|
Name |
Accession |
Description |
Interval |
E-value |
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
125-544 |
4.97e-98 |
|
"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: 305.90 E-value: 4.97e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 125 PEPLPANWSIAPAEDGEVLVSIHERCEFkvdsyralTVKSAGQLPTG-FEPGELYNSRFHPRGLQMSVVAATDAIRSTGI 203
Cdd:cd00828 18 CDEVEEFWEALREGRSGIAPVARLKSRF--------DRGVAGQIPTGdIPGWDAKRTGIVDRTTLLALVATEEALADAGI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 204 DWKTIVDnvqPDEIAVFSGSIMSQLDDNGFGGLMQSRLKGHRVSAKQLPLgfNSMPTDFINAYVLGSVGMTGSITGACAT 283
Cdd:cd00828 90 TDPYEVH---PSEVGVVVGSGMGGLRFLRRGGKLDARAVNPYVSPKWMLS--PNTVAGWVNILLLSSHGPIKTPVGACAT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 284 FLYNLQKGIDVITSGQARVVIVGNSEAPiLPECIEGYSAMGALATEEGLRliegrddvdfRRASRPFGE-NCGFTLAESS 362
Cdd:cd00828 165 ALEALDLAVEAIRSGKADIVVVGGVEDP-LEEGLSGFANMGALSTAEEEP----------EEMSRPFDEtRDGFVEAEGA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 363 QYVVLMDDELALRLGADIHGAVTDVFINADGFKKSISAPGPGNYLTVAKAVASAVQIvgldtVRHASFVHAHGSSTPANR 442
Cdd:cd00828 234 GVLVLERAELALARGAPIYGRVAGTASTTDGAGRSVPAGGKGIARAIRTALAKAGLS-----LDDLDVISAHGTSTPAND 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 443 VTESEILDRVASAFGIDgWPVTAVKAYVGHSLATASADQLISALGTFKYGILPGIKTIDKVADDVHQQRLSISNRDMRQD 522
Cdd:cd00828 309 VAESRAIAEVAGALGAP-LPVTAQKALFGHSKGAAGALQLIGALQSLEHGLIPPTANLDDVDPDVEHLSVVGLSRDLNLK 387
|
410 420
....*....|....*....|..
gi 15600367 523 KplEVCFINSKGFGGNNASGVV 544
Cdd:cd00828 388 V--RAALVNAFGFGGSNAALVL 407
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
151-546 |
2.65e-41 |
|
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: 154.87 E-value: 2.65e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 151 EFKVDSYRaltVKSAGQLPtGFEPGELYN---SRFHPRGLQMSVVAATDAIRSTGIDwktiVDNVQPDEIAVFSGSIMSQ 227
Cdd:COG0304 37 RFDASGLP---VRIAGEVK-DFDPEEYLDrkeLRRMDRFTQYALAAAREALADAGLD----LDEVDPDRTGVIIGSGIGG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 228 LD--DNGFGGLMQSRLKghRVSAKQLPLGFNSMPTDFInAYVLGSVGMTGSITGACATFLYNLQKGIDVITSGQARVVIV 305
Cdd:COG0304 109 LDtlEEAYRALLEKGPR--RVSPFFVPMMMPNMAAGHV-SIRFGLKGPNYTVSTACASGAHAIGEAYRLIRRGRADVMIA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 306 GNSEAPILPECIEGYSAMGALATeeglrliegRDDvDFRRASRPFGEN-CGFTLAESSQYVVLMDDELALRLGADIHGAV 384
Cdd:COG0304 186 GGAEAAITPLGLAGFDALGALST---------RND-DPEKASRPFDKDrDGFVLGEGAGVLVLEELEHAKARGAKIYAEV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 385 TDVFINADGFkkSISAPGPgNYLTVAKAVASAVQIVGLDtvrhAS---FVHAHGSSTPANRVTESEILDRVasaFGIDGW 461
Cdd:COG0304 256 VGYGASSDAY--HITAPAP-DGEGAARAMRAALKDAGLS----PEdidYINAHGTSTPLGDAAETKAIKRV---FGDHAY 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 462 --PVTAVKAYVGHSLATASADQLISALGTFKYGILP---GIKTIDKVAD-DVhqqrlsISNRdmRQDKPLEVCFINSKGF 535
Cdd:COG0304 326 kvPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPptiNLENPDPECDlDY------VPNE--AREAKIDYALSNSFGF 397
|
410
....*....|.
gi 15600367 536 GGNNASgVVLS 546
Cdd:COG0304 398 GGHNAS-LVFK 407
|
|
| PTZ00050 |
PTZ00050 |
3-oxoacyl-acyl carrier protein synthase; Provisional |
172-541 |
3.58e-30 |
|
3-oxoacyl-acyl carrier protein synthase; Provisional
Pssm-ID: 240245 [Multi-domain] Cd Length: 421 Bit Score: 123.26 E-value: 3.58e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 172 FEPGELYNSRFHPRGLQMSVVAATDAIRSTGIDWKTIVDnvqPDEIAVFSGSIMSQLDDNGFGGLMQSRLKGHRVSAKQL 251
Cdd:PTZ00050 63 FDPSDFAPTKRESRATHFAMAAAREALADAKLDILSEKD---QERIGVNIGSGIGSLADLTDEMKTLYEKGHSRVSPYFI 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 252 PLGFNSMPTDFInAYVLGSVGMTGSITGACATFLYNLQKGIDVITSGQARVVIVGNSEAPILPECIEGYSAMGALATeeg 331
Cdd:PTZ00050 140 PKILGNMAAGLV-AIKHKLKGPSGSAVTACATGAHCIGEAFRWIKYGEADIMICGGTEASITPVSFAGFSRMRALCT--- 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 332 lrlieGRDDvDFRRASRPFGEN-CGFTLAESSQYVVLMDDELALRLGADIHGAVTDVFINADGFKksISAPGP---GNYL 407
Cdd:PTZ00050 216 -----KYND-DPQRASRPFDKDrAGFVMGEGAGILVLEELEHALRRGAKIYAEIRGYGSSSDAHH--ITAPHPdgrGARR 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 408 TVAKAVASAVQIvgldTVRHASFVHAHGSSTPANRVTESEILDRVasaFGIDGWP---VTAVKAYVGHSLATASADQLIS 484
Cdd:PTZ00050 288 CMENALKDGANI----NINDVDYVNAHATSTPIGDKIELKAIKKV---FGDSGAPklyVSSTKGGLGHLLGAAGAVESIV 360
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 15600367 485 ALGTFKYGILPGIKTIDKVADDVhqQRLSISNRDMRQDKPLEVCFINSKGFGGNNAS 541
Cdd:PTZ00050 361 TILSLYEQIIPPTINLENPDAEC--DLNLVQGKTAHPLQSIDAVLSTSFGFGGVNTA 415
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
188-373 |
2.76e-10 |
|
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: 61.11 E-value: 2.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 188 QMSVVAATDAIRSTGIDwktiVDNVQPDEIAVFSGSIMSQLDDNGFGGLMQSRLkghRVSAKQLPLGFNSMPTdFInAYV 267
Cdd:pfam00109 89 RLLLEAAWEALEDAGIT----PDSLDGSRTGVFIGSGIGDYAALLLLDEDGGPR---RGSPFAVGTMPSVIAG-RI-SYF 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 268 LGSVGMTGSITGACATFLYNLQKGIDVITSGQARVVIVGNSEAPILPECIEGYSAMGALATEeglrliegrddvDFRRAS 347
Cdd:pfam00109 160 LGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSPD------------GPCKAF 227
|
170 180
....*....|....*....|....*.
gi 15600367 348 RPFGEncGFTLAESSQYVVLMDDELA 373
Cdd:pfam00109 228 DPFAD--GFVRGEGVGAVVLKRLSDA 251
|
|
| GT-D_rel |
NF040628 |
GT-D fold domain; This HMM describes a domain related to the GT-D fold glycotransferase domain ... |
351-553 |
8.92e-04 |
|
GT-D fold domain; This HMM describes a domain related to the GT-D fold glycotransferase domain described in Pfam model PF08759. The two families share the strong motif R[VIL]GDGE, and full-length homology, but only about 16 percent identity overall. As characterized sequences included in PF08759 include glycosyltransferase proteins or domains, members of this family are proposed also to be glycosyltransferases and to share the GT-D fold of PF08759.
Pssm-ID: 468600 Cd Length: 223 Bit Score: 41.06 E-value: 8.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 351 GENcgFTLAessQYVVLMDDElALRLGAdihgavtdvFINADGFKKSISAPGpgnyLTVAKAVASAVQ---IVGLDTVRH 427
Cdd:NF040628 29 GEN--LVLA---QDTVLSIEE-VLQEGW---------ALKANQGYKGVRLPN----LAARDALAESIRkadIVGIPTIRA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 428 ASFvhahgsstpanrvteSEILDRVASAFGIDgwPVTAVKAYVGHSLA-----------------TASADQLISALGTFK 490
Cdd:NF040628 90 PDY---------------RPLTFPVFRAYGID--PLRLTHATVNRELAqqgyfwrmlagrrvllvGNEAAQLAEVLEQDP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 491 YGI-----LP--GIKTIDKVADDVHQQRLSISnrdmrqdkpLEVCFINSkgfggnnasgVVLSPRIAEKM 553
Cdd:NF040628 153 YGLqiagaLPvdGYEDIPRVLKEIARHDFDIA---------LVSAGVNA----------VILAQRIAEEL 203
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
125-544 |
4.97e-98 |
|
"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: 305.90 E-value: 4.97e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 125 PEPLPANWSIAPAEDGEVLVSIHERCEFkvdsyralTVKSAGQLPTG-FEPGELYNSRFHPRGLQMSVVAATDAIRSTGI 203
Cdd:cd00828 18 CDEVEEFWEALREGRSGIAPVARLKSRF--------DRGVAGQIPTGdIPGWDAKRTGIVDRTTLLALVATEEALADAGI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 204 DWKTIVDnvqPDEIAVFSGSIMSQLDDNGFGGLMQSRLKGHRVSAKQLPLgfNSMPTDFINAYVLGSVGMTGSITGACAT 283
Cdd:cd00828 90 TDPYEVH---PSEVGVVVGSGMGGLRFLRRGGKLDARAVNPYVSPKWMLS--PNTVAGWVNILLLSSHGPIKTPVGACAT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 284 FLYNLQKGIDVITSGQARVVIVGNSEAPiLPECIEGYSAMGALATEEGLRliegrddvdfRRASRPFGE-NCGFTLAESS 362
Cdd:cd00828 165 ALEALDLAVEAIRSGKADIVVVGGVEDP-LEEGLSGFANMGALSTAEEEP----------EEMSRPFDEtRDGFVEAEGA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 363 QYVVLMDDELALRLGADIHGAVTDVFINADGFKKSISAPGPGNYLTVAKAVASAVQIvgldtVRHASFVHAHGSSTPANR 442
Cdd:cd00828 234 GVLVLERAELALARGAPIYGRVAGTASTTDGAGRSVPAGGKGIARAIRTALAKAGLS-----LDDLDVISAHGTSTPAND 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 443 VTESEILDRVASAFGIDgWPVTAVKAYVGHSLATASADQLISALGTFKYGILPGIKTIDKVADDVHQQRLSISNRDMRQD 522
Cdd:cd00828 309 VAESRAIAEVAGALGAP-LPVTAQKALFGHSKGAAGALQLIGALQSLEHGLIPPTANLDDVDPDVEHLSVVGLSRDLNLK 387
|
410 420
....*....|....*....|..
gi 15600367 523 KplEVCFINSKGFGGNNASGVV 544
Cdd:cd00828 388 V--RAALVNAFGFGGSNAALVL 407
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
159-541 |
9.59e-47 |
|
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: 170.03 E-value: 9.59e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 159 ALTVKSAGQLPTG-----FEPGELynsRFHPRGLQMSVVAATDAIRSTGIDWktivDNVQPDEIAVFSGSIMSQLDDNGF 233
Cdd:cd00834 42 GFPSRIAGEVPDFdpedyLDRKEL---RRMDRFAQFALAAAEEALADAGLDP----EELDPERIGVVIGSGIGGLATIEE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 234 GGLMQSRLKGHRVSAKQLPLGFNSMPTDFInAYVLGSVGMTGSITGACATFLYNLQKGIDVITSGQARVVIVGNSEAPIL 313
Cdd:cd00834 115 AYRALLEKGPRRVSPFFVPMALPNMAAGQV-AIRLGLRGPNYTVSTACASGAHAIGDAARLIRLGRADVVIAGGAEALIT 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 314 PECIEGYSAMGALATEEGlrliegrddvDFRRASRPFGEN-CGFTLAESSQYVVLMDDELALRLGADIHGAVTDVFINAD 392
Cdd:cd00834 194 PLTLAGFAALRALSTRND----------DPEKASRPFDKDrDGFVLGEGAGVLVLESLEHAKARGAKIYAEILGYGASSD 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 393 GFkkSISAP---GPGNYLTVAKAVASAvqivGLdTVRHASFVHAHGSSTPANRVTESEILDRVasaFG--IDGWPVTAVK 467
Cdd:cd00834 264 AY--HITAPdpdGEGAARAMRAALADA----GL-SPEDIDYINAHGTSTPLNDAAESKAIKRV---FGehAKKVPVSSTK 333
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600367 468 AYVGHSLATASADQLISALGTFKYGILP---GIKTIDKVADdvhqqrLSISNRDMRQdKPLEVCFINSKGFGGNNAS 541
Cdd:cd00834 334 SMTGHLLGAAGAVEAIATLLALRDGVLPptiNLEEPDPECD------LDYVPNEARE-APIRYALSNSFGFGGHNAS 403
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
151-546 |
2.65e-41 |
|
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: 154.87 E-value: 2.65e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 151 EFKVDSYRaltVKSAGQLPtGFEPGELYN---SRFHPRGLQMSVVAATDAIRSTGIDwktiVDNVQPDEIAVFSGSIMSQ 227
Cdd:COG0304 37 RFDASGLP---VRIAGEVK-DFDPEEYLDrkeLRRMDRFTQYALAAAREALADAGLD----LDEVDPDRTGVIIGSGIGG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 228 LD--DNGFGGLMQSRLKghRVSAKQLPLGFNSMPTDFInAYVLGSVGMTGSITGACATFLYNLQKGIDVITSGQARVVIV 305
Cdd:COG0304 109 LDtlEEAYRALLEKGPR--RVSPFFVPMMMPNMAAGHV-SIRFGLKGPNYTVSTACASGAHAIGEAYRLIRRGRADVMIA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 306 GNSEAPILPECIEGYSAMGALATeeglrliegRDDvDFRRASRPFGEN-CGFTLAESSQYVVLMDDELALRLGADIHGAV 384
Cdd:COG0304 186 GGAEAAITPLGLAGFDALGALST---------RND-DPEKASRPFDKDrDGFVLGEGAGVLVLEELEHAKARGAKIYAEV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 385 TDVFINADGFkkSISAPGPgNYLTVAKAVASAVQIVGLDtvrhAS---FVHAHGSSTPANRVTESEILDRVasaFGIDGW 461
Cdd:COG0304 256 VGYGASSDAY--HITAPAP-DGEGAARAMRAALKDAGLS----PEdidYINAHGTSTPLGDAAETKAIKRV---FGDHAY 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 462 --PVTAVKAYVGHSLATASADQLISALGTFKYGILP---GIKTIDKVAD-DVhqqrlsISNRdmRQDKPLEVCFINSKGF 535
Cdd:COG0304 326 kvPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPptiNLENPDPECDlDY------VPNE--AREAKIDYALSNSFGF 397
|
410
....*....|.
gi 15600367 536 GGNNASgVVLS 546
Cdd:COG0304 398 GGHNAS-LVFK 407
|
|
| PTZ00050 |
PTZ00050 |
3-oxoacyl-acyl carrier protein synthase; Provisional |
172-541 |
3.58e-30 |
|
3-oxoacyl-acyl carrier protein synthase; Provisional
Pssm-ID: 240245 [Multi-domain] Cd Length: 421 Bit Score: 123.26 E-value: 3.58e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 172 FEPGELYNSRFHPRGLQMSVVAATDAIRSTGIDWKTIVDnvqPDEIAVFSGSIMSQLDDNGFGGLMQSRLKGHRVSAKQL 251
Cdd:PTZ00050 63 FDPSDFAPTKRESRATHFAMAAAREALADAKLDILSEKD---QERIGVNIGSGIGSLADLTDEMKTLYEKGHSRVSPYFI 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 252 PLGFNSMPTDFInAYVLGSVGMTGSITGACATFLYNLQKGIDVITSGQARVVIVGNSEAPILPECIEGYSAMGALATeeg 331
Cdd:PTZ00050 140 PKILGNMAAGLV-AIKHKLKGPSGSAVTACATGAHCIGEAFRWIKYGEADIMICGGTEASITPVSFAGFSRMRALCT--- 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 332 lrlieGRDDvDFRRASRPFGEN-CGFTLAESSQYVVLMDDELALRLGADIHGAVTDVFINADGFKksISAPGP---GNYL 407
Cdd:PTZ00050 216 -----KYND-DPQRASRPFDKDrAGFVMGEGAGILVLEELEHALRRGAKIYAEIRGYGSSSDAHH--ITAPHPdgrGARR 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 408 TVAKAVASAVQIvgldTVRHASFVHAHGSSTPANRVTESEILDRVasaFGIDGWP---VTAVKAYVGHSLATASADQLIS 484
Cdd:PTZ00050 288 CMENALKDGANI----NINDVDYVNAHATSTPIGDKIELKAIKKV---FGDSGAPklyVSSTKGGLGHLLGAAGAVESIV 360
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 15600367 485 ALGTFKYGILPGIKTIDKVADDVhqQRLSISNRDMRQDKPLEVCFINSKGFGGNNAS 541
Cdd:PTZ00050 361 TILSLYEQIIPPTINLENPDAEC--DLNLVQGKTAHPLQSIDAVLSTSFGFGGVNTA 415
|
|
| PRK08439 |
PRK08439 |
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed |
161-545 |
1.41e-25 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
Pssm-ID: 236265 [Multi-domain] Cd Length: 406 Bit Score: 109.44 E-value: 1.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 161 TVKSAGQLpTGFEPGELYNS-------RFhprgLQMSVVAATDAIRSTGIDwktiVDNVQPDEIAVFSGSimsqlddnGF 233
Cdd:PRK08439 45 PVQIAGEI-TDFDPTEVMDPkevkkadRF----IQLGLKAAREAMKDAGFL----PEELDAERFGVSSAS--------GI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 234 GGL-------MQSRLKG-HRVSAKQLPLGFNSMPTDFINAYvLGSVGMTGSITGACATFLYNLQKGIDVITSGQARVVIV 305
Cdd:PRK08439 108 GGLpnieknsIICFEKGpRKISPFFIPSALVNMLGGFISIE-HGLKGPNLSSVTACAAGTHAIIEAVKTIMLGGADKMLV 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 306 GNSEAPILPECIEGYSAMGALATeeglrliegRDDvDFRRASRPF-GENCGFTLAESSQYVVLMDDELALRLGADIHGAV 384
Cdd:PRK08439 187 VGAESAICPVGIGGFAAMKALST---------RND-DPKKASRPFdKDRDGFVMGEGAGALVLEEYESAKKRGAKIYAEI 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 385 TdvfinadGFKKS-----ISAPGPGNYLtvaKAVASAVQIVGLDTVrhaSFVHAHGSSTPANRVTESEILDRVasaFGID 459
Cdd:PRK08439 257 I-------GFGESgdanhITSPAPEGPL---RAMKAALEMAGNPKI---DYINAHGTSTPYNDKNETAALKEL---FGSK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 460 GW--PVTAVKAYVGHSLATASADQLISALGTFKYGILPgiKTIDKVADDVHQQRLSISNRDMRQDkpLEVCFINSKGFGG 537
Cdd:PRK08439 321 EKvpPVSSTKGQIGHCLGAAGAIEAVISIMAMRDGILP--PTINQETPDPECDLDYIPNVARKAE--LNVVMSNSFGFGG 396
|
....*...
gi 15600367 538 NNasGVVL 545
Cdd:PRK08439 397 TN--GVVI 402
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
159-541 |
7.34e-24 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 104.49 E-value: 7.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 159 ALTVKSAGQLPtGFEPgELYNSRFHPRGL----QMSVVAATDAIRSTGIDwktiVDNVQPDEIAVFSGSimsqlddnGFG 234
Cdd:PRK07314 43 DLAVKIAGEVK-DFNP-DDYMSRKEARRMdrfiQYGIAAAKQAVEDAGLE----ITEENADRIGVIIGS--------GIG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 235 GL-----MQSRL--KG-HRVSakqlPLGFNSMPTDFINAYV---LGSVGMTGSITGACATFLYNLQKGIDVITSGQARVV 303
Cdd:PRK07314 109 GLetieeQHITLleKGpRRVS----PFFVPMAIINMAAGHVsirYGAKGPNHSIVTACATGAHAIGDAARLIAYGDADVM 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 304 IVGNSEAPILPECIEGYSAMGALATeeglrliegRDDvDFRRASRPFGEN-CGFTLAESSQYVVLMDDELALRLGADIHG 382
Cdd:PRK07314 185 VAGGAEAAITPLGIAGFAAARALST---------RND-DPERASRPFDKDrDGFVMGEGAGILVLEELEHAKARGAKIYA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 383 AVTDVFINADGFKksISAPGPGNyLTVAKAVASAVQIVGLdTVRHASFVHAHGSSTPANRVTESEILDRV--ASAFGIdg 460
Cdd:PRK07314 255 EVVGYGMTGDAYH--MTAPAPDG-EGAARAMKLALKDAGI-NPEDIDYINAHGTSTPAGDKAETQAIKRVfgEHAYKV-- 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 461 wPVTAVKAYVGHSLATASADQLISALGTFKYGILP---GIKT------IDKVAddvHQQRlsisnrdmrqDKPLEVCFIN 531
Cdd:PRK07314 329 -AVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPptiNLDNpdeecdLDYVP---NEAR----------ERKIDYALSN 394
|
410
....*....|
gi 15600367 532 SKGFGGNNAS 541
Cdd:PRK07314 395 SFGFGGTNAS 404
|
|
| PRK05952 |
PRK05952 |
beta-ketoacyl-ACP synthase; |
265-540 |
1.18e-23 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 103.21 E-value: 1.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 265 AYVLGSVGMTGSITGACATFLYNLQKGIDVITSGQARVVIVGNSEAPILPECIEGYSAMGALATeeglrliEGRDDVDFR 344
Cdd:PRK05952 130 ARQIGTQGPVLAPMAACATGLWAIAQGVELIQTGQCQRVIAGAVEAPITPLTLAGFQQMGALAK-------TGAYPFDRQ 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 345 RAsrpfgencGFTLAESSQYVVLMDDELALRLGADIHGAVTDVFINADGFKksISAPGPgNYLTVAKAVASAVQIVGLdT 424
Cdd:PRK05952 203 RE--------GLVLGEGGAILVLESAELAQKRGAKIYGQILGFGLTCDAYH--MSAPEP-DGKSAIAAIQQCLARSGL-T 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 425 VRHASFVHAHGSSTPANRVTESEILDRVasaFGiDGWPVTAVKAYVGHSLATASADQLISALGTFKYGILP---GIKTID 501
Cdd:PRK05952 271 PEDIDYIHAHGTATRLNDQREANLIQAL---FP-HRVAVSSTKGATGHTLGASGALGVAFSLLALRHQQLPpcvGLQEPE 346
|
250 260 270
....*....|....*....|....*....|....*....
gi 15600367 502 KVADDVHQQRLSisnrdmrqdkPLEVCFINSKGFGGNNA 540
Cdd:PRK05952 347 FDLNFVRQAQQS----------PLQNVLCLSFGFGGQNA 375
|
|
| PRK06333 |
PRK06333 |
beta-ketoacyl-ACP synthase; |
160-541 |
1.27e-19 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235781 [Multi-domain] Cd Length: 424 Bit Score: 91.60 E-value: 1.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 160 LTVKSAGQLPT-------GFEPGELY---NSRFHPRGLQMSVVAATDAIRSTGidWKtIVDNVQPDEIAVFSGSIMSqld 229
Cdd:PRK06333 46 LATKIGGQVPDlaedaeaGFDPDRYLdpkDQRKMDRFILFAMAAAKEALAQAG--WD-PDTLEDRERTATIIGSGVG--- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 230 dnGFGGLMQ----SRLKGHRvsaKQLPLGFNSMPTDFINAYV---LGSVGMTGSITGACATFLYNLQKGIDVITSGQARV 302
Cdd:PRK06333 120 --GFPAIAEavrtLDSRGPR---RLSPFTIPSFLTNMAAGHVsirYGFKGPLGAPVTACAAGVQAIGDAARLIRSGEADV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 303 VIVGNSEAPILPECIEGYSAMGALATeeglrliegRDDVDFRRASRPFGENC-GFTLAESSQYVVLMDDELALRLGADIH 381
Cdd:PRK06333 195 AVCGGTEAAIDRVSLAGFAAARALST---------RFNDAPEQASRPFDRDRdGFVMGEGAGILVIETLEHALARGAPPL 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 382 GAVTDVFINADGFKksISAPgPGNYLTVAKAVASAVQIVGL--DTVRHasfVHAHGSSTPANRVTEseiLDRVASAFGID 459
Cdd:PRK06333 266 AELVGYGTSADAYH--MTAG-PEDGEGARRAMLIALRQAGIppEEVQH---LNAHATSTPVGDLGE---VAAIKKVFGHV 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 460 GWP-VTAVKAYVGHSLATASADQLISALGTFKYGILPgiKTI-----DKVADDVHQqrLSISNRDMrqdkPLEVCFINSK 533
Cdd:PRK06333 337 SGLaVSSTKSATGHLLGAAGGVEAIFTILALRDQIAP--PTLnlenpDPAAEGLDV--VANKARPM----DMDYALSNGF 408
|
....*...
gi 15600367 534 GFGGNNAS 541
Cdd:PRK06333 409 GFGGVNAS 416
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
265-545 |
6.33e-19 |
|
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: 89.54 E-value: 6.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 265 AYVLGSVGMTGSITGACATFLYNLQKGIDVITSGQARVVIVGNSEAPILPECIEGYSAMGALATEeglrlieGRddvdfr 344
Cdd:cd00833 154 SYFFDLRGPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLSPD-------GR------ 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 345 raSRPF---------GENCGFtlaessqyVVLMDDELALRLGADIHGAVTDVFINADGFKKSISAPGPGNYltvAKAVAS 415
Cdd:cd00833 221 --CRPFdadadgyvrGEGVGV--------VVLKRLSDALRDGDRIYAVIRGSAVNQDGRTKGITAPSGEAQ---AALIRR 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 416 AVQIVGLDtVRHASFVHAHGSSTPANRVTESEILDRVASAFGIDGWP--VTAVKAYVGHSLATASADQLISALGTFKYGI 493
Cdd:cd00833 288 AYARAGVD-PSDIDYVEAHGTGTPLGDPIEVEALAKVFGGSRSADQPllIGSVKSNIGHLEAAAGLAGLIKVVLALEHGV 366
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 15600367 494 LP---GIKTI-DKVADDVHQQRLSISNRDMRQDKPLEVCFINSKGFGGNNASgVVL 545
Cdd:cd00833 367 IPpnlHFETPnPKIDFEESPLRVPTEARPWPAPAGPRRAGVSSFGFGGTNAH-VIL 421
|
|
| PRK08722 |
PRK08722 |
beta-ketoacyl-ACP synthase II; |
187-541 |
2.81e-18 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 181539 [Multi-domain] Cd Length: 414 Bit Score: 87.37 E-value: 2.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 187 LQMSVVAATDAIRSTGIdwKTIVDNVQPDEIAVFSGSIMSQLDDNGFGGLMQsrlKGHRvsaKQLPLGFNSMPTDFINAY 266
Cdd:PRK08722 75 IQYGIAAGIQALDDSGL--EVTEENAHRIGVAIGSGIGGLGLIEAGHQALVE---KGPR---KVSPFFVPSTIVNMIAGN 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 267 VLGSVGMTG---SITGACATFLYNLQKGIDVITSGQARVVIVGNSEAPILPECIEGYSAMGALATeeglrliegRDDvDF 343
Cdd:PRK08722 147 LSIMRGLRGpniAISTACTTGLHNIGHAARMIAYGDADAMVAGGAEKASTPLGMAGFGAAKALST---------RND-EP 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 344 RRASRPFGENC-GFTLAESSQYVVLMDDELALRLGADIHGAVTDVFINADGFKKSISAP-GPGNYLtvakAVASAVQIVG 421
Cdd:PRK08722 217 QKASRPWDKDRdGFVLGDGAGMMVLEEYEHAKARGAKIYAELVGFGMSGDAYHMTSPSEdGSGGAL----AMEAAMRDAG 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 422 LdTVRHASFVHAHGSSTPANRVTESEILDRVASAFGIDGWPVTAVKAYVGHSL-ATASADQLISALGTFKYGILPGIkti 500
Cdd:PRK08722 293 V-TGEQIGYVNAHGTSTPAGDVAEIKGIKRALGEAGSKQVLVSSTKSMTGHLLgAAGSVEAIITVMSLVDQIVPPTI--- 368
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 15600367 501 dKVADDVHQQRLSISNRDMRQDKPLEVCFINSKGFGGNNAS 541
Cdd:PRK08722 369 -NLDDPEEGLDIDLVPHTARKVESMEYAICNSFGFGGTNGS 408
|
|
| PLN02787 |
PLN02787 |
3-oxoacyl-[acyl-carrier-protein] synthase II |
224-547 |
3.33e-18 |
|
3-oxoacyl-[acyl-carrier-protein] synthase II
Pssm-ID: 215421 [Multi-domain] Cd Length: 540 Bit Score: 88.11 E-value: 3.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 224 IMSQLDDNGFGGLMQSRLKGH----------RVSAKQL-----PLGFNSMPTDFInAYVLGSVGMTGSITGACATFLYNL 288
Cdd:PLN02787 220 VMKELDKTKCGVLIGSAMGGMkvfndaiealRISYRKMnpfcvPFATTNMGSAML-AMDLGWMGPNYSISTACATSNFCI 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 289 QKGIDVITSGQARVVIVGNSEAPILPECIEGYSAMGALATeeglrliegRDDvDFRRASRPFGENC-GFTLAESSQYVVL 367
Cdd:PLN02787 299 LNAANHIIRGEADVMLCGGSDAAIIPIGLGGFVACRALSQ---------RND-DPTKASRPWDMNRdGFVMGEGAGVLLL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 368 MDDELALRLGADIHGAVTDVFINADGFKKSISAP-GPGNYLTVAKAVASAvqivGLDTvRHASFVHAHGSSTPANRVTES 446
Cdd:PLN02787 369 EELEHAKKRGANIYAEFLGGSFTCDAYHMTEPHPeGAGVILCIEKALAQS----GVSK-EDVNYINAHATSTKAGDLKEY 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 447 EILDRvasAFGID-GWPVTAVKAYVGHSLATASADQLISALGTFKYG-ILPGIkTIDKVADDVHQQRLsISNRDMRQDkp 524
Cdd:PLN02787 444 QALMR---CFGQNpELRVNSTKSMIGHLLGAAGAVEAIATVQAIRTGwVHPNI-NLENPESGVDTKVL-VGPKKERLD-- 516
|
330 340
....*....|....*....|...
gi 15600367 525 LEVCFINSKGFGGNNASgVVLSP 547
Cdd:PLN02787 517 IKVALSNSFGFGGHNSS-ILFAP 538
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
189-544 |
5.05e-18 |
|
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: 85.77 E-value: 5.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 189 MSVVAATDAIRSTGIDWKtiVDNVQPDEIAVFSGSimsqlddnGFGGLMQSRLKGHRVSAKQLPLGFNSMPTDFINAYVL 268
Cdd:cd00825 14 LGFEAAERAIADAGLSRE--YQKNPIVGVVVGTGG--------GSPRFQVFGADAMRAVGPYVVTKAMFPGASGQIATPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 269 GSVGMTGSITGACATFLYNLQKGIDVITSGQARVVIVGNSEAPILPECIEgYSAMGALATEEglrliegrddvdfrRASR 348
Cdd:cd00825 84 GIHGPAYDVSAACAGSLHALSLAADAVQNGKQDIVLAGGSEELAAPMDCE-FDAMGALSTPE--------------KASR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 349 PFGEN-CGFTLAESSQYVVLMDDELALRLGADIHGAVTDVFINADGFKKSISAPGPGNyltVAKAVASAVQIVGLdTVRH 427
Cdd:cd00825 149 TFDAAaDGFVFGDGAGALVVEELEHALARGAHIYAEIVGTAATIDGAGMGAFAPSAEG---LARAAKEALAVAGL-TVWD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 428 ASFVHAHGSSTPANRVTESEILDrvaSAFGIDGWPVTAVKAYVGHSLATASADQLISALgtfKYGILPGIKTIDKVADDV 507
Cdd:cd00825 225 IDYLVAHGTGTPIGDVKELKLLR---SEFGDKSPAVSATKAMTGNLSSAAVVLAVDEAV---LMLEHGFIPPSIHIEELD 298
|
330 340 350
....*....|....*....|....*....|....*..
gi 15600367 508 HQQRLSISNrdmRQDKPLEVCFINSKGFGGNNASGVV 544
Cdd:cd00825 299 EAGLNIVTE---TTPRELRTALLNGFGLGGTNATLVL 332
|
|
| PLN02836 |
PLN02836 |
3-oxoacyl-[acyl-carrier-protein] synthase |
147-547 |
7.27e-17 |
|
3-oxoacyl-[acyl-carrier-protein] synthase
Pssm-ID: 215449 [Multi-domain] Cd Length: 437 Bit Score: 83.30 E-value: 7.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 147 HERCEFKVDSYRALTVKSAGQLPTGFEPGE-----LYNSRFHPRGLQMSVVAATDAIRSTgiDWKTIvDNVQPDEIAVFS 221
Cdd:PLN02836 49 SEDEETQLYTLDQLPSRVAALVPRGTGPGDfdeelWLNSRSSSRFIGYALCAADEALSDA--RWLPS-EDEAKERTGVSI 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 222 GSIMSQLDDNGFGGLMQSRLKGHRVSAKQLPLGFNSMPTdfinayvlGSVGMTGSITG-------ACATFLYNLQKGIDV 294
Cdd:PLN02836 126 GGGIGSITDILEAAQLICEKRLRRLSPFFVPRILINMAA--------GHVSIRYGFQGpnhaavtACATGAHSIGDAFRM 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 295 ITSGQARVVIVGNSEAPILPECIEGYSAMGALATeeglrliegRDDVDFRRASRPFgeNC---GFTLAESSQYVVLMDDE 371
Cdd:PLN02836 198 IQFGDADVMVAGGTESSIDALSIAGFSRSRALST---------KFNSCPTEASRPF--DCdrdGFVIGEGAGVLVLEELE 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 372 LALRLGADIHGAVTDVFINADGFKksISAP---GPGNYLTVAKAVASAvqivGLDTvRHASFVHAHGSSTPANRVTESEI 448
Cdd:PLN02836 267 HAKRRGAKIYAEVRGYGMSGDAHH--ITQPhedGRGAVLAMTRALQQS----GLHP-NQVDYVNAHATSTPLGDAVEARA 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 449 L-----DRVASAfgidGWPVTAVKAYVGHSLATASADQLISALGTFKYGILPGIKTIDKvADDVHQQRLS--ISNRDMrq 521
Cdd:PLN02836 340 IktvfsEHATSG----GLAFSSTKGATGHLLGAAGAVEAIFSVLAIHHGIAPPTLNLER-PDPIFDDGFVplTASKAM-- 412
|
410 420
....*....|....*....|....*.
gi 15600367 522 dkPLEVCFINSKGFGGNNASGVVLSP 547
Cdd:PLN02836 413 --LIRAALSNSFGFGGTNASLLFTSP 436
|
|
| PRK06501 |
PRK06501 |
beta-ketoacyl-ACP synthase; |
269-543 |
1.35e-16 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235817 [Multi-domain] Cd Length: 425 Bit Score: 82.37 E-value: 1.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 269 GSVGMTGSITGACATFLYNLQKGIDVITSGQARVVIVGNSEAPILPECIEGYSAMGALATeeglrliegRDDVDfRRASR 348
Cdd:PRK06501 163 GTRGLPISLSTACASGATAIQLGVEAIRRGETDRALCIATDGSVSAEALIRFSLLSALST---------QNDPP-EKASK 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 349 PFGENC-GFTLAESSQYVVLMDDELALRLGADIHGAVTDVFINADGFKKSISAPGPGNYL-TVAKAVASAvqivGLdTVR 426
Cdd:PRK06501 233 PFSKDRdGFVMAEGAGALVLESLESAVARGAKILGIVAGCGEKADSFHRTRSSPDGSPAIgAIRAALADA----GL-TPE 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 427 HASFVHAHGSSTPANRVTESEILDRVasaFG--IDGWPVTAVKAYVGHSLATASADQLISALGTFKYGILPgiKTID-KV 503
Cdd:PRK06501 308 QIDYINAHGTSTPENDKMEYLGLSAV---FGerLASIPVSSNKSMIGHTLTAAGAVEAVFSLLTIQTGRLP--PTINyDN 382
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 15600367 504 AD-----DV--HQQRlsisnrdmrqDKPLEVCFINSKGFGGNNASGV 543
Cdd:PRK06501 383 PDpaiplDVvpNVAR----------DARVTAVLSNSFGFGGQNASLV 419
|
|
| PRK07967 |
PRK07967 |
beta-ketoacyl-ACP synthase I; |
272-543 |
9.29e-15 |
|
beta-ketoacyl-ACP synthase I;
Pssm-ID: 181184 [Multi-domain] Cd Length: 406 Bit Score: 76.63 E-value: 9.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 272 GMTGSITGACATFLYNLQKGIDVITSGQARVVIVGNSEApILPECIEGYSAMGALATEeglrliegRDDVDfRRASRPFG 351
Cdd:PRK07967 153 GVNYSISSACATSAHCIGNAVEQIQLGKQDIVFAGGGEE-LDWEMSCLFDAMGALSTK--------YNDTP-EKASRAYD 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 352 ENC-GFTLAESSQYVVLMDDELALRLGADIHGAVTDVFINADGfkksisapgpgnYLTVAKAVASAVQIV--GLDTVRHA 428
Cdd:PRK07967 223 ANRdGFVIAGGGGVVVVEELEHALARGAKIYAEIVGYGATSDG------------YDMVAPSGEGAVRCMqmALATVDTP 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 429 -SFVHAHGSSTPANRVTESEILDRVasaFGIDGWPVTAVKAYVGHSLATASADQLISALGTFKYGILPG---IKTIDKVA 504
Cdd:PRK07967 291 iDYINTHGTSTPVGDVKELGAIREV---FGDKSPAISATKSLTGHSLGAAGVQEAIYSLLMMEHGFIAPsanIEELDPQA 367
|
250 260 270
....*....|....*....|....*....|....*....
gi 15600367 505 DDVHQQRLSISNrdmrqdKPLEVCFINSKGFGGNNASGV 543
Cdd:PRK07967 368 AGMPIVTETTDN------AELTTVMSNSFGFGGTNATLV 400
|
|
| CLF |
cd00832 |
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ... |
165-544 |
2.05e-14 |
|
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: 75.47 E-value: 2.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 165 AGQLPtGFEPGELYNSRFHP---RGLQMSVVAATDAIRSTGIDwktiVDNVQPDEIAVFSGSIMSQLDdngFGGLMQSRL 241
Cdd:cd00832 48 AGEVP-DFDAAEHLPGRLLPqtdRMTRLALAAADWALADAGVD----PAALPPYDMGVVTASAAGGFE---FGQRELQKL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 242 KGH---RVSAKQLPLGFNSMPTdfinayvlGSVGMTGSITGACATFLYNLQKGIDVItsGQAR--------VVIVGNSEA 310
Cdd:cd00832 120 WSKgprHVSAYQSFAWFYAVNT--------GQISIRHGMRGPSGVVVAEQAGGLDAL--AQARrlvrrgtpLVVSGGVDS 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 311 PILPECIEGYSAMGALATEEglrliegrddvDFRRASRPFGEN-CGFTLAESSQYVVLMDDELALRLGADIHGAVTDVFI 389
Cdd:cd00832 190 ALCPWGWVAQLSSGRLSTSD-----------DPARAYLPFDAAaAGYVPGEGGAILVLEDAAAARERGARVYGEIAGYAA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 390 NADGfkksisAPGPGNYLTVAKAVASAVQIVGLdTVRHASFVHAHGSSTPANRVTESEILDRVasaFGIDGWPVTAVKAY 469
Cdd:cd00832 259 TFDP------PPGSGRPPGLARAIRLALADAGL-TPEDVDVVFADAAGVPELDRAEAAALAAV---FGPRGVPVTAPKTM 328
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600367 470 VGHSLATASADQLISALGTFKYGILPGIKTIDKVADDvHQQRLSisnRDMRQDKPLEVCFINSKGFGGNNASGVV 544
Cdd:cd00832 329 TGRLYAGGAPLDVATALLALRDGVIPPTVNVTDVPPA-YGLDLV---TGRPRPAALRTALVLARGRGGFNSALVV 399
|
|
| PRK07910 |
PRK07910 |
beta-ketoacyl-ACP synthase; |
295-541 |
2.06e-12 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236129 [Multi-domain] Cd Length: 418 Bit Score: 69.37 E-value: 2.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 295 ITSGQARVVIVGNSEAPILPECIEGYSAMgalateeglRLIEGRDDVDFRRASRPFGEN-CGFTLAESSQYVVLMDDELA 373
Cdd:PRK07910 185 IVLGEADIAICGGVETRIEAVPIAGFAQM---------RIVMSTNNDDPAGACRPFDKDrDGFVFGEGGALMVIETEEHA 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 374 LRLGADIHGAVTDVFINADGFKksISAPGPgNYLTVAKAVASAVQIVGLDT--VRHasfVHAHGSSTPANRVTESEILDR 451
Cdd:PRK07910 256 KARGANILARIMGASITSDGFH--MVAPDP-NGERAGHAMTRAIELAGLTPgdIDH---VNAHATGTSVGDVAEGKAINN 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 452 vasAFGIDGWPVTAVKAYVGHSLATASADQLISALGTFKYGILP---GIKTIDKVAD-DVhqqrlsISNRDMRQDkpLEV 527
Cdd:PRK07910 330 ---ALGGHRPAVYAPKSALGHSVGAVGAVESILTVLALRDGVIPptlNLENLDPEIDlDV------VAGEPRPGN--YRY 398
|
250
....*....|....
gi 15600367 528 CFINSKGFGGNNAS 541
Cdd:PRK07910 399 AINNSFGFGGHNVA 412
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
188-373 |
2.76e-10 |
|
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: 61.11 E-value: 2.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 188 QMSVVAATDAIRSTGIDwktiVDNVQPDEIAVFSGSIMSQLDDNGFGGLMQSRLkghRVSAKQLPLGFNSMPTdFInAYV 267
Cdd:pfam00109 89 RLLLEAAWEALEDAGIT----PDSLDGSRTGVFIGSGIGDYAALLLLDEDGGPR---RGSPFAVGTMPSVIAG-RI-SYF 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 268 LGSVGMTGSITGACATFLYNLQKGIDVITSGQARVVIVGNSEAPILPECIEGYSAMGALATEeglrliegrddvDFRRAS 347
Cdd:pfam00109 160 LGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSPD------------GPCKAF 227
|
170 180
....*....|....*....|....*.
gi 15600367 348 RPFGEncGFTLAESSQYVVLMDDELA 373
Cdd:pfam00109 228 DPFAD--GFVRGEGVGAVVLKRLSDA 251
|
|
| Ketoacyl-synt_C |
pfam02801 |
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
381-495 |
1.65e-09 |
|
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: 56.04 E-value: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 381 HGAVTDVFINADGFKKSISAP-GPGNYLTVAKAVASAvqivGLD--TVrhaSFVHAHGSSTPANRVTESEILdrvASAFG 457
Cdd:pfam02801 1 YAVIKGSAVNHDGRHNGLTAPnGEGQARAIRRALADA----GVDpeDV---DYVEAHGTGTPLGDPIEAEAL---KRVFG 70
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 15600367 458 IDGW----PVTAVKAYVGHSLATASADQLISALGTFKYGILP 495
Cdd:pfam02801 71 SGARkqplAIGSVKSNIGHLEGAAGAAGLIKVVLALRHGVIP 112
|
|
| PRK09185 |
PRK09185 |
beta-ketoacyl-ACP synthase; |
348-541 |
1.90e-08 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236398 [Multi-domain] Cd Length: 392 Bit Score: 56.77 E-value: 1.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 348 RPFGEN-CGFTLAESSQYVVL---MDDELALrLGAdihGAVTDVFinadgfkkSISAPGP---GNYLTVAKAVASAvqiv 420
Cdd:PRK09185 210 RPFSANrDGINIGEAAAFFLLereDDAAVAL-LGV---GESSDAH--------HMSAPHPeglGAILAMQQALADA---- 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 421 GLDTvRHASFVHAHGSSTPANRVTESEILDRVasaFGiDGWPVTAVKAYVGHSLATASADQLISALGTFKYGILPGI--- 497
Cdd:PRK09185 274 GLAP-ADIGYINLHGTATPLNDAMESRAVAAV---FG-DGVPCSSTKGLTGHTLGAAGAVEAAICWLALRHGLPPHGwnt 348
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15600367 498 KTIDkvADDVHQQRLsisnrDMRQDKPLEVCFINSKGFGGNNAS 541
Cdd:PRK09185 349 GQPD--PALPPLYLV-----ENAQALAIRYVLSNSFAFGGNNCS 385
|
|
| PRK07103 |
PRK07103 |
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated |
267-544 |
2.64e-08 |
|
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
Pssm-ID: 180839 [Multi-domain] Cd Length: 410 Bit Score: 56.58 E-value: 2.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 267 VLGSVGMTGSITGACATFLYNLQKGIDVITSGQARVVIVGNSEAPILPECIEGYSAMGALATEEGLRLIEgrddvdfrRA 346
Cdd:PRK07103 153 QFGIRGEGFTVGGASASGQLAVIQAARLVQSGSVDACIAVGALMDLSYWECQALRSLGAMGSDRFADEPE--------AA 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 347 SRPFGENC-GFTLAESSQYVVLMDDELALRLGADIHGAVTDVFINADGfkKSISAPGPGNYltvAKAVASAVQIVGLDTV 425
Cdd:PRK07103 225 CRPFDQDRdGFIYGEACGAVVLESAESARRRGARPYAKLLGWSMRLDA--NRGPDPSLEGE---MRVIRAALRRAGLGPE 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 426 RhASFVHAHGSSTPANRVTESEILDRVASAfgiDGWpVTAVKAYVGHSLATASADQLISALGTFKYGIL-PGIKTIDKVA 504
Cdd:PRK07103 300 D-IDYVNPHGTGSPLGDETELAALFASGLA---HAW-INATKSLTGHGLSAAGIVELIATLLQMRAGFLhPSRNLDEPID 374
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 15600367 505 DDVHQQRLSISNRDMRqdkpleVCFINSKGFGGNNASGVV 544
Cdd:PRK07103 375 ERFRWVGSTAESARIR------YALSLSFGFGGINTALVL 408
|
|
| PRK09116 |
PRK09116 |
beta-ketoacyl-ACP synthase; |
348-479 |
9.17e-08 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 181657 [Multi-domain] Cd Length: 405 Bit Score: 54.61 E-value: 9.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 348 RPFGENC-GFTLAESSQYVVLMDDELALRLGADIHGAVTDVFINADGfkKSISAPGPGnylTVAKAVASAVQIVGLDTvR 426
Cdd:PRK09116 220 RPFDANRdGLVIGEGAGTLVLEELEHAKARGATIYAEIVGFGTNSDG--AHVTQPQAE---TMQIAMELALKDAGLAP-E 293
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 15600367 427 HASFVHAHGSSTPANRVTESEIldrVASAFGiDGWPVTAVKAYVGHSLATASA 479
Cdd:PRK09116 294 DIGYVNAHGTATDRGDIAESQA---TAAVFG-ARMPISSLKSYFGHTLGACGA 342
|
|
| GT-D_rel |
NF040628 |
GT-D fold domain; This HMM describes a domain related to the GT-D fold glycotransferase domain ... |
351-553 |
8.92e-04 |
|
GT-D fold domain; This HMM describes a domain related to the GT-D fold glycotransferase domain described in Pfam model PF08759. The two families share the strong motif R[VIL]GDGE, and full-length homology, but only about 16 percent identity overall. As characterized sequences included in PF08759 include glycosyltransferase proteins or domains, members of this family are proposed also to be glycosyltransferases and to share the GT-D fold of PF08759.
Pssm-ID: 468600 Cd Length: 223 Bit Score: 41.06 E-value: 8.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 351 GENcgFTLAessQYVVLMDDElALRLGAdihgavtdvFINADGFKKSISAPGpgnyLTVAKAVASAVQ---IVGLDTVRH 427
Cdd:NF040628 29 GEN--LVLA---QDTVLSIEE-VLQEGW---------ALKANQGYKGVRLPN----LAARDALAESIRkadIVGIPTIRA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 428 ASFvhahgsstpanrvteSEILDRVASAFGIDgwPVTAVKAYVGHSLA-----------------TASADQLISALGTFK 490
Cdd:NF040628 90 PDY---------------RPLTFPVFRAYGID--PLRLTHATVNRELAqqgyfwrmlagrrvllvGNEAAQLAEVLEQDP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600367 491 YGI-----LP--GIKTIDKVADDVHQQRLSISnrdmrqdkpLEVCFINSkgfggnnasgVVLSPRIAEKM 553
Cdd:NF040628 153 YGLqiagaLPvdGYEDIPRVLKEIARHDFDIA---------LVSAGVNA----------VILAQRIAEEL 203
|
|
| |
