEKL-----SKYSSVGLLAPNMQAKVVDwSTGCLLPPGNCGELWIQG--PGVMKGYLNNPKATQSTID 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 581 KPfaGYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAVVGIDHEVKGQGIYAFVTLVDGV 660
Cdd:PLN02574 428 KD--GWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGS 505
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1205963319 661 PYSDDlrkSLVMTVRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKI 709
Cdd:PLN02574 506 TLSQE---AVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELKRS 551
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
166-640 |
3.70e-22 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 101.33 E-value: 3.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 166 VDRHVEAgNGDKIAMYWEGNEPSQDgkLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHS 245
Cdd:COG1022 17 LRRRAAR-FPDRVALREKEDGIWQS--LTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 246 VVFAGFSAEALAQRVIDCKPKVVITCNA--VKRGLKII----FLKDIVdaSLDESAknGVDVGICLTYENQSALnkvdtr 319
Cdd:COG1022 94 PIYPTSSAEEVAYILNDSGAKVLFVEDQeqLDKLLEVRdelpSLRHIV--VLDPRG--LRDDPRLLSLDELLAL------ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 320 wttGRDVWWQDVVPDFPTKcdvewVDAEDPLFLLYTSGSTGKPKGVLHTTGGyMVYSATTFKHAFDYKPTDIY-----WC 394
Cdd:COG1022 164 ---GREVADPAELEARRAA-----VKPDDLATIIYTSGTTGRPKGVMLTHRN-LLSNARALLERLPLGPGDRTlsflpLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 395 tadcgWITGHSyVTYGPLLNGATVlvfegapNYPDPGRcwDIVD---KYGVTIF----------YT--------APTLIR 453
Cdd:COG1022 235 -----HVFERT-VSYYALAAGATV-------AFAESPD--TLAEdlrEVKPTFMlavprvwekvYAgiqakaeeAGGLKR 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 454 SLMRDGTEYVARYSRKS--------------------------------LRVLGSVGEPINPTAWRWFYDV-IgdsrcPI 500
Cdd:COG1022 300 KLFRWALAVGRRYARARlagkspslllrlkhaladklvfsklrealggrLRFAVSGGAALGPELARFFRALgI-----PV 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 501 SDTWWQTETGGFMITPLPGAwpQKPGSATFPFFGVQpVIVDEkgremEGEcsgyLCIKKswPGAFRTLYGDKEryETTyf 580
Cdd:COG1022 375 LEGYGLTETSPVITVNRPGD--NRIGTVGPPLPGVE-VKIAE-----DGE----ILVRG--PNVMKGYYKNPE--ATA-- 436
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1205963319 581 KPFA--GYYFSGD-GcSRDKDGYHWLTGRVDDVINVS-GHRIGTAEVESALVSHPKCAEAAVVG 640
Cdd:COG1022 437 EAFDadGWLHTGDiG-ELDEDGFLRITGRKKDLIVTSgGKNVAPQPIENALKASPLIEQAVVVG 499
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
164-716 |
7.30e-22 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 100.46 E-value: 7.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 164 NAVDRHveagnGDKIAMYWEGNEpsqdgkLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAV 243
Cdd:PRK05605 40 NAVARF-----GDRPALDFFGAT------TTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 244 hsVVFAG--FSAEALAQRVIDCKPKVVITCNAVkrglkiiflkdivdASLDESAKNGVDVGICLTYENQSALNKVdTRWT 321
Cdd:PRK05605 109 --VVEHNplYTAHELEHPFEDHGARVAIVWDKV--------------APTVERLRRTTPLETIVSVNMIAAMPLL-QRLA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 322 ---------TGRD---------VWWQDVV----PDFPTKCDVEWVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMVySATT 379
Cdd:PRK05605 172 lrlpipalrKARAaltgpapgtVPWETLVdaaiGGDGSDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFA-NAAQ 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 380 FKHafdykptdiywctadcgWITG---------------HSY-----VTYGPLLNGATVLVfegaPNyPDPGRCWDIVDK 439
Cdd:PRK05605 251 GKA-----------------WVPGlgdgpervlaalpmfHAYgltlcLTLAVSIGGELVLL----PA-PDIDLILDAMKK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 440 YGVTIFYTAPTLIRSLMRDGTEYvaRYSRKSLRvlgsvgepinptawrwfYDVIGDSRCPISDT-WWQTETGGFMI---- 514
Cdd:PRK05605 309 HPPTWLPGVPPLYEKIAEAAEER--GVDLSGVR-----------------NAFSGAMALPVSTVeLWEKLTGGLLVegyg 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 515 ----TPLPGAWP----QKPGSATFPFFGVQPVIVDEK--GREM-EGEcSGYLCIKKswPGAFRTLYGDKERYETTYFkpf 583
Cdd:PRK05605 370 ltetSPIIVGNPmsddRRPGYVGVPFPDTEVRIVDPEdpDETMpDGE-EGELLVRG--PQVFKGYWNRPEETAKSFL--- 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 584 AGYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAVVGIDHEVKGQGIYAFVTLVDGVPYS 663
Cdd:PRK05605 444 DGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPGAALD 523
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 1205963319 664 -DDLRKSLvmtvRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKIASRQLDE 716
Cdd:PRK05605 524 pEGLRAYC----REHLTRYKVPRRFYHVDELPRDQLGKVRRREVREELLEKLGA 573
|
|
| ACAS_N |
pfam16177 |
Acetyl-coenzyme A synthetase N-terminus; This domain is found at the N-terminus of many ... |
104-165 |
9.81e-22 |
|
Acetyl-coenzyme A synthetase N-terminus; This domain is found at the N-terminus of many acetyl-coenzyme A synthetase enzymes.
Pssm-ID: 465043 [Multi-domain] Cd Length: 55 Bit Score: 88.68 E-value: 9.81e-22
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1205963319 104 YREMYQKSIDDPAGFWSEIADEFYWKQKWSpdevcaENLDVTKGPiKIEWFKGGKTNICYNA 165
Cdd:pfam16177 1 YEALYRRSIEDPEGFWGEVAKELDWFKPFD------KVLDGSNGP-FAKWFVGGKLNVCYNC 55
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
194-709 |
1.05e-21 |
|
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: 99.52 E-value: 1.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 194 TYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAEALAQRVIDCKPKVVItcnA 273
Cdd:cd17642 46 SYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVF---C 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 274 VKRGL--------KIIFLKDIVDASLDESakngvdvgicltYENQSALNKVDTRWTTGRDVWWQDVVPDFPTKCDVEWVd 345
Cdd:cd17642 123 SKKGLqkvlnvqkKLKIIKTIIILDSKED------------YKGYQCLYTFITQNLPPGFNEYDFKPPSFDRDEQVALI- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 346 aedplflLYTSGSTGKPKGVLHTTGGYMVysatTFKHAFDykPTDIYWCTADCGWIT----GHSY---VTYGPLLNGATV 418
Cdd:cd17642 190 -------MNSSGSTGLPKGVQLTHKNIVA----RFSHARD--PIFGNQIIPDTAILTvipfHHGFgmfTTLGYLICGFRV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 419 LVFegaPNYpDPGRCWDIVDKYGVTIFYTAPTLIRSLMRdgTEYVARYSRKSLRVLGSVGEPINPTawrwfydvIGDS-- 496
Cdd:cd17642 257 VLM---YKF-EEELFLRSLQDYKVQSALLVPTLFAFFAK--STLVDKYDLSNLHEIASGGAPLSKE--------VGEAva 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 497 ---RCP-ISDTWWQTE-TGGFMITPlpgAWPQKPGSA--TFPFFGVQpVIVDEKGREMEGECSGYLCIKKswPGAFRTLY 569
Cdd:cd17642 323 krfKLPgIRQGYGLTEtTSAILITP---EGDDKPGAVgkVVPFFYAK-VVDLDTGKTLGPNERGELCVKG--PMIMKGYV 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 570 GDKERYETTYFKPfaGYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAVVGIDHEVKGQG 649
Cdd:cd17642 397 NNPEATKALIDKD--GWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGEL 474
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1205963319 650 IYAFVTLVDGVPYSD----DLRKSLVMTVRSQIGAFAAPDKIhwapglPKTRSGKIMRRILRKI 709
Cdd:cd17642 475 PAAVVVLEAGKTMTEkevmDYVASQVSTAKRLRGGVKFVDEV------PKGLTGKIDRRKIREI 532
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
194-710 |
1.11e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 99.64 E-value: 1.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 194 TYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAEALAQRVIDCKPKVVIT--- 270
Cdd:PRK08162 45 TWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFMLRHGEAKVLIVdte 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 271 -CNAVKRGLKI-----IFLKDIVDASLDESAKNGVdvgicLTYENQSALNKVDTRWTTGRDvwwqdvvpdfptkcdvEWv 344
Cdd:PRK08162 125 fAEVAREALALlpgpkPLVIDVDDPEYPGGRFIGA-----LDYEAFLASGDPDFAWTLPAD----------------EW- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 345 daeDPLFLLYTSGSTGKPKGVL-HTTGGY-MVYSATTfkhAFDYKPTDIY-----------WCTAdcgWITGhsyvtygp 411
Cdd:PRK08162 183 ---DAIALNYTSGTTGNPKGVVyHHRGAYlNALSNIL---AWGMPKHPVYlwtlpmfhcngWCFP---WTVA-------- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 412 lLNGATVLVFEGApnypDPGRCWDIVDKYGVTIFYTAPtLIRSLMRDGTEYVARYSRKSLRVLGSVGEPinPTAwrwfyd 491
Cdd:PRK08162 246 -ARAGTNVCLRKV----DPKLIFDLIREHGVTHYCGAP-IVLSALINAPAEWRAGIDHPVHAMVAGAAP--PAA------ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 492 VIGdsrcpisdtwwQTETGGFMITPLPG-----------AWpqKPGSATFPFF---------GV---------------- 535
Cdd:PRK08162 312 VIA-----------KMEEIGFDLTHVYGltetygpatvcAW--QPEWDALPLDeraqlkarqGVryplqegvtvldpdtm 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 536 QPVIVDekGREMeGEC--------SGYLCIKKSWPGAFRtlygdkeryettyfkpfAGYYFSGDGCSRDKDGYHWLTGRV 607
Cdd:PRK08162 379 QPVPAD--GETI-GEImfrgnivmKGYLKNPKATEEAFA-----------------GGWFHTGDLAVLHPDGYIKIKDRS 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 608 DDVINVSGHRIGTAEVESALVSHPKCAEAAVVGIDHEVKGQGIYAFVTLVDGVPYSDDlrkSLVMTVRSQIGAFAAPDKI 687
Cdd:PRK08162 439 KDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVELKDGASATEE---EIIAHCREHLAGFKVPKAV 515
|
570 580
....*....|....*....|...
gi 1205963319 688 HWAPgLPKTRSGKIMRRILRKIA 710
Cdd:PRK08162 516 VFGE-LPKTSTGKIQKFVLREQA 537
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
184-708 |
2.15e-21 |
|
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: 98.27 E-value: 2.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 184 GNEPSQDGKLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAEALAQRVIDC 263
Cdd:cd05915 16 RLHTGEVHRTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 264 KPKVVItcnavkrglkiiflkdiVDASLDESAKNGVDVGICLTyEN---QSALNKVDTRWTTGRdvwwqdvvPDFPTkcd 340
Cdd:cd05915 96 EDKVLL-----------------FDPNLLPLVEAIRGELKTVQ-HFvvmDEKAPEGYLAYEEAL--------GEEAD--- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 341 VEWVDAEDPLFLLYTSGSTGKPKGVLHT-TGGYMVYSATTFKHAFDYKPTDIYWCTADCGWITGHSYVTYGPLLNGATVL 419
Cdd:cd05915 147 PVRVPERAACGMAYTTGTTGLPKGVVYShRALVLHSLAASLVDGTALSEKDVVLPVVPMFHVNAWCLPYAATLVGAKQVL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 420 VFEgapnYPDPGRCWDIVDKYGVTIFYTAPTLIRSLMRdgteyvarySRKSLRvlgsvgepinpTAWRWFYDVIGDSRCP 499
Cdd:cd05915 227 PGP----RLDPASLVELFDGEGVTFTAGVPTVWLALAD---------YLESTG-----------HRLKTLRRLVVGGSAA 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 500 ISDTWWQTETGGFMITPLPGA---------------WPQKPGSATFPF--------FGVQPVIVDEKGREMEGECSGYLC 556
Cdd:cd05915 283 PRSLIARFERMGVEVRQGYGLtetspvvvqnfvkshLESLSEEEKLTLkaktglpiPLVRLRVADEEGRPVPKDGKALGE 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 557 IKKSWPGAFRTLYGDKERYETTYFKpfAGYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEA 636
Cdd:cd05915 363 VQLKGPWITGGYYGNEEATRSALTP--DGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEA 440
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1205963319 637 AVVGIDHEVKGQGIYAFVTLVDgvpySDDLRKSLVMTVRSQIGAFAA-PDKIHWAPGLPKTRSGKIMRRILRK 708
Cdd:cd05915 441 AVVAIPHPKWQERPLAVVVPRG----EKPTPEELNEHLLKAGFAKWQlPDAYVFAEEIPRTSAGKFLKRALRE 509
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
164-714 |
1.59e-20 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 95.83 E-value: 1.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 164 NAVDRHVEAgngDKIAMYwegnepsqDG--KLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIG 241
Cdd:PRK10946 29 DILTRHAAS---DAIAVI--------CGerQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 242 AVhsVVFAGFSAE-----ALAQRVidcKPKVVItcnaVKRGLKIifLKDivDASLDEsakngvdvgicLTYENQSALNKV 316
Cdd:PRK10946 98 VA--PVNALFSHQrselnAYASQI---EPALLI----ADRQHAL--FSD--DDFLNT-----------LVAEHSSLRVVL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 317 DTRWTTGRDV--WWQDVVPDF---PTKCDvewvdaEDPLFLLyTSGSTGKPKGVLHTTGGYMvYSATtfkhafdyKPTDI 391
Cdd:PRK10946 154 LLNDDGEHSLddAINHPAEDFtatPSPAD------EVAFFQL-SGGSTGTPKLIPRTHNDYY-YSVR--------RSVEI 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 392 YWCTAD----CGWITGHSYVTYGP------LLNGATVLvfegAPNyPDPGRCWDIVDKYGVTIFYTAPTLIRSLMRDGTE 461
Cdd:PRK10946 218 CGFTPQtrylCALPAAHNYPMSSPgalgvfLAGGTVVL----APD-PSATLCFPLIEKHQVNVTALVPPAVSLWLQAIAE 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 462 YVARYSRKSLRVLGSVGEPINPTAWRWFYDVIGdsrCPIS----------------DTWWQT-ETGGFMITPLPGAWpqk 524
Cdd:PRK10946 293 GGSRAQLASLKLLQVGGARLSETLARRIPAELG---CQLQqvfgmaeglvnytrldDSDERIfTTQGRPMSPDDEVW--- 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 525 pgsatfpffgvqpvIVDEKGREM-EGEcSGYLCIKKswPGAFRTLYGDKErYETTYFKPfAGYYFSGDGCSRDKDGYHWL 603
Cdd:PRK10946 367 --------------VADADGNPLpQGE-VGRLMTRG--PYTFRGYYKSPQ-HNASAFDA-NGFYCSGDLVSIDPDGYITV 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 604 TGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAVVGIDHEVKGQGIYAFVTLVDGVPySDDLRKSLvmtvRSQ-IGAFA 682
Cdd:PRK10946 428 VGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVVKEPLK-AVQLRRFL----REQgIAEFK 502
|
570 580 590
....*....|....*....|....*....|..
gi 1205963319 683 APDKIHWAPGLPKTRSGKIMRRILRKIASRQL 714
Cdd:PRK10946 503 LPDRVECVDSLPLTAVGKVDKKQLRQWLASRA 534
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
344-708 |
1.88e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 95.52 E-value: 1.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 344 VDAEDPLFLLYTSGSTGKPKGVLhTTGGYMVYSATTFKHAFDYKPTDIYWCTAD--------CGWITGhsyvtygpLLNG 415
Cdd:PRK07867 149 ADPDDLFMLIFTSGTSGDPKAVR-CTHRKVASAGVMLAQRFGLGPDDVCYVSMPlfhsnavmAGWAVA--------LAAG 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 416 ATVLV---FEGAPNYPDpgrcwdiVDKYGVTIF--------YTAPTLIRSLMRDGTeyvarysrksLRVL-GSVGEPINP 483
Cdd:PRK07867 220 ASIALrrkFSASGFLPD-------VRRYGATYAnyvgkplsYVLATPERPDDADNP----------LRIVyGNEGAPGDI 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 484 TAWRWFYDvigdsrCPISDTWWQTEtGGFMITPLPGAwpqKPGSATFPFFGVQ-----------PVIVDEKGREMEGECS 552
Cdd:PRK07867 283 ARFARRFG------CVVVDGFGSTE-GGVAITRTPDT---PPGALGPLPPGVAivdpdtgtecpPAEDADGRLLNADEAI 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 553 GYLcIKKSWPGAFRTLYGDKEryeTTYFKPFAGYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPK 632
Cdd:PRK07867 353 GEL-VNTAGPGGFEGYYNDPE---ADAERMRGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPD 428
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1205963319 633 CAEAAVVGIDHEVKGQGIYAFVTLVDGVPYsDDLRKSLVMTVRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRK 708
Cdd:PRK07867 429 ATEVAVYAVPDPVVGDQVMAALVLAPGAKF-DPDAFAEFLAAQPDLGPKQWPSYVRVCAELPRTATFKVLKRQLSA 503
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
190-706 |
2.49e-20 |
|
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: 94.24 E-value: 2.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 190 DGKLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAEALAQRVIDCKPKVVI 269
Cdd:cd17652 10 DETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYMLADARPALLL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 270 TcnavkrglkiiflkdivdasldesakngvdvgicltyenqsalnkvdtrwttgrdvwwqdvvpdfptkcdvewvDAEDP 349
Cdd:cd17652 90 T--------------------------------------------------------------------------TPDNL 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 350 LFLLYTSGSTGKPKGVLHTTGGYMVYSATTFKHaFDYKPTDiywCTADCGWITGHSYVT--YGPLLNGATVLVFEGAPNY 427
Cdd:cd17652 96 AYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAA-FDVGPGS---RVLQFASPSFDASVWelLMALLAGATLVLAPAEELL 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 428 PDPGRCwDIVDKYGVTIFYTAPTLIRSLMRDGTEyvarysrkSLRVLGSVGEPINPT-AWRW-----FYDVIGDSRCPIS 501
Cdd:cd17652 172 PGEPLA-DLLREHRITHVTLPPAALAALPPDDLP--------DLRTLVVAGEACPAElVDRWapgrrMINAYGPTETTVC 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 502 DTWWQTETGGFMItPLPGAWPqkpgsatfpffGVQPVIVDEKGREMEGECSGYLCIkkSWPGAFRTlYGDK-----ERYE 576
Cdd:cd17652 243 ATMAGPLPGGGVP-PIGRPVP-----------GTRVYVLDARLRPVPPGVPGELYI--AGAGLARG-YLNRpgltaERFV 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 577 TtyfKPFAG----YYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAVVGIDHEVKGQGIYA 652
Cdd:cd17652 308 A---DPFGApgsrMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVA 384
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1205963319 653 FVTLVDGV-PYSDDLRKSLvmtvRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRIL 706
Cdd:cd17652 385 YVVPAPGAaPTAAELRAHL----AERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
193-640 |
6.59e-20 |
|
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: 93.43 E-value: 6.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 193 LTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAEALAQRVIDCKPKVVItcn 272
Cdd:cd05907 6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALF--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 273 avkrglkiiflkdivdasldesakngvdvgicltyenqsalnkvdtrwttgrdvwwqdvvpdfptkcdVEwvDAEDPLFL 352
Cdd:cd05907 83 --------------------------------------------------------------------VE--DPDDLATI 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 353 LYTSGSTGKPKGVLHTTGGYMvYSATTFKHAFDYKPTDIYWCTADCGWITGHSYVTYGPLLNGATVLVFEGAPNYPDpgr 432
Cdd:cd05907 93 IYTSGTTGRPKGVMLSHRNIL-SNALALAERLPATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFASSAETLLD--- 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 433 cwDIVdKYGVTIFYTAPTLIRSL-----MRDGTEY----VARYSRKSLRVLGSVGEPINPTAWRWFYdVIGdsrCPISDT 503
Cdd:cd05907 169 --DLS-EVRPTVFLAVPRVWEKVyaaikVKAVPGLkrklFDLAVGGRLRFAASGGAPLPAELLHFFR-ALG---IPVYEG 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 504 WWQTETGGFMITPLPGAWpqKPGSATFPFFGVQPVIVDekgremEGE--CSGylcikkswPGAFRTLYGDKEryETTYFK 581
Cdd:cd05907 242 YGLTETSAVVTLNPPGDN--RIGTVGKPLPGVEVRIAD------DGEilVRG--------PNVMLGYYKNPE--ATAEAL 303
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 582 PFAGYYFSGDGCSRDKDGYHWLTGRVDDVI-NVSGHRIGTAEVESALVSHPKCAEAAVVG 640
Cdd:cd05907 304 DADGWLHTGDLGEIDEDGFLHITGRKKDLIiTSGGKNISPEPIENALKASPLISQAVVIG 363
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
348-703 |
7.58e-20 |
|
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: 91.56 E-value: 7.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 348 DPLFLLYTSGSTGKPKGVLHTTGGyMVYSATTFKHAFDYKPTDIYWCTADCGWITGhsyvtygplLNGATVLVFEGAPNY 427
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGN-LIAANLQLIHAMGLTEADVYLNMLPLFHIAG---------LNLALATFHAGGANV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 428 P----DPGRCWDIVDKYGVTIFYTAPTLIRSLMrdgtEYVARYSRK--SLRVLGSVGEPinptawrwfyDVIGDSRCPIS 501
Cdd:cd17637 71 VmekfDPAEALELIEEEKVTLMGSFPPILSNLL----DAAEKSGVDlsSLRHVLGLDAP----------ETIQRFEETTG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 502 DTWW----QTETGGFmITPLPGAwpQKPGSATFPFFGVQPVIVDEKGREMEGECSGYLCIKKswPGAFRTLYGDKERYET 577
Cdd:cd17637 137 ATFWslygQTETSGL-VTLSPYR--ERPGSAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRG--PLVFQGYWNLPELTAY 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 578 TYFKpfaGYYFSGDGCSRDKDGYHWLTGRV--DDVINVSGHRIGTAEVESALVSHPKCAEAAVVGIDHEVKGQGIYAFVT 655
Cdd:cd17637 212 TFRN---GWHHTGDLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCV 288
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1205963319 656 LVDGVPYSDDlrkSLVMTVRSQIGAFAAPDKIHWAPGLPKTRSGKIMR 703
Cdd:cd17637 289 LKPGATLTAD---ELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
345-707 |
9.99e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 92.75 E-value: 9.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 345 DAEDPLFLLYTSGSTGKPKGVlhttggymVYSATTFKHAFDYKPTDIYWcTADCGWITG------HSYV--TYGPLLNGA 416
Cdd:PRK07787 126 DPDAPALIVYTSGTTGPPKGV--------VLSRRAIAADLDALAEAWQW-TADDVLVHGlplfhvHGLVlgVLGPLRIGN 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 417 TVlVFEGAPNyPDPgrcWDIVDKYGVTIFYTAPTLIRSLMRDgTEYVARYSRKSLRVLGSVGEPInPTawrwFYDVIGDS 496
Cdd:PRK07787 197 RF-VHTGRPT-PEA---YAQALSEGGTLYFGVPTVWSRIAAD-PEAARALRGARLLVSGSAALPV-PV----FDRLAALT 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 497 RCPISDTWWQTETggFMITPLPGAWPQKPGSATFPFFGVQPVIVDEKGREM--EGECSGYLCIKKswPGAFrtlygdker 574
Cdd:PRK07787 266 GHRPVERYGMTET--LITLSTRADGERRPGWVGLPLAGVETRLVDEDGGPVphDGETVGELQVRG--PTLF--------- 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 575 yeTTYF-KPFA--------GYYFSGDGCSRDKDGYHWLTGRVD-DVINVSGHRIGTAEVESALVSHPKCAEAAVVGIDHE 644
Cdd:PRK07787 333 --DGYLnRPDAtaaaftadGWFRTGDVAVVDPDGMHRIVGREStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDD 410
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1205963319 645 VKGQGIYAFVtlvdgVPYSDDLRKSLVMTVRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRILR 707
Cdd:PRK07787 411 DLGQRIVAYV-----VGADDVAADELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLL 468
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
192-706 |
1.25e-19 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 94.34 E-value: 1.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 192 KLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAEALAQRVIDCKPKVVITc 271
Cdd:PRK10252 483 QFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLIT- 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 272 navkrglkiiflkdivdaSLDESAK-NGVDVGICLTYENQSALnkvdtrwttgrdvwwQDVVPDFPTKCDvewvdaeDPL 350
Cdd:PRK10252 562 ------------------TADQLPRfADVPDLTSLCYNAPLAP---------------QGAAPLQLSQPH-------HTA 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 351 FLLYTSGSTGKPKGVL--HTTggyMVYSATTFKHAFDYKPTDIYW----CTADCG-----WitghsyvtygPLLNGATvL 419
Cdd:PRK10252 602 YIIFTSGSTGRPKGVMvgQTA---IVNRLLWMQNHYPLTADDVVLqktpCSFDVSvweffW----------PFIAGAK-L 667
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 420 VFEGAPNYPDPGRCWDIVDKYGVTIFYTAPTLIRSLMRDGTEYVARYSRKSLRVLGSVGEPInPTAW--RW-------FY 490
Cdd:PRK10252 668 VMAEPEAHRDPLAMQQFFAEYGVTTTHFVPSMLAAFVASLTPEGARQSCASLRQVFCSGEAL-PADLcrEWqqltgapLH 746
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 491 DVIGDSRCPISDTWWqtetggfmitPLPGAWPQKPGSAT----FPFFGVQPVIVDEKGRE----MEGE--------CSGY 554
Cdd:PRK10252 747 NLYGPTEAAVDVSWY----------PAFGEELAAVRGSSvpigYPVWNTGLRILDARMRPvppgVAGDlyltgiqlAQGY 816
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 555 LCikksWPGAfrtlygDKERYETTYFKPFAGYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCA 634
Cdd:PRK10252 817 LG----RPDL------TASRFIADPFAPGERMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVE 886
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1205963319 635 EA---AVVGIDHEVKGQG---IYAFVTLVDGVPY-SDDLRKSLvmtvRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRIL 706
Cdd:PRK10252 887 QAvthACVINQAAATGGDarqLVGYLVSQSGLPLdTSALQAQL----RERLPPHMVPVVLLQLDQLPLSANGKLDRKAL 961
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
342-708 |
2.49e-19 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 92.12 E-value: 2.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 342 EWVDAEDPLF------------LLYTSGSTGKPKGVLHTTGGYMVYS-ATTFKHAFDYKPTDIY-----------WCTAD 397
Cdd:PRK06018 160 EWIAEADGDFawktfdentaagMCYTSGTTGDPKGVLYSHRSNVLHAlMANNGDALGTSAADTMlpvvplfhansWGIAF 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 398 CGWITGHSYVTYGPLLNGATVlvfegapnypdpgrcWDIVDKYGVTIFYTAPTLIRSLMrdgtEYVARySRKSLRVLGSV 477
Cdd:PRK06018 240 SAPSMGTKLVMPGAKLDGASV---------------YELLDTEKVTFTAGVPTVWLMLL----QYMEK-EGLKLPHLKMV 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 478 gepinptawrwfydVIGDSRCPIS-------------DTWWQTETGGF-MITPLPGAWPQKPGSAT--------FPFFGV 535
Cdd:PRK06018 300 --------------VCGGSAMPRSmikafedmgvevrHAWGMTEMSPLgTLAALKPPFSKLPGDARldvlqkqgYPPFGV 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 536 QPVIVDEKGREM--EGECSGYLciKKSWPGAFRTLYgdkeRYETTYFKPfAGYYFSGDGCSRDKDGYHWLTGRVDDVINV 613
Cdd:PRK06018 366 EMKITDDAGKELpwDGKTFGRL--KVRGPAVAAAYY----RVDGEILDD-DGFFDTGDVATIDAYGYMRITDRSKDVIKS 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 614 SGHRIGTAEVESALVSHPKCAEAAVVGIDHEVKGQGIYAFVTLVDGV-PYSDDLRKSLvmtvRSQIGAFAAPDKIHWAPG 692
Cdd:PRK06018 439 GGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKPGEtATREEILKYM----DGKIAKWWMPDDVAFVDA 514
|
410
....*....|....*.
gi 1205963319 693 LPKTRSGKIMRRILRK 708
Cdd:PRK06018 515 IPHTATGKILKTALRE 530
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
190-714 |
2.55e-19 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 93.87 E-value: 2.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 190 DGKLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAEALAQRVIDCKPKVVI 269
Cdd:PRK12316 3080 EQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLL 3159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 270 TCNAVKRGLKIIFLKDIVDASLDESAKNGVDVGicltyenqsalnkvdtrwttgrdvwwqdvvpdfptkcdvewVDAEDP 349
Cdd:PRK12316 3160 SQSHLRLPLAQGVQVLDLDRGDENYAEANPAIR-----------------------------------------TMPENL 3198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 350 LFLLYTSGSTGKPKGV-----------------LHTTGGYMVYSATTFkhAFDYKPTDIYWctadcgwitghsyvtygPL 412
Cdd:PRK12316 3199 AYVIYTSGSTGKPKGVgirhsalsnhlcwmqqaYGLGVGDRVLQFTTF--SFDVFVEELFW-----------------PL 3259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 413 LNGATVLVfEGAPNYPDPGRCWDIVDKYGVTIFYTAPTLIRSLMRDgtEYVARYsrKSLRVLGSVGEPINP-TAWRWF-- 489
Cdd:PRK12316 3260 MSGARVVL-AGPEDWRDPALLVELINSEGVDVLHAYPSMLQAFLEE--EDAHRC--TSLKRIVCGGEALPAdLQQQVFag 3334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 490 ---YDVIGDSRCPISDTWWQTETGGFMITPLPGAWPQKpgSATFPFFGVQPVIVDEKGREM---EGECSGYLcikkSWPG 563
Cdd:PRK12316 3335 lplYNLYGPTEATITVTHWQCVEEGKDAVPIGRPIANR--ACYILDGSLEPVPVGALGELYlggEGLARGYH----NRPG 3408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 564 AfrtlygDKERYETTYFKPFAGYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAVVgidh 643
Cdd:PRK12316 3409 L------TAERFVPDPFVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVL---- 3478
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1205963319 644 EVKGQGIYAFVTLVDGVPysdDLRKSLVMTVRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKIASRQL 714
Cdd:PRK12316 3479 AVDGRQLVAYVVPEDEAG---DLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPRPDAALL 3546
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
192-716 |
2.62e-19 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 93.87 E-value: 2.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 192 KLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAEALAQRVIDCKPKVVITC 271
Cdd:PRK12316 4576 KLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALLLTQ 4655
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 272 NAVKRGLKIiflkdivdasldesaKNGVDvgiCLTYEnqsalnkvdtrwttgRDVWWQDvvpdFPTKCDVEWVDAEDPLF 351
Cdd:PRK12316 4656 SHLLQRLPI---------------PDGLA---SLALD---------------RDEDWEG----FPAHDPAVRLHPDNLAY 4698
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 352 LLYTSGSTGKPKGVLHTTGGYMVYSATTFKHafdykptdiYWCTADCGWITGHSYV-------TYGPLLNGATVLVfeGA 424
Cdd:PRK12316 4699 VIYTSGSTGRPKGVAVSHGSLVNHLHATGER---------YELTPDDRVLQFMSFSfdgshegLYHPLINGASVVI--RD 4767
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 425 PNYPDPGRCWDIVDKYGVTIFYTAPTLIRSLMRDGTEyvaRYSRKSLRVLGSVGEPINPT----AWR-----WFYDVIGD 495
Cdd:PRK12316 4768 DSLWDPERLYAEIHEHRVTVLVFPPVYLQQLAEHAER---DGEPPSLRVYCFGGEAVAQAsydlAWRalkpvYLFNGYGP 4844
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 496 SRCPISDTWWQTETGgfmitplpgawpQKPGSATFPFFGVQP----VIVDEKGREMEGECSGYLCIKKSW--PGAFRTLY 569
Cdd:PRK12316 4845 TETTVTVLLWKARDG------------DACGAAYMPIGTPLGnrsgYVLDGQLNPLPVGVAGELYLGGEGvaRGYLERPA 4912
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 570 GDKERYETTYF-KPFAGYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAVVGIDHEVkGQ 648
Cdd:PRK12316 4913 LTAERFVPDPFgAPGGRLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAV-GK 4991
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1205963319 649 GIYAFVT-----LVDGVPYSDDLRKSLVMTVRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKIASRQLDE 716
Cdd:PRK12316 4992 QLVGYVVpqdpaLADADEAQAELRDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKALPQPDASLLQQ 5064
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
189-706 |
3.92e-19 |
|
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: 91.00 E-value: 3.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 189 QDGKLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAEALAQRVIDCKPKVV 268
Cdd:cd17656 10 ENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRVV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 269 ITCNAVKRGL---KIIFLKDIVDASlDESAKNgvdvgicLTYENqsalnkvdtrwttgrdvwwqdvvpdfptkcdvewvD 345
Cdd:cd17656 90 LTQRHLKSKLsfnKSTILLEDPSIS-QEDTSN-------IDYIN-----------------------------------N 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 346 AEDPLFLLYTSGSTGKPKGVL--HTTggymvySATTFKHAFDYKPTDIYwctADCGWITGHSY-VTY----GPLLNGATV 418
Cdd:cd17656 127 SDDLLYIIYTSGTTGKPKGVQleHKN------MVNLLHFEREKTNINFS---DKVLQFATCSFdVCYqeifSTLLSGGTL 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 419 LVFEGAPNYpDPGRCWDIVDKYGVTIFYTAPTLIRSLMRDgTEYVARYSrKSLRVLGSVGEPINPTawRWFYDVIGDSRC 498
Cdd:cd17656 198 YIIREETKR-DVEQLFDLVKRHNIEVVFLPVAFLKFIFSE-REFINRFP-TCVKHIITAGEQLVIT--NEFKEMLHEHNV 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 499 PISDTWWQTET---GGFMITPLPgAWPQKPGSATfPFFGVQPVIVDEKGREMEGECSGYLCIkkSWPGAFRTLYGDK--- 572
Cdd:cd17656 273 HLHNHYGPSEThvvTTYTINPEA-EIPELPPIGK-PISNTWIYILDQEQQLQPQGIVGELYI--SGASVARGYLNRQelt 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 573 -ERYETTYFKPFAGYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAVVGIDHEVKGQGIY 651
Cdd:cd17656 349 aEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLC 428
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1205963319 652 AFVTLVDGVPYSdDLRKSLvmtvRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRIL 706
Cdd:cd17656 429 AYFVMEQELNIS-QLREYL----AKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
347-703 |
7.91e-19 |
|
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: 88.47 E-value: 7.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 347 EDPLFLLYTSGSTGKPKGVLHTTGGYMVYSATTFKHAFDykptdiyWCTADCGWITGHSYVTYGpLLNGATVLVFEGA-- 424
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLN-------WVVGDVTYLPLPATHIGG-LWWILTCLIHGGLcv 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 425 --PNYPDPGRCWDIVDKYGVTIFYTAPTL---IRSLMRDGTEYVarysrKSLRVLGSVGE-PINptAWRWFYDVIGDSRc 498
Cdd:cd17635 73 tgGENTTYKSLFKILTTNAVTTTCLVPTLlskLVSELKSANATV-----PSLRLIGYGGSrAIA--ADVRFIEATGLTN- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 499 pISDTWWQTETGGFMITPLpGAWPQKPGSATFPFFGVQPVIVDEKGREMEGECSGYLCIKKSWpgafrTLYGDKERYETT 578
Cdd:cd17635 145 -TAQVYGLSETGTALCLPT-DDDSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPA-----NMLGYWNNPERT 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 579 YFKPFAGYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAVVGIDHEVKGQGIYAFVTLvd 658
Cdd:cd17635 218 AEVLIDGWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVA-- 295
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1205963319 659 gvpySDDLRKS----LVMTVRSQIGAFAAPDKIHWAPGLPKTRSGKIMR 703
Cdd:cd17635 296 ----SAELDENairaLKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
188-712 |
9.23e-19 |
|
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: 89.91 E-value: 9.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 188 SQDGKLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAvhsvVFAGFSAEALAQR----VIDC 263
Cdd:cd05918 20 AWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGG----AFVPLDPSHPLQRlqeiLQDT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 264 KPKVVITCnavkrglkiiflkdivdasldesakngvdvgicltyenqsalnkvdtrwttgrdvwwqdvvpdfptkcdvew 343
Cdd:cd05918 96 GAKVVLTS------------------------------------------------------------------------ 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 344 vDAEDPLFLLYTSGSTGKPKGVL--HTTggyMVYSATTFKHAFDYKPTDIYWCTAdcgwitghSYV-------TYGPLLN 414
Cdd:cd05918 104 -SPSDAAYVIFTSGSTGKPKGVVieHRA---LSTSALAHGRALGLTSESRVLQFA--------SYTfdvsileIFTTLAA 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 415 GATVLVfegaPnyPDPGRCWDIVD---KYGVT-IFYTaPTLIRSLMRDGTEyvarysrkSLRVLGSVGEPINPtawrwfy 490
Cdd:cd05918 172 GGCLCI----P--SEEDRLNDLAGfinRLRVTwAFLT-PSVARLLDPEDVP--------SLRTLVLGGEALTQ------- 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 491 DVIgdsrcpisDTWWQ----------TETGGFMITPLPGAwPQKPGSATFPfFGVQPVIVDEKGRE------MEGE---- 550
Cdd:cd05918 230 SDV--------DTWADrvrlinaygpAECTIAATVSPVVP-STDPRNIGRP-LGATCWVVDPDNHDrlvpigAVGEllie 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 551 ----CSGYL---------------CIKKSWPGAFRTLY--GDKERYettyfkpfagyyfsgdgcsrDKDG---YHwltGR 606
Cdd:cd05918 300 gpilARGYLndpektaaafiedpaWLKQEGSGRGRRLYrtGDLVRY--------------------NPDGsleYV---GR 356
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 607 VDDVINVSGHRIGTAEVESALVSHPKCAEAAVVGI----DHEVKGQgIYAFVTLvDGVPYSDDLRKSLVMTVRSQigAFA 682
Cdd:cd05918 357 KDTQVKIRGQRVELGEIEHHLRQSLPGAKEVVVEVvkpkDGSSSPQ-LVAFVVL-DGSSSGSGDGDSLFLEPSDE--FRA 432
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 1205963319 683 APDKI---------------HWAP--GLPKTRSGKIMRRILRKIASR 712
Cdd:cd05918 433 LVAELrsklrqrlpsymvpsVFLPlsHLPLTASGKIDRRALRELAES 479
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
188-708 |
1.24e-18 |
|
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: 89.29 E-value: 1.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 188 SQDGKLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAEALAQRVIDCKPKV 267
Cdd:cd17653 18 SLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARIQAILRTSGATL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 268 VITCNAvkrglkiiflkdivdasldesakngvdvgicltyenqsalnkvdtrwttgrdvwwqdvvpdfptkcdvewvdAE 347
Cdd:cd17653 98 LLTTDS------------------------------------------------------------------------PD 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 348 DPLFLLYTSGSTGKPKGV-----------------LHTTGGYMVysATTFKHAFDYkptdiywCTAdcgwitghsyVTYG 410
Cdd:cd17653 106 DLAYIIFTSGSTGIPKGVmvphrgvlnyvsqpparLDVGPGSRV--AQVLSIAFDA-------CIG----------EIFS 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 411 PLLNGATvLVFEgapnypDPGRCWDIVDKyGVTIFYTAPTLIRSLMRDgteyvaRYSRKSLRVLGsvGEPINPT---AW- 486
Cdd:cd17653 167 TLCNGGT-LVLA------DPSDPFAHVAR-TVDALMSTPSILSTLSPQ------DFPNLKTIFLG--GEAVPPSlldRWs 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 487 --RWFYDVIGDSRCPISDTWWQTETGGFMI--TPLPGAwpqkpgsatfpffGVqpVIVDEKGREMEGECSGYLCIkkSWP 562
Cdd:cd17653 231 pgRRLYNAYGPTECTISSTMTELLPGQPVTigKPIPNS-------------TC--YILDADLQPVPEGVVGEICI--SGV 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 563 GAFRTLYGDKERyETTYFKPFAGY-----YFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAA 637
Cdd:cd17653 294 QVARGYLGNPAL-TASKFVPDPFWpgsrmYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQSQPEVTQA 372
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1205963319 638 VVgidhEVKGQGIYAFVT--LVDGvpysDDLRKSLvmtvRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRK 708
Cdd:cd17653 373 AA----IVVNGRLVAFVTpeTVDV----DGLRSEL----AKHLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
445-706 |
2.66e-18 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 88.90 E-value: 2.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 445 FYTAPTLIRSLMRDGTEYVARYSRKSLRVLGSVGEPINPTAWRWFYDVIGDSrcpISDTWWQTETG-GFMITPLP-GAWP 522
Cdd:PRK13383 268 FTAVPVVLARILELPPRVRARNPLPQLRVVMSSGDRLDPTLGQRFMDTYGDI---LYNGYGSTEVGiGALATPADlRDAP 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 523 QKPGSatfPFFGVQPVIVDEKGREMEGECSGYLCIKKSWPGAFRTLYGDKERYEttyfkpfaGYYFSGDGCSRDKDGYHW 602
Cdd:PRK13383 345 ETVGK---PVAGCPVRILDRNNRPVGPRVTGRIFVGGELAGTRYTDGGGKAVVD--------GMTSTGDMGYLDNAGRLF 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 603 LTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAVVGIDHEVKGQGIYAFVTLVDGVPY-SDDLRKSLvmtvRSQIGAF 681
Cdd:PRK13383 414 IVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSGVdAAQLRDYL----KDRVSRF 489
|
250 260
....*....|....*....|....*
gi 1205963319 682 AAPDKIHWAPGLPKTRSGKIMRRIL 706
Cdd:PRK13383 490 EQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
191-708 |
3.49e-18 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 88.50 E-value: 3.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 191 GK-LTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVhsvvFAGFSAEALAQRvidckpkvvI 269
Cdd:PLN02330 53 GKaVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGV----FSGANPTALESE---------I 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 270 TCNAVKRGLKIIflkdIVDASLDESAKN-GVDVGICLTYENQSALNkvdtrwttgrdvwWQDVVpDFPTKC----DVEWV 344
Cdd:PLN02330 120 KKQAEAAGAKLI----VTNDTNYGKVKGlGLPVIVLGEEKIEGAVN-------------WKELL-EAADRAgdtsDNEEI 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 345 DAEDPLFLLYTSGSTGKPKGVLHT--------------TGGYMVYSATT-----FKHafdykptdIYWCTADCgwitghs 405
Cdd:PLN02330 182 LQTDLCALPFSSGTTGISKGVMLThrnlvanlcsslfsVGPEMIGQVVTlglipFFH--------IYGITGIC------- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 406 yvtYGPLLNGATVLVfegapnypdpgrcwdiVDKYGVTIFYTA------------PTLIRSLMRDGTEYVARYSRKSLRV 473
Cdd:PLN02330 247 ---CATLRNKGKVVV----------------MSRFELRTFLNAlitqevsfapivPPIILNLVKNPIVEEFDLSKLKLQA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 474 LGSVGEPINPTAWRWFydvigDSRCP---ISDTWWQTETGGFMIT---PLPGAWPQKPGSATFPFFGVQPVIVD-EKGRE 546
Cdd:PLN02330 308 IMTAAAPLAPELLTAF-----EAKFPgvqVQEAYGLTEHSCITLThgdPEKGHGIAKKNSVGFILPNLEVKFIDpDTGRS 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 547 MEGECSGYLCIKKSWpgAFRTLYGDKERYETTYFKpfAGYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESA 626
Cdd:PLN02330 383 LPKNTPGELCVRSQC--VMQGYYNNKEETDRTIDE--DGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAI 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 627 LVSHPKCAEAAVVGIDHEVKGQGIYAFVTLvdgVPYSDDLRKSLVMTVRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRIL 706
Cdd:PLN02330 459 LLTHPSVEDAAVVPLPDEEAGEIPAACVVI---NPKAKESEEDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLL 535
|
..
gi 1205963319 707 RK 708
Cdd:PLN02330 536 KE 537
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
193-707 |
4.42e-18 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 88.01 E-value: 4.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 193 LTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAEALAQRVIDCKPKVVItCN 272
Cdd:PRK07514 29 YTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAEPALVV-CD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 273 ----------AVKRGLKIIF-LKDIVDASLDESAkngvdvgicltyenqsalnkvdtrwttgrdvwwQDVVPDFPTkcdV 341
Cdd:PRK07514 108 panfawlskiAAAAGAPHVEtLDADGTGSLLEAA---------------------------------AAAPDDFET---V 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 342 EwVDAEDPLFLLYTSGSTGKPKGVLHTTGGyMVYSATTFKHAFDYKPTD-------IYwctadcgwitgHSY----VTYG 410
Cdd:PRK07514 152 P-RGADDLAAILYTSGTTGRSKGAMLSHGN-LLSNALTLVDYWRFTPDDvlihalpIF-----------HTHglfvATNV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 411 PLLNGATVLVFegaPNYpDPGRCWDIVDK----YGVTIFYTaptliRSLMRDG-TEYVARYSRksLRVLGSVgePINPTA 485
Cdd:PRK07514 219 ALLAGASMIFL---PKF-DPDAVLALMPRatvmMGVPTFYT-----RLLQEPRlTREAAAHMR--LFISGSA--PLLAET 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 486 WRWFYDVIGDsrcPISDTWWQTETGgfMIT--PLPGAwpQKPGSATFPFFGVQPVIVD-EKGREMEGECSGYLCIKKswP 562
Cdd:PRK07514 286 HREFQERTGH---AILERYGMTETN--MNTsnPYDGE--RRAGTVGFPLPGVSLRVTDpETGAELPPGEIGMIEVKG--P 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 563 GAFRtlyG-----DKERYEttyFKPfAGYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAA 637
Cdd:PRK07514 357 NVFK---GywrmpEKTAEE---FRA-DGFFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESA 429
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 638 VVGIDHEVKGQGIYAFVTLVDGVPYSDDlrkSLVMTVRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRILR 707
Cdd:PRK07514 430 VIGVPHPDFGEGVTAVVVPKPGAALDEA---AILAALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLLR 496
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
193-707 |
5.56e-18 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 88.19 E-value: 5.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 193 LTYSELLEKVCQLSNYLKS-VGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAEALAQRVIDCKPK-VVIT 270
Cdd:PRK08974 49 MTFRKLEERSRAFAAYLQNgLGLKKGDRVALMMPNLLQYPIALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAKaIVIV 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 271 CNAVKRGLKIIF---LKDIVDASLDE--SAKNGVDVGICLTYENQ--------------SALNKvdtrwttGRDVwwQDV 331
Cdd:PRK08974 129 SNFAHTLEKVVFktpVKHVILTRMGDqlSTAKGTLVNFVVKYIKRlvpkyhlpdaisfrSALHK-------GRRM--QYV 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 332 VPDfptkcdvewVDAEDPLFLLYTSGSTGKPKGVLHTTGGyMVysATTFKhafdykptdiywctadCGWItghsyvtYGP 411
Cdd:PRK08974 200 KPE---------LVPEDLAFLQYTGGTTGVAKGAMLTHRN-ML--ANLEQ----------------AKAA-------YGP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 412 LLNGATVLVFEGAPNY----------------------PDPgRcwDI------VDKYGVTIFYTAPTLIRSLMRDGTEYV 463
Cdd:PRK08974 245 LLHPGKELVVTALPLYhifaltvncllfielggqnlliTNP-R--DIpgfvkeLKKYPFTAITGVNTLFNALLNNEEFQE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 464 ARYSRKSLRVLGsvGEPINPT-AWRWfYDVIGdsrCPISDTWWQTETggfmiTPLPGAWP----QKPGSATFPFFGVQPV 538
Cdd:PRK08974 322 LDFSSLKLSVGG--GMAVQQAvAERW-VKLTG---QYLLEGYGLTEC-----SPLVSVNPydldYYSGSIGLPVPSTEIK 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 539 IVDEKGREMEGECSGYLCIKKSwpgafRTLYGDKERYETTYFKPFAGYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRI 618
Cdd:PRK08974 391 LVDDDGNEVPPGEPGELWVKGP-----QVMLGYWQRPEATDEVIKDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNV 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 619 GTAEVESALVSHPKCAEAAVVGIDHEVKGQGIYAFVTLVDGVPYSDDLRKSlvmtVRSQIGAFAAPDKIHWAPGLPKTRS 698
Cdd:PRK08974 466 YPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFVVKKDPSLTEEELITH----CRRHLTGYKVPKLVEFRDELPKSNV 541
|
....*....
gi 1205963319 699 GKIMRRILR 707
Cdd:PRK08974 542 GKILRRELR 550
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
347-707 |
6.29e-18 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 85.79 E-value: 6.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 347 EDPLFLLYTSGSTGKPKGVLHT-----TGGYMVysattfKHAFDYKPTDI-------YWCTadcGWITGH-SYVTYGpll 413
Cdd:cd05917 2 DDVINIQFTSGTTGSPKGATLThhnivNNGYFI------GERLGLTEQDRlcipvplFHCF---GSVLGVlACLTHG--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 414 nGATVLVfegAPNYpDPGRCWDIVDKYGVTIFYTAPTL-IRSLmrdGTEYVARYSRKSLR--VLGsvGEPINPTAWRwfy 490
Cdd:cd05917 70 -ATMVFP---SPSF-DPLAVLEAIEKEKCTALHGVPTMfIAEL---EHPDFDKFDLSSLRtgIMA--GAPCPPELMK--- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 491 DVIGDSRCP-ISDTWWQTET--GGFMITPLPGAwPQKPGSATFPFFGVQPVIVDEKGRE-----MEGE--CSGYLCIKKS 560
Cdd:cd05917 137 RVIEVMNMKdVTIAYGMTETspVSTQTRTDDSI-EKRVNTVGRIMPHTEAKIVDPEGGIvppvgVPGElcIRGYSVMKGY 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 561 WpgafrtlyGDKERYETTYFKpfAGYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAVVG 640
Cdd:cd05917 216 W--------NDPEKTAEAIDG--DGWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVG 285
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1205963319 641 IDHEVKGQGIYAFVTLVDGVPYS-DDLRKSLvmtvRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRILR 707
Cdd:cd05917 286 VPDERYGEEVCAWIRLKEGAELTeEDIKAYC----KGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
167-730 |
1.31e-17 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 87.39 E-value: 1.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 167 DRHVEAGNGDKIAMYwegnEPSQdgkLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSV 246
Cdd:PRK06060 12 EQASEAGWYDRPAFY----AADV---VTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 247 VFAGFSAEALAQRVIDCKPKVVITCNAVKRGLKIiflKDIVDAS--LDESAKNGvdvgicltyenqsalnkvdtrwttgr 324
Cdd:PRK06060 85 ANPELHRDDHALAARNTEPALVVTSDALRDRFQP---SRVAEAAelMSEAARVA-------------------------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 325 dvwwqdvvpdfPTkcDVEWVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMVYSATTFKHAFDYKPTDIYWCTADCGWITGH 404
Cdd:PRK06060 136 -----------PG--GYEPMGGDALAYATYTSGTTGPPKAAIHRHADPLTFVDAMCRKALRLTPEDTGLCSARMYFAYGL 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 405 SYVTYGPLLNGATVLVfEGAPNYPDPGRCwdIVDKYGVTIFYTAPTLIRSLMrdgtEYVARYSRKSLRVLGSVGEPINPT 484
Cdd:PRK06060 203 GNSVWFPLATGGSAVI-NSAPVTPEAAAI--LSARFGPSVLYGVPNFFARVI----DSCSPDSFRSLRCVVSAGEALELG 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 485 AWRWFYDVIGDsrCPISDTWWQTETGGFMITPLPGAWpqKPGS--ATFPFFGVQPVIVDEKGREMEGEcsGYLCIKKswP 562
Cdd:PRK06060 276 LAERLMEFFGG--IPILDGIGSTEVGQTFVSNRVDEW--RLGTlgRVLPPYEIRVVAPDGTTAGPGVE--GDLWVRG--P 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 563 GAFRTLYGDKERYETTyfkpfAGYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAVVGID 642
Cdd:PRK06060 348 AIAKGYWNRPDSPVAN-----EGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVR 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 643 HEVKGQGIYAFVTLVDGVPYSDDLRKSLVMTVRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRILR-KIASRQLDELGDTS 721
Cdd:PRK06060 423 ESTGASTLQAFLVATSGATIDGSVMRDLHRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALRkQSPTKPIWELSLTE 502
|
570
....*....|
gi 1205963319 722 TLAD-PGVVD 730
Cdd:PRK06060 503 PGSGvRAQRD 512
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
174-706 |
1.63e-17 |
|
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: 85.95 E-value: 1.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 174 NGDKIAMYWEgnepsqDGKLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSA 253
Cdd:cd17644 13 TPDAVAVVFE------DQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLDPNYPQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 254 EALAQRVIDCKPKVVITcnavkrglkiiflkdivdasldesakngvdvgicltyenqsalnkvdtrwttgrdvwwqdvvp 333
Cdd:cd17644 87 ERLTYILEDAQISVLLT--------------------------------------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 334 dfptkcdvewvDAEDPLFLLYTSGSTGKPKGVL--------HTTGGYMVYSATTFKH-------AFDYKPTDIywctadc 398
Cdd:cd17644 104 -----------QPENLAYVIYTSGSTGKPKGVMiehqslvnLSHGLIKEYGITSSDRvlqfasiAFDVAAEEI------- 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 399 gwitghsYVTygpLLNGATvLVFEGAPNYPDPGRCWDIVDKYGVTIFYTAPTLIRSLMRDGTEYVARySRKSLRVLGSVG 478
Cdd:cd17644 166 -------YVT---LLSGAT-LVLRPEEMRSSLEDFVQYIQQWQLTVLSLPPAYWHLLVLELLLSTID-LPSSLRLVIVGG 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 479 EPINPTAWR-W---------FYDVIGDSRCPISDTWwqtetggFMITPLPGAWPQKPGSATfPFFGVQPVIVDEKGREME 548
Cdd:cd17644 234 EAVQPELVRqWqknvgnfiqLINVYGPTEATIAATV-------CRLTQLTERNITSVPIGR-PIANTQVYILDENLQPVP 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 549 GECSGYLCIkkswpGAFRTLYGDKERYETTYFK----PFAG-----YYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIG 619
Cdd:cd17644 306 VGVPGELHI-----GGVGLARGYLNRPELTAEKfishPFNSseserLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIE 380
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 620 TAEVESALVSHPKCAEAAVVGIDHEVKGQGIYAF-VTLVDGVPYSDDLRKSLvmtvRSQIGAFAAPDKIHWAPGLPKTRS 698
Cdd:cd17644 381 LGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYiVPHYEESPSTVELRQFL----KAKLPDYMIPSAFVVLEELPLTPN 456
|
....*...
gi 1205963319 699 GKIMRRIL 706
Cdd:cd17644 457 GKIDRRAL 464
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
192-714 |
1.74e-17 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 87.91 E-value: 1.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 192 KLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAEALAQRVIDCKPKVVITC 271
Cdd:PRK12467 1599 ELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQ 1678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 272 NAVKRGLKIIflkdivdasldesakNGVDvgiCLTYENQSAlnkvdtrWTTGRDvwwqDVVPDFPtkcdvewVDAEDPLF 351
Cdd:PRK12467 1679 SHLQARLPLP---------------DGLR---SLVLDQEDD-------WLEGYS----DSNPAVN-------LAPQNLAY 1722
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 352 LLYTSGSTGKPKGVLHTTGGyMVYSATTFKHAFDYkptdiywCTADCgWITGHSYV-------TYGPLLNGATVLVfeGA 424
Cdd:PRK12467 1723 VIYTSGSTGRPKGAGNRHGA-LVNRLCATQEAYQL-------SAADV-VLQFTSFAfdvsvweLFWPLINGARLVI--AP 1791
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 425 PN-YPDPGRCWDIVDKYGVTIFYTAPTLIRSLMrdgtEYVARYSR-KSLRVLGSVGEPINPTAWR-WF--------YDVI 493
Cdd:PRK12467 1792 PGaHRDPEQLIQLIERQQVTTLHFVPSMLQQLL----QMDEQVEHpLSLRRVVCGGEALEVEALRpWLerlpdtglFNLY 1867
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 494 GDSRCPISDTWW----QTETGGFMI---TPLPG-AW--------PQKPGSATFPFFGvqpvivdekgreMEGECSGYLci 557
Cdd:PRK12467 1868 GPTETAVDVTHWtcrrKDLEGRDSVpigQPIANlSTyildaslnPVPIGVAGELYLG------------GVGLARGYL-- 1933
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 558 kkSWPGAfrtlygDKERYETTYF-KPFAGYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEA 636
Cdd:PRK12467 1934 --NRPAL------TAERFVADPFgTVGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREA 2005
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 637 AVVGIDHEvKGQGIYAFVTLVD-GVPYSDDLRKSLVMTVRSQIGAfAAPDKI---HWA--PGLPKTRSGKIMRRILRKIA 710
Cdd:PRK12467 2006 VVIAQDGA-NGKQLVAYVVPTDpGLVDDDEAQVALRAILKNHLKA-SLPEYMvpaHLVflARMPLTPNGKLDRKALPAPD 2083
|
....
gi 1205963319 711 SRQL 714
Cdd:PRK12467 2084 ASEL 2087
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
348-704 |
2.07e-17 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 86.09 E-value: 2.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 348 DPLFLLYTSGSTGKPKGVLHTTGGyMVYSATTFKHAFDYKPTDIywCTADCGWITGHSYVT--YGPLLNGATVLVfegap 425
Cdd:PRK05852 177 DDAMIMFTGGTTGLPKMVPWTHAN-IASSVRAIITGYRLSPRDA--TVAVMPLYHGHGLIAalLATLASGGAVLL----- 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 426 nyPDPGRC-----WDIVDKYGVTIFYTAPTLIRSLMRDGTEYVARYSRKSLRVLGSVGEPINPTAWRWFYDVIGdsrCPI 500
Cdd:PRK05852 249 --PARGRFsahtfWDDIKAVGATWYTAVPTIHQILLERAATEPSGRKPAALRFIRSCSAPLTAETAQALQTEFA---APV 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 501 SDTWWQTET---------GGFMITPLPGAWPQKPGSATfpffGVQPVIVDEKGREMEGECSGYLCIkkSWPGAFRTLYGD 571
Cdd:PRK05852 324 VCAFGMTEAthqvtttqiEGIGQTENPVVSTGLVGRST----GAQIRIVGSDGLPLPAGAVGEVWL--RGTTVVRGYLGD 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 572 KERYETTYFKpfaGYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAVVGIDHEVKGQGIY 651
Cdd:PRK05852 398 PTITAANFTD---GWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVA 474
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1205963319 652 AFVTLVDGVPYSDDlrkSLVMTVRSQIGAFAAPDKIHWAPGLPKTRSGKIMRR 704
Cdd:PRK05852 475 AVIVPRESAPPTAE---ELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRR 524
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
164-708 |
2.33e-17 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 86.08 E-value: 2.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 164 NAVDRHveagnGDKIAMYWEgnepsqDGKLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAV 243
Cdd:PRK08279 45 EAAARH-----PDRPALLFE------DQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 244 HSVVFAGFSAEALAQRVIDCKPKVVitcnavkrglkiiflkdIVDASLDE---SAKNGVDVGICLTYENQsalnkvDTRW 320
Cdd:PRK08279 114 VALLNTQQRGAVLAHSLNLVDAKHL-----------------IVGEELVEafeEARADLARPPRLWVAGG------DTLD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 321 TTGRDVWWQDVVPDFPTKCDVEW--VDAEDPLFLLYTSGSTGKPKGVLHTTGGYMVYSAtTFKHAFDYKPTDIYWCTADC 398
Cdd:PRK08279 171 DPEGYEDLAAAAAGAPTTNPASRsgVTAKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMG-GFGGLLRLTPDDVLYCCLPL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 399 GWITGHSYVTYGPLLNGATVLVFE--GAPNYpdpgrcWDIVDKYGVTIFYTAPTLIRSLMRDGTEyvARYSRKSLRVLgs 476
Cdd:PRK08279 250 YHNTGGTVAWSSVLAAGATLALRRkfSASRF------WDDVRRYRATAFQYIGELCRYLLNQPPK--PTDRDHRLRLM-- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 477 VGEPINPTAWRWFYDVIGDSRcpISDTWWQTEtGGFMITPLPGawpqKPGSATF-PFFGVQPV-IV-----------DEK 543
Cdd:PRK08279 320 IGNGLRPDIWDEFQQRFGIPR--ILEFYAASE-GNVGFINVFN----FDGTVGRvPLWLAHPYaIVkydvdtgepvrDAD 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 544 GREME---GEcSGyLCIKKSWPGAFRTLYGDKERYE----TTYFKPFAGYYFSGDGCSRDKDGYHWLTGRVDDVI----- 611
Cdd:PRK08279 393 GRCIKvkpGE-VG-LLIGRITDRGPFDGYTDPEASEkkilRDVFKKGDAWFNTGDLMRDDGFGHAQFVDRLGDTFrwkge 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 612 NVSghrigTAEVESALVSHPKCAEAAVVGIdhEVKGQ----GIYAfVTLVDGVPYsdDLrKSLVMTVRSQIGAFAAPDKI 687
Cdd:PRK08279 471 NVA-----TTEVENALSGFPGVEEAVVYGV--EVPGTdgraGMAA-IVLADGAEF--DL-AALAAHLYERLPAYAVPLFV 539
|
570 580
....*....|....*....|.
gi 1205963319 688 HWAPGLPKTRSGKIMRRILRK 708
Cdd:PRK08279 540 RLVPELETTGTFKYRKVDLRK 560
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
176-706 |
9.28e-17 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 85.22 E-value: 9.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 176 DKIAMYWEGnepsqdGKLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAEA 255
Cdd:PRK05691 1146 ERIALVWDG------GSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAER 1219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 256 LAQRVIDCKPKVVITCNAVKRGLkiiflkdivdasldeSAKNGVDVgICLTyenqsalnkvdtrwTTGRDVWwqdvvpdf 335
Cdd:PRK05691 1220 LAYMLADSGVELLLTQSHLLERL---------------PQAEGVSA-IALD--------------SLHLDSW-------- 1261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 336 PTKCDVEWVDAEDPLFLLYTSGSTGKPKGVLHTTGGyMVYSATTFKHAFDYKPTDIYWCTA---------DCGWitghsy 406
Cdd:PRK05691 1262 PSQAPGLHLHGDNLAYVIYTSGSTGQPKGVGNTHAA-LAERLQWMQATYALDDSDVLMQKApisfdvsvwECFW------ 1334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 407 vtygPLLNGATvLVFEGAPNYPDPGRCWDIVDKYGVTIFYTAPTLIRSLMRdgtEYVARYSRkSLRVLGSVGEPINPTAW 486
Cdd:PRK05691 1335 ----PLITGCR-LVLAGPGEHRDPQRIAELVQQYGVTTLHFVPPLLQLFID---EPLAAACT-SLRRLFSGGEALPAELR 1405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 487 RWFYDVI---------GDSRCPISDTWWQTETGGFMITPLpgawpqkpGSatfPFFGVQPVIVDEKGREMEGECSGYLCI 557
Cdd:PRK05691 1406 NRVLQRLpqvqlhnryGPTETAINVTHWQCQAEDGERSPI--------GR---PLGNVLCRVLDAELNLLPPGVAGELCI 1474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 558 KKSwpGAFRTLYG----DKERY-ETTYFKPFAGYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPK 632
Cdd:PRK05691 1475 GGA--GLARGYLGrpalTAERFvPDPLGEDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPG 1552
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1205963319 633 CAEAAVVgIDHEVKGQGIYAFVTLVDGvpySDDLRKSLVMTVRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRIL 706
Cdd:PRK05691 1553 VAQAAVL-VREGAAGAQLVGYYTGEAG---QEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRAL 1622
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
585-710 |
2.96e-16 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 82.58 E-value: 2.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 585 GYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAVVGIDHEVKGQGIYAFVTLVDGVPYSD 664
Cdd:PLN02479 430 GWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFVTLKPGVDKSD 509
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1205963319 665 D--LRKSLVMTVRSQIGAFAAPDKIHWAPgLPKTRSGKIMRRILRKIA 710
Cdd:PLN02479 510 EaaLAEDIMKFCRERLPAYWVPKSVVFGP-LPKTATGKIQKHVLRAKA 556
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
336-707 |
3.52e-16 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 82.06 E-value: 3.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 336 PTKCDVEWVDAED-----PLF-------LLYTSGSTGKPKGVLhttggymvYS-ATTFKHAFDYKPTDIYWCTA-DC--- 398
Cdd:PRK07008 153 PLLCYETLVGAQDgdydwPRFdenqassLCYTSGTTGNPKGAL--------YShRSTVLHAYGAALPDAMGLSArDAvlp 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 399 --------GW-------ITGHSYVTYGPLLNGATVlvfegapnypdpgrcWDIVDKYGVTIFYTAPTLIRSLMRDGTEYV 463
Cdd:PRK07008 225 vvpmfhvnAWglpysapLTGAKLVLPGPDLDGKSL---------------YELIEAERVTFSAGVPTVWLGLLNHMREAG 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 464 ARYSRKSLRVLGsvGEPINPTAWRWFYDVIGdsrCPISDTWWQTETGGF-MITPLPGAWPQKPGSATF--------PFFG 534
Cdd:PRK07008 290 LRFSTLRRTVIG--GSACPPAMIRTFEDEYG---VEVIHAWGMTEMSPLgTLCKLKWKHSQLPLDEQRkllekqgrVIYG 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 535 VQPVIVDEKGREM--EGECSGYLCIKKSWpgafrtlygdkerYETTYFK----PF-AGYYFSGDGCSRDKDGYHWLTGRV 607
Cdd:PRK07008 365 VDMKIVGDDGRELpwDGKAFGDLQVRGPW-------------VIDRYFRgdasPLvDGWFPTGDVATIDADGFMQITDRS 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 608 DDVINVSGHRIGTAEVESALVSHPKCAEAAVVGIDHEVKGQGIYAFVTLVDGVPYSddlRKSLVMTVRSQIGAFAAPDKI 687
Cdd:PRK07008 432 KDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRPGAEVT---REELLAFYEGKVAKWWIPDDV 508
|
410 420
....*....|....*....|
gi 1205963319 688 HWAPGLPKTRSGKIMRRILR 707
Cdd:PRK07008 509 VFVDAIPHTATGKLQKLKLR 528
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
336-708 |
6.19e-16 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 81.38 E-value: 6.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 336 PTKCDVEWVdAEDPLFLLYTSGSTGKPKGVLHTTGGYMVYSATtfKHAF-DYKPTDIYWCTADCGWITGHSYVTYGPLLN 414
Cdd:PLN02860 162 TTELDYAWA-PDDAVLICFTSGTTGRPKGVTISHSALIVQSLA--KIAIvGYGEDDVYLHTAPLCHIGGLSSALAMLMVG 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 415 GATVLVfegaPNYpDPGRCWDIVDKYGVTIFYTAPTLIRSLMRDGTEYVARYSRKSLRVL----GSVGEPINPTAWRWFy 490
Cdd:PLN02860 239 ACHVLL----PKF-DAKAALQAIKQHNVTSMITVPAMMADLISLTRKSMTWKVFPSVRKIlnggGSLSSRLLPDAKKLF- 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 491 dvigdSRCPISDTWWQTETGG---FMitPLPGAWPQKPGSATFPFFGVQPVIVDEKGremeGECSG----YLCIKKSWPG 563
Cdd:PLN02860 313 -----PNAKLFSAYGMTEACSsltFM--TLHDPTLESPKQTLQTVNQTKSSSVHQPQ----GVCVGkpapHVELKIGLDE 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 564 AFRT-----------LYGDKERYETTYFKPFAGYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPK 632
Cdd:PLN02860 382 SSRVgriltrgphvmLGYWGQNSETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPG 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 633 CAEAAVVGIDHEVKGQGIYAFVTLVDGVPYSD----DLRKSLVMT-------VRSQ-IGAFAAPDKI-HWAPGLPKTRSG 699
Cdd:PLN02860 462 VASVVVVGVPDSRLTEMVVACVRLRDGWIWSDnekeNAKKNLTLSsetlrhhCREKnLSRFKIPKLFvQWRKPFPLTTTG 541
|
....*....
gi 1205963319 700 KIMRRILRK 708
Cdd:PLN02860 542 KIRRDEVRR 550
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
190-708 |
7.49e-16 |
|
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: 80.86 E-value: 7.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 190 DGKLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAEALAQRVIDCKPKVVI 269
Cdd:cd05940 1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 270 TcnavkrglkiiflkdivdasldesakngvdvgicltyenqsalnkvdtrwttgrdvwwqdvvpdfptkcdvewvdaeDP 349
Cdd:cd05940 81 V-----------------------------------------------------------------------------DA 83
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 350 LFLLYTSGSTGKPKGVLHTTGGYmVYSATTFKHAFDYKPTDIYWCTADCGWITGHSYVTYGPLLNGATVLVFE--GAPNY 427
Cdd:cd05940 84 ALYIYTSGTTGLPKAAIISHRRA-WRGGAFFAGSGGALPSDVLYTCLPLYHSTALIVGWSACLASGATLVIRKkfSASNF 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 428 pdpgrcWDIVDKYGVTIFYTAPTLIRSLMRDGTEYVARysRKSLRVLgsVGEPINPTAWRWFYDVIGDSRcpISDTWWQT 507
Cdd:cd05940 163 ------WDDIRKYQATIFQYIGELCRYLLNQPPKPTER--KHKVRMI--FGNGLRPDIWEEFKERFGVPR--IAEFYAAT 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 508 E--TGGFMITPLPGAWPQKPgSATFPFFGVQPVIVD-EKGREMEGEcSGYlCIK--KSWPGAFRTLYGDKERYETtYFKP 582
Cdd:cd05940 231 EgnSGFINFFGKPGAIGRNP-SLLRKVAPLALVKYDlESGEPIRDA-EGR-CIKvpRGEPGLLISRINPLEPFDG-YTDP 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 583 FA--------------GYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAVVGIdhEVKG- 647
Cdd:cd05940 307 AAtekkilrdvfkkgdAWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGV--QVPGt 384
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1205963319 648 QGIYAFVTLVDGVPYSDDLrKSLVMTVRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRK 708
Cdd:cd05940 385 DGRAGMAAIVLQPNEEFDL-SALAAHLEKNLPGYARPLFLRLQPEMEITGTFKQQKVDLRN 444
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
193-708 |
8.26e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 82.13 E-value: 8.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 193 LTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAEALAQRVIDCKPKVVITcn 272
Cdd:PRK12467 538 LSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLT-- 615
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 273 avkrglkiiflkdivdaslDESAKNGVDVGICLTYenqsALNKVDTRWTTGRdvwwQDVVPDFPtkcdvewVDAEDPLFL 352
Cdd:PRK12467 616 -------------------QSHLLAQLPVPAGLRS----LCLDEPADLLCGY----SGHNPEVA-------LDPDNLAYV 661
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 353 LYTSGSTGKPKGVLHTTGGYMVYSATTFKHafdykptdiYWCTADCGWITGHSY-------VTYGPLLNGATVLVFeGAP 425
Cdd:PRK12467 662 IYTSGSTGQPKGVAISHGALANYVCVIAER---------LQLAADDSMLMVSTFafdlgvtELFGALASGATLHLL-PPD 731
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 426 NYPDPGRCWDIVDKYGVTIFYTAPTLIRSLMRDGTEYVARySRKSLRVLGSVGEPINPTAWRWFYDvigdsRCPISDTWW 505
Cdd:PRK12467 732 CARDAEAFAALMADQGVTVLKIVPSHLQALLQASRVALPR-PQRALVCGGEALQVDLLARVRALGP-----GARLINHYG 805
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 506 QTETG-GFMITPLPGAwPQKPGSATF--PFFGVQPVIVDEKGREMEGECSGYLCIkkSWPGAFRTLYG----DKERYETT 578
Cdd:PRK12467 806 PTETTvGVSTYELSDE-ERDFGNVPIgqPLANLGLYILDHYLNPVPVGVVGELYI--GGAGLARGYHRrpalTAERFVPD 882
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 579 YFKPFAG-YYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAVVGIDHEVKGQgIYAFvtLV 657
Cdd:PRK12467 883 PFGADGGrLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQ-LVAY--LV 959
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1205963319 658 DGVPYSD----DLRKSLVMTVRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRK 708
Cdd:PRK12467 960 PAAVADGaehqATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPK 1014
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
328-707 |
1.01e-15 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 80.84 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 328 WQDVVPDFPTKCDVEWVDAEDPLFLLYTSGSTGKPKGVLhTTGGYMVYSATTFKHAFDYKPTDIYWCTADcgwiTGHS-- 405
Cdd:PRK13388 131 YAELVAAAGALTPHREVDAMDPFMLIFTSGTTGAPKAVR-CSHGRLAFAGRALTERFGLTRDDVCYVSMP----LFHSna 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 406 -YVTYGPLL-NGATVLV---FEGAPNYPDpgrcwdiVDKYGVTIF--------YTAPTLIRSLMRDGTeyvarysrksLR 472
Cdd:PRK13388 206 vMAGWAPAVaSGAAVALpakFSASGFLDD-------VRRYGATYFnyvgkplaYILATPERPDDADNP----------LR 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 473 V-LGSVGEPINPTAW-RWFydvigdsRCPISDTWWQTETGGfMITPLPGAwpqKPGSATFPFFGVQ-----------PVI 539
Cdd:PRK13388 269 VaFGNEASPRDIAEFsRRF-------GCQVEDGYGSSEGAV-IVVREPGT---PPGSIGRGAPGVAiynpetltecaVAR 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 540 VDEKGREMEG-ECSGYLcIKKSWPGAFRTLYGDKEryeTTYFKPFAGYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRI 618
Cdd:PRK13388 338 FDAHGALLNAdEAIGEL-VNTAGAGFFEGYYNNPE---ATAERMRHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENL 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 619 GTAEVESALVSHPKCAEAAVVGIDHEVKGQGIYAFVTLVDGVPYSDDlrkSLVMTVRSQ--IGAFAAPDKIHWAPGLPKT 696
Cdd:PRK13388 414 SAAPIERILLRHPAINRVAVYAVPDERVGDQVMAALVLRDGATFDPD---AFAAFLAAQpdLGTKAWPRYVRIAADLPST 490
|
410
....*....|.
gi 1205963319 697 RSGKIMRRILR 707
Cdd:PRK13388 491 ATNKVLKRELI 501
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
190-708 |
1.16e-15 |
|
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: 80.16 E-value: 1.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 190 DGKLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAEALAQRVIDCKPKVVI 269
Cdd:cd05939 1 DRHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 270 TcnavkrglkiiflkDIVDASLDESakngvdvgicltyenqsalnkvdtrwttgrdvwwqdvvPDFPTKCDVewVDAEDP 349
Cdd:cd05939 81 F--------------NLLDPLLTQS--------------------------------------STEPPSQDD--VNFRDK 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 350 LFLLYTSGSTGKPKGVLHTTGGYMVYSATTFKhAFDYKPTDI-YWC-----TAdcGWITGHSYVtygpLLNGATVLVFE- 422
Cdd:cd05939 107 LFYIYTSGTTGLPKAAVIVHSRYYRIAAGAYY-AFGMRPEDVvYDClplyhSA--GGIMGVGQA----LLHGSTVVIRKk 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 423 -GAPNYpdpgrcWDIVDKYGVTIFYTAPTLIRSLMrdGTEYVARYSRKSLRVLgsVGEPINPTAWRWFYDVIGDSRcpIS 501
Cdd:cd05939 180 fSASNF------WDDCVKYNCTIVQYIGEICRYLL--AQPPSEEEQKHNVRLA--VGNGLRPQIWEQFVRRFGIPQ--IG 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 502 DTWWQTE-----------TG--GFMITPLPGAWPqkpgsatfpffgVQPVIVDEKGREMEGECSGyLCI--KKSWPGAF- 565
Cdd:cd05939 248 EFYGATEgnsslvnidnhVGacGFNSRILPSVYP------------IRLIKVDEDTGELIRDSDG-LCIpcQPGEPGLLv 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 566 -RTLYGDKERYETTY--------------FKPFAGYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSH 630
Cdd:cd05939 315 gKIIQNDPLRRFDGYvnegatnkkiardvFKKGDSAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNV 394
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 631 PKCAEAAVVGIdhEVKGQ-------GIYAFVTLVDGVPYSDDLRKSLVmtvrsqigAFAAPDKIHWAPGLPKTRSGKIMR 703
Cdd:cd05939 395 LGLEDVVVYGV--EVPGVegragmaAIVDPERKVDLDRFSAVLAKSLP--------PYARPQFIRLLPEVDKTGTFKLQK 464
|
....*
gi 1205963319 704 RILRK 708
Cdd:cd05939 465 TDLQK 469
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
191-707 |
1.54e-15 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 80.45 E-value: 1.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 191 GK-LTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAEALAQRVIDCKPKVVI 269
Cdd:PRK07059 46 GKaITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPLYTPRELEHQLKDSGAEAIV 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 270 T----CNAVKRGLKIIFLKDIVDASL-DESAKNGVDVGICLtyenqSALNKVDTRWTTGRDVWWQDVVPD------FPTK 338
Cdd:PRK07059 126 VlenfATTVQQVLAKTAVKHVVVASMgDLLGFKGHIVNFVV-----RRVKKMVPAWSLPGHVRFNDALAEgarqtfKPVK 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 339 cdvewVDAEDPLFLLYTSGSTGKPKG--VLHTT-GGYMVYSATTFKHAFDYKPTD-------------IYWCTAdCGWIt 402
Cdd:PRK07059 201 -----LGPDDVAFLQYTGGTTGVSKGatLLHRNiVANVLQMEAWLQPAFEKKPRPdqlnfvcalplyhIFALTV-CGLL- 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 403 ghsyvtyGPLLNGATVLVfegaPNYPD-PGRCWDIvDKYGVTIFYTAPTLIRSLMRdgTEYVARYSRKSLRV-LG---SV 477
Cdd:PRK07059 274 -------GMRTGGRNILI----PNPRDiPGFIKEL-KKYQVHIFPAVNTLYNALLN--NPDFDKLDFSKLIVaNGggmAV 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 478 GEPInptAWRWfYDVIGdsrCPISDTWWQTETGGfMITPLPGAWPQKPGSATFPFFGVQPVIVDEKGREME-GEcSGYLC 556
Cdd:PRK07059 340 QRPV---AERW-LEMTG---CPITEGYGLSETSP-VATCNPVDATEFSGTIGLPLPSTEVSIRDDDGNDLPlGE-PGEIC 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 557 IKKSwpgafRTLYGDKERYETTYFKPFA-GYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAE 635
Cdd:PRK07059 411 IRGP-----QVMAGYWNRPDETAKVMTAdGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLE 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 636 AAVVGIDHEVKGQGIYAFVtlvdgvpysddLRKSLVMTvRSQIGAFAA--------PDKIHWAPGLPKTRSGKIMRRILR 707
Cdd:PRK07059 486 VAAVGVPDEHSGEAVKLFV-----------VKKDPALT-EEDVKAFCKerltnykrPKFVEFRTELPKTNVGKILRRELR 553
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
175-727 |
1.60e-15 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 80.21 E-value: 1.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 175 GDKIAMYWEGNEPSQdgkLTYSELLEKVCQLSNYLK-SVGVGKGDAVVIYLPMLMELPIAMLACARIGAV---------- 243
Cdd:PRK05620 24 GDTTVTTWGGAEQEQ---TTFAAIGARAAALAHALHdELGITGDQRVGSMMYNCAEHLEVLFAVACMGAVfnplnkqlmn 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 244 HSVVFAGFSAEalaQRVIDCKPK-------VVITCNAVKrglKIIFlkdIVDASLDESAKNGVDVGICLTYEnqsALnkV 316
Cdd:PRK05620 101 DQIVHIINHAE---DEVIVADPRlaeqlgeILKECPCVR---AVVF---IGPSDADSAAAHMPEGIKVYSYE---AL--L 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 317 DTRWTtgrdvwwqdvVPDFPTkcdvewVDAEDPLFLLYTSGSTGKPKGVlhttggymVYS-ATTFKHAFDYKPTD----- 390
Cdd:PRK05620 167 DGRST----------VYDWPE------LDETTAAAICYSTGTTGAPKGV--------VYShRSLYLQSLSLRTTDslavt 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 391 ----------IY----WCTADCGWITGhsyvtygpllngaTVLVFEGAPnyPDPGRCWDIVDKYGVTIFYTAPTLIRSLM 456
Cdd:PRK05620 223 hgesflccvpIYhvlsWGVPLAAFMSG-------------TPLVFPGPD--LSAPTLAKIIATAMPRVAHGVPTLWIQLM 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 457 rdgtEYVARYS--RKSLRVLGSVGEPINP---TAW--RWFYDVIgdsrcpisDTWWQTETG--GFMITPLPGA-----WP 522
Cdd:PRK05620 288 ----VHYLKNPpeRMSLQEIYVGGSAVPPiliKAWeeRYGVDVV--------HVWGMTETSpvGTVARPPSGVsgearWA 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 523 QKPGSATFPFfGVQPVIVDEkGREMEG--ECSGYLCIKKSW-------------PGAFRTLYGDKERYETTYFKPfAGYY 587
Cdd:PRK05620 356 YRVSQGRFPA-SLEYRIVND-GQVMEStdRNEGEIQVRGNWvtasyyhspteegGGAASTFRGEDVEDANDRFTA-DGWL 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 588 FSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAVVGIDHEVKGQGIYAFVTLVDGVPYS---- 663
Cdd:PRK05620 433 RTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGIEPTreta 512
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1205963319 664 DDLRKSLvmtvRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRK-IASRQLDELgdtsTLADPG 727
Cdd:PRK05620 513 ERLRDQL----RDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLRQhLADGDFEII----KLKGPG 569
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
192-710 |
2.45e-15 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 79.68 E-value: 2.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 192 KLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAEALAQRVIDCKPKVVItc 271
Cdd:PLN03102 39 RFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILF-- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 272 naVKRGLKIIFLKDIVDASLDESAKNgvdVGICLTYENQSalnkvdTRWTTGRDVWWQDVVPDF-PTKCDVEWV----DA 346
Cdd:PLN03102 117 --VDRSFEPLAREVLHLLSSEDSNLN---LPVIFIHEIDF------PKRPSSEELDYECLIQRGePTPSLVARMfriqDE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 347 EDPLFLLYTSGSTGKPKGVLHT-TGGYMvySATTFKHAFDYKPTDIYWCTA---DC-GWItghsyVTYGPLLNGATVLVF 421
Cdd:PLN03102 186 HDPISLNYTSGTTADPKGVVIShRGAYL--STLSAIIGWEMGTCPVYLWTLpmfHCnGWT-----FTWGTAARGGTSVCM 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 422 E--GAPnypdpgRCWDIVDKYGVTIFYTAPTLIRSLMRdGTEYVARYSRKSLRVLGSVGEPinPTAWRWFYDVIGDSrcp 499
Cdd:PLN03102 259 RhvTAP------EIYKNIEMHNVTHMCCVPTVFNILLK-GNSLDLSPRSGPVHVLTGGSPP--PAALVKKVQRLGFQ--- 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 500 ISDTWWQTE-TGGFMITPLPGAWPQKPGSATFPFFGVQPVI------VDEKGREM------EGECSGYLCIKKSwpgAFR 566
Cdd:PLN03102 327 VMHAYGLTEaTGPVLFCEWQDEWNRLPENQQMELKARQGVSilgladVDVKNKETqesvprDGKTMGEIVIKGS---SIM 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 567 TLYGDKERYETTYFKpfAGYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAVVGIDHEVK 646
Cdd:PLN03102 404 KGYLKNPKATSEAFK--HGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTW 481
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1205963319 647 GQGIYAFVTLVDGVPYSDDLRKSLVMT-------VRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKIA 710
Cdd:PLN03102 482 GETPCAFVVLEKGETTKEDRVDKLVTRerdlieyCRENLPHFMCPRKVVFLQELPKNGNGKILKPKLRDIA 552
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
193-640 |
4.11e-15 |
|
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: 78.66 E-value: 4.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 193 LTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAEALAQrvidckpkvVITcn 272
Cdd:cd05932 7 FTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRY---------VLE-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 273 avKRGLKIIFLkdivdASLD--ESAKNGVDVGI--CLTYEnQSALNKVDTrwttgrdvwWQDVVPDFPTKCDVEWVDAED 348
Cdd:cd05932 76 --HSESKALFV-----GKLDdwKAMAPGVPEGLisISLPP-PSAANCQYQ---------WDDLIAQHPPLEERPTRFPEQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 349 PLFLLYTSGSTGKPKGVLHTTGGYmVYSATTFKHAFDYKPTDIYWCTADCGWITGHSYVTYGPLLNGATVLVFEGAPNYP 428
Cdd:cd05932 139 LATLIYTSGTTGQPKGVMLTFGSF-AWAAQAGIEHIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAESLDTFV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 429 DPgrcwdiVDKYGVTIFYTAPTLIrSLMRDG-------------------TEYVARYSRKSL-----RVLGSVGEPINPT 484
Cdd:cd05932 218 ED------VQRARPTLFFSVPRLW-TKFQQGvqdkipqqklnlllkipvvNSLVKRKVLKGLgldqcRLAGCGSAPVPPA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 485 AWRWfYDVIGdsrCPISDTWWQTETGGFMITPLPGAwpQKPGSATFPFFGVQPVIVDEkgremegecsGYLCIKKswPGA 564
Cdd:cd05932 291 LLEW-YRSLG---LNILEAYGMTENFAYSHLNYPGR--DKIGTVGNAGPGVEVRISED----------GEILVRS--PAL 352
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1205963319 565 FRTLYGDKERYETTYFKPfaGYYFSGDGCSRDKDGYHWLTGRVDDVINVS-GHRIGTAEVESALVSHPKCAEAAVVG 640
Cdd:cd05932 353 MMGYYKDPEATAEAFTAD--GFLRTGDKGELDADGNLTITGRVKDIFKTSkGKYVAPAPIENKLAEHDRVEMVCVIG 427
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
193-710 |
7.63e-15 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 77.99 E-value: 7.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 193 LTYSELLEKVCQLSNYL-KSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAEALAQRVIDCKPKVVIT- 270
Cdd:PRK08751 51 ITYREADQLVEQFAAYLlGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLVVi 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 271 ---CNAVKRGLKIIFLKDIVDASLdesakngvdvGICLTYENQSALNKVDTrwttgrdvWWQDVVPDFPTKCDVEWVDA- 346
Cdd:PRK08751 131 dnfGTTVQQVIADTPVKQVITTGL----------GDMLGFPKAALVNFVVK--------YVKKLVPEYRINGAIRFREAl 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 347 ---------------EDPLFLLYTSGSTGKPKGVLHTTGGyMVYSATTFKHafdykptdiyWCTADCGWITGHSYV-TYG 410
Cdd:PRK08751 193 algrkhsmptlqiepDDIAFLQYTGGTTGVAKGAMLTHRN-LVANMQQAHQ----------WLAGTGKLEEGCEVViTAL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 411 PLLN----GATVLVFE--GAPNY----PD--PGRCWDIvDKYGVTIFYTAPTLIRSLMrdGTEYVARYSRKSLRVLGSVG 478
Cdd:PRK08751 262 PLYHifalTANGLVFMkiGGCNHlisnPRdmPGFVKEL-KKTRFTAFTGVNTLFNGLL--NTPGFDQIDFSSLKMTLGGG 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 479 EPIN-PTAWRWfYDVIGdsrCPISDTWWQTETG-GFMITPLpgAWPQKPGSATFPFFGVQPVIVDEKGREME-GECsGYL 555
Cdd:PRK08751 339 MAVQrSVAERW-KQVTG---LTLVEAYGLTETSpAACINPL--TLKEYNGSIGLPIPSTDACIKDDAGTVLAiGEI-GEL 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 556 CIKKswPGAFRTLYGDKEryETTYFKPFAGYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAE 635
Cdd:PRK08751 412 CIKG--PQVMKGYWKRPE--ETAKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLE 487
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1205963319 636 AAVVGIDHEVKGQGIYAFVTLVDGVPYSDDLRKSlvmtVRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKIA 710
Cdd:PRK08751 488 VAAVGVPDEKSGEIVKVVIVKKDPALTAEDVKAH----ARANLTGYKQPRIIEFRKELPKTNVGKILRRELRDAA 558
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
352-703 |
7.86e-15 |
|
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: 76.39 E-value: 7.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 352 LLYTSGSTGKPKGVL----HTTGGYMVYSATT-------------FKHAFDYKptdiywctadCGWITGhsyvtygpLLN 414
Cdd:cd17638 5 IMFTSGTTGRSKGVMcahrQTLRAAAAWADCAdlteddryliinpFFHTFGYK----------AGIVAC--------LLT 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 415 GATVL---VFegapnypDPGRCWDIVDKYGVTIFYTAPTLIRSLMrdGTEYVARYSRKSLRVLGSVGEPINPTAWRWFYD 491
Cdd:cd17638 67 GATVVpvaVF-------DVDAILEAIERERITVLPGPPTLFQSLL--DHPGRKKFDLSSLRAAVTGAATVPVELVRRMRS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 492 VIGDSRcpISDTWWQTETG-GFMITPLPGAWPQKPGSATfPFFGVQPVIVDEKGREMEGE--CSGYLcikkswpgafrtl 568
Cdd:cd17638 138 ELGFET--VLTAYGLTEAGvATMCRPGDDAETVATTCGR-ACPGFEVRIADDGEVLVRGYnvMQGYL------------- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 569 yGDKERYETTYFKPfaGYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAVVGIDHEVKGQ 648
Cdd:cd17638 202 -DDPEATAEAIDAD--GWLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGE 278
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1205963319 649 GIYAFVTLVDGVPYSDDlrkSLVMTVRSQIGAFAAPDKIHWAPGLPKTRSGKIMR 703
Cdd:cd17638 279 VGKAFVVARPGVTLTEE---DVIAWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
194-708 |
8.14e-15 |
|
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: 77.47 E-value: 8.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 194 TYSELLEKVCQLSNYLKSV-GVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAEALAQRVIDCKPKVVItcn 272
Cdd:cd05937 7 TYSETYDLVLRYAHWLHDDlGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSRFVI--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 273 avkrglkiiflkdivdasldesakngvdvgicltyenqsalnkvdtrwttgrdvwwqdvvpdfptkcdvewVDAEDPLFL 352
Cdd:cd05937 84 -----------------------------------------------------------------------VDPDDPAIL 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 353 LYTSGSTGKPKGVLHTTGGYMVySATTFKHAFDYKPTDIYWCTADCGWITGHSYVTYGPLLNGATVLVfegAPNYpDPGR 432
Cdd:cd05937 93 IYTSGTTGLPKAAAISWRRTLV-TSNLLSHDLNLKNGDRTYTCMPLYHGTAAFLGACNCLMSGGTLAL---SRKF-SASQ 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 433 CWDIVDKYGVTIFYTAPTLIRSLMRDGTEyvaRYSRKSlRVLGSVGEPINPTAWRWFYDVIGDSRcpISDTWWQTETGGF 512
Cdd:cd05937 168 FWKDVRDSGATIIQYVGELCRYLLSTPPS---PYDRDH-KVRVAWGNGLRPDIWERFRERFNVPE--IGEFYAATEGVFA 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 513 MITPLPGAWP----QKPGSATFPFFGVQPVIV------------DEKG------REMEGECSGYLCIK--KSWPGAFRTL 568
Cdd:cd05937 242 LTNHNVGDFGagaiGHHGLIRRWKFENQVVLVkmdpetddpirdPKTGfcvrapVGEPGEMLGRVPFKnrEAFQGYLHNE 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 569 YGDKERYETTYFKPFAGYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAVVGI---DHEv 645
Cdd:cd05937 322 DATESKLVRDVFRKGDIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVkvpGHD- 400
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1205963319 646 kGQGIYAFVTLVDGVPYSDDLRKSLVMTV-RSQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRK 708
Cdd:cd05937 401 -GRAGCAAITLEESSAVPTEFTKSLLASLaRKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLRD 463
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
481-710 |
9.00e-15 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 77.94 E-value: 9.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 481 INPTAWRWfYDVIGdsrCPISDTWWQTETggfmiTPLPGAWP----QKPGSATFPFFGVQPVIVDEKGREME-GEcSGYL 555
Cdd:PRK12492 346 VKATAERW-EQLTG---CTIVEGYGLTET-----SPVASTNPygelARLGTVGIPVPGTALKVIDDDGNELPlGE-RGEL 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 556 CIKKSwpgafRTLYGDKERYETTYFKPFA-GYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCA 634
Cdd:PRK12492 416 CIKGP-----QVMKGYWQQPEATAEALDAeGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVA 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1205963319 635 EAAVVGIDHEVKGQGIYAFVTLVDGVPYSDDLRKslvmTVRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKIA 710
Cdd:PRK12492 491 NCAAIGVPDERSGEAVKLFVVARDPGLSVEELKA----YCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELRDIA 562
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
484-714 |
1.66e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 77.11 E-value: 1.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 484 TAWRWfYDVIGdsrCPISDTWWQTETggfmiTPLPGAWPQK---PGSATFPFFGVQPVIVDEKGREMEGECSGYLCIKKs 560
Cdd:PRK05677 342 TAERW-KEVTG---CAICEGYGMTET-----SPVVSVNPSQaiqVGTIGIPVPSTLCKVIDDDGNELPLGEVGELCVKG- 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 561 wPGAFRTLYGDKEryETTYFKPFAGYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAVVG 640
Cdd:PRK05677 412 -PQVMKGYWQRPE--ATDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIG 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1205963319 641 IDHEVKGQGIYAFVTLVDGVpysdDLRKSLVMT-VRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKIASRQL 714
Cdd:PRK05677 489 VPDEKSGEAIKVFVVVKPGE----TLTKEQVMEhMRANLTGYKVPKAVEFRDELPTTNVGKILRRELRDEELKKA 559
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
348-699 |
3.43e-13 |
|
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: 71.18 E-value: 3.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 348 DPLFLLYTSGSTGKPKGVLHTTGGYMVYSattfkhafdykptdiyWCTADCGWITGHS-YVTYGPL------LNGATVLV 420
Cdd:cd17636 1 DPVLAIYTAAFSGRPNGALLSHQALLAQA----------------LVLAVLQAIDEGTvFLNSGPLfhigtlMFTLATFH 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 421 FEGAPNY---PDPGRCWDIVDKYGVT-IFYTAPTL--IRSLMRDGteyvaRYSRKSLRVLgsvgepinPTAWRWFYDVig 494
Cdd:cd17636 65 AGGTNVFvrrVDAEEVLELIEAERCThAFLLPPTIdqIVELNADG-----LYDLSSLRSS--------PAAPEWNDMA-- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 495 dsrcPISDTWW--------QTETGGFMITPLPGAwpQKPGSATFPFFGVQPVIVDEKGREM-EGEcSGYLCIKKswPGAF 565
Cdd:cd17636 130 ----TVDTSPWgrkpggygQTEVMGLATFAALGG--GAIGGAGRPSPLVQVRILDEDGREVpDGE-VGEIVARG--PTVM 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 566 RTLYGdkeRYETTYFKPFAGYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAVVGIDHEV 645
Cdd:cd17636 201 AGYWN---RPEVNARRTRGGWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPR 277
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1205963319 646 KGQGIYAFVTLVDGVPYSDDlrkSLVMTVRSQIGAFAAPDKIHWAPGLPKTRSG 699
Cdd:cd17636 278 WAQSVKAIVVLKPGASVTEA---ELIEHCRARIASYKKPKSVEFADALPRTAGG 328
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
190-706 |
3.98e-13 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 72.73 E-value: 3.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 190 DG--KLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAEALAQRVIDCKPKV 267
Cdd:PRK05857 37 DGtsALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAAIERFCQITDPAA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 268 VItcnaVKRGLKIiflkdiVDASLDESAKNGVDVGICLTYENQSALNKVDTRWTTGRdvwwqdvvPDFptkcdvewvDAE 347
Cdd:PRK05857 117 AL----VAPGSKM------ASSAVPEALHSIPVIAVDIAAVTRESEHSLDAASLAGN--------ADQ---------GSE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 348 DPLFLLYTSGSTGKPKGVLhttggymVYSATTFKHAFDYKPTDIYWCTadcgWITGHSyvTYGPL-----------LNGA 416
Cdd:PRK05857 170 DPLAMIFTSGTTGEPKAVL-------LANRTFFAVPDILQKEGLNWVT----WVVGET--TYSPLpathigglwwiLTCL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 417 T--VLVFEGAPNypdPGRCWDIVDKYGVTIFYTAPTLIRSLMRDGTeyVARYSRKSLRVLGSVGEPINPTAWRwFYDVIG 494
Cdd:PRK05857 237 MhgGLCVTGGEN---TTSLLEILTTNAVATTCLVPTLLSKLVSELK--SANATVPSLRLVGYGGSRAIAADVR-FIEATG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 495 dsrCPISDTWWQTETGGFMITpLP---GAWPQ-KPGSATFPFFGVQPVIVDEKG------REMEGECSGYLCIKKswPGA 564
Cdd:PRK05857 311 ---VRTAQVYGLSETGCTALC-LPtddGSIVKiEAGAVGRPYPGVDVYLAATDGigptapGAGPSASFGTLWIKS--PAN 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 565 FRTLYGDKERYETTYFKpfaGYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAVVGIDHE 644
Cdd:PRK05857 385 MLGYWNNPERTAEVLID---GWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDE 461
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 645 VKGqgiyAFVTLvdGVPYSDDLRKSLVMTVRSQIGA--------FAAPDKIHWAPGLPKTRSGKIMRRIL 706
Cdd:PRK05857 462 EFG----ALVGL--AVVASAELDESAARALKHTIAArfrresepMARPSTIVIVTDIPRTQSGKVMRASL 525
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
580-708 |
2.95e-12 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 68.92 E-value: 2.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 580 FKPFA--GYYFSGDGCSRDkDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAVVGIDHEVKGQGIYA-FVTL 656
Cdd:PRK07824 227 PDPFAepGWFRTDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAaVVGD 305
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1205963319 657 VDGVPYSDDLRKSLVMTvrsqIGAFAAPDKIHWAPGLPKTRSGKIMRRILRK 708
Cdd:PRK07824 306 GGPAPTLEALRAHVART----LDRTAAPRELHVVDELPRRGIGKVDRRALVR 353
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
176-706 |
7.72e-12 |
|
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: 67.96 E-value: 7.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 176 DKIAMYWEGNepsqdgKLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAEA 255
Cdd:cd17645 13 DHVAVVDRGQ------SLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGER 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 256 LAQRVIDCKPKVVITcnavkrglkiiflkdivdasldesakngvdvgicltyenqsalnkvdtrwttgrdvwwqdvvpdf 335
Cdd:cd17645 87 IAYMLADSSAKILLT----------------------------------------------------------------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 336 ptkcdvewvDAEDPLFLLYTSGSTGKPKGVL--HTTggyMVYSATTFKHAFDYKPTDIYWCTADCGWiTGHSYVTYGPLL 413
Cdd:cd17645 102 ---------NPDDLAYVIYTSGSTGLPKGVMieHHN---LVNLCEWHRPYFGVTPADKSLVYASFSF-DASAWEIFPHLT 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 414 NGATVLVFEGAPNYpDPGRCWDIVDKYGVTIFYTaPTLIrslmrdgTEYVARYSRKSLRVLGSVGEPINPTAWRWF--YD 491
Cdd:cd17645 169 AGAALHVVPSERRL-DLDALNDYFNQEGITISFL-PTGA-------AEQFMQLDNQSLRVLLTGGDKLKKIERKGYklVN 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 492 VIGDSRCPIsdtwwqtetggfMITPLPGAWPQKPGSATFPFFGVQPVIVDEKGREMEGECSGYLCIKKSwpGAFRTLYG- 570
Cdd:cd17645 240 NYGPTENTV------------VATSFEIDKPYANIPIGKPIDNTRVYILDEALQLQPIGVAGELCIAGE--GLARGYLNr 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 571 ---DKERYETTYFKPFAGYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAVVGIDHEVKG 647
Cdd:cd17645 306 pelTAEKFIVHPFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGR 385
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1205963319 648 QGIYAFVTLVDGVPYsDDLRKSLvmtvRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRIL 706
Cdd:cd17645 386 KYLVAYVTAPEEIPH-EELREWL----KNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
193-627 |
1.77e-11 |
|
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: 67.31 E-value: 1.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 193 LTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACarigavhsvVFAGFSAealaqrVIDCKPKVVITCN 272
Cdd:cd05906 40 QSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWAC---------VLAGFVP------APLTVPPTYDEPN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 273 AVKRGLKIIFlkdivdASLDEsakngvdvGICLT-YENQSALNKVDTRWttGRDVWWQDVVPDFP-TKCDVEWV--DAED 348
Cdd:cd05906 105 ARLRKLRHIW------QLLGS--------PVVLTdAELVAEFAGLETLS--GLPGIRVLSIEELLdTAADHDLPqsRPDD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 349 PLFLLYTSGSTGKPKGVLHTTGGYMVYSATTFKHaFDYKPTDIY--WCTADcgWITGHSYVTYGPLLNG------ATVLV 420
Cdd:cd05906 169 LALLMLTSGSTGFPKAVPLTHRNILARSAGKIQH-NGLTPQDVFlnWVPLD--HVGGLVELHLRAVYLGcqqvhvPTEEI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 421 FEgapnypDPGRCWDIVDKYGVTIFYtAPTLIRSLMRDGTEYV--ARYSRKSLRVLGSVGEPINPTAWRWFYDVIGDSRC 498
Cdd:cd05906 246 LA------DPLRWLDLIDRYRVTITW-APNFAFALLNDLLEEIedGTWDLSSLRYLVNAGEAVVAKTIRRLLRLLEPYGL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 499 P---ISDTWWQTETGGFMITPLPGAWPQKPGSATF-----PFFGVQPVIVDEKGREMEGECSGYLCIKKswPGAFRTLYG 570
Cdd:cd05906 319 PpdaIRPAFGMTETCSGVIYSRSFPTYDHSQALEFvslgrPIPGVSMRIVDDEGQLLPEGEVGRLQVRG--PVVTKGYYN 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1205963319 571 DKERYETTYFKpfAGYYFSGD-GCSRDkdGYHWLTGRVDDVINVSGHRIGTAEVESAL 627
Cdd:cd05906 397 NPEANAEAFTE--DGWFRTGDlGFLDN--GNLTITGRTKDTIIVNGVNYYSHEIEAAV 450
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
193-412 |
3.21e-11 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 66.92 E-value: 3.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 193 LTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAEAL--AQRVIDCKpkvVIT 270
Cdd:PTZ00216 122 ITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALayALRETECK---AIV 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 271 CNA--VKR-----------GLKIIFLkDIVDASLDesaKNGVDVgicltyenqsalnkvdtrwttgrdVWWQDVV----- 332
Cdd:PTZ00216 199 CNGknVPNllrlmksggmpNTTIIYL-DSLPASVD---TEGCRL------------------------VAWTDVVakghs 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 333 ------PDFPTKCDvewvdaeDPLFLLYTSGSTGKPKGVLHTTGgymvySATTFKHAFDYKPTDIYWCTADcgwitGHSY 406
Cdd:PTZ00216 251 agshhpLNIPENND-------DLALIMYTSGTTGDPKGVMHTHG-----SLTAGILALEDRLNDLIGPPEE-----DETY 313
|
....*.
gi 1205963319 407 VTYGPL 412
Cdd:PTZ00216 314 CSYLPL 319
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
190-706 |
3.76e-11 |
|
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: 65.88 E-value: 3.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 190 DGKLTYSELLEKVCQLSNYLKSVGVGKGDAVV-IYLPMLMELPIAMLACARIGAVHSVVFAGFSAEALAQRVIDCKPKVV 268
Cdd:cd17648 10 DKRLTYRELNERANRLAHYLLSVAEIRPDDLVgLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFILEDTGARVV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 269 ITcnavkrglkiiflkdivdasldesakngvdvgicltyenqsalnkvdtrwttgrdvwwqdvvpdfptkcdvewvDAED 348
Cdd:cd17648 90 IT--------------------------------------------------------------------------NSTD 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 349 PLFLLYTSGSTGKPKGVLHTTGGyMVYSATTFKHAFDYKptdiywCTADCGWITGHSYV-------TYGPLLNGATVLVF 421
Cdd:cd17648 96 LAYAIYTSGTTGKPKGVLVEHGS-VVNLRTSLSERYFGR------DNGDEAVLFFSNYVfdffveqMTLALLNGQKLVVP 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 422 EGAPNYpDPGRCWDIVDKYGVTIFYTAPTLIRslmrdgtEYVARySRKSLRVLGSVGEPINPTAwrwFYDVIGDSRCPIS 501
Cdd:cd17648 169 PDEMRF-DPDRFYAYINREKVTYLSGTPSVLQ-------QYDLA-RLPHLKRVDAAGEEFTAPV---FEKLRSRFAGLII 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 502 DTWWQTETGGF-MITPLPGAwPQKPGSATFPFFGV---------QPVIVDEKGR-EMEGEC--SGY-----LCIKKSWPG 563
Cdd:cd17648 237 NAYGPTETTVTnHKRFFPGD-QRFDKSLGRPVRNTkcyvlndamKRVPVGAVGElYLGGDGvaRGYlnrpeLTAERFLPN 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 564 AFRTlygDKERYETTYfkpfAGYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAVVGIDH 643
Cdd:cd17648 316 PFQT---EQERARGRN----ARLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKED 388
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1205963319 644 EVKGQG-----IYAFVTLVDGVPYSDDLRKSLvmtvRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRIL 706
Cdd:cd17648 389 ASQAQSriqkyLVGYYLPEPGHVPESDLLSFL----RAKLPRYMVPARLVRLEGIPVTINGKLDVRAL 452
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
351-706 |
1.85e-10 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 64.80 E-value: 1.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 351 FLLYTSGSTGKPKGVLHTTGG----------YMVYS-----ATTFKHAFDykptdiywctadcgwITGHSYVTyGPLLNG 415
Cdd:PRK05691 3873 YVIYTSGSTGLPKGVMVEQRGmlnnqlskvpYLALSeadviAQTASQSFD---------------ISVWQFLA-APLFGA 3936
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 416 ATVLVfegaPN--YPDPGRCWDIVDKYGVTIFYTAPTLIRSLMRDgteyvARYSRKSLRVLGSVGEPINPT-AWRWF--Y 490
Cdd:PRK05691 3937 RVEIV----PNaiAHDPQGLLAHVQAQGITVLESVPSLIQGMLAE-----DRQALDGLRWMLPTGEAMPPElARQWLqrY 4007
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 491 DVIGdsrcpisdtwwqtetggfmitpLPGAWPQKPGSATFPFFGVQ---------PV----------IVDEKGREMEGEC 551
Cdd:PRK05691 4008 PQIG----------------------LVNAYGPAECSDDVAFFRVDlastrgsylPIgsptdnnrlyLLDEALELVPLGA 4065
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 552 SGYLCIKKSwpGAFRTLYGDKERYETTYF-KPFAG----YYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESA 626
Cdd:PRK05691 4066 VGELCVAGT--GVGRGYVGDPLRTALAFVpHPFGApgerLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEAR 4143
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 627 LVSHPKCAEAAvVGIDHEVKGQGIYAFVTLVDGVPYSDDLRKSLVMTVRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRIL 706
Cdd:PRK05691 4144 LHEQAEVREAA-VAVQEGVNGKHLVGYLVPHQTVLAQGALLERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKAL 4222
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
193-701 |
2.47e-10 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 63.26 E-value: 2.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 193 LTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVhsvvFAGFSAEALAQRVIDCKPKVVITCN 272
Cdd:cd17654 17 VSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAA----YAPIDPASPEQRSLTVMKKCHVSYL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 273 AVKRGLKIIFLKDIvdaslDESAKNGVDVGICLTYenqsalnkvdtrwttgrdvwwqdvvpdfptkcdvewvdaedplfL 352
Cdd:cd17654 93 LQNKELDNAPLSFT-----PEHRHFNIRTDECLAY--------------------------------------------V 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 353 LYTSGSTGKPKGVlHTTGGYMVYSATTFKHAFDYKPTDIYWCTadcgwitghSYVTYGP--------LLNGATVLVFEGA 424
Cdd:cd17654 124 IHTSGTTGTPKIV-AVPHKCILPNIQHFRSLFNITSEDILFLT---------SPLTFDPsvveiflsLSSGATLLIVPTS 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 425 PNyPDPGRCWDIVDK-YGVTIFYTAPTLIRSLMRDGTEYVARYSRKSLRVLGSVGEPInPT-----AWRWFYDvigdsRC 498
Cdd:cd17654 194 VK-VLPSKLADILFKrHRITVLQATPTLFRRFGSQSIKSTVLSATSSLRVLALGGEPF-PSlvilsSWRGKGN-----RT 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 499 PISDTWWQTETGGFMIT--------PLPGAwpqkpgsatFPFFGVQPVIVDEKGREMEGECSGYLCIKkswpGAFRtlyg 570
Cdd:cd17654 267 RIFNIYGITEVSCWALAykvpeedsPVQLG---------SPLLGTVIEVRDQNGSEGTGQVFLGGLNR----VCIL---- 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 571 dkERYETTyfkPFAGYYFSGDGCSRdKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAVVGIDHevkgQGI 650
Cdd:cd17654 330 --DDEVTV---PKGTMRATGDFVTV-KDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAVTLSDQ----QRL 399
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1205963319 651 YAFVTlvdGVPYSDDLRKSLVMTVRSqigAFAAPDKIHWAPGLPKTRSGKI 701
Cdd:cd17654 400 IAFIV---GESSSSRIHKELQLTLLS---SHAIPDTFVQIDKLPLTSHGKV 444
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
193-511 |
2.94e-10 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 63.38 E-value: 2.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 193 LTYSELLEKVCQLSNYLKSVGVGKGD-AVVIYLPMLmELPIAMLACARIGAVHSVVFAGFSAEALAQRVIDCKPKVVITc 271
Cdd:PRK09274 42 LSFAELDARSDAIAHGLNAAGIGRGMrAVLMVTPSL-EFFALTFALFKAGAVPVLVDPGMGIKNLKQCLAEAQPDAFIG- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 272 NAVKRGLKIIFLKdivdasldesAKNGVDvgicltyenqsalnkvdTRWTTGRDVWWQDVVPDFPTKCDVE------WVD 345
Cdd:PRK09274 120 IPKAHLARRLFGW----------GKPSVR-----------------RLVTVGGRLLWGGTTLATLLRDGAAapfpmaDLA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 346 AEDPLFLLYTSGSTGKPKGVlhttggymVYSATTF-------KHAFDYKPTDIYWCTADCgwitghsYVTYGPLLNGATV 418
Cdd:PRK09274 173 PDDMAAILFTSGSTGTPKGV--------VYTHGMFeaqiealREDYGIEPGEIDLPTFPL-------FALFGPALGMTSV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 419 lVFEGAPNYP---DPGRCWDIVDKYGVTIFYTAPTLIRSLMRDGTEYVARYSrkSLRVLGSVGEPINPTAWRWFYDVIGD 495
Cdd:PRK09274 238 -IPDMDPTRPatvDPAKLFAAIERYGVTNLFGSPALLERLGRYGEANGIKLP--SLRRVISAGAPVPIAVIERFRAMLPP 314
|
330 340 350
....*....|....*....|....*....|....*.
gi 1205963319 496 --------------------SRCPISDTWWQTETGG 511
Cdd:PRK09274 315 daeiltpygatealpissieSREILFATRAATDNGA 350
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
584-716 |
5.09e-10 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 62.52 E-value: 5.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 584 AGYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAVVGIDHEVKGQGIYAFVTLVDGVPYS 663
Cdd:PRK08315 426 DGWMHTGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGATLT 505
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1205963319 664 -DDLRKSLvmtvRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKIASRQLDE 716
Cdd:PRK08315 506 eEDVRDFC----RGKIAHYKIPRYIRFVDEFPMTVTGKIQKFKMREMMIEELGL 555
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
189-703 |
1.07e-09 |
|
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: 61.30 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 189 QDGKLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAEALAQRVIDCKPKVV 268
Cdd:cd05914 4 GGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 269 ITCnavkrglkiiflkdivdasldesakngvdvgicltyenqsalnkvdtrwttgrdvwwqdvvpdfptkcdvewvDAED 348
Cdd:cd05914 84 FVS-------------------------------------------------------------------------DEDD 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 349 PLFLLYTSGSTGKPKGVLhTTGGYMVYSATTFKHAFDYKPTDIYWCTADCGWITGHSYVTYGPLLNGATVlVF------- 421
Cdd:cd05914 91 VALINYTSGTTGNSKGVM-LTYRNIVSNVDGVKEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHV-VFldkipsa 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 422 --------EGAPNYPDPgRCWDIVDKYGVTI------------FYTAP--TLIRSLMRdgteyvarysRKSLRVLG---- 475
Cdd:cd05914 169 kiialafaQVTPTLGVP-VPLVIEKIFKMDIipkltlkkfkfkLAKKInnRKIRKLAF----------KKVHEAFGgnik 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 476 ---SVGEPINPTAWRWFYDVigdsRCPISDTWWQTETGGFMITPLPGAwpQKPGSATFPFFGVQPVIVDEKGREMEGE-- 550
Cdd:cd05914 238 efvIGGAKINPDVEEFLRTI----GFPYTIGYGMTETAPIISYSPPNR--IRLGSAGKVIDGVEVRIDSPDPATGEGEii 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 551 CSGYLCIKKSW--PGAFRTLYgDKEryettyfkpfaGYYFSGDGCSRDKDGYHWLTGRVDDVI-NVSGHRIGTAEVESAL 627
Cdd:cd05914 312 VRGPNVMKGYYknPEATAEAF-DKD-----------GWFHTGDLGKIDAEGYLYIRGRKKEMIvLSSGKNIYPEEIEAKI 379
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 628 VSHPKCAEAAVVGIDhevkgqgiYAFVTLVdgVPYSDDLR----------KSLVMTVRSQIGAfAAPD-------KIHWA 690
Cdd:cd05914 380 NNMPFVLESLVVVQE--------KKLVALA--YIDPDFLDvkalkqrniiDAIKWEVRDKVNQ-KVPNykkiskvKIVKE 448
|
570
....*....|...
gi 1205963319 691 PgLPKTRSGKIMR 703
Cdd:cd05914 449 E-FEKTPKGKIKR 460
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
186-392 |
1.15e-09 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 61.67 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 186 EPSQDGK------------LTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSA 253
Cdd:PLN02387 88 ETSSDGRkfeklhlgeyewITYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGE 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 254 EALAQRVIDCKPKVVItCNAVKrglkiifLKDIVDASLD-ESAKNGV---DVGICLTYENQSALNKVDTRWTT----GRD 325
Cdd:PLN02387 168 EALCHSLNETEVTTVI-CDSKQ-------LKKLIDISSQlETVKRVIymdDEGVDSDSSLSGSSNWTVSSFSEveklGKE 239
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1205963319 326 vwwQDVVPDFPTKCDVEWVdaedplflLYTSGSTGKPKGVLHTTGGYMVYSATTFKHAFDYKPTDIY 392
Cdd:PLN02387 240 ---NPVDPDLPSPNDIAVI--------MYTSGSTGLPKGVMMTHGNIVATVAGVMTVVPKLGKNDVY 295
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
580-714 |
1.33e-09 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 61.16 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 580 FKPFAGYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAVVGIDHEVKGQGIYAFVTLVDG 659
Cdd:PRK07445 319 ILDSQGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVPKDP 398
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1205963319 660 VPYSDDLRkslvMTVRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKIASRQL 714
Cdd:PRK07445 399 SISLEELK----TAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQIAVQRL 449
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
351-706 |
2.58e-09 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 60.95 E-value: 2.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 351 FLLYTSGSTGKPKGVLHTTGGYMVYSATTFKhAFDYKPTD----IYWCTADCGwitghSYVTYGPLLNGA-TVLVFEGAp 425
Cdd:PRK05691 2337 YLIYTSGSTGKPKGVVVSHGEIAMHCQAVIE-RFGMRADDcelhFYSINFDAA-----SERLLVPLLCGArVVLRAQGQ- 2409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 426 nypdpgrcWD------IVDKYGVTIFYTAPTLIRSLmrdgTEYVA-RYSRKSLRVLGSVGEPINPTAWR---------WF 489
Cdd:PRK05691 2410 --------WGaeeicqLIREQQVSILGFTPSYGSQL----AQWLAgQGEQLPVRMCITGGEALTGEHLQrirqafapqLF 2477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 490 YDVIGdsrcpisdtwwQTETggfMITPLPGAWPQ--KPGSATFPFFGV----QPVIVDEKGREMEGECSGYLCI--KKSW 561
Cdd:PRK05691 2478 FNAYG-----------PTET---VVMPLACLAPEqlEEGAASVPIGRVvgarVAYILDADLALVPQGATGELYVggAGLA 2543
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 562 PGAFRTLYGDKERYETTYFKPFAG-YYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAVVG 640
Cdd:PRK05691 2544 QGYHDRPGLTAERFVADPFAADGGrLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLA 2623
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1205963319 641 IDHEVKGQGIYAFVTLVDGVP--YSDDLRKSLVMTVRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRIL 706
Cdd:PRK05691 2624 LDTPSGKQLAGYLVSAVAGQDdeAQAALREALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRAL 2691
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
193-379 |
1.17e-07 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 55.23 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 193 LTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIG-------------AV-----HSVVFAGFSAE 254
Cdd:PLN02861 78 LTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGityvplydtlganAVefiinHAEVSIAFVQE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 255 ALAQRVIDCKPKvvitCNAVKRglKIIFLKDIVDASLDESAKNGVDvgiCLTYENQSALNKVDTrwttgrdvwwqdvvpD 334
Cdd:PLN02861 158 SKISSILSCLPK----CSSNLK--TIVSFGDVSSEQKEEAEELGVS---CFSWEEFSLMGSLDC---------------E 213
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1205963319 335 FPTKCDvewvdaEDPLFLLYTSGSTGKPKGVLHTTGGYMVYSATT 379
Cdd:PLN02861 214 LPPKQK------TDICTIMYTSGTTGEPKGVILTNRAIIAEVLST 252
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
346-641 |
1.01e-06 |
|
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: 51.69 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 346 AEDPLFLLYTSGSTGKPKGVLHTTGGYmVYSATTFKHAFDYKPTDIYWCTADCgwitghsYVTYGPLLnGATVLVFEGAP 425
Cdd:cd05910 84 ADEPAAILFTSGSTGTPKGVVYRHGTF-AAQIDALRQLYGIRPGEVDLATFPL-------FALFGPAL-GLTSVIPDMDP 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 426 NYP---DPGRCWDIVDKYGVTIFYTAPTLIRSLmrdgTEYVARYSRK--SLRVLGSVGEPINPTAWRWFYDVIGDSR--- 497
Cdd:cd05910 155 TRParaDPQKLVGAIRQYGVSIVFGSPALLERV----ARYCAQHGITlpSLRRVLSAGAPVPIALAARLRKMLSDEAeil 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 498 -----------CPISDTWWQTETggfmiTPLPgawpqKPGSAT---FPFFGVQPVIV---DEKGREMEGECS------GY 554
Cdd:cd05910 231 tpygatealpvSSIGSRELLATT-----TAAT-----SGGAGTcvgRPIPGVRVRIIeidDEPIAEWDDTLElprgeiGE 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 555 LCIkkSWPGAFRTLYGDKEryETTYFKPFAG----YYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSH 630
Cdd:cd05910 301 ITV--TGPTVTPTYVNRPV--ATALAKIDDNsegfWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTH 376
|
330
....*....|.
gi 1205963319 631 PKCAEAAVVGI 641
Cdd:cd05910 377 PGVRRSALVGV 387
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
190-684 |
1.64e-06 |
|
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: 51.52 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 190 DGKLTYSELLEKVCQLSNYLKS-VGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAEALAQRVIDCKPKVV 268
Cdd:cd05938 3 GETYTYRDVDRRSNQAARALLAhAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 269 ITCNAvkrglkiifLKDIVDASLDESAKNGVDVGI----CLTYENQSALNKVDTrwttgrdvwwqdvVPDFPTKCDVEW- 343
Cdd:cd05938 83 VVAPE---------LQEAVEEVLPALRADGVSVWYlshtSNTEGVISLLDKVDA-------------ASDEPVPASLRAh 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 344 VDAEDPLFLLYTSGSTGKPKGVLHTTggYMVYSATTFKHAFDYKPTDIYWctadcgwITGHSYVTYGPLLN-------GA 416
Cdd:cd05938 141 VTIKSPALYIYTSGTTGLPKAARISH--LRVLQCSGFLSLCGVTADDVIY-------ITLPLYHSSGFLLGiggcielGA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 417 TVLVfegAPNYpDPGRCWDIVDKYGVTIF-YtaptlIRSLMRDGTEYVARYSRKSLRVLGSVGEPINPTAWRWFYDVIGD 495
Cdd:cd05938 212 TCVL---KPKF-SASQFWDDCRKHNVTVIqY-----IGELLRYLCNQPQSPNDRDHKVRLAIGNGLRADVWREFLRRFGP 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 496 SRcpISDTWWQTE-TGGFM-ITPLPGA-----WPQKpgsATFPF----FGVQ---PViVDEKGREME---GEcSGYLCIK 558
Cdd:cd05938 283 IR--IREFYGSTEgNIGFFnYTGKIGAvgrvsYLYK---LLFPFelikFDVEkeePV-RDAQGFCIPvakGE-PGLLVAK 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 559 KSWPGAFRTLYGDKERYETT----YFKPFAGYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVESALVSHPKCA 634
Cdd:cd05938 356 ITQQSPFLGYAGDKEQTEKKllrdVFKKGDVYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQ 435
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1205963319 635 EAAVVGI---DHEvkGQGIYAFVTLVDGvpYSDDLRKsLVMTVRSQIGAFAAP 684
Cdd:cd05938 436 EVNVYGVtvpGHE--GRIGMAAVKLKPG--HEFDGKK-LYQHVREYLPAYARP 483
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
587-706 |
2.91e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 50.42 E-value: 2.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 587 YFSGDGcsrdkdGYHWLtGRVDDVINVSGHRIGTAEVESALVSHPKCAEAAVVGIDHEVKGQGIYAFVTlVDGVPYSDDL 666
Cdd:PRK08308 300 YKSERG------TLHFM-GRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVI-SHEEIDPVQL 371
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1205963319 667 RKslvmTVRSQIGAFAAPDKIHWAPGLPKTRSGKIMRRIL 706
Cdd:PRK08308 372 RE----WCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLL 407
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
193-368 |
5.41e-06 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.
Pssm-ID: 341294 [Multi-domain] Cd Length: 507 Bit Score: 49.52 E-value: 5.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 193 LTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAEALAQrvidckpkvvitcn 272
Cdd:cd17639 6 MSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIH-------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 273 avkrglkiiflkdivdaSLDESAKNGVdvgICltyenqsalnkvdtrwttgrdvwwqDVVPDfptkcdvewvdaeDPLFL 352
Cdd:cd17639 72 -----------------SLNETECSAI---FT-------------------------DGKPD-------------DLACI 93
|
170
....*....|....*.
gi 1205963319 353 LYTSGSTGKPKGVLHT 368
Cdd:cd17639 94 MYTSGSTGNPKGVMLT 109
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
188-365 |
5.72e-06 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 49.51 E-value: 5.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 188 SQDGKLTYSELLEKVCQLSNYLKSVGVGKGDAVVIYLPMLMELPIAMLACARIG------AVHSvvfagfSAEALAQrVI 261
Cdd:PRK04813 23 YLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGhayipvDVSS------PAERIEM-II 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 262 D-CKPKVVITcnavkrglkiiflkdIVDASLDESaknGVDVgicLTYENQSalnkvdtrwttgrDVWWQDVVPDFPtkcd 340
Cdd:PRK04813 96 EvAKPSLIIA---------------TEELPLEIL---GIPV---ITLDELK-------------DIFATGNPYDFD---- 137
|
170 180
....*....|....*....|....*
gi 1205963319 341 vEWVDAEDPLFLLYTSGSTGKPKGV 365
Cdd:PRK04813 138 -HAVKGDDNYYIIFTSGTTGKPKGV 161
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
191-710 |
7.87e-06 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 49.54 E-value: 7.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 191 GKLTYSELLEKVCQLSNYLKSvGVGKGDAVVIYLPMLMELPIAMLACARIGAVhsVVFAGFSA--EALAQRVIDCKPKVV 268
Cdd:PRK08633 640 GELSYGKALTGALALARLLKR-ELKDEENVGILLPPSVAGALANLALLLAGKV--PVNLNYTAseAALKSAIEQAQIKTV 716
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 269 ITCNAVKRGLKiiflKDIVDASLDEsakngvDVGICLTYENQSALNKVDTRWTTGRdVWwqdVVPdfptKCDVEW----- 343
Cdd:PRK08633 717 ITSRKFLEKLK----NKGFDLELPE------NVKVIYLEDLKAKISKVDKLTALLA-AR---LLP----ARLLKRlygpt 778
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 344 VDAEDPLFLLYTSGSTGKPKGV-----------------LHTTGGYMVYSATTFKHAFDYKPTdiywctadcgwitghsy 406
Cdd:PRK08633 779 FKPDDTATIIFSSGSEGEPKGVmlshhnilsnieqisdvFNLRNDDVILSSLPFFHSFGLTVT----------------- 841
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 407 vTYGPLLNGATVlVFegapnYPDP------GRcwdIVDKYGVTIFYTAPTLIRSLMRDGTEYVARYSrkSLRVLGSVGEP 480
Cdd:PRK08633 842 -LWLPLLEGIKV-VY-----HPDPtdalgiAK---LVAKHRATILLGTPTFLRLYLRNKKLHPLMFA--SLRLVVAGAEK 909
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 481 INPTAWRWFYDVIGdsrCPISDTWWQTETggfmiTPL----------PGAWPQ---KPGSATFPFFGVQPVIVD-EKGRE 546
Cdd:PRK08633 910 LKPEVADAFEEKFG---IRILEGYGATET-----SPVasvnlpdvlaADFKRQtgsKEGSVGMPLPGVAVRIVDpETFEE 981
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 547 MEGECSGYLCIKKswPGAFRTLYGDKERY-ETTYFKPFAGYYFSGDGCSRDKDGYHWLTGRVDDVINVSGHRIGTAEVES 625
Cdd:PRK08633 982 LPPGEDGLILIGG--PQVMKGYLGDPEKTaEVIKDIDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEE 1059
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 626 ALV-----SHPKCaeaAVVGIDHEVKGQGIYAFVTLVDGVPysDDLRKSLvmtVRSQIGAFAAPDKIHWAPGLPKTRSGK 700
Cdd:PRK08633 1060 ELAkalggEEVVF---AVTAVPDEKKGEKLVVLHTCGAEDV--EELKRAI---KESGLPNLWKPSRYFKVEALPLLGSGK 1131
|
570
....*....|
gi 1205963319 701 IMRRILRKIA 710
Cdd:PRK08633 1132 LDLKGLKELA 1141
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
193-392 |
7.96e-06 |
|
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: 49.14 E-value: 7.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 193 LTYSELLEKVCQLSNYLKSVGV--GKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAEALAQRVIDCKPKVVIt 270
Cdd:cd05927 6 ISYKEVAERADNIGSALRSLGGkpAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVF- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 271 cnaVKRGLKIIFLKDIvdasldesakngvdvgicltyENQSALNKVDtrwttgrdvwwqdVVPdfPTKcdvewvdaEDPL 350
Cdd:cd05927 85 ---CDAGVKVYSLEEF---------------------EKLGKKNKVP-------------PPP--PKP--------EDLA 117
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1205963319 351 FLLYTSGSTGKPKGVLHTTGGYMVYSATTFKHAFDYK---PTDIY 392
Cdd:cd05927 118 TICYTSGTTGNPKGVMLTHGNIVSNVAGVFKILEILNkinPTDVY 162
|
|
| PRK09188 |
PRK09188 |
serine/threonine protein kinase; Provisional |
626-719 |
1.68e-05 |
|
serine/threonine protein kinase; Provisional
Pssm-ID: 236400 [Multi-domain] Cd Length: 365 Bit Score: 47.84 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 626 ALVSHPKCAEAAVVGIDHEVKGQGIYAFVTlvdgvPYSDDLRKSLVMTVRSQIGAfAAPDKIHWAPGLPKTRSGKIMRRI 705
Cdd:PRK09188 248 ALKSDPAVSDVAIALFSLPAKGVGLYAFVE-----AELPADEKSLRARLAGAKPP-KPPEHIQPVAALPRDADGTVRDDI 321
|
90
....*....|....
gi 1205963319 706 LRKIASRQLDELGD 719
Cdd:PRK09188 322 LRLIAMNQIDELDD 335
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
340-714 |
5.15e-05 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 46.53 E-value: 5.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 340 DVEWVDAEDPLFLLYTSGSTGKPKGVLhTTGGYMVYSATTFKHAFDYKP-TD--IYW--CTADCGWItghSYVTYgPLLN 414
Cdd:PRK07768 145 DPVETGEDDLALMQLTSGSTGSPKAVQ-ITHGNLYANAEAMFVAAEFDVeTDvmVSWlpLFHDMGMV---GFLTV-PMYF 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 415 GATVLVFEGAPNYPDPGRCWDIVDKYGVTIfYTAP----TLIRSLMRDGTEYvARYSRKSLRVLGSVGEPINPTAWRWFY 490
Cdd:PRK07768 220 GAELVKVTPMDFLRDPLLWAELISKYRGTM-TAAPnfayALLARRLRRQAKP-GAFDLSSLRFALNGAEPIDPADVEDLL 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 491 DV---IGDSRCPISDTWWQTET----------GGFMITP--------LPGAWPQKPGSAT------FPFFGVQPVIVDEK 543
Cdd:PRK07768 298 DAgarFGLRPEAILPAYGMAEAtlavsfspcgAGLVVDEvdadllaaLRRAVPATKGNTRrlatlgPPLPGLEVRVVDED 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 544 GR----------EMEGEC--SGYLCikkswPGAFRTLYGDkeryettyfkpfAGYYFSGDGCSRDKDGYHWLTGRVDDVI 611
Cdd:PRK07768 378 GQvlpprgvgviELRGESvtPGYLT-----MDGFIPAQDA------------DGWLDTGDLGYLTEEGEVVVCGRVKDVI 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 612 NVSGHRIGTAEVESALVS----HPKCAEAavVGIDHEVKGQGiyaFVTLVDGVPYSDD-----LRKSLVMTVRSQIGafA 682
Cdd:PRK07768 441 IMAGRNIYPTDIERAAARvegvRPGNAVA--VRLDAGHSREG---FAVAVESNAFEDPaevrrIRHQVAHEVVAEVG--V 513
|
410 420 430
....*....|....*....|....*....|....
gi 1205963319 683 APDKIH-WAPG-LPKTRSGKimrriLRKIASRQL 714
Cdd:PRK07768 514 RPRNVVvLGPGsIPKTPSGK-----LRRANAAEL 542
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
192-368 |
8.59e-05 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 46.03 E-value: 8.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 192 KLTYSELLEKVCQLSNYLKSVGVGKGDAVVIylpmLMELPIA----MLACARIGAVHSVVFAGFS--AEALAQ--RVID- 262
Cdd:PRK08180 69 RLTYAEALERVRAIAQALLDRGLSAERPLMI----LSGNSIEhallALAAMYAGVPYAPVSPAYSlvSQDFGKlrHVLEl 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 263 CKPKVVITCNAVK--RGLKIIFLKDIVDASldesAKNGVDVGICLTYEnqsALnkVDTRWTTGRDVWWQDVVPDFPTKcd 340
Cdd:PRK08180 145 LTPGLVFADDGAAfaRALAAVVPADVEVVA----VRGAVPGRAATPFA---AL--LATPPTAAVDAAHAAVGPDTIAK-- 213
|
170 180
....*....|....*....|....*...
gi 1205963319 341 vewvdaedplfLLYTSGSTGKPKGVLHT 368
Cdd:PRK08180 214 -----------FLFTSGSTGLPKAVINT 230
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
176-444 |
1.37e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 45.54 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 176 DKIAMYWEGNEPSQDGKLTYSELLEKVCQLSNYLKSVGvGKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSA-- 253
Cdd:PRK05691 24 DRLALRFLADDPGEGVVLSYRDLDLRARTIAAALQARA-SFGDRAVLLFPSGPDYVAAFFGCLYAGVIAVPAYPPESArr 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 254 ---EALAQRVIDCKPKVVITCNAVKRGLkiiflkdivdASLDESAKNGVDVGICltyenqsalnkVDTRWTTGRDVWwqd 330
Cdd:PRK05691 103 hhqERLLSIIADAEPRLLLTVADLRDSL----------LQMEELAAANAPELLC-----------VDTLDPALAEAW--- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 331 VVPDfptkcdvewVDAEDPLFLLYTSGSTGKPKGVlHTTGGYMVYSATTFKHAF--DYKPTDIY--WCTA--DCGWITGh 404
Cdd:PRK05691 159 QEPA---------LQPDDIAFLQYTSGSTALPKGV-QVSHGNLVANEQLIRHGFgiDLNPDDVIvsWLPLyhDMGLIGG- 227
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1205963319 405 syvTYGPLLNGATVLVFegAPNY--PDPGRCWDIVDKYGVTI 444
Cdd:PRK05691 228 ---LLQPIFSGVPCVLM--SPAYflERPLRWLEAISEYGGTI 264
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
605-719 |
9.07e-04 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 42.45 E-value: 9.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 605 GRVDDVINVSGHRIGTAEVESALVSHPKCAEAAVV--GIDHEVKGQGIYAFVTLVDgvPYSDDLRKSLVMTVRSQIGAFA 682
Cdd:PRK05851 415 GRAKELITVAGRNIFPTEIERVAAQVRGVREGAVVavGTGEGSARPGLVIAAEFRG--PDEAGARSEVVQRVASECGVVP 492
|
90 100 110
....*....|....*....|....*....|....*...
gi 1205963319 683 ApDKIHWAPG-LPKTRSGKimrriLRKIASRQLDELGD 719
Cdd:PRK05851 493 S-DVVFVAPGsLPRTSSGK-----LRRLAVKRSLEAAD 524
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
327-477 |
7.59e-03 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 39.41 E-value: 7.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 327 WWQDVVPDFPTKCDVEWV---------DAEDPLFLLYTSGSTGKPKGVLHTTGGYMVYSATTFKHaFDYKPTDIYWCTAD 397
Cdd:PRK06334 154 FWEKCRIGIYMSIPFEWLmrwfgvsdkDPEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKF-FSPKEDDVMMSFLP 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205963319 398 CGWITGHSYVTYGPLLNGATVlVFEGAPNYPDpgRCWDIVDKYGVTIFYTAPTLIrslmrdgtEYVARYSRKSLRVLGSV 477
Cdd:PRK06334 233 PFHAYGFNSCTLFPLLSGVPV-VFAYNPLYPK--KIVEMIDEAKVTFLGSTPVFF--------DYILKTAKKQESCLPSL 301
|
|
| |
