|
Name |
Accession |
Description |
Interval |
E-value |
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
806-1351 |
0e+00 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 724.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 806 PHEPVAIVGMACRLPGgVRSADDLWELVREGRDAVTRFPSDRgWDLAELYSADPARPGTFYQREAALLDDVAGFDAAFFG 885
Cdd:COG3321 2 ADEPIAIIGMACRFPG-ADDPEEFWRNLRAGRDAITEVPADR-WDADAYYDPDPDAPGKTYVRWGGFLDDVDEFDALFFG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 886 ISQREALAMDPQQRLLLETTWEAVEDSGITADTLRGSRTGVFAGVMHLPYGTPLGRTRPDLEGYVMTGTTSSVVSGRLAY 965
Cdd:COG3321 80 ISPREAEAMDPQQRLLLEVAWEALEDAGYDPESLAGSRTGVFVGASSNDYALLLLADPEAIDAYALTGNAKSVLAGRISY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 966 FYGLEGPAVTVDTACSSSLVALHLACQSLRAGECDRALVGAATVMAEPGLFVEFSRLRALAPDGRCKPFSAAADGFGMAE 1045
Cdd:COG3321 160 KLDLRGPSVTVDTACSSSLVAVHLACQSLRSGECDLALAGGVNLMLTPESFILFSKGGMLSPDGRCRAFDADADGYVRGE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 1046 GVGVLVVERLSDAERWGHRVLAVVRGSAVNQDGASNGLTAPSGPAQERVIHAALHNARTPAAEIDLLEAHGTGTRLGDPI 1125
Cdd:COG3321 240 GVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRSNGLTAPNGPAQAAVIRRALADAGVDPATVDYVEAHGTGTPLGDPI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 1126 EAQALLATYGRQRDAERPLWLGSLKSNIGHTQAAAGVSGLIKTVLALRHRTMPATLHVQQPSAQVDWSAGTVRLLTEART 1205
Cdd:COG3321 320 EAAALTAAFGQGRPADQPCAIGSVKSNIGHLEAAAGVAGLIKAVLALRHGVLPPTLHFETPNPHIDFENSPFYVNTELRP 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 1206 WAAPsGRPRRAGVSSFGISGTNAHVILEEAPRgvrgtESAEPPAWAHVAVPLVLSAKSPQALREQASALSRHLRDHPEEP 1285
Cdd:COG3321 400 WPAG-GGPRRAGVSSFGFGGTNAHVVLEEAPA-----AAPAAAAAARPPQLLVLSAKTEEALRALAARLAAFLEAHPDLD 473
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2762205949 1286 LHHTAHTLACHRTHHPYRTAATG-TRNHLIKTL-------NNTHTHTRARPTPPGITALYTGQGSQHPGMGQQL 1351
Cdd:COG3321 474 LADVAYTLATGRAHFEHRLAVVAsSREELAAKLralaageAAPGVVTGAAAAAPKVAFLFPGQGSQYVGMGREL 547
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
808-1232 |
0e+00 |
|
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different products, called polyketides, by successive decarboxylating Claisen condensations. PKSs can be divided into 2 groups, modular type I PKSs consisting of one or more large multifunctional proteins and iterative type II PKSs, complexes of several monofunctional subunits.
Pssm-ID: 238429 [Multi-domain] Cd Length: 421 Bit Score: 619.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 808 EPVAIVGMACRLPGGVrSADDLWELVREGRDAVTRFPSDRgWDLAELYsADPARPGTFYQREAALLDDVAGFDAAFFGIS 887
Cdd:cd00833 1 EPIAIVGMACRFPGAA-DPDEFWENLLEGRDAISEIPEDR-WDADGYY-PDPGKPGKTYTRRGGFLDDVDAFDAAFFGIS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 888 QREALAMDPQQRLLLETTWEAVEDSGITADTLRGSRTGVFAGVMHLPYGTPLGRTRPDLEGYVMTGTTSSVVSGRLAYFY 967
Cdd:cd00833 78 PREAEAMDPQQRLLLEVAWEALEDAGYSPESLAGSRTGVFVGASSSDYLELLARDPDEIDAYAATGTSRAFLANRISYFF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 968 GLEGPAVTVDTACSSSLVALHLACQSLRAGECDRALVGAATVMAEPGLFVEFSRLRALAPDGRCKPFSAAADGFGMAEGV 1047
Cdd:cd00833 158 DLRGPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLSPDGRCRPFDADADGYVRGEGV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 1048 GVLVVERLSDAERWGHRVLAVVRGSAVNQDGASNGLTAPSGPAQERVIHAALHNARTPAAEIDLLEAHGTGTRLGDPIEA 1127
Cdd:cd00833 238 GVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRTKGITAPSGEAQAALIRRAYARAGVDPSDIDYVEAHGTGTPLGDPIEV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 1128 QALLATYGRQRDAERPLWLGSLKSNIGHTQAAAGVSGLIKTVLALRHRTMPATLHVQQPSAQVDWSAGTVRLLTEARTWA 1207
Cdd:cd00833 318 EALAKVFGGSRSADQPLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKIDFEESPLRVPTEARPWP 397
|
410 420
....*....|....*....|....*
gi 2762205949 1208 APSgRPRRAGVSSFGISGTNAHVIL 1232
Cdd:cd00833 398 APA-GPRRAGVSSFGFGGTNAHVIL 421
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
810-1234 |
8.14e-171 |
|
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the thiolase family and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.
Pssm-ID: 214836 [Multi-domain] Cd Length: 298 Bit Score: 509.95 E-value: 8.14e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 810 VAIVGMACRLPGgVRSADDLWELVREGrdavtrfpsdrgwdlaelysadparpgtfyqreaalLDDVAGFDAAFFGISQR 889
Cdd:smart00825 1 IAIVGMSCRFPG-ADDPEEFWDLLLAG------------------------------------LDDVDLFDAAFFGISPR 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 890 EALAMDPQQRLLLETTWEAVEDSGITADTLRGSRTGVFAGVMHLPYgtplgrtrpdlegyvmtgttssvvsgrlayfygl 969
Cdd:smart00825 44 EAEAMDPQQRLLLEVAWEALEDAGIDPESLRGSRTGVFVGVSSSDY---------------------------------- 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 970 egpAVTVDTACSSSLVALHLACQSLRAGECDRALVGAATVMAEPGLFVEFSRLRALAPDGRCKPFSAAADGFGMAEGVGV 1049
Cdd:smart00825 90 ---SVTVDTACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLSPDGRCKTFDASADGYVRGEGVGV 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 1050 LVVERLSDAERWGHRVLAVVRGSAVNQDGASNGLTAPSGPAQervihaalhnartpaaeidlleahgtgtrlgdpieaqa 1129
Cdd:smart00825 167 VVLKRLSDALRDGDPILAVIRGSAVNQDGRSNGITAPSGPAQ-------------------------------------- 208
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 1130 llatygrqrdaerpLWLGSLKSNIGHTQAAAGVSGLIKTVLALRHRTMPATLHVQQPSAQVDWSAGTVRLLTEARTWaAP 1209
Cdd:smart00825 209 --------------LLIGSVKSNIGHLEAAAGVAGLIKVVLALKHGVIPPTLHFETPNPHIDLEESPLRVPTELTPW-PP 273
|
410 420
....*....|....*....|....*
gi 2762205949 1210 SGRPRRAGVSSFGISGTNAHVILEE 1234
Cdd:smart00825 274 PGRPRRAGVSSFGFGGTNAHVILEE 298
|
|
| mycolic_Pks13 |
NF040607 |
polyketide synthase Pks13; |
704-1351 |
6.05e-144 |
|
polyketide synthase Pks13;
Pssm-ID: 468580 [Multi-domain] Cd Length: 1671 Bit Score: 479.03 E-value: 6.05e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 704 VADAlgpEGREAAAADPDRDFRSLGLDSAGAVRVRRRLVELTGLRLPVTALFDHPTPRALAREIVrrlfgaAPEPRTAAL 783
Cdd:NF040607 14 VANA---TGQPADQITDDRPMEEFGLSSRDAVALSGDIEDLTGVTLTATVAYQHPTIASLATRII------EGEPEVAAD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 784 TTTSPPGPRAEGATSGDsaagvphepVAIVGMACRLPGGVRSADDLWELVREGRDAVTRFPSDRgWdlAElYSADPArpg 863
Cdd:NF040607 85 DDDDADWSRRPRSDAHD---------IAIVGLATRFPGAGNTPEEMWEALIEGRDGITDLPEGR-W--SE-FAADPR--- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 864 tFYQR--EAAL----LDDVAGFDAAFFGISQREALAMDPQQRLLLETTWEAVEDSGITADTLRGSRTGVFAGVMHLPYG- 936
Cdd:NF040607 149 -IAERvaKANTrggyLDDIKGFDAEFFALSPLEAENVDPQQRLALELTWEALEHARIPASSLRGEPVGVFIGSSNNDYQm 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 937 ---TPLGRTRPdlegYVMTGTTSSVVSGRLAYFYGLEGPAVTVDTACSSSLVALHLACQSLRAGECDRALVGAATVMAEP 1013
Cdd:NF040607 228 lavADPAEAHP----YALTGTSSSIIANRVSYFFDFRGPSVAVDTACSSSLVAVHQAVRALRSGEADVAVAGGVNMLLTP 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 1014 GLFVEFSRLR-ALAPDGRCKPFSAAADGFGMAEGVGVLVVERLSDAERWGHRVLAVVRGSAVNQDGASNGLTAPSGPAQE 1092
Cdd:NF040607 304 AVTLGFDELGgVLAPDGRIKAFSSDADGMVRSEGGGVVVLKRLADARRDGDTILAVIAGSAVNSDGRSNGLTAPNPDAQV 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 1093 RVIHAALHNARTPAAEIDLLEAHGTGTRLGDPIEAQALLATYGRQRDAERPLWLGSLKSNIGHTQAAAGVSGLIKTVLAL 1172
Cdd:NF040607 384 DVLRRAYADAGIDPRTVDYVEAHGTGTILGDPIEADALGRVVGRGRDADKPALLGSAKTNFGHLESAAGAAGLAKVVLAM 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 1173 RHRTMPATLHVQQPSAQVDWSAGTVRLLTEARTWAAPSGRPrRAGVSSFGISGTNAHVIL-------------------- 1232
Cdd:NF040607 464 QHDKLPPSLNYAGPNPYIDFDAEHLKVVDEPTEWPRYSGHA-VAGVSGFGFGGTNAHVVVrevlpadlvepeaqpdedte 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 1233 -------EEAPRGVRGTESAEPPAWAHV---AVPLVLSAKSPQALREQASALSRHLRDHPEE--PLHHTAHTLAcHRTHH 1300
Cdd:NF040607 543 aelagltAEAKRLLAEAELAAEFAPAAPegpVVPLPVSGFLPSRRRAAAADLADWLESEEGRatPLADVARALA-RRNHG 621
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 2762205949 1301 PYRTAAT-GTRNHLIKTL-------NNTHTHTRARPTPPGITALYTGQGSQHPGMGQQL 1351
Cdd:NF040607 622 RSRAVVLaHTHEEAIKGLravaegkPGPGVFSADAPAANGPVWVLSGFGSQHRKMAKQL 680
|
|
| PKS_AT |
smart00827 |
Acyl transferase domain in polyketide synthase (PKS) enzymes; |
332-625 |
3.39e-105 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes;
Pssm-ID: 214838 [Multi-domain] Cd Length: 298 Bit Score: 335.53 E-value: 3.39e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 332 VFPGQGPQWAGMAGELARAEPAFRKKLAECARALRPWLEVDPDELLFG---ARPLDRVELVQPALFSVMVSLAHLWRSHG 408
Cdd:smart00827 1 VFTGQGSQWAGMGRELYETEPVFREALDECDAALQPLLGWSLLDVLLGedgAASLLDTEVAQPALFAVQVALARLLRSWG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 409 MTPAAMVGHSFGEIAAVTAAGGLSLTDGARLVAAVSTALARIEGQGDMVAVALTPDETEALLAEEGLDLGIAVVNGPRST 488
Cdd:smart00827 81 VRPDAVVGHSSGEIAAAYVAGVLSLEDAARLVAARGRLMQALPGGGAMLAVGLSEEEVEPLLAGVPDRVSVAAVNSPSSV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 489 VVSGTRDAATKLLGRLAARGVRARRLPVGIAGHSPHMDRIRDVLVRGAAAVRPRRSAVPVYGSTTTAPLDTAAL-DADHW 567
Cdd:smart00827 161 VLSGDEDAVDELAARLEAEGIFARRLKVDHAFHSPHMEPILDEFRAALAGLTPRPPRIPFVSTVTGTLIDGAELdDADYW 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2762205949 568 FRAMRGTARFHDVVAGLLSA-GHRLFVEISPHPVLAMSIEDTAAHLERDVVVLdTMRRD 625
Cdd:smart00827 241 VRNLREPVRFADAVRALLAEgGVTVFLEVGPHPVLTGPIKQTLAAAGSAVVLP-SLRRG 298
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
808-1058 |
3.98e-98 |
|
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains. The N-terminal domain contains most of the structures involved in dimer formation and also the active site cysteine.
Pssm-ID: 425468 [Multi-domain] Cd Length: 251 Bit Score: 314.19 E-value: 3.98e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 808 EPVAIVGMACRLPGGVrSADDLWELVREGRDAVTRFPSDRgWDLAELYSADPARPGTFYQREAALlDDVAGFDAAFFGIS 887
Cdd:pfam00109 1 EPVAIVGMGCRFPGGN-DPEEFWENLLEGRDGISEIPADR-WDPDKLYDPPSRIAGKIYTKWGGL-DDIFDFDPLFFGIS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 888 QREALAMDPQQRLLLETTWEAVEDSGITADTLRGSRTGVFAGVMHLPYGTPLGRTRP--DLEGYV-MTGTTSSVVSGRLA 964
Cdd:pfam00109 78 PREAERMDPQQRLLLEAAWEALEDAGITPDSLDGSRTGVFIGSGIGDYAALLLLDEDggPRRGSPfAVGTMPSVIAGRIS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 965 YFYGLEGPAVTVDTACSSSLVALHLACQSLRAGECDRALVGAATVMAEPGLFVEFSRLRALAPDGRCKPFSAAADGFGMA 1044
Cdd:pfam00109 158 YFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSPDGPCKAFDPFADGFVRG 237
|
250
....*....|....
gi 2762205949 1045 EGVGVLVVERLSDA 1058
Cdd:pfam00109 238 EGVGAVVLKRLSDA 251
|
|
| omega_3_PfaA |
TIGR02813 |
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ... |
809-1352 |
8.80e-68 |
|
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this alignment are involved in omega-3 polyunsaturated fatty acid biosynthesis, such as the protein PfaA from the eicosapentaenoic acid biosynthesis operon in Photobacterium profundum strain SS9. PfaA is encoded together with PfaB, PfaC, and PfaD, and the functions of the individual polypeptides have not yet been described. More distant homologs of PfaA, also included with the reach of this model, appear to be involved in polyketide-like biosynthetic mechanisms of polyunsaturated fatty acid biosynthesis, an alternative to the more familiar iterated mechanism of chain extension and desaturation, and in most cases are encoded near genes for homologs of PfaB, PfaC, and/or PfaD.
Pssm-ID: 274311 [Multi-domain] Cd Length: 2582 Bit Score: 253.00 E-value: 8.80e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 809 PVAIVGMAcRLPGGVRSADDLWELVREGRDAVTRFPSDRgWDLAELYSADPARPGTFYQREAALLDDVaGFDAAFFGISQ 888
Cdd:TIGR02813 8 PIAIVGMA-SIFANSRYLNKFWDLIFEKIDAITDVPSDH-WAKDDYYDSDKSEADKSYCKRGGFLPEV-DFNPMEFGLPP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 889 REALAMDPQQRLLLETTWEAVEDSGItADTLRGSRTGVFAGV-----------MHLPYgtPL--------GRTRPDLE-- 947
Cdd:TIGR02813 85 NILELTDISQLLSLVVAKEVLNDAGL-PDGYDRDKIGITLGVgggqkqssslnARLQY--PVlkkvfkasGVEDEDSEml 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 948 ------GYV------MTGTTSSVVSGRLAYFYGLEGPAVTVDTACSSSLVALHLACQSLRAGECDRALVGAATVMAEPGL 1015
Cdd:TIGR02813 162 ikkfqdQYIhweensFPGSLGNVISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGGVCTDNSPFM 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 1016 FVEFSRLRALAPDGRCKPFSAAADGFGMAEGVGVLVVERLSDAERWGHRVLAVVRGSAVNQDGASNGLTAPSGPAQERVI 1095
Cdd:TIGR02813 242 YMSFSKTPAFTTNEDIQPFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGKFKSIYAPRPEGQAKAL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 1096 HAALHNARTPAAEIDLLEAHGTGTRLGDPIEAQALLATYGRQRDAERPLWLGSLKSNIGHTQAAAGVSGLIKTVLALRHR 1175
Cdd:TIGR02813 322 KRAYDDAGFAPHTCGLIEAHGTGTAAGDVAEFGGLVSVFSQDNDQKQHIALGSVKSQIGHTKSTAGTAGMIKAVLALHHK 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 1176 TMPATLHVQQPSAQVDWSAGTVRLLTEARTWAAPS-GRPRRAGVSSFGISGTNAHVILEE-APRGVRGTESAEppawAHV 1253
Cdd:TIGR02813 402 VLPPTINVDQPNPKLDIENSPFYLNTETRPWMQREdGTPRRAGISSFGFGGTNFHMVLEEySPKHQRDDQYRQ----RAV 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 1254 AVPLVLSAKSPQALREQASALSRHLRDHPE-EPLHHTA----HTLACHRTHHPYRTAATGTRNHLIKTLNNTHTHTRARP 1328
Cdd:TIGR02813 478 AQTLLFTAANEKALVSSLKDWKNKLSAKADdQPYAFNAlaveNTLRTIAVALARLGFVAKNADELITMLEQAITQLEAKS 557
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 2762205949 1329 T-----PPGIT--------------ALYTGQGSQHPGMGQQLA 1352
Cdd:TIGR02813 558 CeewqlPSGISyrksalvvesgkvaALFAGQGSQYLNMGRELA 600
|
|
| Acyl_transf_1 |
pfam00698 |
Acyl transferase domain; |
330-646 |
3.80e-67 |
|
Acyl transferase domain;
Pssm-ID: 395567 Cd Length: 319 Bit Score: 229.67 E-value: 3.80e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 330 VFVFPGQGPQWAGMAGELARAEPAFRKKLAECARALRPWLEVDPDELLFGARP--LDRVELVQPALFSVMVSLAHLWRSH 407
Cdd:pfam00698 1 VFVFSGQGSQWAGMGMQLLKTSPAFAAVIDRADEAFKPQYGFSVSDVLRNNPEgtLDGTQFVQPALFAMQIALAALLQSY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 408 GMTPAAMVGHSFGEIAAVTAAGGLSLTDGARLVAAVSTALARIEGQGDMVAVALTPDETEALLAEeglDLGIAVVNGPRS 487
Cdd:pfam00698 81 GVRPDAVVGHSLGEYAAAVVAGALSPEEALLAAVLRSRLMMQLAGPGGMAAVELSAEEVEQRWPD---DVVGAVVNSPRS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 488 TVVSGTRDAATKLLGRLAARGVRARRLPVGIAGHSPHMDRIRDVLVRGAAAVRPRRSAVPVYGSTTTAPLDTAALDADHW 567
Cdd:pfam00698 158 VVISGPQEAVRELVERVSKEGVGALVENVNYAVHSPQMDAIAPALLSALADIAPRTPRVPFISSTSIDPSDQRTLSAEYW 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 568 FRAMRGTARFHDVVAGLLSAGHRLFVEISPHPVLAMSIEDT--AAHLERDVVVLDTMRRD-DAGAGRYVRALAEAQLHGA 644
Cdd:pfam00698 238 VRNLRSPVRFAEAILSAAEPGPLVFIEISPHPLLLAALIDTlkSASDGKVATLVGTLIRDqTDFLVTFLYILAVAHLTGS 317
|
..
gi 2762205949 645 DP 646
Cdd:pfam00698 318 AP 319
|
|
| FabD |
COG0331 |
Malonyl CoA-acyl carrier protein transacylase [Lipid transport and metabolism]; Malonyl ... |
327-602 |
1.17e-50 |
|
Malonyl CoA-acyl carrier protein transacylase [Lipid transport and metabolism]; Malonyl CoA-acyl carrier protein transacylase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440100 [Multi-domain] Cd Length: 306 Bit Score: 181.48 E-value: 1.17e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 327 TRTVFVFPGQGPQWAGMAGELARAEPAFRKKLAECARALrpwlEVDPDELLFGARP--LDRVELVQPALFSVMVSLAHLW 404
Cdd:COG0331 1 MKLAFLFPGQGSQYVGMGKDLYENFPVAREVFEEASEAL----GYDLSALCFEGPEeeLNLTENTQPAILAASVAAYRAL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 405 RSHGMTPAAMVGHSFGEIAAVTAAGGLSLTDGARLVAAVSTALARI--EGQGDMVAVA-LTPDETEALLAE--EGLDLGI 479
Cdd:COG0331 77 EEEGIRPDAVAGHSLGEYSALVAAGALSFEDALRLVRLRGRLMQEAvpAGPGGMAAVLgLDDEEVEALCAEaaQGEVVEI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 480 AVVNGPRSTVVSGTRDAATKLLGRLAARGV-RARRLPVGIAGHSPHMDRIRDVLVRGAAAVRPRRSAVPVYGSTTTAPLD 558
Cdd:COG0331 157 ANYNSPGQIVISGEKEAVEAAAELAKEAGAkRAVPLPVSGPFHTPLMAPAAEKLAEALAAVTFADPKIPVVSNVDAAPVT 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2762205949 559 TAALDADHWFRAMRGTARFHDVVAGLLSAGHRLFVEISPHPVLA 602
Cdd:COG0331 237 DPEEIRELLVRQLTSPVRWDESVEALAEAGVTTFVELGPGKVLS 280
|
|
| PTZ00050 |
PTZ00050 |
3-oxoacyl-acyl carrier protein synthase; Provisional |
820-1228 |
8.22e-40 |
|
3-oxoacyl-acyl carrier protein synthase; Provisional
Pssm-ID: 240245 [Multi-domain] Cd Length: 421 Bit Score: 153.69 E-value: 8.22e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 820 PGGVrSADDLWELVREGR---DAVTRFP------SDRGWDLAELYSADPARPGTFYQREAallddvagFDAAFFGISQRE 890
Cdd:PTZ00050 4 PLGV-GAESTWEALIAGKsgiRKLTEFPkflpdcIPEQKALENLVAAMPCQIAAEVDQSE--------FDPSDFAPTKRE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 891 alamDPQQRLLLETTWEAVEDSGIT--ADTLRgSRTGVFAGVMhLPYGTPLGRTRPDLEG--------YVMTGTTSSVVS 960
Cdd:PTZ00050 75 ----SRATHFAMAAAREALADAKLDilSEKDQ-ERIGVNIGSG-IGSLADLTDEMKTLYEkghsrvspYFIPKILGNMAA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 961 GRLAYFYGLEGPAVTVDTACSSSLVALHLACQSLRAGECDRALVGAATVMAEPGLFVEFSRLRALA------PDGRCKPF 1034
Cdd:PTZ00050 149 GLVAIKHKLKGPSGSAVTACATGAHCIGEAFRWIKYGEADIMICGGTEASITPVSFAGFSRMRALCtkynddPQRASRPF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 1035 SAAADGFGMAEGVGVLVVERLSDAERWGHRVLAVVRGSAVNQDGASNGLTAPSGPAQERVIHAAL-HNARTPAAEIDLLE 1113
Cdd:PTZ00050 229 DKDRAGFVMGEGAGILVLEELEHALRRGAKIYAEIRGYGSSSDAHHITAPHPDGRGARRCMENALkDGANININDVDYVN 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 1114 AHGTGTRLGDPIEAQALLATYGrqRDAERPLWLGSLKSNIGHTQAAAGVSGLIKTVLALRHRTMPATLHVQQPSAQVDws 1193
Cdd:PTZ00050 309 AHATSTPIGDKIELKAIKKVFG--DSGAPKLYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINLENPDAECD-- 384
|
410 420 430
....*....|....*....|....*....|....*.
gi 2762205949 1194 agtVRLLTEArtwAAPSGRPRRAGVS-SFGISGTNA 1228
Cdd:PTZ00050 385 ---LNLVQGK---TAHPLQSIDAVLStSFGFGGVNT 414
|
|
| fabD |
TIGR00128 |
malonyl CoA-acyl carrier protein transacylase; This enzyme of fatty acid biosynthesis ... |
327-601 |
2.57e-30 |
|
malonyl CoA-acyl carrier protein transacylase; This enzyme of fatty acid biosynthesis transfers the malonyl moeity from coenzyme A to acyl-carrier protein. The seed alignment for this family of proteins contains a single member each from a number of bacterial species but also an additional pair of closely related, uncharacterized proteins from B. subtilis, one of which has a long C-terminal extension. [Fatty acid and phospholipid metabolism, Biosynthesis]
Pssm-ID: 272922 [Multi-domain] Cd Length: 290 Bit Score: 122.19 E-value: 2.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 327 TRTVFVFPGQGPQWAGMAGELARAEPAFRKKLAECARALrpwlEVDPDELLFG--ARPLDRVELVQPALFSVMVSLAHLW 404
Cdd:TIGR00128 1 MKIAYVFPGQGSQTVGMGKDLYEQYPIAKELFDQASEAL----GYDLKKLCQEgpAEELNKTQYTQPALYVVSAILYLKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 405 R-SHGMTPAAMVGHSFGEIAAVTAAGGLSLTDGARLVAAVSTALARI--EGQGDMVAVALTPDE--TEALLAEEGLDLGI 479
Cdd:TIGR00128 77 KeQGGLKPDFAAGHSLGEYSALVAAGALDFETALKLVKKRGELMQEAvpEGGGAMAAVIGLDEEqlAQACEEATENDVDL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 480 AVVNGPRSTVVSGTRDAATKLLGRLAARGV-RARRLPVGIAGHSPHMDRIRDVLVRGAAAVRPRRSAVPVYGSTTTAPLD 558
Cdd:TIGR00128 157 ANFNSPGQVVISGTKDGVEAAAALFKEMGAkRAVPLEVSGAFHSRFMKPAAEKFAETLEACQFNDPTVPVISNVDAKPYT 236
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2762205949 559 TAALDADHWFRAMRGTARFHDVVAGLLSAGHRLFVEISPHPVL 601
Cdd:TIGR00128 237 NGDRIKEKLSEQLTSPVRWTDSVEKLMARGVTEFAEVGPGKVL 279
|
|
| PKS_PP |
smart00823 |
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ... |
688-771 |
1.21e-17 |
|
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.
Pssm-ID: 214834 [Multi-domain] Cd Length: 86 Bit Score: 78.83 E-value: 1.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 688 LTGHRPDERADQAVQLV----ADALGpeGREAAAADPDRDFRSLGLDSAGAVRVRRRLVELTGLRLPVTALFDHPTPRAL 763
Cdd:smart00823 1 LAALPPAERRRLLLDLVreqvAAVLG--HAAAEAIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAAL 78
|
....*...
gi 2762205949 764 AREIVRRL 771
Cdd:smart00823 79 AEHLAAEL 86
|
|
| PLN02752 |
PLN02752 |
[acyl-carrier protein] S-malonyltransferase |
325-602 |
4.04e-15 |
|
[acyl-carrier protein] S-malonyltransferase
Pssm-ID: 215401 [Multi-domain] Cd Length: 343 Bit Score: 78.27 E-value: 4.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 325 PDTRTVFVFPGQGPQWAGMAGELARAEPAfrKKLAECARALRPW--LEV---DPDEllfgarPLDRVELVQPALFsvMVS 399
Cdd:PLN02752 36 YKPTTAFLFPGQGAQAVGMGKEAAEVPAA--KALFDKASEILGYdlLDVcvnGPKE------KLDSTVVSQPAIY--VAS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 400 LA--HLWRSHGMTPAAM------VGHSFGEIAAVTAAGGLSLTDGARLVAAVSTAL--ARIEGQGDMVAV-ALTPDETEA 468
Cdd:PLN02752 106 LAavEKLRARDGGQAVIdsvdvcAGLSLGEYTALVFAGALSFEDGLKLVKLRGEAMqaAADAGPSGMVSViGLDSDKVQE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 469 LLAE------EGLDLGIAVVNGPRSTVVSGTRDAATKLLGRLAARGVR-ARRLPVGIAGHSPHMDRIRDVLVRGAAAVRP 541
Cdd:PLN02752 186 LCAAaneevgEDDVVQIANYLCPGNYAVSGGKKGIDAVEAKAKSFKARmTVRLAVAGAFHTSFMEPAVDALEAALAAVEI 265
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2762205949 542 RRSAVPVYGSTTTAPLDTAALDADHWFRAMRGTARFHDVVAGLLSAGHRLFVEISPHPVLA 602
Cdd:PLN02752 266 RTPRIPVISNVDAQPHSDPATIKKILARQVTSPVQWETTVKTLLEKGLEKSYELGPGKVIA 326
|
|
| PP-binding |
pfam00550 |
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
701-762 |
8.48e-11 |
|
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.
Pssm-ID: 425746 [Multi-domain] Cd Length: 62 Bit Score: 58.73 E-value: 8.48e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2762205949 701 VQLVADALGpegREAAAADPDRDFRSLGLDSAGAVRVRRRLVELTGLRLPVTALFDHPTPRA 762
Cdd:pfam00550 4 RELLAEVLG---VPAEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLAE 62
|
|
| AcpP |
COG0236 |
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ... |
692-771 |
9.85e-11 |
|
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440006 [Multi-domain] Cd Length: 80 Bit Score: 59.10 E-value: 9.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 692 RPDERADQAVQLVADALGpegREAAAADPDRDFRS-LGLDSAGAVRVRRRLVELTGLRLPVTALFDHPTPRALAREIVRR 770
Cdd:COG0236 2 PREELEERLAEIIAEVLG---VDPEEITPDDSFFEdLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEEK 78
|
.
gi 2762205949 771 L 771
Cdd:COG0236 79 L 79
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
702-780 |
3.67e-03 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 41.56 E-value: 3.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 702 QLVADAL-GPEGREAAAADP---DRD--FRSLGLDSAGAVRVRRRLVELTGLRLPVTALFDHPTPRALAREIVRRLFGAA 775
Cdd:PRK06060 544 RLVVDAVcAEAAKMLGEPDPwsvDQDlaFSELGFDSQMTVTLCKRLAAVTGLRLPETVGWDYGSISGLAQYLEAELAGGH 623
|
....*
gi 2762205949 776 PEPRT 780
Cdd:PRK06060 624 GRLKS 628
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
806-1351 |
0e+00 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 724.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 806 PHEPVAIVGMACRLPGgVRSADDLWELVREGRDAVTRFPSDRgWDLAELYSADPARPGTFYQREAALLDDVAGFDAAFFG 885
Cdd:COG3321 2 ADEPIAIIGMACRFPG-ADDPEEFWRNLRAGRDAITEVPADR-WDADAYYDPDPDAPGKTYVRWGGFLDDVDEFDALFFG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 886 ISQREALAMDPQQRLLLETTWEAVEDSGITADTLRGSRTGVFAGVMHLPYGTPLGRTRPDLEGYVMTGTTSSVVSGRLAY 965
Cdd:COG3321 80 ISPREAEAMDPQQRLLLEVAWEALEDAGYDPESLAGSRTGVFVGASSNDYALLLLADPEAIDAYALTGNAKSVLAGRISY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 966 FYGLEGPAVTVDTACSSSLVALHLACQSLRAGECDRALVGAATVMAEPGLFVEFSRLRALAPDGRCKPFSAAADGFGMAE 1045
Cdd:COG3321 160 KLDLRGPSVTVDTACSSSLVAVHLACQSLRSGECDLALAGGVNLMLTPESFILFSKGGMLSPDGRCRAFDADADGYVRGE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 1046 GVGVLVVERLSDAERWGHRVLAVVRGSAVNQDGASNGLTAPSGPAQERVIHAALHNARTPAAEIDLLEAHGTGTRLGDPI 1125
Cdd:COG3321 240 GVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRSNGLTAPNGPAQAAVIRRALADAGVDPATVDYVEAHGTGTPLGDPI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 1126 EAQALLATYGRQRDAERPLWLGSLKSNIGHTQAAAGVSGLIKTVLALRHRTMPATLHVQQPSAQVDWSAGTVRLLTEART 1205
Cdd:COG3321 320 EAAALTAAFGQGRPADQPCAIGSVKSNIGHLEAAAGVAGLIKAVLALRHGVLPPTLHFETPNPHIDFENSPFYVNTELRP 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 1206 WAAPsGRPRRAGVSSFGISGTNAHVILEEAPRgvrgtESAEPPAWAHVAVPLVLSAKSPQALREQASALSRHLRDHPEEP 1285
Cdd:COG3321 400 WPAG-GGPRRAGVSSFGFGGTNAHVVLEEAPA-----AAPAAAAAARPPQLLVLSAKTEEALRALAARLAAFLEAHPDLD 473
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2762205949 1286 LHHTAHTLACHRTHHPYRTAATG-TRNHLIKTL-------NNTHTHTRARPTPPGITALYTGQGSQHPGMGQQL 1351
Cdd:COG3321 474 LADVAYTLATGRAHFEHRLAVVAsSREELAAKLralaageAAPGVVTGAAAAAPKVAFLFPGQGSQYVGMGREL 547
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
808-1232 |
0e+00 |
|
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different products, called polyketides, by successive decarboxylating Claisen condensations. PKSs can be divided into 2 groups, modular type I PKSs consisting of one or more large multifunctional proteins and iterative type II PKSs, complexes of several monofunctional subunits.
Pssm-ID: 238429 [Multi-domain] Cd Length: 421 Bit Score: 619.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 808 EPVAIVGMACRLPGGVrSADDLWELVREGRDAVTRFPSDRgWDLAELYsADPARPGTFYQREAALLDDVAGFDAAFFGIS 887
Cdd:cd00833 1 EPIAIVGMACRFPGAA-DPDEFWENLLEGRDAISEIPEDR-WDADGYY-PDPGKPGKTYTRRGGFLDDVDAFDAAFFGIS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 888 QREALAMDPQQRLLLETTWEAVEDSGITADTLRGSRTGVFAGVMHLPYGTPLGRTRPDLEGYVMTGTTSSVVSGRLAYFY 967
Cdd:cd00833 78 PREAEAMDPQQRLLLEVAWEALEDAGYSPESLAGSRTGVFVGASSSDYLELLARDPDEIDAYAATGTSRAFLANRISYFF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 968 GLEGPAVTVDTACSSSLVALHLACQSLRAGECDRALVGAATVMAEPGLFVEFSRLRALAPDGRCKPFSAAADGFGMAEGV 1047
Cdd:cd00833 158 DLRGPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLSPDGRCRPFDADADGYVRGEGV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 1048 GVLVVERLSDAERWGHRVLAVVRGSAVNQDGASNGLTAPSGPAQERVIHAALHNARTPAAEIDLLEAHGTGTRLGDPIEA 1127
Cdd:cd00833 238 GVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRTKGITAPSGEAQAALIRRAYARAGVDPSDIDYVEAHGTGTPLGDPIEV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 1128 QALLATYGRQRDAERPLWLGSLKSNIGHTQAAAGVSGLIKTVLALRHRTMPATLHVQQPSAQVDWSAGTVRLLTEARTWA 1207
Cdd:cd00833 318 EALAKVFGGSRSADQPLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKIDFEESPLRVPTEARPWP 397
|
410 420
....*....|....*....|....*
gi 2762205949 1208 APSgRPRRAGVSSFGISGTNAHVIL 1232
Cdd:cd00833 398 APA-GPRRAGVSSFGFGGTNAHVIL 421
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
810-1234 |
8.14e-171 |
|
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the thiolase family and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.
Pssm-ID: 214836 [Multi-domain] Cd Length: 298 Bit Score: 509.95 E-value: 8.14e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 810 VAIVGMACRLPGgVRSADDLWELVREGrdavtrfpsdrgwdlaelysadparpgtfyqreaalLDDVAGFDAAFFGISQR 889
Cdd:smart00825 1 IAIVGMSCRFPG-ADDPEEFWDLLLAG------------------------------------LDDVDLFDAAFFGISPR 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 890 EALAMDPQQRLLLETTWEAVEDSGITADTLRGSRTGVFAGVMHLPYgtplgrtrpdlegyvmtgttssvvsgrlayfygl 969
Cdd:smart00825 44 EAEAMDPQQRLLLEVAWEALEDAGIDPESLRGSRTGVFVGVSSSDY---------------------------------- 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 970 egpAVTVDTACSSSLVALHLACQSLRAGECDRALVGAATVMAEPGLFVEFSRLRALAPDGRCKPFSAAADGFGMAEGVGV 1049
Cdd:smart00825 90 ---SVTVDTACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLSPDGRCKTFDASADGYVRGEGVGV 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 1050 LVVERLSDAERWGHRVLAVVRGSAVNQDGASNGLTAPSGPAQervihaalhnartpaaeidlleahgtgtrlgdpieaqa 1129
Cdd:smart00825 167 VVLKRLSDALRDGDPILAVIRGSAVNQDGRSNGITAPSGPAQ-------------------------------------- 208
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 1130 llatygrqrdaerpLWLGSLKSNIGHTQAAAGVSGLIKTVLALRHRTMPATLHVQQPSAQVDWSAGTVRLLTEARTWaAP 1209
Cdd:smart00825 209 --------------LLIGSVKSNIGHLEAAAGVAGLIKVVLALKHGVIPPTLHFETPNPHIDLEESPLRVPTELTPW-PP 273
|
410 420
....*....|....*....|....*
gi 2762205949 1210 SGRPRRAGVSSFGISGTNAHVILEE 1234
Cdd:smart00825 274 PGRPRRAGVSSFGFGGTNAHVILEE 298
|
|
| mycolic_Pks13 |
NF040607 |
polyketide synthase Pks13; |
704-1351 |
6.05e-144 |
|
polyketide synthase Pks13;
Pssm-ID: 468580 [Multi-domain] Cd Length: 1671 Bit Score: 479.03 E-value: 6.05e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 704 VADAlgpEGREAAAADPDRDFRSLGLDSAGAVRVRRRLVELTGLRLPVTALFDHPTPRALAREIVrrlfgaAPEPRTAAL 783
Cdd:NF040607 14 VANA---TGQPADQITDDRPMEEFGLSSRDAVALSGDIEDLTGVTLTATVAYQHPTIASLATRII------EGEPEVAAD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 784 TTTSPPGPRAEGATSGDsaagvphepVAIVGMACRLPGGVRSADDLWELVREGRDAVTRFPSDRgWdlAElYSADPArpg 863
Cdd:NF040607 85 DDDDADWSRRPRSDAHD---------IAIVGLATRFPGAGNTPEEMWEALIEGRDGITDLPEGR-W--SE-FAADPR--- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 864 tFYQR--EAAL----LDDVAGFDAAFFGISQREALAMDPQQRLLLETTWEAVEDSGITADTLRGSRTGVFAGVMHLPYG- 936
Cdd:NF040607 149 -IAERvaKANTrggyLDDIKGFDAEFFALSPLEAENVDPQQRLALELTWEALEHARIPASSLRGEPVGVFIGSSNNDYQm 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 937 ---TPLGRTRPdlegYVMTGTTSSVVSGRLAYFYGLEGPAVTVDTACSSSLVALHLACQSLRAGECDRALVGAATVMAEP 1013
Cdd:NF040607 228 lavADPAEAHP----YALTGTSSSIIANRVSYFFDFRGPSVAVDTACSSSLVAVHQAVRALRSGEADVAVAGGVNMLLTP 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 1014 GLFVEFSRLR-ALAPDGRCKPFSAAADGFGMAEGVGVLVVERLSDAERWGHRVLAVVRGSAVNQDGASNGLTAPSGPAQE 1092
Cdd:NF040607 304 AVTLGFDELGgVLAPDGRIKAFSSDADGMVRSEGGGVVVLKRLADARRDGDTILAVIAGSAVNSDGRSNGLTAPNPDAQV 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 1093 RVIHAALHNARTPAAEIDLLEAHGTGTRLGDPIEAQALLATYGRQRDAERPLWLGSLKSNIGHTQAAAGVSGLIKTVLAL 1172
Cdd:NF040607 384 DVLRRAYADAGIDPRTVDYVEAHGTGTILGDPIEADALGRVVGRGRDADKPALLGSAKTNFGHLESAAGAAGLAKVVLAM 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 1173 RHRTMPATLHVQQPSAQVDWSAGTVRLLTEARTWAAPSGRPrRAGVSSFGISGTNAHVIL-------------------- 1232
Cdd:NF040607 464 QHDKLPPSLNYAGPNPYIDFDAEHLKVVDEPTEWPRYSGHA-VAGVSGFGFGGTNAHVVVrevlpadlvepeaqpdedte 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 1233 -------EEAPRGVRGTESAEPPAWAHV---AVPLVLSAKSPQALREQASALSRHLRDHPEE--PLHHTAHTLAcHRTHH 1300
Cdd:NF040607 543 aelagltAEAKRLLAEAELAAEFAPAAPegpVVPLPVSGFLPSRRRAAAADLADWLESEEGRatPLADVARALA-RRNHG 621
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 2762205949 1301 PYRTAAT-GTRNHLIKTL-------NNTHTHTRARPTPPGITALYTGQGSQHPGMGQQL 1351
Cdd:NF040607 622 RSRAVVLaHTHEEAIKGLravaegkPGPGVFSADAPAANGPVWVLSGFGSQHRKMAKQL 680
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
231-1144 |
1.68e-127 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 428.52 E-value: 1.68e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 231 QAAGRDRPLPRVVPLLVSGRSRAGLRAYAEALAGHLVAHPDISLTDTAFTLAGARPLWPYRSLVPAGDRDTAVAALRALA 310
Cdd:COG3321 431 AAPAAAAAARPPQLLVLSAKTEEALRALAARLAAFLEAHPDLDLADVAYTLATGRAHFEHRLAVVASSREELAAKLRALA 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 311 AGAPGDDVVQAEPGPDTRTVFVFPGQGPQWAGMAGELARAEPAFRKKLAECARALRPWLEVDPDELLFG---ARPLDRVE 387
Cdd:COG3321 511 AGEAAPGVVTGAAAAAPKVAFLFPGQGSQYVGMGRELYETEPVFRAALDECDALLRPHLGWSLREVLFPdeeESRLDRTE 590
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 388 LVQPALFSVMVSLAHLWRSHGMTPAAMVGHSFGEIAAVTAAGGLSLTDGARLVAAVSTALARIEGQGDMVAVALTPDETE 467
Cdd:COG3321 591 VAQPALFAVEYALARLWRSWGVRPDAVIGHSVGEYAAACVAGVLSLEDALRLVAARGRLMQALPGGGAMLAVGLSEEEVE 670
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 468 ALLAEEGlDLGIAVVNGPRSTVVSGTRDAATKLLGRLAARGVRARRLPVGIAGHSPHMDRIRDVLVRGAAAVRPRRSAVP 547
Cdd:COG3321 671 ALLAGYD-GVSIAAVNGPRSTVVSGPAEAVEALAARLEARGIRARRLPVSHAFHSPLMEPALEEFRAALAGVTPRAPRIP 749
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 548 VYGSTTTAPLDTAALDADHWFRAMRGTARFHDVVAGLLSAGHRLFVEISPHPVLAMSIEDTAAHLErDVVVLDTMRRDDA 627
Cdd:COG3321 750 LISNVTGTWLTGEALDADYWVRHLRQPVRFADAVEALLADGVRVFLEVGPGPVLTGLVRQCLAAAG-DAVVLPSLRRGED 828
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 628 GAGRYVRALAEAQLHGAdPPDWSAVLP--SAARVTLPPYRFERDTREGDGAEGDGADALRARLTGHRPDERADQAVQLVA 705
Cdd:COG3321 829 ELAQLLTALAQLWVAGV-PVDWSALYPgrGRRRVPLPTYPFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAA 907
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 706 DALGPEGREAAAADPDRDFRSLGLDSAGAV------------------RVRRRLVELTGLRLPVTALFDHPTPRALAREI 767
Cdd:COG3321 908 LLALAAAAAAALALAAAALAALLALVALAAaaaallalaaaaaaaaaaLAAAEAGALLLLAAAAAAAAAAAAAAAAAAAA 987
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 768 VRRLFGAAPEPRTAALTTTSPPGPRAEGATSGDSAAGVPHEPVAIVGMACRLPGGVRSADDLWELVREGRDAVTRFPsDR 847
Cdd:COG3321 988 AAAAAAAALAAAAALALLAAAALLLAAAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALA-LA 1066
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 848 GWDLAELYSADPARPGTFYQREAALLDDVAGFDAAFFGISQREALAMDPQQRLLLETTWEAVEDSGITADTLRGSRTGVF 927
Cdd:COG3321 1067 ALLLLAALAELALAAAALALAAALAAAALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAA 1146
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 928 AGVMHLPYGTPLGRTRPDLEGYVMTGTTSSVVSGRLAYFYGLEGPAVTVDTACSSSLVALHLACQSLRAGECDRALVGAA 1007
Cdd:COG3321 1147 AAALALAAAAAALAAALAAALLAAAALLLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAA 1226
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 1008 TVMAEPGLFVEFSRLRALAPDGRCKPFSAAADGFGMAEGVGVLVVERLSDAERWGHRVLAVVRGSAVNQDGASNGLTAPS 1087
Cdd:COG3321 1227 AAAAAALALLALAAAAAAVAALAAAAAALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAA 1306
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*..
gi 2762205949 1088 GPAQERVIHAALHNARTPAAEIDLLEAHGTGTRLGDPIEAQALLATYGRQRDAERPL 1144
Cdd:COG3321 1307 AAAAAAAAAAAAAALAAALLAAALAALAAAVAAALALAAAAAAAAAAAAAAAAAAAL 1363
|
|
| PKS_AT |
smart00827 |
Acyl transferase domain in polyketide synthase (PKS) enzymes; |
332-625 |
3.39e-105 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes;
Pssm-ID: 214838 [Multi-domain] Cd Length: 298 Bit Score: 335.53 E-value: 3.39e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 332 VFPGQGPQWAGMAGELARAEPAFRKKLAECARALRPWLEVDPDELLFG---ARPLDRVELVQPALFSVMVSLAHLWRSHG 408
Cdd:smart00827 1 VFTGQGSQWAGMGRELYETEPVFREALDECDAALQPLLGWSLLDVLLGedgAASLLDTEVAQPALFAVQVALARLLRSWG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 409 MTPAAMVGHSFGEIAAVTAAGGLSLTDGARLVAAVSTALARIEGQGDMVAVALTPDETEALLAEEGLDLGIAVVNGPRST 488
Cdd:smart00827 81 VRPDAVVGHSSGEIAAAYVAGVLSLEDAARLVAARGRLMQALPGGGAMLAVGLSEEEVEPLLAGVPDRVSVAAVNSPSSV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 489 VVSGTRDAATKLLGRLAARGVRARRLPVGIAGHSPHMDRIRDVLVRGAAAVRPRRSAVPVYGSTTTAPLDTAAL-DADHW 567
Cdd:smart00827 161 VLSGDEDAVDELAARLEAEGIFARRLKVDHAFHSPHMEPILDEFRAALAGLTPRPPRIPFVSTVTGTLIDGAELdDADYW 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2762205949 568 FRAMRGTARFHDVVAGLLSA-GHRLFVEISPHPVLAMSIEDTAAHLERDVVVLdTMRRD 625
Cdd:smart00827 241 VRNLREPVRFADAVRALLAEgGVTVFLEVGPHPVLTGPIKQTLAAAGSAVVLP-SLRRG 298
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
808-1058 |
3.98e-98 |
|
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains. The N-terminal domain contains most of the structures involved in dimer formation and also the active site cysteine.
Pssm-ID: 425468 [Multi-domain] Cd Length: 251 Bit Score: 314.19 E-value: 3.98e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 808 EPVAIVGMACRLPGGVrSADDLWELVREGRDAVTRFPSDRgWDLAELYSADPARPGTFYQREAALlDDVAGFDAAFFGIS 887
Cdd:pfam00109 1 EPVAIVGMGCRFPGGN-DPEEFWENLLEGRDGISEIPADR-WDPDKLYDPPSRIAGKIYTKWGGL-DDIFDFDPLFFGIS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 888 QREALAMDPQQRLLLETTWEAVEDSGITADTLRGSRTGVFAGVMHLPYGTPLGRTRP--DLEGYV-MTGTTSSVVSGRLA 964
Cdd:pfam00109 78 PREAERMDPQQRLLLEAAWEALEDAGITPDSLDGSRTGVFIGSGIGDYAALLLLDEDggPRRGSPfAVGTMPSVIAGRIS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 965 YFYGLEGPAVTVDTACSSSLVALHLACQSLRAGECDRALVGAATVMAEPGLFVEFSRLRALAPDGRCKPFSAAADGFGMA 1044
Cdd:pfam00109 158 YFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSPDGPCKAFDPFADGFVRG 237
|
250
....*....|....
gi 2762205949 1045 EGVGVLVVERLSDA 1058
Cdd:pfam00109 238 EGVGAVVLKRLSDA 251
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
809-1232 |
4.33e-68 |
|
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible for the elongation steps in fatty acid biosynthesis. KASIII catalyses the initial condensation and KAS I and II catalyze further elongation steps by Claisen condensation of malonyl-acyl carrier protein (ACP) with acyl-ACP.
Pssm-ID: 238430 [Multi-domain] Cd Length: 406 Bit Score: 235.51 E-value: 4.33e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 809 PVAIVGMACRLPGGVrSADDLWELVREGRDAVTRFPSDRgwdlaelYSADPARPGTFyqreaallddVAGFDAAFFgISQ 888
Cdd:cd00834 2 RVVITGLGAVTPLGN-GVEEFWEALLAGRSGIRPITRFD-------ASGFPSRIAGE----------VPDFDPEDY-LDR 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 889 REALAMDPQQRLLLETTWEAVEDSGITADTLRGSRTGVFAGV-------MHLPYGTPLGRTRPDLEGYVMTGTTSSVVSG 961
Cdd:cd00834 63 KELRRMDRFAQFALAAAEEALADAGLDPEELDPERIGVVIGSgigglatIEEAYRALLEKGPRRVSPFFVPMALPNMAAG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 962 RLAYFYGLEGPAVTVDTACSSSLVALHLACQSLRAGECDRALVGAATVMAEPGLFVEFSRLRALA-----PDGRCKPFSA 1036
Cdd:cd00834 143 QVAIRLGLRGPNYTVSTACASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALRALStrnddPEKASRPFDK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 1037 AADGFGMAEGVGVLVVERLSDAERWGHRVLAVVRGSAVNQDGASngLTAPS--GPAQERVIHAALHNARTPAAEIDLLEA 1114
Cdd:cd00834 223 DRDGFVLGEGAGVLVLESLEHAKARGAKIYAEILGYGASSDAYH--ITAPDpdGEGAARAMRAALADAGLSPEDIDYINA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 1115 HGTGTRLGDPIEAQALLATYGrqrDAERPLWLGSLKSNIGHTQAAAGVSGLIKTVLALRHRTMPATLHVQQPSAQVDwsa 1194
Cdd:cd00834 301 HGTSTPLNDAAESKAIKRVFG---EHAKKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPECD--- 374
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2762205949 1195 gtVRLLT-EARTWaapsgrPRRAGVS-SFGISGTNAHVIL 1232
Cdd:cd00834 375 --LDYVPnEAREA------PIRYALSnSFGFGGHNASLVF 406
|
|
| omega_3_PfaA |
TIGR02813 |
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ... |
809-1352 |
8.80e-68 |
|
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this alignment are involved in omega-3 polyunsaturated fatty acid biosynthesis, such as the protein PfaA from the eicosapentaenoic acid biosynthesis operon in Photobacterium profundum strain SS9. PfaA is encoded together with PfaB, PfaC, and PfaD, and the functions of the individual polypeptides have not yet been described. More distant homologs of PfaA, also included with the reach of this model, appear to be involved in polyketide-like biosynthetic mechanisms of polyunsaturated fatty acid biosynthesis, an alternative to the more familiar iterated mechanism of chain extension and desaturation, and in most cases are encoded near genes for homologs of PfaB, PfaC, and/or PfaD.
Pssm-ID: 274311 [Multi-domain] Cd Length: 2582 Bit Score: 253.00 E-value: 8.80e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 809 PVAIVGMAcRLPGGVRSADDLWELVREGRDAVTRFPSDRgWDLAELYSADPARPGTFYQREAALLDDVaGFDAAFFGISQ 888
Cdd:TIGR02813 8 PIAIVGMA-SIFANSRYLNKFWDLIFEKIDAITDVPSDH-WAKDDYYDSDKSEADKSYCKRGGFLPEV-DFNPMEFGLPP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 889 REALAMDPQQRLLLETTWEAVEDSGItADTLRGSRTGVFAGV-----------MHLPYgtPL--------GRTRPDLE-- 947
Cdd:TIGR02813 85 NILELTDISQLLSLVVAKEVLNDAGL-PDGYDRDKIGITLGVgggqkqssslnARLQY--PVlkkvfkasGVEDEDSEml 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 948 ------GYV------MTGTTSSVVSGRLAYFYGLEGPAVTVDTACSSSLVALHLACQSLRAGECDRALVGAATVMAEPGL 1015
Cdd:TIGR02813 162 ikkfqdQYIhweensFPGSLGNVISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGGVCTDNSPFM 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 1016 FVEFSRLRALAPDGRCKPFSAAADGFGMAEGVGVLVVERLSDAERWGHRVLAVVRGSAVNQDGASNGLTAPSGPAQERVI 1095
Cdd:TIGR02813 242 YMSFSKTPAFTTNEDIQPFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGKFKSIYAPRPEGQAKAL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 1096 HAALHNARTPAAEIDLLEAHGTGTRLGDPIEAQALLATYGRQRDAERPLWLGSLKSNIGHTQAAAGVSGLIKTVLALRHR 1175
Cdd:TIGR02813 322 KRAYDDAGFAPHTCGLIEAHGTGTAAGDVAEFGGLVSVFSQDNDQKQHIALGSVKSQIGHTKSTAGTAGMIKAVLALHHK 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 1176 TMPATLHVQQPSAQVDWSAGTVRLLTEARTWAAPS-GRPRRAGVSSFGISGTNAHVILEE-APRGVRGTESAEppawAHV 1253
Cdd:TIGR02813 402 VLPPTINVDQPNPKLDIENSPFYLNTETRPWMQREdGTPRRAGISSFGFGGTNFHMVLEEySPKHQRDDQYRQ----RAV 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 1254 AVPLVLSAKSPQALREQASALSRHLRDHPE-EPLHHTA----HTLACHRTHHPYRTAATGTRNHLIKTLNNTHTHTRARP 1328
Cdd:TIGR02813 478 AQTLLFTAANEKALVSSLKDWKNKLSAKADdQPYAFNAlaveNTLRTIAVALARLGFVAKNADELITMLEQAITQLEAKS 557
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 2762205949 1329 T-----PPGIT--------------ALYTGQGSQHPGMGQQLA 1352
Cdd:TIGR02813 558 CeewqlPSGISyrksalvvesgkvaALFAGQGSQYLNMGRELA 600
|
|
| Acyl_transf_1 |
pfam00698 |
Acyl transferase domain; |
330-646 |
3.80e-67 |
|
Acyl transferase domain;
Pssm-ID: 395567 Cd Length: 319 Bit Score: 229.67 E-value: 3.80e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 330 VFVFPGQGPQWAGMAGELARAEPAFRKKLAECARALRPWLEVDPDELLFGARP--LDRVELVQPALFSVMVSLAHLWRSH 407
Cdd:pfam00698 1 VFVFSGQGSQWAGMGMQLLKTSPAFAAVIDRADEAFKPQYGFSVSDVLRNNPEgtLDGTQFVQPALFAMQIALAALLQSY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 408 GMTPAAMVGHSFGEIAAVTAAGGLSLTDGARLVAAVSTALARIEGQGDMVAVALTPDETEALLAEeglDLGIAVVNGPRS 487
Cdd:pfam00698 81 GVRPDAVVGHSLGEYAAAVVAGALSPEEALLAAVLRSRLMMQLAGPGGMAAVELSAEEVEQRWPD---DVVGAVVNSPRS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 488 TVVSGTRDAATKLLGRLAARGVRARRLPVGIAGHSPHMDRIRDVLVRGAAAVRPRRSAVPVYGSTTTAPLDTAALDADHW 567
Cdd:pfam00698 158 VVISGPQEAVRELVERVSKEGVGALVENVNYAVHSPQMDAIAPALLSALADIAPRTPRVPFISSTSIDPSDQRTLSAEYW 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 568 FRAMRGTARFHDVVAGLLSAGHRLFVEISPHPVLAMSIEDT--AAHLERDVVVLDTMRRD-DAGAGRYVRALAEAQLHGA 644
Cdd:pfam00698 238 VRNLRSPVRFAEAILSAAEPGPLVFIEISPHPLLLAALIDTlkSASDGKVATLVGTLIRDqTDFLVTFLYILAVAHLTGS 317
|
..
gi 2762205949 645 DP 646
Cdd:pfam00698 318 AP 319
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
810-1232 |
1.61e-64 |
|
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism]; 3-oxoacyl-(acyl-carrier-protein) synthase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440073 [Multi-domain] Cd Length: 409 Bit Score: 225.36 E-value: 1.61e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 810 VAIVGMACRLPGGVrSADDLWELVREGRDAVTRFPSdrgWDLAELysadPARPgtfyqreAALlddVAGFDAAFFgISQR 889
Cdd:COG0304 3 VVITGLGAVSPLGN-GVEEFWEALLAGRSGIRPITR---FDASGL----PVRI-------AGE---VKDFDPEEY-LDRK 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 890 EALAMDPQQRLLLETTWEAVEDSGITADTLRGSRTGVFAG-------VMHLPYGTPLGRTRPDLEGYVMTGTTSSVVSGR 962
Cdd:COG0304 64 ELRRMDRFTQYALAAAREALADAGLDLDEVDPDRTGVIIGsgiggldTLEEAYRALLEKGPRRVSPFFVPMMMPNMAAGH 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 963 LAYFYGLEGPAVTVDTACSSSLVALHLACQSLRAGECDRALVGAATVMAEPGLFVEFSRLRALA-----PDGRCKPFSAA 1037
Cdd:COG0304 144 VSIRFGLKGPNYTVSTACASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLAGFDALGALStrnddPEKASRPFDKD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 1038 ADGFGMAEGVGVLVVERLSDAERWGHRVLAVVRGSAVNQDGASNGLTAPSGPAQERVIHAALHNARTPAAEIDLLEAHGT 1117
Cdd:COG0304 224 RDGFVLGEGAGVLVLEELEHAKARGAKIYAEVVGYGASSDAYHITAPAPDGEGAARAMRAALKDAGLSPEDIDYINAHGT 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 1118 GTRLGDPIEAQALLATYGrqrDAERPLWLGSLKSNIGHTQAAAGVSGLIKTVLALRHRTMPATLHVQQ--PSAQVDWsag 1195
Cdd:COG0304 304 STPLGDAAETKAIKRVFG---DHAYKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENpdPECDLDY--- 377
|
410 420 430
....*....|....*....|....*....|....*...
gi 2762205949 1196 tvrLLTEARTwaapsgRPRRAGVS-SFGISGTNAHVIL 1232
Cdd:COG0304 378 ---VPNEARE------AKIDYALSnSFGFGGHNASLVF 406
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
897-1232 |
2.68e-58 |
|
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new carbon-carbon bond by a decarboxylating Claisen-like condensation reaction. Members are involved in the synthesis of fatty acids and polyketides, a diverse group of natural products. Both pathways are an iterative series of additions of small carbon units, usually acetate, to a nascent acyl group. There are 2 classes of decarboxylating condensing enzymes, which can be distinguished by sequence similarity, type of active site residues and type of primer units (acetyl CoA or acyl carrier protein (ACP) linked units).
Pssm-ID: 238421 [Multi-domain] Cd Length: 332 Bit Score: 204.79 E-value: 2.68e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 897 QQRLLLETTWEAVEDSGITADTLRGSRTGVFAGVMHLPY--GTPLGRTRPDLEGYVMTGTTSSVVSGRLAYFYGLEGPAV 974
Cdd:cd00825 11 VSILGFEAAERAIADAGLSREYQKNPIVGVVVGTGGGSPrfQVFGADAMRAVGPYVVTKAMFPGASGQIATPLGIHGPAY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 975 TVDTACSSSLVALHLACQSLRAGECDRALVGAATVMAEPGLFVEFSRLRALAPDGRCKPFSAAADGFGMAEGVGVLVVER 1054
Cdd:cd00825 91 DVSAACAGSLHALSLAADAVQNGKQDIVLAGGSEELAAPMDCEFDAMGALSTPEKASRTFDAAADGFVFGDGAGALVVEE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 1055 LSDAERWGHRVLAVVRGSAVNQDGASNGLTAPSGPAQERVIHAALHNARTPAAEIDLLEAHGTGTRLGDPIEAQAllaty 1134
Cdd:cd00825 171 LEHALARGAHIYAEIVGTAATIDGAGMGAFAPSAEGLARAAKEALAVAGLTVWDIDYLVAHGTGTPIGDVKELKL----- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 1135 GRQRDAERPLWLGSLKSNIGHTQAAAGVSGLIKTVLALRHRTMPATLHVQQPSAQVDWSAGTVRllteartwaapSGRPR 1214
Cdd:cd00825 246 LRSEFGDKSPAVSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIPPSIHIEELDEAGLNIVTETT-----------PRELR 314
|
330
....*....|....*...
gi 2762205949 1215 RAGVSSFGISGTNAHVIL 1232
Cdd:cd00825 315 TALLNGFGLGGTNATLVL 332
|
|
| FabD |
COG0331 |
Malonyl CoA-acyl carrier protein transacylase [Lipid transport and metabolism]; Malonyl ... |
327-602 |
1.17e-50 |
|
Malonyl CoA-acyl carrier protein transacylase [Lipid transport and metabolism]; Malonyl CoA-acyl carrier protein transacylase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440100 [Multi-domain] Cd Length: 306 Bit Score: 181.48 E-value: 1.17e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 327 TRTVFVFPGQGPQWAGMAGELARAEPAFRKKLAECARALrpwlEVDPDELLFGARP--LDRVELVQPALFSVMVSLAHLW 404
Cdd:COG0331 1 MKLAFLFPGQGSQYVGMGKDLYENFPVAREVFEEASEAL----GYDLSALCFEGPEeeLNLTENTQPAILAASVAAYRAL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 405 RSHGMTPAAMVGHSFGEIAAVTAAGGLSLTDGARLVAAVSTALARI--EGQGDMVAVA-LTPDETEALLAE--EGLDLGI 479
Cdd:COG0331 77 EEEGIRPDAVAGHSLGEYSALVAAGALSFEDALRLVRLRGRLMQEAvpAGPGGMAAVLgLDDEEVEALCAEaaQGEVVEI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 480 AVVNGPRSTVVSGTRDAATKLLGRLAARGV-RARRLPVGIAGHSPHMDRIRDVLVRGAAAVRPRRSAVPVYGSTTTAPLD 558
Cdd:COG0331 157 ANYNSPGQIVISGEKEAVEAAAELAKEAGAkRAVPLPVSGPFHTPLMAPAAEKLAEALAAVTFADPKIPVVSNVDAAPVT 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2762205949 559 TAALDADHWFRAMRGTARFHDVVAGLLSAGHRLFVEISPHPVLA 602
Cdd:COG0331 237 DPEEIRELLVRQLTSPVRWDESVEALAEAGVTTFVELGPGKVLS 280
|
|
| Ketoacyl-synt_C |
pfam02801 |
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
1066-1183 |
1.21e-46 |
|
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.
Pssm-ID: 426989 Cd Length: 118 Bit Score: 162.74 E-value: 1.21e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 1066 LAVVRGSAVNQDGASNGLTAPSGPAQERVIHAALHNARTPAAEIDLLEAHGTGTRLGDPIEAQALLATYGRQRDaERPLW 1145
Cdd:pfam02801 1 YAVIKGSAVNHDGRHNGLTAPNGEGQARAIRRALADAGVDPEDVDYVEAHGTGTPLGDPIEAEALKRVFGSGAR-KQPLA 79
|
90 100 110
....*....|....*....|....*....|....*...
gi 2762205949 1146 LGSLKSNIGHTQAAAGVSGLIKTVLALRHRTMPATLHV 1183
Cdd:pfam02801 80 IGSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLNL 117
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
808-1232 |
1.31e-44 |
|
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, including beta-ketoacyl [ACP] synthase, type I and II and polyketide synthases.They are characterized by the utlization of acyl carrier protein (ACP) thioesters as primer substrates, as well as the nature of their active site residues.
Pssm-ID: 238424 [Multi-domain] Cd Length: 407 Bit Score: 167.23 E-value: 1.31e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 808 EPVAIVGMACRLPGG--VRSADDLWELVREGRDAVtrfpsdrgwdlaelySADPARPGTFYQREAALLD--DVAGFDAAF 883
Cdd:cd00828 1 SRVVITGIGVVSPHGegCDEVEEFWEALREGRSGI---------------APVARLKSRFDRGVAGQIPtgDIPGWDAKR 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 884 FGIsqrealaMDPQQRLLLETTWEAVEDSGITADT-LRGSRTGVFAGvMHLPYGTPLGRT----RPDLEGYVMTGT--TS 956
Cdd:cd00828 66 TGI-------VDRTTLLALVATEEALADAGITDPYeVHPSEVGVVVG-SGMGGLRFLRRGgkldARAVNPYVSPKWmlSP 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 957 SVVSGRLAYFYGLE-GPAVTVDTACSSSLVALHLACQSLRAGECDRALVGAATVMAEPGLFvEFSRLRALA-----PDGR 1030
Cdd:cd00828 138 NTVAGWVNILLLSShGPIKTPVGACATALEALDLAVEAIRSGKADIVVVGGVEDPLEEGLS-GFANMGALStaeeePEEM 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 1031 CKPFSAAADGFGMAEGVGVLVVERLSDAERWGHRVLAVVRGSAVNQDGASNGLTAPsGPAQERVIHAALHNARTPAAEID 1110
Cdd:cd00828 217 SRPFDETRDGFVEAEGAGVLVLERAELALARGAPIYGRVAGTASTTDGAGRSVPAG-GKGIARAIRTALAKAGLSLDDLD 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 1111 LLEAHGTGTRLGDPIEAQALLATYGrqrDAERPLWLGSLKSNIGHTQAAAGVSGLIKTVLALRHRTMPATLHVQQPSAQV 1190
Cdd:cd00828 296 VISAHGTSTPANDVAESRAIAEVAG---ALGAPLPVTAQKALFGHSKGAAGALQLIGALQSLEHGLIPPTANLDDVDPDV 372
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2762205949 1191 DWSAGTvrllTEARTWAapsGRPRRAGVSSFGISGTNAHVIL 1232
Cdd:cd00828 373 EHLSVV----GLSRDLN---LKVRAALVNAFGFGGSNAALVL 407
|
|
| PTZ00050 |
PTZ00050 |
3-oxoacyl-acyl carrier protein synthase; Provisional |
820-1228 |
8.22e-40 |
|
3-oxoacyl-acyl carrier protein synthase; Provisional
Pssm-ID: 240245 [Multi-domain] Cd Length: 421 Bit Score: 153.69 E-value: 8.22e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 820 PGGVrSADDLWELVREGR---DAVTRFP------SDRGWDLAELYSADPARPGTFYQREAallddvagFDAAFFGISQRE 890
Cdd:PTZ00050 4 PLGV-GAESTWEALIAGKsgiRKLTEFPkflpdcIPEQKALENLVAAMPCQIAAEVDQSE--------FDPSDFAPTKRE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 891 alamDPQQRLLLETTWEAVEDSGIT--ADTLRgSRTGVFAGVMhLPYGTPLGRTRPDLEG--------YVMTGTTSSVVS 960
Cdd:PTZ00050 75 ----SRATHFAMAAAREALADAKLDilSEKDQ-ERIGVNIGSG-IGSLADLTDEMKTLYEkghsrvspYFIPKILGNMAA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 961 GRLAYFYGLEGPAVTVDTACSSSLVALHLACQSLRAGECDRALVGAATVMAEPGLFVEFSRLRALA------PDGRCKPF 1034
Cdd:PTZ00050 149 GLVAIKHKLKGPSGSAVTACATGAHCIGEAFRWIKYGEADIMICGGTEASITPVSFAGFSRMRALCtkynddPQRASRPF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 1035 SAAADGFGMAEGVGVLVVERLSDAERWGHRVLAVVRGSAVNQDGASNGLTAPSGPAQERVIHAAL-HNARTPAAEIDLLE 1113
Cdd:PTZ00050 229 DKDRAGFVMGEGAGILVLEELEHALRRGAKIYAEIRGYGSSSDAHHITAPHPDGRGARRCMENALkDGANININDVDYVN 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 1114 AHGTGTRLGDPIEAQALLATYGrqRDAERPLWLGSLKSNIGHTQAAAGVSGLIKTVLALRHRTMPATLHVQQPSAQVDws 1193
Cdd:PTZ00050 309 AHATSTPIGDKIELKAIKKVFG--DSGAPKLYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINLENPDAECD-- 384
|
410 420 430
....*....|....*....|....*....|....*.
gi 2762205949 1194 agtVRLLTEArtwAAPSGRPRRAGVS-SFGISGTNA 1228
Cdd:PTZ00050 385 ---LNLVQGK---TAHPLQSIDAVLStSFGFGGVNT 414
|
|
| PRK06501 |
PRK06501 |
beta-ketoacyl-ACP synthase; |
959-1236 |
5.33e-33 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235817 [Multi-domain] Cd Length: 425 Bit Score: 133.60 E-value: 5.33e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 959 VSGRLAYFYGLEGPAVTVDTACSSSLVALHLACQSLRAGECDRALVGAATVMAEPGLFVEFSRLRAL-----APDGRCKP 1033
Cdd:PRK06501 154 IADRLADRFGTRGLPISLSTACASGATAIQLGVEAIRRGETDRALCIATDGSVSAEALIRFSLLSALstqndPPEKASKP 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 1034 FSAAADGFGMAEGVGVLVVERLSDAERWGHRVLAVVRGSAVNQDGASNGLTAPSGPAQERVIHAALHNARTPAAEIDLLE 1113
Cdd:PRK06501 234 FSKDRDGFVMAEGAGALVLESLESAVARGAKILGIVAGCGEKADSFHRTRSSPDGSPAIGAIRAALADAGLTPEQIDYIN 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 1114 AHGTGTRLGDPIEAQALLATYGrQRDAERPlwLGSLKSNIGHTQAAAGVSGLIKTVLALRHRTMPATL--HVQQPSAQVD 1191
Cdd:PRK06501 314 AHGTSTPENDKMEYLGLSAVFG-ERLASIP--VSSNKSMIGHTLTAAGAVEAVFSLLTIQTGRLPPTInyDNPDPAIPLD 390
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2762205949 1192 WSAGTVRlltEARTWAAPSgrprragvSSFGISGTNAHVILEEAP 1236
Cdd:PRK06501 391 VVPNVAR---DARVTAVLS--------NSFGFGGQNASLVLTAEP 424
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
876-1232 |
8.03e-32 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 129.91 E-value: 8.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 876 VAGFDAAFFgISQREALAMDPQQRLLLETTWEAVEDSGITADTLRGSRTGVFAGvmhlpygTPLGrtrpDLEGYVMTGTT 955
Cdd:PRK07314 52 VKDFNPDDY-MSRKEARRMDRFIQYGIAAAKQAVEDAGLEITEENADRIGVIIG-------SGIG----GLETIEEQHIT 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 956 ------------------SSVVSGRLAYFYGLEGPAVTVDTACSSSLVALHLACQSLRAGECDRALVGAATVMAEPGLFV 1017
Cdd:PRK07314 120 llekgprrvspffvpmaiINMAAGHVSIRYGAKGPNHSIVTACATGAHAIGDAARLIAYGDADVMVAGGAEAAITPLGIA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 1018 EFSRLRALA-----PDGRCKPFSAAADGFGMAEGVGVLVVERLSDAERWGHRVLAVVRGSAVNQDGASngLTAPS--GPA 1090
Cdd:PRK07314 200 GFAAARALStrnddPERASRPFDKDRDGFVMGEGAGILVLEELEHAKARGAKIYAEVVGYGMTGDAYH--MTAPApdGEG 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 1091 QERVIHAALHNARTPAAEIDLLEAHGTGTRLGDPIEAQALLATYGrqrDAERPLWLGSLKSNIGHTQAAAGVSGLIKTVL 1170
Cdd:PRK07314 278 AARAMKLALKDAGINPEDIDYINAHGTSTPAGDKAETQAIKRVFG---EHAYKVAVSSTKSMTGHLLGAAGAVEAIFSVL 354
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2762205949 1171 ALRHRTMPATLHVQQPSAQV--DWSAGtvrlltEARTwaapsgRPRRAGVS-SFGISGTNAHVIL 1232
Cdd:PRK07314 355 AIRDQVIPPTINLDNPDEECdlDYVPN------EARE------RKIDYALSnSFGFGGTNASLVF 407
|
|
| PRK07103 |
PRK07103 |
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated |
860-1233 |
9.24e-32 |
|
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
Pssm-ID: 180839 [Multi-domain] Cd Length: 410 Bit Score: 129.38 E-value: 9.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 860 ARPGTFYQREAALLDDVAGFDAAFFGISQREALAMDPQQRLLLE------TTWEAVEDSGitADTLRGSRTGVFAG---- 929
Cdd:PRK07103 37 RRPGRQVPDDAGAGLASAFIGAELDSLALPERLDAKLLRRASLSaqaalaAAREAWRDAA--LGPVDPDRIGLVVGgsnl 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 930 ------VMHLPYGTPLGRTRPDLEGYVMtgttSSVVSGRLAYFYGLEGPAVTVDTACSSSLVALHLACQSLRAGECDRAL 1003
Cdd:PRK07103 115 qqreqaLVHETYRDRPAFLRPSYGLSFM----DTDLVGLCSEQFGIRGEGFTVGGASASGQLAVIQAARLVQSGSVDACI 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 1004 VGAAtvMAEPGlFVEFSRLRAL----------APDGRCKPFSAAADGFGMAEGVGVLVVERLSDAERWGHRVLAVVRGSA 1073
Cdd:PRK07103 191 AVGA--LMDLS-YWECQALRSLgamgsdrfadEPEAACRPFDQDRDGFIYGEACGAVVLESAESARRRGARPYAKLLGWS 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 1074 VNQDGasNGLTAPSGPAQERVIHAALHNARTPAAEIDLLEAHGTGTRLGDPIEAQALLATYGRQrdaerpLWLGSLKSNI 1153
Cdd:PRK07103 268 MRLDA--NRGPDPSLEGEMRVIRAALRRAGLGPEDIDYVNPHGTGSPLGDETELAALFASGLAH------AWINATKSLT 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 1154 GHTQAAAGVSGLIKTVLALRHRTMPATLHVQQP-SAQVDWSAGTVRllteartwaapSGRPRRAGVSSFGISGTNAHVIL 1232
Cdd:PRK07103 340 GHGLSAAGIVELIATLLQMRAGFLHPSRNLDEPiDERFRWVGSTAE-----------SARIRYALSLSFGFGGINTALVL 408
|
.
gi 2762205949 1233 E 1233
Cdd:PRK07103 409 E 409
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
897-1232 |
2.86e-31 |
|
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) Claisen-like condensation reaction. Members are share strong structural similarity, and are involved in the synthesis and degradation of fatty acids, and the production of polyketides, a diverse group of natural products.
Pssm-ID: 238201 [Multi-domain] Cd Length: 254 Bit Score: 123.71 E-value: 2.86e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 897 QQRLLLETTWEAVEDSGITAdtlrGSRTGVFAGVMhlpYGTPLGrtrpdlegyvmtgttsSVVSGRLAYFYGL-EGPAVT 975
Cdd:cd00327 7 ASELGFEAAEQAIADAGLSK----GPIVGVIVGTT---GGSGEF----------------SGAAGQLAYHLGIsGGPAYS 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 976 VDTACSSSLVALHLACQSLRAGECDRALVGAAtvmaepglfvefsrlralapdgrckpfsaaaDGFGMAEGVGVLVVERL 1055
Cdd:cd00327 64 VNQACATGLTALALAVQQVQNGKADIVLAGGS-------------------------------EEFVFGDGAAAAVVESE 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 1056 SDAERWGHRVLAVVRGSAVNQDGASnGLTAPSGPAQERVIHAALHNARTPAAEIDLLEAHGTGTRLGDPIEAQAllatyG 1135
Cdd:cd00327 113 EHALRRGAHPQAEIVSTAATFDGAS-MVPAVSGEGLARAARKALEGAGLTPSDIDYVEAHGTGTPIGDAVELAL-----G 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 1136 RQRDAERPLWLGSLKSNIGHTQAAAGVSGLIKTVLALRHRTMPATlhvqqpsaqvdwsagtvrllteartwaapSGRPRR 1215
Cdd:cd00327 187 LDPDGVRSPAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIPPT-----------------------------PREPRT 237
|
330
....*....|....*..
gi 2762205949 1216 AGVSSFGISGTNAHVIL 1232
Cdd:cd00327 238 VLLLGFGLGGTNAAVVL 254
|
|
| PRK06333 |
PRK06333 |
beta-ketoacyl-ACP synthase; |
874-1232 |
1.83e-30 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235781 [Multi-domain] Cd Length: 424 Bit Score: 125.88 E-value: 1.83e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 874 DDVAGFDAAFFgISQREALAMDPQQRLLLETTWEAVEDSGITADTLRGS-RTGVF--AGVMHLPYGTPLGRTRpDLEG-- 948
Cdd:PRK06333 60 DAEAGFDPDRY-LDPKDQRKMDRFILFAMAAAKEALAQAGWDPDTLEDReRTATIigSGVGGFPAIAEAVRTL-DSRGpr 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 949 --------YVMTGTTSSVVSGRlayfYGLEGPAVTVDTACSSSLVALHLACQSLRAGECDRALVGAATVMAEPGLFVEFS 1020
Cdd:PRK06333 138 rlspftipSFLTNMAAGHVSIR----YGFKGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGGTEAAIDRVSLAGFA 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 1021 RLRAL------APDGRCKPFSAAADGFGMAEGVGVLVVERLSDAERWGHRVLAVVRGSAVNQDGASngLTAP--SGPAQE 1092
Cdd:PRK06333 214 AARALstrfndAPEQASRPFDRDRDGFVMGEGAGILVIETLEHALARGAPPLAELVGYGTSADAYH--MTAGpeDGEGAR 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 1093 RVIHAALHNARTPAAEIDLLEAHGTGTRLGDPIEAQALLATYGRqrdaERPLWLGSLKSNIGHTQAAAGVSGLIKTVLAL 1172
Cdd:PRK06333 292 RAMLIALRQAGIPPEEVQHLNAHATSTPVGDLGEVAAIKKVFGH----VSGLAVSSTKSATGHLLGAAGGVEAIFTILAL 367
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 1173 RHRTMPATLHVQQPSAQVDwsaGTVRLLTEARTWAApsgrpRRAGVSSFGISGTNAHVIL 1232
Cdd:PRK06333 368 RDQIAPPTLNLENPDPAAE---GLDVVANKARPMDM-----DYALSNGFGFGGVNASILF 419
|
|
| fabD |
TIGR00128 |
malonyl CoA-acyl carrier protein transacylase; This enzyme of fatty acid biosynthesis ... |
327-601 |
2.57e-30 |
|
malonyl CoA-acyl carrier protein transacylase; This enzyme of fatty acid biosynthesis transfers the malonyl moeity from coenzyme A to acyl-carrier protein. The seed alignment for this family of proteins contains a single member each from a number of bacterial species but also an additional pair of closely related, uncharacterized proteins from B. subtilis, one of which has a long C-terminal extension. [Fatty acid and phospholipid metabolism, Biosynthesis]
Pssm-ID: 272922 [Multi-domain] Cd Length: 290 Bit Score: 122.19 E-value: 2.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 327 TRTVFVFPGQGPQWAGMAGELARAEPAFRKKLAECARALrpwlEVDPDELLFG--ARPLDRVELVQPALFSVMVSLAHLW 404
Cdd:TIGR00128 1 MKIAYVFPGQGSQTVGMGKDLYEQYPIAKELFDQASEAL----GYDLKKLCQEgpAEELNKTQYTQPALYVVSAILYLKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 405 R-SHGMTPAAMVGHSFGEIAAVTAAGGLSLTDGARLVAAVSTALARI--EGQGDMVAVALTPDE--TEALLAEEGLDLGI 479
Cdd:TIGR00128 77 KeQGGLKPDFAAGHSLGEYSALVAAGALDFETALKLVKKRGELMQEAvpEGGGAMAAVIGLDEEqlAQACEEATENDVDL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 480 AVVNGPRSTVVSGTRDAATKLLGRLAARGV-RARRLPVGIAGHSPHMDRIRDVLVRGAAAVRPRRSAVPVYGSTTTAPLD 558
Cdd:TIGR00128 157 ANFNSPGQVVISGTKDGVEAAAALFKEMGAkRAVPLEVSGAFHSRFMKPAAEKFAETLEACQFNDPTVPVISNVDAKPYT 236
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2762205949 559 TAALDADHWFRAMRGTARFHDVVAGLLSAGHRLFVEISPHPVL 601
Cdd:TIGR00128 237 NGDRIKEKLSEQLTSPVRWTDSVEKLMARGVTEFAEVGPGKVL 279
|
|
| PLN02836 |
PLN02836 |
3-oxoacyl-[acyl-carrier-protein] synthase |
960-1236 |
4.17e-30 |
|
3-oxoacyl-[acyl-carrier-protein] synthase
Pssm-ID: 215449 [Multi-domain] Cd Length: 437 Bit Score: 125.29 E-value: 4.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 960 SGRLAYFYGLEGPAVTVDTACSSSLVALHLACQSLRAGECDRALVGAATVMAEPGLFVEFSRLRAL------APDGRCKP 1033
Cdd:PLN02836 164 AGHVSIRYGFQGPNHAAVTACATGAHSIGDAFRMIQFGDADVMVAGGTESSIDALSIAGFSRSRALstkfnsCPTEASRP 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 1034 FSAAADGFGMAEGVGVLVVERLSDAERWGHRVLAVVRGSAVNQDGASNGLTAPSGPAQERVIHAALHNARTPAAEIDLLE 1113
Cdd:PLN02836 244 FDCDRDGFVIGEGAGVLVLEELEHAKRRGAKIYAEVRGYGMSGDAHHITQPHEDGRGAVLAMTRALQQSGLHPNQVDYVN 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 1114 AHGTGTRLGDPIEAQALLATYGRQRDAERpLWLGSLKSNIGHTQAAAGVSGLIKTVLALRHRTMPATLHVQQPSAQvdws 1193
Cdd:PLN02836 324 AHATSTPLGDAVEARAIKTVFSEHATSGG-LAFSSTKGATGHLLGAAGAVEAIFSVLAIHHGIAPPTLNLERPDPI---- 398
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2762205949 1194 agtvrLLTEARTWAAPSGRPRRAGVS-SFGISGTNAHVILEEAP 1236
Cdd:PLN02836 399 -----FDDGFVPLTASKAMLIRAALSnSFGFGGTNASLLFTSPP 437
|
|
| PRK08439 |
PRK08439 |
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed |
894-1231 |
1.77e-28 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
Pssm-ID: 236265 [Multi-domain] Cd Length: 406 Bit Score: 119.84 E-value: 1.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 894 MDPQQ--------RLLLETTWEAVEDSGITADTLRGSRTGVF--AGVMHLP-----YGTPLGRTRPDLEGYVMTGTTSSV 958
Cdd:PRK08439 61 MDPKEvkkadrfiQLGLKAAREAMKDAGFLPEELDAERFGVSsaSGIGGLPnieknSIICFEKGPRKISPFFIPSALVNM 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 959 VSGRLAYFYGLEGPAVTVDTACSSSLVALHLACQSLRAGECDRALVGAATVMAEPGLFVEFSRLRALA-----PDGRCKP 1033
Cdd:PRK08439 141 LGGFISIEHGLKGPNLSSVTACAAGTHAIIEAVKTIMLGGADKMLVVGAESAICPVGIGGFAAMKALStrnddPKKASRP 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 1034 FSAAADGFGMAEGVGVLVVERLSDAERWGHRVLAVVRGsaVNQDGASNGLTAPSGPAQERVIHAALHNARTPaaEIDLLE 1113
Cdd:PRK08439 221 FDKDRDGFVMGEGAGALVLEEYESAKKRGAKIYAEIIG--FGESGDANHITSPAPEGPLRAMKAALEMAGNP--KIDYIN 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 1114 AHGTGTRLGDPIEAQALLATYGRQRDAerPLwLGSLKSNIGHTQAAAGVSGLIKTVLALRHRTMPATLH--VQQPSAQVD 1191
Cdd:PRK08439 297 AHGTSTPYNDKNETAALKELFGSKEKV--PP-VSSTKGQIGHCLGAAGAIEAVISIMAMRDGILPPTINqeTPDPECDLD 373
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2762205949 1192 WSAGTVRlltEARTWAAPSgrprragvSSFGISGTNAHVI 1231
Cdd:PRK08439 374 YIPNVAR---KAELNVVMS--------NSFGFGGTNGVVI 402
|
|
| PRK14691 |
PRK14691 |
3-oxoacyl-(acyl carrier protein) synthase II; Provisional |
918-1233 |
1.37e-26 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
Pssm-ID: 173154 [Multi-domain] Cd Length: 342 Bit Score: 112.90 E-value: 1.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 918 TLRGSRTGVFAGVMHlPYGTPLGRTRPDLEGYVMTGTTSSVVSGRLAYFYGLEGPAVTVDTACSSSLVALHLACQSLRAG 997
Cdd:PRK14691 30 TIIGAGIGGFPAIAH-AVRTSDSRGPKRLSPFTVPSFLVNLAAGHVSIKHHFKGPIGAPVTACAAGVQAIGDAVRMIRNN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 998 ECDRALVGAATVMAEPGLFVEFSRLRALA------PDGRCKPFSAAADGFGMAEGVGVLVVERLSDAERWGHRVLAVVRG 1071
Cdd:PRK14691 109 EADVALCGGAEAVIDTVSLAGFAAARALSthfnstPEKASRPFDTARDGFVMGEGAGLLIIEELEHALARGAKPLAEIVG 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 1072 SAVNQDGASNGLTAPSGPAQERVIHAALHNARTPAAEIDLLEAHGTGTRLGDPIEAQALLATYGRQrdaeRPLWLGSLKS 1151
Cdd:PRK14691 189 YGTSADAYHMTSGAEDGDGAYRAMKIALRQAGITPEQVQHLNAHATSTPVGDLGEINAIKHLFGES----NALAITSTKS 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 1152 NIGHTQAAAGVSGLIKTVLALRHRTMPATLHVQQP---SAQVDWSAGTVRllTEARTWAAPSGrprragvssFGISGTNA 1228
Cdd:PRK14691 265 ATGHLLGAAGGLETIFTVLALRDQIVPATLNLENPdpaAKGLNIIAGNAQ--PHDMTYALSNG---------FGFAGVNA 333
|
....*
gi 2762205949 1229 HVILE 1233
Cdd:PRK14691 334 SILLK 338
|
|
| PRK09185 |
PRK09185 |
beta-ketoacyl-ACP synthase; |
963-1236 |
4.67e-26 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236398 [Multi-domain] Cd Length: 392 Bit Score: 112.24 E-value: 4.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 963 LAYFYGLEGPAVTVDTACSSSLVALHLACQSLRAGECDRALVGAATVMAEPGLFvEFSRLRALAPdGRCKPFSAAADGFG 1042
Cdd:PRK09185 143 LRAYLGLSGPAYTISTACSSSAKVFASARRLLEAGLCDAAIVGGVDSLCRLTLN-GFNSLESLSP-QPCRPFSANRDGIN 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 1043 MAEGVGVLVVERLSDAERWghrvlavVRGSAVNQDGASNGLTAPSGPAQERVIHAALHNARTPAAEIDLLEAHGTGTRLG 1122
Cdd:PRK09185 221 IGEAAAFFLLEREDDAAVA-------LLGVGESSDAHHMSAPHPEGLGAILAMQQALADAGLAPADIGYINLHGTATPLN 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 1123 DPIEAQALLATYGRQrdaerpLWLGSLKSNIGHTQAAAGVSGLIKTVLALRHRTMPATLHVQQPSAQVDwsagtVRLLTE 1202
Cdd:PRK09185 294 DAMESRAVAAVFGDG------VPCSSTKGLTGHTLGAAGAVEAAICWLALRHGLPPHGWNTGQPDPALP-----PLYLVE 362
|
250 260 270
....*....|....*....|....*....|....
gi 2762205949 1203 ARTWAApsgrPRRAGVSSFGISGTNAHVILEEAP 1236
Cdd:PRK09185 363 NAQALA----IRYVLSNSFAFGGNNCSLIFGRAD 392
|
|
| PRK05952 |
PRK05952 |
beta-ketoacyl-ACP synthase; |
968-1232 |
7.89e-26 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 111.30 E-value: 7.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 968 GLEGPAVTVDTACSSSLVALHLACQSLRAGECDRALVGAATVMAEPGLFVEFSRLRALAPDGrCKPFSAAADGFGMAEGV 1047
Cdd:PRK05952 134 GTQGPVLAPMAACATGLWAIAQGVELIQTGQCQRVIAGAVEAPITPLTLAGFQQMGALAKTG-AYPFDRQREGLVLGEGG 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 1048 GVLVVERLSDAERWGHRVLAVVRGSAVNQDGASNGLTAPSGPAQERVIHAALHNARTPAAEIDLLEAHGTGTRLGDPIEA 1127
Cdd:PRK05952 213 AILVLESAELAQKRGAKIYGQILGFGLTCDAYHMSAPEPDGKSAIAAIQQCLARSGLTPEDIDYIHAHGTATRLNDQREA 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 1128 QALLATYGRQrdaerpLWLGSLKSNIGHTQAAAGVSGLIKTVLALRHRTMPATLHVQQPSAQVDwsagtvrLLTEARtwa 1207
Cdd:PRK05952 293 NLIQALFPHR------VAVSSTKGATGHTLGASGALGVAFSLLALRHQQLPPCVGLQEPEFDLN-------FVRQAQ--- 356
|
250 260
....*....|....*....|....*
gi 2762205949 1208 apSGRPRRAGVSSFGISGTNAHVIL 1232
Cdd:PRK05952 357 --QSPLQNVLCLSFGFGGQNAAIAL 379
|
|
| PRK07967 |
PRK07967 |
beta-ketoacyl-ACP synthase I; |
907-1232 |
3.21e-25 |
|
beta-ketoacyl-ACP synthase I;
Pssm-ID: 181184 [Multi-domain] Cd Length: 406 Bit Score: 109.76 E-value: 3.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 907 EAVEDSGITADTLRGSRTGVFAGVmhlpyGTPlgRTRPDLEG---------------YVMTGTTSSVVSGRLAYFYGLEG 971
Cdd:PRK07967 81 QAIADAGLSEEQVSNPRTGLIAGS-----GGG--STRNQVEAadamrgprgpkrvgpYAVTKAMASTVSACLATPFKIKG 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 972 PAVTVDTACSSSLVALHLACQSLRAGECDRALVGAATVMaEPGLFVEFSRLRALA------PDGRCKPFSAAADGFGMAE 1045
Cdd:PRK07967 154 VNYSISSACATSAHCIGNAVEQIQLGKQDIVFAGGGEEL-DWEMSCLFDAMGALStkyndtPEKASRAYDANRDGFVIAG 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 1046 GVGVLVVERLSDAERWGHRVLAVVRGSAVNQDGASngLTAPSGPAQERVIHAALHNARTPaaeIDLLEAHGTGTRLGDPI 1125
Cdd:PRK07967 233 GGGVVVVEELEHALARGAKIYAEIVGYGATSDGYD--MVAPSGEGAVRCMQMALATVDTP---IDYINTHGTSTPVGDVK 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 1126 EAQALLATYGRQRDAerplwLGSLKSNIGHTQAAAGVSGLIKTVLALRHRTMPATLHVQqpsaQVDWSAGTVRLLTEart 1205
Cdd:PRK07967 308 ELGAIREVFGDKSPA-----ISATKSLTGHSLGAAGVQEAIYSLLMMEHGFIAPSANIE----ELDPQAAGMPIVTE--- 375
|
330 340 350
....*....|....*....|....*....|..
gi 2762205949 1206 waapsgRPRRAGV-----SSFGISGTNAHVIL 1232
Cdd:PRK07967 376 ------TTDNAELttvmsNSFGFGGTNATLVF 401
|
|
| PRK08722 |
PRK08722 |
beta-ketoacyl-ACP synthase II; |
865-1234 |
4.22e-24 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 181539 [Multi-domain] Cd Length: 414 Bit Score: 106.63 E-value: 4.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 865 FYQREAALLDDvagFDAAFFgISQREALAMDPQQRLLLETTWEAVEDSGITADTLRGSRTGVFAG-------VMHLPYGT 937
Cdd:PRK08722 46 FSTRFAGLVKD---FNCEEY-MSKKDARKMDLFIQYGIAAGIQALDDSGLEVTEENAHRIGVAIGsgigglgLIEAGHQA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 938 PLGRTRPDLEGYVMTGTTSSVVSGRLAYFYGLEGPAVTVDTACSSSLVALHLACQSLRAGECDRALVGAATVMAEPGLFV 1017
Cdd:PRK08722 122 LVEKGPRKVSPFFVPSTIVNMIAGNLSIMRGLRGPNIAISTACTTGLHNIGHAARMIAYGDADAMVAGGAEKASTPLGMA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 1018 EFSRLRALA-----PDGRCKPFSAAADGFGMAEGVGVLVVERLSDAERWGHRVLAVVRGSAVNQDGASNGLTAPSGPAQE 1092
Cdd:PRK08722 202 GFGAAKALStrndePQKASRPWDKDRDGFVLGDGAGMMVLEEYEHAKARGAKIYAELVGFGMSGDAYHMTSPSEDGSGGA 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 1093 RVIHAALHNARTPAAEIDLLEAHGTGTRLGDPIEAQALLATYGRQrdAERPLWLGSLKSNIGHTQAAAGVSGLIKTVLAL 1172
Cdd:PRK08722 282 LAMEAAMRDAGVTGEQIGYVNAHGTSTPAGDVAEIKGIKRALGEA--GSKQVLVSSTKSMTGHLLGAAGSVEAIITVMSL 359
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2762205949 1173 RHRTMPATLHVQQPSA--QVDWSAGTVRLLtEARTWAApsgrprragVSSFGISGTNAHVILEE 1234
Cdd:PRK08722 360 VDQIVPPTINLDDPEEglDIDLVPHTARKV-ESMEYAI---------CNSFGFGGTNGSLIFKK 413
|
|
| PRK09116 |
PRK09116 |
beta-ketoacyl-ACP synthase; |
810-1161 |
3.03e-22 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 181657 [Multi-domain] Cd Length: 405 Bit Score: 100.83 E-value: 3.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 810 VAIVGMacrlpGGVRSADDLWELVRE----GRDAVTRFPSdrgWD-LAELYSadparpgtfyqREAALLDDvagfdaafF 884
Cdd:PRK09116 4 VVVTGM-----GGVTALGEDWQTIAArlkaGRNAVRRMPE---WDrYDGLNT-----------RLAAPIDD--------F 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 885 GI----SQREALAMDPQQRLLLETTWEAVEDSGITAD-TLRGSRTGVfagvmhlPYGTPLGRTRPDLEGYVM--TGTTSS 957
Cdd:PRK09116 57 ELpahyTRKKIRSMGRVSLMATRASELALEDAGLLGDpILTDGRMGI-------AYGSSTGSTDPIGAFGTMllEGSMSG 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 958 VVSG------------RLAYFYGLEGPAVTVDTACSSSLVALHLACQSLRAGECDRALVGAATVMAEPGLFVeFSRLRAL 1025
Cdd:PRK09116 130 ITATtyvrmmphttavNVGLFFGLKGRVIPTSSACTSGSQGIGYAYEAIKYGYQTVMLAGGAEELCPTEAAV-FDTLFAT 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 1026 -----APDGRCKPFSAAADGFGMAEGVGVLVVERLSDAERWGHRVLAVVRGSAVNQDGASngLTAPSGPAQERVIHAALH 1100
Cdd:PRK09116 209 strndAPELTPRPFDANRDGLVIGEGAGTLVLEELEHAKARGATIYAEIVGFGTNSDGAH--VTQPQAETMQIAMELALK 286
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2762205949 1101 NARTPAAEIDLLEAHGTGTRLGDPIEAQALLATYGrqrdAERPlwLGSLKSNIGHTQAAAG 1161
Cdd:PRK09116 287 DAGLAPEDIGYVNAHGTATDRGDIAESQATAAVFG----ARMP--ISSLKSYFGHTLGACG 341
|
|
| PLN02787 |
PLN02787 |
3-oxoacyl-[acyl-carrier-protein] synthase II |
862-1191 |
1.12e-20 |
|
3-oxoacyl-[acyl-carrier-protein] synthase II
Pssm-ID: 215421 [Multi-domain] Cd Length: 540 Bit Score: 97.74 E-value: 1.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 862 PGTFYQReaaLLDDVAG------FDAAFFG---------------ISQREALAMDPQQRLLLETTWEAVEDSGITADT-- 918
Cdd:PLN02787 146 PDVFYNN---LLEGVSGiseierFDCSQFPtriageiksfstdgwVAPKLSKRMDKFMLYLLTAGKKALADGGITEDVmk 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 919 -LRGSRTGVFAGV----MHLPYGT--PLGRTRPDLEGYVMTGTTSSVVSGRLAYFYGLEGPAVTVDTACSSSLVALHLAC 991
Cdd:PLN02787 223 eLDKTKCGVLIGSamggMKVFNDAieALRISYRKMNPFCVPFATTNMGSAMLAMDLGWMGPNYSISTACATSNFCILNAA 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 992 QSLRAGECDRALVGAATVMAEPGLFVEFSRLRALA-----PDGRCKPFSAAADGFGMAEGVGVLVVERLSDAERWGHRVL 1066
Cdd:PLN02787 303 NHIIRGEADVMLCGGSDAAIIPIGLGGFVACRALSqrnddPTKASRPWDMNRDGFVMGEGAGVLLLEELEHAKKRGANIY 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 1067 AVVRGSAVNQDGASNGLTAPSGPAQERVIHAALHNARTPAAEIDLLEAHGTGTRLGDPIEAQALLATYGRQRDaerpLWL 1146
Cdd:PLN02787 383 AEFLGGSFTCDAYHMTEPHPEGAGVILCIEKALAQSGVSKEDVNYINAHATSTKAGDLKEYQALMRCFGQNPE----LRV 458
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 2762205949 1147 GSLKSNIGHTQAAAGVSGLIKTVLALRHRTMPATLHVQQPSAQVD 1191
Cdd:PLN02787 459 NSTKSMIGHLLGAAGAVEAIATVQAIRTGWVHPNINLENPESGVD 503
|
|
| PRK07910 |
PRK07910 |
beta-ketoacyl-ACP synthase; |
968-1227 |
1.92e-20 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236129 [Multi-domain] Cd Length: 418 Bit Score: 95.57 E-value: 1.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 968 GLEGPA----VTVDTACSSSLVALHLACQSLRAGECDRALVGAATVMAEPGLFVEFSRLRALA------PDGRCKPFSAA 1037
Cdd:PRK07910 155 GLERHAkagvITPVSACASGSEAIAQAWRQIVLGEADIAICGGVETRIEAVPIAGFAQMRIVMstnnddPAGACRPFDKD 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 1038 ADGFGMAEGVGVLVVERLSDAERWGHRVLAVVRGSAVNQDGASNGLTAPSGPAQERVIHAALHNARTPAAEIDLLEAHGT 1117
Cdd:PRK07910 235 RDGFVFGEGGALMVIETEEHAKARGANILARIMGASITSDGFHMVAPDPNGERAGHAMTRAIELAGLTPGDIDHVNAHAT 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 1118 GTRLGDPIEAQALLATYGRQRDAerplwLGSLKSNIGHTQAAAGVSGLIKTVLALRHRTMPATLHVQQPSAQVDWS--AG 1195
Cdd:PRK07910 315 GTSVGDVAEGKAINNALGGHRPA-----VYAPKSALGHSVGAVGAVESILTVLALRDGVIPPTLNLENLDPEIDLDvvAG 389
|
250 260 270
....*....|....*....|....*....|..
gi 2762205949 1196 TVRllteartwaapSGRPRRAGVSSFGISGTN 1227
Cdd:PRK07910 390 EPR-----------PGNYRYAINNSFGFGGHN 410
|
|
| omega_3_PfaA |
TIGR02813 |
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ... |
327-619 |
9.78e-20 |
|
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this alignment are involved in omega-3 polyunsaturated fatty acid biosynthesis, such as the protein PfaA from the eicosapentaenoic acid biosynthesis operon in Photobacterium profundum strain SS9. PfaA is encoded together with PfaB, PfaC, and PfaD, and the functions of the individual polypeptides have not yet been described. More distant homologs of PfaA, also included with the reach of this model, appear to be involved in polyketide-like biosynthetic mechanisms of polyunsaturated fatty acid biosynthesis, an alternative to the more familiar iterated mechanism of chain extension and desaturation, and in most cases are encoded near genes for homologs of PfaB, PfaC, and/or PfaD.
Pssm-ID: 274311 [Multi-domain] Cd Length: 2582 Bit Score: 96.61 E-value: 9.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 327 TRTVFVFPGQGPQWAGMAGELARAEPAFRKKLAEC------------ARALRPWLEVDPDELLFGARPLDRVELVQPALF 394
Cdd:TIGR02813 579 GKVAALFAGQGSQYLNMGRELACNFPEVRQAAADMdsvftqagkgalSPVLYPIPVFNDESRKAQEEALTNTQHAQSAIG 658
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 395 SVMVSLAHLWRSHGMTPAAMVGHSFGEIAAVTAAGGLSLTDGARLVAAVSTALARIEGQGD---MVAVALTPD---ETEA 468
Cdd:TIGR02813 659 TLSMGQYKLFTQAGFKADMTAGHSFGELSALCAAGVISDDDYMMLAFSRGQAMAAPTGEADigfMYAVILAVVgspTVIA 738
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 469 LLAEEGLDLGIAVVNGPRSTVVSGTRDAATKLLGRLAARGVRARRLPVGIAGHSP---HMDRIRDVLVRGAAAVRPrrsA 545
Cdd:TIGR02813 739 NCIKDFEGVSIANYNSPTQLVIAGVSTQIQIAAKALKEKGFKAIPLPVSGAFHTPlvaHAQKPFSAAIDKAKFNTP---L 815
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2762205949 546 VPVYGSTTTA--PLDTAALDA---DHwfraMRGTARFHDVVAGLLSAGHRLFVEISPHPVLAMSIEDTAAHLERDVVVL 619
Cdd:TIGR02813 816 VPLYSNGTGKlhSNDAAAIKKalkNH----MLQSVHFSEQLEAMYAAGARVFVEFGPKNILQKLVENTLKDKENELCAI 890
|
|
| KAsynt_C_assoc |
pfam16197 |
Ketoacyl-synthetase C-terminal extension; KAsynt_C_assoc represents the very C-terminus of a ... |
1186-1303 |
2.88e-18 |
|
Ketoacyl-synthetase C-terminal extension; KAsynt_C_assoc represents the very C-terminus of a subset of proteins from the keto-acyl-synthetase 2 family. It is found in proteins ranging from bacteria to human.
Pssm-ID: 465059 [Multi-domain] Cd Length: 111 Bit Score: 81.44 E-value: 2.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 1186 PSAQVD-WSAGTVRLLTEARTWaapsgRPRRAGVSSFGISGTNAHVILEEAPRgvrgtesAEPPAWAHVAVP--LVLSAK 1262
Cdd:pfam16197 1 PNPDIPaLLDGRLKVVTEPTPW-----PGGIVGVNSFGFGGANAHVILKSNPK-------PKIPPESPDNLPrlVLLSGR 68
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2762205949 1263 SPQALREQASALSRHLRDHPEEPLHHTAHTLacHRTHHPYR 1303
Cdd:pfam16197 69 TEEAVKALLEKLENHLDDAEFLSLLNDIHSL--PISGHPYR 107
|
|
| PKS_PP |
smart00823 |
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ... |
688-771 |
1.21e-17 |
|
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.
Pssm-ID: 214834 [Multi-domain] Cd Length: 86 Bit Score: 78.83 E-value: 1.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 688 LTGHRPDERADQAVQLV----ADALGpeGREAAAADPDRDFRSLGLDSAGAVRVRRRLVELTGLRLPVTALFDHPTPRAL 763
Cdd:smart00823 1 LAALPPAERRRLLLDLVreqvAAVLG--HAAAEAIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAAL 78
|
....*...
gi 2762205949 764 AREIVRRL 771
Cdd:smart00823 79 AEHLAAEL 86
|
|
| CLF |
cd00832 |
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ... |
809-1232 |
1.44e-15 |
|
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic antibiotic-producing polyketide synthases (PKSs) of filamentous bacteria. CLFs have been shown to have decarboxylase activity towards malonyl-acyl carrier protein (ACP). CLFs are similar to other elongation ketosynthase domains, but their active site cysteine is replaced by a conserved glutamine.
Pssm-ID: 238428 [Multi-domain] Cd Length: 399 Bit Score: 80.48 E-value: 1.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 809 PVAIVGMACRLPGGVrSADDLWELVREGR---DAVTRFpsdrgwdlaelysaDPARpgtfyqREAALLDDVAGFDAAFfG 885
Cdd:cd00832 2 RAVVTGIGVVAPNGL-GVEEYWKAVLDGRsglGPITRF--------------DPSG------YPARLAGEVPDFDAAE-H 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 886 ISQREALAMDPQQRLLLETTWEAVEDSGITADTLRGSRTGVFAGVM-------HLPYGTPLGRTRPDLEGYVMTGTTSSV 958
Cdd:cd00832 60 LPGRLLPQTDRMTRLALAAADWALADAGVDPAALPPYDMGVVTASAaggfefgQRELQKLWSKGPRHVSAYQSFAWFYAV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 959 VSGRLAYFYGLEGPAVTVDTACSSSLVALHLACQSLRAGECDRALVGAATVMAEPGLFVEFS--RLRALA-PDGRCKPFS 1035
Cdd:cd00832 140 NTGQISIRHGMRGPSGVVVAEQAGGLDALAQARRLVRRGTPLVVSGGVDSALCPWGWVAQLSsgRLSTSDdPARAYLPFD 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 1036 AAADGFGMAEGVGVLVVERLSDAERWGHRVLAVVRGSAVNQDGASNgltAPSGPAQERVIHAALHNARTPAAEIDLLEAH 1115
Cdd:cd00832 220 AAAAGYVPGEGGAILVLEDAAAARERGARVYGEIAGYAATFDPPPG---SGRPPGLARAIRLALADAGLTPEDVDVVFAD 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 1116 GTGTRLGDPIEAQALLATYGRQRdaerpLWLGSLKSNIGHTQAAAGVSGLIKTVLALRHRTMPATLHVQQ--PSAQVDWS 1193
Cdd:cd00832 297 AAGVPELDRAEAAALAAVFGPRG-----VPVTAPKTMTGRLYAGGAPLDVATALLALRDGVIPPTVNVTDvpPAYGLDLV 371
|
410 420 430
....*....|....*....|....*....|....*....
gi 2762205949 1194 AGTVRLLteartwaapsgRPRRAGVSSFGISGTNAHVIL 1232
Cdd:cd00832 372 TGRPRPA-----------ALRTALVLARGRGGFNSALVV 399
|
|
| PLN02752 |
PLN02752 |
[acyl-carrier protein] S-malonyltransferase |
325-602 |
4.04e-15 |
|
[acyl-carrier protein] S-malonyltransferase
Pssm-ID: 215401 [Multi-domain] Cd Length: 343 Bit Score: 78.27 E-value: 4.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 325 PDTRTVFVFPGQGPQWAGMAGELARAEPAfrKKLAECARALRPW--LEV---DPDEllfgarPLDRVELVQPALFsvMVS 399
Cdd:PLN02752 36 YKPTTAFLFPGQGAQAVGMGKEAAEVPAA--KALFDKASEILGYdlLDVcvnGPKE------KLDSTVVSQPAIY--VAS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 400 LA--HLWRSHGMTPAAM------VGHSFGEIAAVTAAGGLSLTDGARLVAAVSTAL--ARIEGQGDMVAV-ALTPDETEA 468
Cdd:PLN02752 106 LAavEKLRARDGGQAVIdsvdvcAGLSLGEYTALVFAGALSFEDGLKLVKLRGEAMqaAADAGPSGMVSViGLDSDKVQE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 469 LLAE------EGLDLGIAVVNGPRSTVVSGTRDAATKLLGRLAARGVR-ARRLPVGIAGHSPHMDRIRDVLVRGAAAVRP 541
Cdd:PLN02752 186 LCAAaneevgEDDVVQIANYLCPGNYAVSGGKKGIDAVEAKAKSFKARmTVRLAVAGAFHTSFMEPAVDALEAALAAVEI 265
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2762205949 542 RRSAVPVYGSTTTAPLDTAALDADHWFRAMRGTARFHDVVAGLLSAGHRLFVEISPHPVLA 602
Cdd:PLN02752 266 RTPRIPVISNVDAQPHSDPATIKKILARQVTSPVQWETTVKTLLEKGLEKSYELGPGKVIA 326
|
|
| PP-binding |
pfam00550 |
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
701-762 |
8.48e-11 |
|
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.
Pssm-ID: 425746 [Multi-domain] Cd Length: 62 Bit Score: 58.73 E-value: 8.48e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2762205949 701 VQLVADALGpegREAAAADPDRDFRSLGLDSAGAVRVRRRLVELTGLRLPVTALFDHPTPRA 762
Cdd:pfam00550 4 RELLAEVLG---VPAEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLAE 62
|
|
| AcpP |
COG0236 |
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ... |
692-771 |
9.85e-11 |
|
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440006 [Multi-domain] Cd Length: 80 Bit Score: 59.10 E-value: 9.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 692 RPDERADQAVQLVADALGpegREAAAADPDRDFRS-LGLDSAGAVRVRRRLVELTGLRLPVTALFDHPTPRALAREIVRR 770
Cdd:COG0236 2 PREELEERLAEIIAEVLG---VDPEEITPDDSFFEdLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEEK 78
|
.
gi 2762205949 771 L 771
Cdd:COG0236 79 L 79
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
199-709 |
3.85e-09 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 61.43 E-value: 3.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 199 QMAPGQQAVPGSEGVPEPHGAQGPQAEDAGAGQAAGRDRPLPRVVPLLVSGRSRAGLRAYAEALAGHLVAHPDISLTDTA 278
Cdd:COG3321 874 AAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAAAALLALAAAAAAAA 953
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 279 FTLAGARPLWPYRSLVPAGDRDTAVAALRALAAGAPGDDVVQAEPGPDTRTVFVFPGQGPQWAGMAGELARAEPAFRKKL 358
Cdd:COG3321 954 AALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAALLALAALLAAAAA 1033
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 359 AECARALRPWLEVDPDELLFGARPLDRVELVQPALFSVMVSLAHLWRSHGMTPAAMVGHSFGEIAAVTAAGGLSLTDGAR 438
Cdd:COG3321 1034 ALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALALAALAAALLLLALLA 1113
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 439 LVAAVSTALARIEGQGDMVAVALTPDETEALLAEEGLDLGIAVVNGPRSTVVSGTRDAATKLLGRLAARGVRARRLPVGI 518
Cdd:COG3321 1114 ALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALALALAAALAAALAGLA 1193
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 519 AG-HSPHMDRIRDVLVRGAAAVRPRRSAVPVYGSTTTAPLDTAALDADHWFRAMRGTARFHDVVAGLLSAGHRLFVEISP 597
Cdd:COG3321 1194 ALlLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALLAALAALALLAAAAGLAA 1273
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 598 HPVLAMSIEDTAAHLERDVVVLDTMRRDDAGAGRYVRALAEAQLHGADPPDWSAVLPSAARVTLPPYRFERDTREGDGAE 677
Cdd:COG3321 1274 LAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAALAAAVAAALALAAAAAAAAAA 1353
|
490 500 510
....*....|....*....|....*....|..
gi 2762205949 678 GDGADALRARLTGHRPDERADQAVQLVADALG 709
Cdd:COG3321 1354 AAAAAAAAALAAAAGAAAAAAALALAALAAAV 1385
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
97-639 |
7.37e-09 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 60.66 E-value: 7.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 97 AAGVVLARAGHHDGHYG---PLPRGPRERTARLSSLSPRFRRGTGTDGKATAGGARRTNSGRQAVPGQQPVTSQPQVTPG 173
Cdd:COG3321 842 VAGVPVDWSALYPGRGRrrvPLPTYPFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALAL 921
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 174 QPVPTQPPGTPGPPVPTQPPGTPGQQMAPGQQAVPgsegVPEPHGAQGPQAEDAGAGQAAGRDRPLPRVVPLLVSGRSRA 253
Cdd:COG3321 922 AAAALAALLALVALAAAAAALLALAAAAAAAAAAL----AAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALA 997
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 254 GLRAYAEALAGHLVAHPDISLTDTAFTLAGARPLWPYRSLVPAGDRDTAVAALRALAAGAPGDDVVQAEPGPDTRTVFVF 333
Cdd:COG3321 998 AAAALALLAAAALLLAAAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAEL 1077
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 334 PGQGPQWAGMAGELARAEPAFRKKLAECARALRPWLEVDPDELLFGARPLDRVELVQPALFSVMVSLAHLWRSHGMTPAA 413
Cdd:COG3321 1078 ALAAAALALAAALAAAALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAA 1157
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 414 MVGHSFGEIAAVTAAGGLSLTDGARLVAAVSTALARIEGQGDMVAVALTPDETEALLAEEGLDLGIAVVNGPRSTVVSGT 493
Cdd:COG3321 1158 ALAAALAAALLAAAALLLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLA 1237
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 494 RDAATKLLGRLAARGVRARRLPVGIAGHSPHMDRIRDVLVRGAAAVRPRRSAVPVYGSTTTAPLDTAALDADHWFRAMRG 573
Cdd:COG3321 1238 LAAAAAAVAALAAAAAALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAA 1317
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2762205949 574 TARFHDVVAGLLSAGHRLFVEISPHPVLAMSIEDTAAHLERDVVVLDTMRRDDAGAGRYVRALAEA 639
Cdd:COG3321 1318 AAALAAALLAAALAALAAAVAAALALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALALAALAA 1383
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
221-783 |
8.37e-09 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 60.27 E-value: 8.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 221 GPQAEDAGAGQAAGRDRPLPRVVPLLvsGRSRAGLRAYAEALAGHLVA---------HPD-----ISLTDTAFTLAGARP 286
Cdd:COG3321 798 GPGPVLTGLVRQCLAAAGDAVVLPSL--RRGEDELAQLLTALAQLWVAgvpvdwsalYPGrgrrrVPLPTYPFQREDAAA 875
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 287 LWPYRSLVPAGDRDTAVAALRALAAGAPGDDVVQAEPGPDTRTVFVFPGQGPQWAGMAGELARAEPAFRKKLAECARALR 366
Cdd:COG3321 876 ALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAAAALLALAAAAAAAAAA 955
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 367 PWLEVDPDELLFGARPLDRVELVQPALFSVMVSLAHLWRSHGMTPAAMVGHSFGEIAAVTAAGGLSLTDGARLVAAVSTA 446
Cdd:COG3321 956 LAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAALLALAALLAAAAAAL 1035
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 447 LARIEGQGDMVAVALTPDETEALLAEEGLDLGIAVVNGPRSTVVSGTRDAATKLLGRLAARGVRARRLP-----VGIAGH 521
Cdd:COG3321 1036 AAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALALAALAAallllALLAAL 1115
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 522 SPHMDRIRDVLVRGAAAVRPRRSAVPVYGSTTTAPLDTAALDADHWFRAMRGTARFHDVVAGLLSAGHRLFVEISPHPVL 601
Cdd:COG3321 1116 ALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALALALAAALAAALAGLAAL 1195
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 602 AMSIEDTAAHLERDVVVLDTMRRDDAGAGRYVRALAEAQLHGADPPDWSAVLPSAARVTLPPYRFERDTREGDGAEGDGA 681
Cdd:COG3321 1196 LLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALLAALAALALLAAAAGLAALA 1275
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 682 DALRARLTGHRPDERADQAVQLVADALGPEGREAAAADPDRDFRSLGLDSAGAVRVRRRLVELTGLRLPVTALFDHPTPR 761
Cdd:COG3321 1276 AAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAALAAAVAAALALAAAAAAAAAAAA 1355
|
570 580
....*....|....*....|..
gi 2762205949 762 ALAREIVRRLFGAAPEPRTAAL 783
Cdd:COG3321 1356 AAAAAAALAAAAGAAAAAAALA 1377
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
900-1019 |
5.14e-06 |
|
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; SCP-2 has multiple roles in intracellular lipid circulation and metabolism. The N-terminal presequence in the SCP-x isoform represents a peroxisomal 3-ketacyl-Coa thiolase specific for branched-chain acyl CoAs, which is proteolytically cleaved from the sterol carrier protein.
Pssm-ID: 238425 [Multi-domain] Cd Length: 375 Bit Score: 50.34 E-value: 5.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 900 LLLETTWEAVEDSGITADTLRGSRTGVFAGvmhlpygtplgrtrpdlegyvmtGTTSSVVSGRLAYFYGLEG-PAVTVDT 978
Cdd:cd00829 19 LAAEAARAALDDAGLEPADIDAVVVGNAAG-----------------------GRFQSFPGALIAEYLGLLGkPATRVEA 75
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2762205949 979 ACSSSLVALHLACQSLRAGECDRALVGAATVMAEPGLFVEF 1019
Cdd:cd00829 76 AGASGSAAVRAAAAAIASGLADVVLVVGAEKMSDVPTGDEA 116
|
|
| Thiolase_N |
pfam00108 |
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl ... |
972-1010 |
1.01e-04 |
|
Thiolase, N-terminal domain; Thiolase is reported to be structurally related to beta-ketoacyl synthase (pfam00109), and also chalcone synthase.
Pssm-ID: 459676 [Multi-domain] Cd Length: 260 Bit Score: 45.76 E-value: 1.01e-04
10 20 30
....*....|....*....|....*....|....*....
gi 2762205949 972 PAVTVDTACSSSLVALHLACQSLRAGECDRALVGAATVM 1010
Cdd:pfam00108 77 PAVTINKVCGSGLKAVYLAAQSIASGDADVVLAGGVESM 115
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
972-1010 |
3.51e-04 |
|
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of 3-ketoacyl-CoA into acyl-CoA and acetyl-CoA, a 2-step reaction involving a covalent intermediate formed with a catalytic cysteine. They are found in prokaryotes and eukaryotes (cytosol, microbodies and mitochondria). There are 2 functional different classes: thiolase-I (3-ketoacyl-CoA thiolase) and thiolase-II (acetoacetyl-CoA thiolase). Thiolase-I can cleave longer fatty acid molecules and plays an important role in the beta-oxidative degradation of fatty acids. Thiolase-II has a high substrate specificity. Although it can cleave acetoacyl-CoA, its main function is the synthesis of acetoacyl-CoA from two molecules of acetyl-CoA, which gives it importance in several biosynthetic pathways.
Pssm-ID: 238383 [Multi-domain] Cd Length: 386 Bit Score: 44.39 E-value: 3.51e-04
10 20 30
....*....|....*....|....*....|....*....
gi 2762205949 972 PAVTVDTACSSSLVALHLACQSLRAGECDRALVGAATVM 1010
Cdd:cd00751 76 PATTVNRVCGSGLQAVALAAQSIAAGEADVVVAGGVESM 114
|
|
| AcpA |
COG3433 |
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ... |
505-771 |
8.22e-04 |
|
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442659 [Multi-domain] Cd Length: 295 Bit Score: 43.20 E-value: 8.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 505 AARGVRARRLPVGIAGHSPHMDRIRDVLVRGAAAVRPRRSAVPVYGSTTTAPLDTAALDADHWFRAMRGTARFHDVVAGL 584
Cdd:COG3433 26 QARALLLIVDLQGYFGGFGGEGGLLGAGLLLRIRLLAAAARAPFIPVPYPAQPGRQADDLRLLLRRGLGPGGGLERLVQQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 585 LSAGHRLFVEISPHPVLAMSIEDTAAHLERDVVVLDTMRRDDAGAGRYVRALAEAQLHG-----ADPPDWSAVLPSAARV 659
Cdd:COG3433 106 VVIRAERGEEEELLLVLRAAAVVRVAVLAALRGAGVGLLLIVGAVAALDGLAAAAALAAldkvpPDVVAASAVVALDALL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 660 TLPPYRFERDTREGDGAEGDGADALRArlTGHRPDERADQAVQLVADALGpegREAAAADPDRDFRSLGLDSAGAVRVRR 739
Cdd:COG3433 186 LLALKVVARAAPALAAAEALLAAASPA--PALETALTEEELRADVAELLG---VDPEEIDPDDNLFDLGLDSIRLMQLVE 260
|
250 260 270
....*....|....*....|....*....|..
gi 2762205949 740 RLvELTGLRLPVTALFDHPTPRALAREIVRRL 771
Cdd:COG3433 261 RW-RKAGLDVSFADLAEHPTLAAWWALLAAAQ 291
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
972-1010 |
9.96e-04 |
|
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 439953 [Multi-domain] Cd Length: 391 Bit Score: 43.13 E-value: 9.96e-04
10 20 30
....*....|....*....|....*....|....*....
gi 2762205949 972 PAVTVDTACSSSLVALHLACQSLRAGECDRALVGAATVM 1010
Cdd:COG0183 80 PAVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESM 118
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
614-903 |
2.04e-03 |
|
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: 42.54 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 614 RDVVVLdtMRRDDAGAGR---YVRALAEAQLHGADPPDWSAVLPSAARVTLPPYRFERDTREGDGAEGDGADALRARLTG 690
Cdd:COG1020 899 REAVVV--AREDAPGDKRlvaYVVPEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAAAAA 976
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 691 HRPDERADQAVQLVADALGPEGREAAAADPDRDFRSLGLDSAGAVRVRRRLVELTGLRLPVTALFDHPTPRALAREIVRR 770
Cdd:COG1020 977 AAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLLFLAAAAAAAAAAAAAAA 1056
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 771 LFGAAPEPRTAALTTTSPPGPRAEGATSGDSAAGVPHEPVAIVGMACRLPGGVRSAD--DLWELVREGRDAVTRFPSDRG 848
Cdd:COG1020 1057 AAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLllALLLALLAALRARRAVRQEGP 1136
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2762205949 849 WDLAELYSADPARPGTFYQREAALLDDVAGFDAAFFGISQREALAMDPQQRLLLE 903
Cdd:COG1020 1137 RLRLLVALAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLL 1191
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
702-780 |
3.67e-03 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 41.56 E-value: 3.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2762205949 702 QLVADAL-GPEGREAAAADP---DRD--FRSLGLDSAGAVRVRRRLVELTGLRLPVTALFDHPTPRALAREIVRRLFGAA 775
Cdd:PRK06060 544 RLVVDAVcAEAAKMLGEPDPwsvDQDlaFSELGFDSQMTVTLCKRLAAVTGLRLPETVGWDYGSISGLAQYLEAELAGGH 623
|
....*
gi 2762205949 776 PEPRT 780
Cdd:PRK06060 624 GRLKS 628
|
|
| |
