|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09185 |
PRK09185 |
beta-ketoacyl-ACP synthase; |
1-399 |
0e+00 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236398 [Multi-domain] Cd Length: 392 Bit Score: 624.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 1 MNPLLLSHFTSTSCIGRGVDATVDALRTAR-GGLSPCRFERAELDTWIGAVDGLDAQPVRADLADFDCRNNRLAQLALEQ 79
Cdd:PRK09185 1 MTPVYISAFGATSALGRGLDAILAALRAGRaSGMRPCDFWLVDLPTWVGEVVGVELPALPAALAAFDCRNNRLALLALQQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 80 dgFDARVAAAVARYGAQRVGVFVGTSTSGILETERAYMRRDPASGALPANFRYTHtHNPYSAAAFVRAYCGLRGPATAIS 159
Cdd:PRK09185 81 --IEPAVEAAIARYGADRIGVVLGTSTSGILEGELAYRRRDPAHGALPADYHYAQ-QELGSLADFLRAYLGLSGPAYTIS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 160 SACSSGAKVFGSARRMIEAGLIDAAVVGGVDTLCLTTLYGFNSLELLSRQPCRPFDVARDGISIGEAAAFALLERVPaar 239
Cdd:PRK09185 158 TACSSSAKVFASARRLLEAGLCDAAIVGGVDSLCRLTLNGFNSLESLSPQPCRPFSANRDGINIGEAAAFFLLERED--- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 240 gtldDDAILLLGIGESSDAHHMSSPHPEGLGARLAIEQALASAGLDATDIDYVNLHGTATPSNDAAESRAVGALL-ARTP 318
Cdd:PRK09185 235 ----DAAVALLGVGESSDAHHMSAPHPEGLGAILAMQQALADAGLAPADIGYINLHGTATPLNDAMESRAVAAVFgDGVP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 319 CSSTKGATGHTLGAAGALEAVITALALREGFVPAGVNTTQPDPALAADYVLASR-AAQMRTALSNSFGFGGTNCTLVFGR 397
Cdd:PRK09185 311 CSSTKGLTGHTLGAAGAVEAAICWLALRHGLPPHGWNTGQPDPALPPLYLVENAqALAIRYVLSNSFAFGGNNCSLIFGR 390
|
..
gi 981242683 398 AD 399
Cdd:PRK09185 391 AD 392
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
12-395 |
4.89e-126 |
|
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: 369.95 E-value: 4.89e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 12 TSCIGRGVDATVDALRTARGGLSPCRFERAELD--TWIGAVDGLDAQPV--RADLAdfdcRNNRLAQL-------ALEQD 80
Cdd:cd00834 11 VTPLGNGVEEFWEALLAGRSGIRPITRFDASGFpsRIAGEVPDFDPEDYldRKELR----RMDRFAQFalaaaeeALADA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 81 GFDARVaaavarYGAQRVGVFVGTSTSGILETERAYMRRDPASGALPANFRYTHTHnPYSAAAFVRAYCGLRGPATAISS 160
Cdd:cd00834 87 GLDPEE------LDPERIGVVIGSGIGGLATIEEAYRALLEKGPRRVSPFFVPMAL-PNMAAGQVAIRLGLRGPNYTVST 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 161 ACSSGAKVFGSARRMIEAGLIDAAVVGGVDTLC-LTTLYGFNSLELLSRQ------PCRPFDVARDGISIGEAAAFALLE 233
Cdd:cd00834 160 ACASGAHAIGDAARLIRLGRADVVIAGGAEALItPLTLAGFAALRALSTRnddpekASRPFDKDRDGFVLGEGAGVLVLE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 234 RVPAARGTLDDDAILLLGIGESSDAHHMSSPHPEGLGARLAIEQALASAGLDATDIDYVNLHGTATPSNDAAESRAVGAL 313
Cdd:cd00834 240 SLEHAKARGAKIYAEILGYGASSDAYHITAPDPDGEGAARAMRAALADAGLSPEDIDYINAHGTSTPLNDAAESKAIKRV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 314 LA----RTPCSSTKGATGHTLGAAGALEAVITALALREGFVPAGVNTTQPDPALAADYVL-ASRAAQMRTALSNSFGFGG 388
Cdd:cd00834 320 FGehakKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPECDLDYVPnEAREAPIRYALSNSFGFGG 399
|
....*..
gi 981242683 389 TNCTLVF 395
Cdd:cd00834 400 HNASLVF 406
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
12-398 |
4.08e-116 |
|
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: 344.77 E-value: 4.08e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 12 TSCIGRGVDATVDALRTARGGLSPC-RFERAELDTWIGA-VDGLD-AQPVRADLADFDCRNNRLA----QLALEQDGFDA 84
Cdd:COG0304 11 VSPLGNGVEEFWEALLAGRSGIRPItRFDASGLPVRIAGeVKDFDpEEYLDRKELRRMDRFTQYAlaaaREALADAGLDL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 85 RVaaavarYGAQRVGVFVGTSTSGILETERAYMRRDpASGALPANFRYTHTHNPYSAAAFVRAYCGLRGPATAISSACSS 164
Cdd:COG0304 91 DE------VDPDRTGVIIGSGIGGLDTLEEAYRALL-EKGPRRVSPFFVPMMMPNMAAGHVSIRFGLKGPNYTVSTACAS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 165 GAKVFGSARRMIEAGLIDAAVVGGVD-TLCLTTLYGFNSLELLSRQ------PCRPFDVARDGISIGEAAAFALLERVPA 237
Cdd:COG0304 164 GAHAIGEAYRLIRRGRADVMIAGGAEaAITPLGLAGFDALGALSTRnddpekASRPFDKDRDGFVLGEGAGVLVLEELEH 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 238 A--RGtldddA-IL--LLGIGESSDAHHMSSPHPEGLGARLAIEQALASAGLDATDIDYVNLHGTATPSNDAAESRAVGA 312
Cdd:COG0304 244 AkaRG-----AkIYaeVVGYGASSDAYHITAPAPDGEGAARAMRAALKDAGLSPEDIDYINAHGTSTPLGDAAETKAIKR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 313 LL----ARTPCSSTKGATGHTLGAAGALEAVITALALREGFVPAGVNTTQPDPALAADYVL-ASRAAQMRTALSNSFGFG 387
Cdd:COG0304 319 VFgdhaYKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPECDLDYVPnEAREAKIDYALSNSFGFG 398
|
410
....*....|.
gi 981242683 388 GTNCTLVFGRA 398
Cdd:COG0304 399 GHNASLVFKRY 409
|
|
| Ketoacyl-synt_C |
pfam02801 |
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
249-355 |
8.87e-33 |
|
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: 119.60 E-value: 8.87e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 249 LLGIGESSDAHHMSSPHPEGLGARLAIEQALASAGLDATDIDYVNLHGTATPSNDAAESRAVGALLARTPC------SST 322
Cdd:pfam02801 4 IKGSAVNHDGRHNGLTAPNGEGQARAIRRALADAGVDPEDVDYVEAHGTGTPLGDPIEAEALKRVFGSGARkqplaiGSV 83
|
90 100 110
....*....|....*....|....*....|...
gi 981242683 323 KGATGHTLGAAGALEAVITALALREGFVPAGVN 355
Cdd:pfam02801 84 KSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLN 116
|
|
| omega_3_PfaA |
TIGR02813 |
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ... |
212-401 |
9.11e-19 |
|
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: 88.91 E-value: 9.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 212 RPFDVARDGISIGEAAAFALLERVPAARGTLDDDAILLLGIGESSDAHHMS--SPHPEGLGArlAIEQALASAGLDATDI 289
Cdd:TIGR02813 258 QPFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGKFKSiyAPRPEGQAK--ALKRAYDDAGFAPHTC 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 290 DYVNLHGTATPSNDAAESRAVGALLAR-------TPCSSTKGATGHTLGAAGALEAVITALALREGFVPAGVNTTQPDPA 362
Cdd:TIGR02813 336 GLIEAHGTGTAAGDVAEFGGLVSVFSQdndqkqhIALGSVKSQIGHTKSTAGTAGMIKAVLALHHKVLPPTINVDQPNPK 415
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 981242683 363 LAAD---YVLASRA--------AQMRTALSNSFGFGGTNCTLVFG--RADHA 401
Cdd:TIGR02813 416 LDIEnspFYLNTETrpwmqredGTPRRAGISSFGFGGTNFHMVLEeySPKHQ 467
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
155-394 |
1.48e-15 |
|
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: 76.60 E-value: 1.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 155 ATAISSACSSGAKVFGSARRMIEAGLIDAAVVGGVdTLCLT--TLYGFNSLELLSRQ-PCRPFDVARDGISIGEAAAFAL 231
Cdd:smart00825 90 SVTVDTACSSSLVALHLACQSLRSGECDMALAGGV-NLILSpdTFVGLSRAGMLSPDgRCKTFDASADGYVRGEGVGVVV 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 232 LERVPAARgtLDDDAIL--LLGIGESSDAhhmssphpeglgarlaieqalASAGLdatdidyvnlhgTAtPSNDAaeSRA 309
Cdd:smart00825 169 LKRLSDAL--RDGDPILavIRGSAVNQDG---------------------RSNGI------------TA-PSGPA--QLL 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 310 VGallartpcsSTKGATGHTLGAAGaLEAVI-TALALREGFVPAGVNTTQPDPALAAD----YVLAS-----RAAQMRTA 379
Cdd:smart00825 211 IG---------SVKSNIGHLEAAAG-VAGLIkVVLALKHGVIPPTLHFETPNPHIDLEesplRVPTEltpwpPPGRPRRA 280
|
250
....*....|....*
gi 981242683 380 LSNSFGFGGTNCTLV 394
Cdd:smart00825 281 GVSSFGFGGTNAHVI 295
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09185 |
PRK09185 |
beta-ketoacyl-ACP synthase; |
1-399 |
0e+00 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236398 [Multi-domain] Cd Length: 392 Bit Score: 624.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 1 MNPLLLSHFTSTSCIGRGVDATVDALRTAR-GGLSPCRFERAELDTWIGAVDGLDAQPVRADLADFDCRNNRLAQLALEQ 79
Cdd:PRK09185 1 MTPVYISAFGATSALGRGLDAILAALRAGRaSGMRPCDFWLVDLPTWVGEVVGVELPALPAALAAFDCRNNRLALLALQQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 80 dgFDARVAAAVARYGAQRVGVFVGTSTSGILETERAYMRRDPASGALPANFRYTHtHNPYSAAAFVRAYCGLRGPATAIS 159
Cdd:PRK09185 81 --IEPAVEAAIARYGADRIGVVLGTSTSGILEGELAYRRRDPAHGALPADYHYAQ-QELGSLADFLRAYLGLSGPAYTIS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 160 SACSSGAKVFGSARRMIEAGLIDAAVVGGVDTLCLTTLYGFNSLELLSRQPCRPFDVARDGISIGEAAAFALLERVPaar 239
Cdd:PRK09185 158 TACSSSAKVFASARRLLEAGLCDAAIVGGVDSLCRLTLNGFNSLESLSPQPCRPFSANRDGINIGEAAAFFLLERED--- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 240 gtldDDAILLLGIGESSDAHHMSSPHPEGLGARLAIEQALASAGLDATDIDYVNLHGTATPSNDAAESRAVGALL-ARTP 318
Cdd:PRK09185 235 ----DAAVALLGVGESSDAHHMSAPHPEGLGAILAMQQALADAGLAPADIGYINLHGTATPLNDAMESRAVAAVFgDGVP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 319 CSSTKGATGHTLGAAGALEAVITALALREGFVPAGVNTTQPDPALAADYVLASR-AAQMRTALSNSFGFGGTNCTLVFGR 397
Cdd:PRK09185 311 CSSTKGLTGHTLGAAGAVEAAICWLALRHGLPPHGWNTGQPDPALPPLYLVENAqALAIRYVLSNSFAFGGNNCSLIFGR 390
|
..
gi 981242683 398 AD 399
Cdd:PRK09185 391 AD 392
|
|
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
12-395 |
4.89e-126 |
|
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: 369.95 E-value: 4.89e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 12 TSCIGRGVDATVDALRTARGGLSPCRFERAELD--TWIGAVDGLDAQPV--RADLAdfdcRNNRLAQL-------ALEQD 80
Cdd:cd00834 11 VTPLGNGVEEFWEALLAGRSGIRPITRFDASGFpsRIAGEVPDFDPEDYldRKELR----RMDRFAQFalaaaeeALADA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 81 GFDARVaaavarYGAQRVGVFVGTSTSGILETERAYMRRDPASGALPANFRYTHTHnPYSAAAFVRAYCGLRGPATAISS 160
Cdd:cd00834 87 GLDPEE------LDPERIGVVIGSGIGGLATIEEAYRALLEKGPRRVSPFFVPMAL-PNMAAGQVAIRLGLRGPNYTVST 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 161 ACSSGAKVFGSARRMIEAGLIDAAVVGGVDTLC-LTTLYGFNSLELLSRQ------PCRPFDVARDGISIGEAAAFALLE 233
Cdd:cd00834 160 ACASGAHAIGDAARLIRLGRADVVIAGGAEALItPLTLAGFAALRALSTRnddpekASRPFDKDRDGFVLGEGAGVLVLE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 234 RVPAARGTLDDDAILLLGIGESSDAHHMSSPHPEGLGARLAIEQALASAGLDATDIDYVNLHGTATPSNDAAESRAVGAL 313
Cdd:cd00834 240 SLEHAKARGAKIYAEILGYGASSDAYHITAPDPDGEGAARAMRAALADAGLSPEDIDYINAHGTSTPLNDAAESKAIKRV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 314 LA----RTPCSSTKGATGHTLGAAGALEAVITALALREGFVPAGVNTTQPDPALAADYVL-ASRAAQMRTALSNSFGFGG 388
Cdd:cd00834 320 FGehakKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPECDLDYVPnEAREAPIRYALSNSFGFGG 399
|
....*..
gi 981242683 389 TNCTLVF 395
Cdd:cd00834 400 HNASLVF 406
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
12-398 |
4.08e-116 |
|
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: 344.77 E-value: 4.08e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 12 TSCIGRGVDATVDALRTARGGLSPC-RFERAELDTWIGA-VDGLD-AQPVRADLADFDCRNNRLA----QLALEQDGFDA 84
Cdd:COG0304 11 VSPLGNGVEEFWEALLAGRSGIRPItRFDASGLPVRIAGeVKDFDpEEYLDRKELRRMDRFTQYAlaaaREALADAGLDL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 85 RVaaavarYGAQRVGVFVGTSTSGILETERAYMRRDpASGALPANFRYTHTHNPYSAAAFVRAYCGLRGPATAISSACSS 164
Cdd:COG0304 91 DE------VDPDRTGVIIGSGIGGLDTLEEAYRALL-EKGPRRVSPFFVPMMMPNMAAGHVSIRFGLKGPNYTVSTACAS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 165 GAKVFGSARRMIEAGLIDAAVVGGVD-TLCLTTLYGFNSLELLSRQ------PCRPFDVARDGISIGEAAAFALLERVPA 237
Cdd:COG0304 164 GAHAIGEAYRLIRRGRADVMIAGGAEaAITPLGLAGFDALGALSTRnddpekASRPFDKDRDGFVLGEGAGVLVLEELEH 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 238 A--RGtldddA-IL--LLGIGESSDAHHMSSPHPEGLGARLAIEQALASAGLDATDIDYVNLHGTATPSNDAAESRAVGA 312
Cdd:COG0304 244 AkaRG-----AkIYaeVVGYGASSDAYHITAPAPDGEGAARAMRAALKDAGLSPEDIDYINAHGTSTPLGDAAETKAIKR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 313 LL----ARTPCSSTKGATGHTLGAAGALEAVITALALREGFVPAGVNTTQPDPALAADYVL-ASRAAQMRTALSNSFGFG 387
Cdd:COG0304 319 VFgdhaYKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPECDLDYVPnEAREAKIDYALSNSFGFG 398
|
410
....*....|.
gi 981242683 388 GTNCTLVFGRA 398
Cdd:COG0304 399 GHNASLVFKRY 409
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
12-397 |
2.43e-81 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 255.48 E-value: 2.43e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 12 TSCIGRGVDATVDALRTARGGLSPC-RFERAELDTWIGA-VDGLDAQP--VRADLADFDcrnnRLAQL-------ALEQD 80
Cdd:PRK07314 12 VSPLGNDVESTWKNLLAGKSGIGPItHFDTSDLAVKIAGeVKDFNPDDymSRKEARRMD----RFIQYgiaaakqAVEDA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 81 GFDARVAaavaryGAQRVGVFVGTSTSG---ILETERAYMRRDPA-------SGALPaNFryththnpysAAAFVRAYCG 150
Cdd:PRK07314 88 GLEITEE------NADRIGVIIGSGIGGletIEEQHITLLEKGPRrvspffvPMAII-NM----------AAGHVSIRYG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 151 LRGPATAISSACSSGAKVFGSARRMIEAGLIDAAVVGGVD-TLCLTTLYGFNSLELLS------RQPCRPFDVARDGISI 223
Cdd:PRK07314 151 AKGPNHSIVTACATGAHAIGDAARLIAYGDADVMVAGGAEaAITPLGIAGFAAARALStrnddpERASRPFDKDRDGFVM 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 224 GEAAAFALLERVPAA--RGTldddAIL--LLGIGESSDAHHMSSPHPEGLGARLAIEQALASAGLDATDIDYVNLHGTAT 299
Cdd:PRK07314 231 GEGAGILVLEELEHAkaRGA----KIYaeVVGYGMTGDAYHMTAPAPDGEGAARAMKLALKDAGINPEDIDYINAHGTST 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 300 PSNDAAESRAVGALL----ARTPCSSTKGATGHTLGAAGALEAVITALALREGFVPAGVNTTQPDPALAADYV-LASRAA 374
Cdd:PRK07314 307 PAGDKAETQAIKRVFgehaYKVAVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPTINLDNPDEECDLDYVpNEARER 386
|
410 420
....*....|....*....|...
gi 981242683 375 QMRTALSNSFGFGGTNCTLVFGR 397
Cdd:PRK07314 387 KIDYALSNSFGFGGTNASLVFKR 409
|
|
| PTZ00050 |
PTZ00050 |
3-oxoacyl-acyl carrier protein synthase; Provisional |
50-397 |
1.19e-65 |
|
3-oxoacyl-acyl carrier protein synthase; Provisional
Pssm-ID: 240245 [Multi-domain] Cd Length: 421 Bit Score: 215.33 E-value: 1.19e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 50 VDGLDAQPVRADLADFDCRNNRLA----QLALEQDGFDARVAAAvarygAQRVGVFVGTSTSGILETERAYmrrdpasgA 125
Cdd:PTZ00050 58 VDQSEFDPSDFAPTKRESRATHFAmaaaREALADAKLDILSEKD-----QERIGVNIGSGIGSLADLTDEM--------K 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 126 LPANFRYTHThNPY--------SAAAFVRAYCGLRGPATAISSACSSGAKVFGSARRMIEAGLIDAAVVGGVDTlCLTTL 197
Cdd:PTZ00050 125 TLYEKGHSRV-SPYfipkilgnMAAGLVAIKHKLKGPSGSAVTACATGAHCIGEAFRWIKYGEADIMICGGTEA-SITPV 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 198 --YGFNSLELLSRQ-------PCRPFDVARDGISIGEAAAFALLERVPAA--RGTldddAIL--LLGIGESSDAHHMSSP 264
Cdd:PTZ00050 203 sfAGFSRMRALCTKynddpqrASRPFDKDRAGFVMGEGAGILVLEELEHAlrRGA----KIYaeIRGYGSSSDAHHITAP 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 265 HPEGLGARLAIEQALA-SAGLDATDIDYVNLHGTATPSNDAAESRAVGALLARTPC-----SSTKGATGHTLGAAGALEA 338
Cdd:PTZ00050 279 HPDGRGARRCMENALKdGANININDVDYVNAHATSTPIGDKIELKAIKKVFGDSGApklyvSSTKGGLGHLLGAAGAVES 358
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 981242683 339 VITALALREGFVPAGVNTTQPDPALAADYVLASRAAQM---RTALSNSFGFGGTNCTLVFGR 397
Cdd:PTZ00050 359 IVTILSLYEQIIPPTINLENPDAECDLNLVQGKTAHPLqsiDAVLSTSFGFGGVNTALLFTK 420
|
|
| PRK06333 |
PRK06333 |
beta-ketoacyl-ACP synthase; |
141-397 |
4.71e-65 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235781 [Multi-domain] Cd Length: 424 Bit Score: 213.71 E-value: 4.71e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 141 AAAFVRAYCGLRGPATAISSACSSGAKVFGSARRMIEAGLIDAAVVGGVDTlCLT--TLYGFNSLELLS-------RQPC 211
Cdd:PRK06333 152 AAGHVSIRYGFKGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGGTEA-AIDrvSLAGFAAARALStrfndapEQAS 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 212 RPFDVARDGISIGEAAAFALLERVPAA--RGTldddAIL--LLGIGESSDAHHMSSPHPEGLGARLAIEQALASAGLDAT 287
Cdd:PRK06333 231 RPFDRDRDGFVMGEGAGILVIETLEHAlaRGA----PPLaeLVGYGTSADAYHMTAGPEDGEGARRAMLIALRQAGIPPE 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 288 DIDYVNLHGTATPSNDAAESRAVGALLAR---TPCSSTKGATGHTLGAAGALEAVITALALREGFVPAGVNTTQPDPALA 364
Cdd:PRK06333 307 EVQHLNAHATSTPVGDLGEVAAIKKVFGHvsgLAVSSTKSATGHLLGAAGGVEAIFTILALRDQIAPPTLNLENPDPAAE 386
|
250 260 270
....*....|....*....|....*....|....*
gi 981242683 365 A-DYV-LASRAAQMRTALSNSFGFGGTNCTLVFGR 397
Cdd:PRK06333 387 GlDVVaNKARPMDMDYALSNGFGFGGVNASILFRR 421
|
|
| PLN02836 |
PLN02836 |
3-oxoacyl-[acyl-carrier-protein] synthase |
141-395 |
1.16e-64 |
|
3-oxoacyl-[acyl-carrier-protein] synthase
Pssm-ID: 215449 [Multi-domain] Cd Length: 437 Bit Score: 213.12 E-value: 1.16e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 141 AAAFVRAYCGLRGPATAISSACSSGAKVFGSARRMIEAGLIDAAVVGG----VDTLCLTtlyGFNSLELLS-------RQ 209
Cdd:PLN02836 163 AAGHVSIRYGFQGPNHAAVTACATGAHSIGDAFRMIQFGDADVMVAGGtessIDALSIA---GFSRSRALStkfnscpTE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 210 PCRPFDVARDGISIGEAAAFALLERVPAARGTLDDDAILLLGIGESSDAHHMSSPHPEGLGARLAIEQALASAGLDATDI 289
Cdd:PLN02836 240 ASRPFDCDRDGFVIGEGAGVLVLEELEHAKRRGAKIYAEVRGYGMSGDAHHITQPHEDGRGAVLAMTRALQQSGLHPNQV 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 290 DYVNLHGTATPSNDAAESRAVGALLA------RTPCSSTKGATGHTLGAAGALEAVITALALREGFVPAGVNTTQPDPAL 363
Cdd:PLN02836 320 DYVNAHATSTPLGDAVEARAIKTVFSehatsgGLAFSSTKGATGHLLGAAGAVEAIFSVLAIHHGIAPPTLNLERPDPIF 399
|
250 260 270
....*....|....*....|....*....|....
gi 981242683 364 AADYV--LASRAAQMRTALSNSFGFGGTNCTLVF 395
Cdd:PLN02836 400 DDGFVplTASKAMLIRAALSNSFGFGGTNASLLF 433
|
|
| PRK08439 |
PRK08439 |
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed |
144-395 |
1.03e-60 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
Pssm-ID: 236265 [Multi-domain] Cd Length: 406 Bit Score: 201.89 E-value: 1.03e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 144 FVRAYCGLRGPATAISSACSSGAKVFGSARRMIEAGLIDAA-VVGGVDTLCLTTLYGFNSLELLS------RQPCRPFDV 216
Cdd:PRK08439 144 FISIEHGLKGPNLSSVTACAAGTHAIIEAVKTIMLGGADKMlVVGAESAICPVGIGGFAAMKALStrnddpKKASRPFDK 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 217 ARDGISIGEAAAFALLERVPAA--RGTldddAIL--LLGIGESSDAHHMSSPHPEGlgARLAIEQALASAGldATDIDYV 292
Cdd:PRK08439 224 DRDGFVMGEGAGALVLEEYESAkkRGA----KIYaeIIGFGESGDANHITSPAPEG--PLRAMKAALEMAG--NPKIDYI 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 293 NLHGTATPSNDAAESRAVGALLART----PCSSTKGATGHTLGAAGALEAVITALALREGFVPAGVNTTQPDPALAADYV 368
Cdd:PRK08439 296 NAHGTSTPYNDKNETAALKELFGSKekvpPVSSTKGQIGHCLGAAGAIEAVISIMAMRDGILPPTINQETPDPECDLDYI 375
|
250 260
....*....|....*....|....*...
gi 981242683 369 L-ASRAAQMRTALSNSFGFGGTNCTLVF 395
Cdd:PRK08439 376 PnVARKAELNVVMSNSFGFGGTNGVVIF 403
|
|
| PRK09116 |
PRK09116 |
beta-ketoacyl-ACP synthase; |
138-396 |
3.77e-60 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 181657 [Multi-domain] Cd Length: 405 Bit Score: 200.60 E-value: 3.77e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 138 PYSAAAFVRAYCGLRGPATAISSACSSGAKVFGSARRMIEAGLIDAAVVGGVDTLCLTTLYGFNSLELLSRQ-------P 210
Cdd:PRK09116 140 PHTTAVNVGLFFGLKGRVIPTSSACTSGSQGIGYAYEAIKYGYQTVMLAGGAEELCPTEAAVFDTLFATSTRndapeltP 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 211 cRPFDVARDGISIGEAAAFALLERV--PAARGtldddAIL---LLGIGESSDAHHMSSPHPEGLgaRLAIEQALASAGLD 285
Cdd:PRK09116 220 -RPFDANRDGLVIGEGAGTLVLEELehAKARG-----ATIyaeIVGFGTNSDGAHVTQPQAETM--QIAMELALKDAGLA 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 286 ATDIDYVNLHGTATPSNDAAESRAVGALL-ARTPCSSTKGATGHTLGAAGALEAVITALALREGFVPAGVNTTQPDPALA 364
Cdd:PRK09116 292 PEDIGYVNAHGTATDRGDIAESQATAAVFgARMPISSLKSYFGHTLGACGALEAWMSIEMMNEGWFAPTLNLTQVDPACG 371
|
250 260 270
....*....|....*....|....*....|....
gi 981242683 365 A-DYVLA-SRAAQMRTALSNSFGFGGTNCTLVFG 396
Cdd:PRK09116 372 AlDYIMGeAREIDTEYVMSNNFAFGGINTSLIFK 405
|
|
| PRK05952 |
PRK05952 |
beta-ketoacyl-ACP synthase; |
99-397 |
1.56e-55 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 187.57 E-value: 1.56e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 99 GVFVGTSTS--GILETERAYMRRDPAS---GALPANFRYTHTHNPYSAAAfvrAYCGLRGPATAISSACSSGAKVFGSAR 173
Cdd:PRK05952 81 GVVIGSSRGcqGQWEKLARQMYQGDDSpdeELDLENWLDTLPHQAAIAAA---RQIGTQGPVLAPMAACATGLWAIAQGV 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 174 RMIEAGLIDAAVVGGVDT-LCLTTLYGFNSLELLSRQPCRPFDVARDGISIGEAAAFALLERVPAA--RGTldddAIL-- 248
Cdd:PRK05952 158 ELIQTGQCQRVIAGAVEApITPLTLAGFQQMGALAKTGAYPFDRQREGLVLGEGGAILVLESAELAqkRGA----KIYgq 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 249 LLGIGESSDAHHMSSPHPEGLGARLAIEQALASAGLDATDIDYVNLHGTATPSNDAAESRAVGALL-ARTPCSSTKGATG 327
Cdd:PRK05952 234 ILGFGLTCDAYHMSAPEPDGKSAIAAIQQCLARSGLTPEDIDYIHAHGTATRLNDQREANLIQALFpHRVAVSSTKGATG 313
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 328 HTLGAAGALEAVITALALREGFVPAGVNTTQPDPALaaDYVLASRAAQMRTALSNSFGFGGTNCTLVFGR 397
Cdd:PRK05952 314 HTLGASGALGVAFSLLALRHQQLPPCVGLQEPEFDL--NFVRQAQQSPLQNVLCLSFGFGGQNAAIALGK 381
|
|
| PRK08722 |
PRK08722 |
beta-ketoacyl-ACP synthase II; |
150-397 |
2.70e-54 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 181539 [Multi-domain] Cd Length: 414 Bit Score: 185.21 E-value: 2.70e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 150 GLRGPATAISSACSSGAKVFGSARRMIEAGLIDAAVVGGVDTLCLTT-LYGFNSLELLS------RQPCRPFDVARDGIS 222
Cdd:PRK08722 152 GLRGPNIAISTACTTGLHNIGHAARMIAYGDADAMVAGGAEKASTPLgMAGFGAAKALStrndepQKASRPWDKDRDGFV 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 223 IGEAAAFALLERVPAARGTLDDDAILLLGIGESSDAHHMSSPHPEGLGARLAIEQALASAGLDATDIDYVNLHGTATPSN 302
Cdd:PRK08722 232 LGDGAGMMVLEEYEHAKARGAKIYAELVGFGMSGDAYHMTSPSEDGSGGALAMEAAMRDAGVTGEQIGYVNAHGTSTPAG 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 303 DAAESRAVGALLARTPC-----SSTKGATGHTLGAAGALEAVITALALREGFVPAGVNTTQPDPALAADYV--LASRAAQ 375
Cdd:PRK08722 312 DVAEIKGIKRALGEAGSkqvlvSSTKSMTGHLLGAAGSVEAIITVMSLVDQIVPPTINLDDPEEGLDIDLVphTARKVES 391
|
250 260
....*....|....*....|..
gi 981242683 376 MRTALSNSFGFGGTNCTLVFGR 397
Cdd:PRK08722 392 MEYAICNSFGFGGTNGSLIFKK 413
|
|
| PRK07910 |
PRK07910 |
beta-ketoacyl-ACP synthase; |
97-398 |
7.02e-54 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236129 [Multi-domain] Cd Length: 418 Bit Score: 184.16 E-value: 7.02e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 97 RVGVFVGTSTSGILETERAY--MRrdpASGALPANFRYTHTHNPYSAAAFVRAYCGLRGPATAISSACSSGAKVFGSARR 174
Cdd:PRK07910 107 RLMVSIGTGLGSAEELVFAYddMR---ARGLRAVSPLAVQMYMPNGPAAAVGLERHAKAGVITPVSACASGSEAIAQAWR 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 175 MIEAGLIDAAVVGGVDT-LCLTTLYGFNSLEL-LSRQ------PCRPFDVARDGISIGEAAAFALLERVPAARGTLDDDA 246
Cdd:PRK07910 184 QIVLGEADIAICGGVETrIEAVPIAGFAQMRIvMSTNnddpagACRPFDKDRDGFVFGEGGALMVIETEEHAKARGANIL 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 247 ILLLGIGESSDAHHMSSPHPEGLGARLAIEQALASAGLDATDIDYVNLHGTATPSNDAAESRAVGALLA--RTPCSSTKG 324
Cdd:PRK07910 264 ARIMGASITSDGFHMVAPDPNGERAGHAMTRAIELAGLTPGDIDHVNAHATGTSVGDVAEGKAINNALGghRPAVYAPKS 343
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 981242683 325 ATGHTLGAAGALEAVITALALREGFVPAGVNTTQPDPALAADYVLAS-RAAQMRTALSNSFGFGGTNCTLVFGRA 398
Cdd:PRK07910 344 ALGHSVGAVGAVESILTVLALRDGVIPPTLNLENLDPEIDLDVVAGEpRPGNYRYAINNSFGFGGHNVALAFGRY 418
|
|
| PRK06501 |
PRK06501 |
beta-ketoacyl-ACP synthase; |
150-397 |
1.60e-48 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235817 [Multi-domain] Cd Length: 425 Bit Score: 170.20 E-value: 1.60e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 150 GLRGPATAISSACSSGAKVFGSARRMIEAGLIDAAVVGGVD-TLCLTTLYGFNSLELLSRQ------PCRPFDVARDGIS 222
Cdd:PRK06501 163 GTRGLPISLSTACASGATAIQLGVEAIRRGETDRALCIATDgSVSAEALIRFSLLSALSTQndppekASKPFSKDRDGFV 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 223 IGEAAAFALLERVPAA--RGTldddAIL--LLGIGESSDAHHMSSPHPEGLGARLAIEQALASAGLDATDIDYVNLHGTA 298
Cdd:PRK06501 243 MAEGAGALVLESLESAvaRGA----KILgiVAGCGEKADSFHRTRSSPDGSPAIGAIRAALADAGLTPEQIDYINAHGTS 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 299 TPSNDAAE----SRAVGALLARTPCSSTKGATGHTLGAAGALEAVITALALREGFVPAGVNTTQPDPALAADYVL-ASRA 373
Cdd:PRK06501 319 TPENDKMEylglSAVFGERLASIPVSSNKSMIGHTLTAAGAVEAVFSLLTIQTGRLPPTINYDNPDPAIPLDVVPnVARD 398
|
250 260
....*....|....*....|....
gi 981242683 374 AQMRTALSNSFGFGGTNCTLVFGR 397
Cdd:PRK06501 399 ARVTAVLSNSFGFGGQNASLVLTA 422
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
97-394 |
5.19e-48 |
|
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: 168.89 E-value: 5.19e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 97 RVGVFVGTSTSGileteraYMRRDPASGALPANFRYTHTHNPYSAAAFvrAYC-GLRGPATAISSACSSGAKVFGSARRM 175
Cdd:cd00833 113 RTGVFVGASSSD-------YLELLARDPDEIDAYAATGTSRAFLANRI--SYFfDLRGPSLTVDTACSSSLVALHLACQS 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 176 IEAGLIDAAVVGGVDTLC-LTTLYGFNSLELLSRQP-CRPFDVARDGISIGEAAAFALLERVPAARgtLDDDAIL--LLG 251
Cdd:cd00833 184 LRSGECDLALVGGVNLILsPDMFVGFSKAGMLSPDGrCRPFDADADGYVRGEGVGVVVLKRLSDAL--RDGDRIYavIRG 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 252 IGESSDAH--HMSSPHPEGlgARLAIEQALASAGLDATDIDYVNLHGTATPSNDAAESRAVGALLAR-----TPC--SST 322
Cdd:cd00833 262 SAVNQDGRtkGITAPSGEA--QAALIRRAYARAGVDPSDIDYVEAHGTGTPLGDPIEVEALAKVFGGsrsadQPLliGSV 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 323 KGATGHTLGAAGALEAVITALALREGFVPAGVNTTQPDPALAAD----YVLAS-----RAAQMRTALSNSFGFGGTNCTL 393
Cdd:cd00833 340 KSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKIDFEesplRVPTEarpwpAPAGPRRAGVSSFGFGGTNAHV 419
|
.
gi 981242683 394 V 394
Cdd:cd00833 420 I 420
|
|
| PRK14691 |
PRK14691 |
3-oxoacyl-(acyl carrier protein) synthase II; Provisional |
141-397 |
1.50e-47 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
Pssm-ID: 173154 [Multi-domain] Cd Length: 342 Bit Score: 165.67 E-value: 1.50e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 141 AAAFVRAYCGLRGPATAISSACSSGAKVFGSARRMIEAGLIDAAVVGGVDTLCLT-TLYGFNSLELLS-------RQPCR 212
Cdd:PRK14691 70 AAGHVSIKHHFKGPIGAPVTACAAGVQAIGDAVRMIRNNEADVALCGGAEAVIDTvSLAGFAAARALSthfnstpEKASR 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 213 PFDVARDGISIGEAAAFALLERVPAARGTLDDDAILLLGIGESSDAHHMSSPHPEGLGARLAIEQALASAGLDATDIDYV 292
Cdd:PRK14691 150 PFDTARDGFVMGEGAGLLIIEELEHALARGAKPLAEIVGYGTSADAYHMTSGAEDGDGAYRAMKIALRQAGITPEQVQHL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 293 NLHGTATPSNDAAESRAVGALLART---PCSSTKGATGHTLGAAGALEAVITALALREGFVPAGVNTTQPDPALAADYVL 369
Cdd:PRK14691 230 NAHATSTPVGDLGEINAIKHLFGESnalAITSTKSATGHLLGAAGGLETIFTVLALRDQIVPATLNLENPDPAAKGLNII 309
|
250 260 270
....*....|....*....|....*....|
gi 981242683 370 ASRAA--QMRTALSNSFGFGGTNCTLVFGR 397
Cdd:PRK14691 310 AGNAQphDMTYALSNGFGFAGVNASILLKR 339
|
|
| PLN02787 |
PLN02787 |
3-oxoacyl-[acyl-carrier-protein] synthase II |
150-395 |
3.31e-43 |
|
3-oxoacyl-[acyl-carrier-protein] synthase II
Pssm-ID: 215421 [Multi-domain] Cd Length: 540 Bit Score: 158.60 E-value: 3.31e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 150 GLRGPATAISSACSSGAKVFGSARRMIEAGLIDAAVVGGVDTLCLTT-LYGFNSLELLSR------QPCRPFDVARDGIS 222
Cdd:PLN02787 279 GWMGPNYSISTACATSNFCILNAANHIIRGEADVMLCGGSDAAIIPIgLGGFVACRALSQrnddptKASRPWDMNRDGFV 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 223 IGEAAAFALLERVPAARGTLDDDAILLLGIGESSDAHHMSSPHPEGLGARLAIEQALASAGLDATDIDYVNLHGTATPSN 302
Cdd:PLN02787 359 MGEGAGVLLLEELEHAKKRGANIYAEFLGGSFTCDAYHMTEPHPEGAGVILCIEKALAQSGVSKEDVNYINAHATSTKAG 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 303 DAAESRAVGALLARTP---CSSTKGATGHTLGAAGALEAVITALALREGFVPAGVNTTQPDPALAADYVLASRAAQM--R 377
Cdd:PLN02787 439 DLKEYQALMRCFGQNPelrVNSTKSMIGHLLGAAGAVEAIATVQAIRTGWVHPNINLENPESGVDTKVLVGPKKERLdiK 518
|
250
....*....|....*...
gi 981242683 378 TALSNSFGFGGTNCTLVF 395
Cdd:PLN02787 519 VALSNSFGFGGHNSSILF 536
|
|
| PRK07967 |
PRK07967 |
beta-ketoacyl-ACP synthase I; |
151-399 |
3.79e-43 |
|
beta-ketoacyl-ACP synthase I;
Pssm-ID: 181184 [Multi-domain] Cd Length: 406 Bit Score: 155.60 E-value: 3.79e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 151 LRGPATAISSACSSGAKVFGSARRMIEAGLIDAAVVGGVDTLCLTTLYGFNSLELLSRQ-------PCRPFDVARDGISI 223
Cdd:PRK07967 151 IKGVNYSISSACATSAHCIGNAVEQIQLGKQDIVFAGGGEELDWEMSCLFDAMGALSTKyndtpekASRAYDANRDGFVI 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 224 GEAAAFALLERV--PAARGTLDDDAILllGIGESSDAHHMSSPhpEGLGARLAIEQALAsaGLDaTDIDYVNLHGTATPS 301
Cdd:PRK07967 231 AGGGGVVVVEELehALARGAKIYAEIV--GYGATSDGYDMVAP--SGEGAVRCMQMALA--TVD-TPIDYINTHGTSTPV 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 302 NDAAESRAVGALLART--PCSSTKGATGHTLGAAGALEAVITALALREGFVPAGVNTTQPDPALAADYVLASRA--AQMR 377
Cdd:PRK07967 304 GDVKELGAIREVFGDKspAISATKSLTGHSLGAAGVQEAIYSLLMMEHGFIAPSANIEELDPQAAGMPIVTETTdnAELT 383
|
250 260
....*....|....*....|..
gi 981242683 378 TALSNSFGFGGTNCTLVFGRAD 399
Cdd:PRK07967 384 TVMSNSFGFGGTNATLVFRRYK 405
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
97-394 |
1.88e-42 |
|
"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: 153.75 E-value: 1.88e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 97 RVGVFVGTSTSGILETERAYMRRDPASGALPANfryTHTHNPYSAAAFVRAYCGL-RGPATAISSACSSGAKVFGSARRM 175
Cdd:cd00828 99 EVGVVVGSGMGGLRFLRRGGKLDARAVNPYVSP---KWMLSPNTVAGWVNILLLSsHGPIKTPVGACATALEALDLAVEA 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 176 IEAGLIDAAVVGGVDTLCLTTLYGF-------NSLELLSRQpCRPFDVARDGISIGEAAAFALLERVPAARGTLDDDAIL 248
Cdd:cd00828 176 IRSGKADIVVVGGVEDPLEEGLSGFanmgalsTAEEEPEEM-SRPFDETRDGFVEAEGAGVLVLERAELALARGAPIYGR 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 249 LLGIGESSDAHHMSSPHPeGLGARLAIEQALASAGLDATDIDYVNLHGTATPSNDAAESRAV----GALLARTPCSSTKG 324
Cdd:cd00828 255 VAGTASTTDGAGRSVPAG-GKGIARAIRTALAKAGLSLDDLDVISAHGTSTPANDVAESRAIaevaGALGAPLPVTAQKA 333
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 981242683 325 ATGHTLGAAGALEAVITALALREGFVPAGVNTTQPDPALAAD---YVLASRAAQMRTALSNSFGFGGTNCTLV 394
Cdd:cd00828 334 LFGHSKGAAGALQLIGALQSLEHGLIPPTANLDDVDPDVEHLsvvGLSRDLNLKVRAALVNAFGFGGSNAALV 406
|
|
| PRK07103 |
PRK07103 |
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated |
150-397 |
3.20e-39 |
|
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
Pssm-ID: 180839 [Multi-domain] Cd Length: 410 Bit Score: 145.17 E-value: 3.20e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 150 GLRGPATAISSACSSGAKVFGSARRMIEAGLIDAA-VVGGVDTLCLTTLYGFNSL-----ELLSRQP---CRPFDVARDG 220
Cdd:PRK07103 155 GIRGEGFTVGGASASGQLAVIQAARLVQSGSVDACiAVGALMDLSYWECQALRSLgamgsDRFADEPeaaCRPFDQDRDG 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 221 ISIGEAAAFALLERVPAA--RGTLDDDAilLLGIGESSDAHHMSSPHPEGLGArlAIEQALASAGLDATDIDYVNLHGTA 298
Cdd:PRK07103 235 FIYGEACGAVVLESAESArrRGARPYAK--LLGWSMRLDANRGPDPSLEGEMR--VIRAALRRAGLGPEDIDYVNPHGTG 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 299 TPSNDAAESRAV-GALLARTPCSSTKGATGHTLGAAGALEAVITALALREGFVPAGVNTTQP-DPALaaDYVLA-SRAAQ 375
Cdd:PRK07103 311 SPLGDETELAALfASGLAHAWINATKSLTGHGLSAAGIVELIATLLQMRAGFLHPSRNLDEPiDERF--RWVGStAESAR 388
|
250 260
....*....|....*....|..
gi 981242683 376 MRTALSNSFGFGGTNCTLVFGR 397
Cdd:PRK07103 389 IRYALSLSFGFGGINTALVLER 410
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
95-394 |
1.35e-36 |
|
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: 136.23 E-value: 1.35e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 95 AQRVGVFVGTSTSGILETERAymrrdpaSGALPANFRYTHTHNPYSAAAFVRAY-CGLRGPATAISSACSSGAKVFGSAR 173
Cdd:cd00825 35 NPIVGVVVGTGGGSPRFQVFG-------ADAMRAVGPYVVTKAMFPGASGQIATpLGIHGPAYDVSAACAGSLHALSLAA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 174 RMIEAGLIDAAVVGGVDTLCLT--TLYGFNSLELLSRQPCRPFDVARDGISIGEAAAFALLERVPAARGTLDDDAILLLG 251
Cdd:cd00825 108 DAVQNGKQDIVLAGGSEELAAPmdCEFDAMGALSTPEKASRTFDAAADGFVFGDGAGALVVEELEHALARGAHIYAEIVG 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 252 IGESSDAHHMSSPHPEGLGARLAIEQALASAGLDATDIDYVNLHGTATPSNDAAESRAVGALL--ARTPCSSTKGATGHT 329
Cdd:cd00825 188 TAATIDGAGMGAFAPSAEGLARAAKEALAVAGLTVWDIDYLVAHGTGTPIGDVKELKLLRSEFgdKSPAVSATKAMTGNL 267
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 981242683 330 LGAAGALEAVITALALREGFVPAGVNTTQPDPAlAADYVLASRAAQMRTALSNSFGFGGTNCTLV 394
Cdd:cd00825 268 SSAAVVLAVDEAVLMLEHGFIPPSIHIEELDEA-GLNIVTETTPRELRTALLNGFGLGGTNATLV 331
|
|
| Ketoacyl-synt_C |
pfam02801 |
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
249-355 |
8.87e-33 |
|
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: 119.60 E-value: 8.87e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 249 LLGIGESSDAHHMSSPHPEGLGARLAIEQALASAGLDATDIDYVNLHGTATPSNDAAESRAVGALLARTPC------SST 322
Cdd:pfam02801 4 IKGSAVNHDGRHNGLTAPNGEGQARAIRRALADAGVDPEDVDYVEAHGTGTPLGDPIEAEALKRVFGSGARkqplaiGSV 83
|
90 100 110
....*....|....*....|....*....|...
gi 981242683 323 KGATGHTLGAAGALEAVITALALREGFVPAGVN 355
Cdd:pfam02801 84 KSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLN 116
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
97-409 |
2.10e-32 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 129.99 E-value: 2.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 97 RVGVFVGTSTSGILeterAYMRRDPASGAlpanfRYTHTHNPYSAAAFVRAYC-GLRGPATAISSACSSGAKVFGSARRM 175
Cdd:COG3321 117 RTGVFVGASSNDYA----LLLLADPEAID-----AYALTGNAKSVLAGRISYKlDLRGPSVTVDTACSSSLVAVHLACQS 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 176 IEAGLIDAAVVGGVDTLCL-TTLYGFNSLELLSRQ-PCRPFDVARDGISIGEAAAFALLERVPAARgtLDDDAIL--LLG 251
Cdd:COG3321 188 LRSGECDLALAGGVNLMLTpESFILFSKGGMLSPDgRCRAFDADADGYVRGEGVGVVVLKRLSDAL--RDGDRIYavIRG 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 252 IGESSDAHHMSSPHPEGLGARLAIEQALASAGLDATDIDYVNLHGTATPSNDAAESRAVGALL-----ARTPC--SSTKG 324
Cdd:COG3321 266 SAVNQDGRSNGLTAPNGPAQAAVIRRALADAGVDPATVDYVEAHGTGTPLGDPIEAAALTAAFgqgrpADQPCaiGSVKS 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 325 ATGHTLGAAGALeAVI-TALALREGFVPAGVNTTQPDPALAAD----YVLAS-----RAAQMRTALSNSFGFGGTNCTLV 394
Cdd:COG3321 346 NIGHLEAAAGVA-GLIkAVLALRHGVLPPTLHFETPNPHIDFEnspfYVNTElrpwpAGGGPRRAGVSSFGFGGTNAHVV 424
|
330
....*....|....*
gi 981242683 395 FGRADHASANRREPT 409
Cdd:COG3321 425 LEEAPAAAPAAAAAA 439
|
|
| CLF |
cd00832 |
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ... |
150-394 |
1.17e-25 |
|
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: 107.45 E-value: 1.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 150 GLRGPATAISSACSSGAKVFGSARRMIEAGLiDAAVVGGVD-TLCLTTLYGFNSLELLSR-----QPCRPFDVARDGISI 223
Cdd:cd00832 149 GMRGPSGVVVAEQAGGLDALAQARRLVRRGT-PLVVSGGVDsALCPWGWVAQLSSGRLSTsddpaRAYLPFDAAAAGYVP 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 224 GEAAAFALLERVPAARGTLDDDAILLLGIGESSDAHHmSSPHPEGLGArlAIEQALASAGLDATDIDYVNLHGTATPSND 303
Cdd:cd00832 228 GEGGAILVLEDAAAARERGARVYGEIAGYAATFDPPP-GSGRPPGLAR--AIRLALADAGLTPEDVDVVFADAAGVPELD 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 304 AAESRAVGALLA--RTPCSSTKGATGHTLGAAGALEAVITALALREGFVPAGVNTTQPDPALAADYVLAS-RAAQMRTAL 380
Cdd:cd00832 305 RAEAAALAAVFGprGVPVTAPKTMTGRLYAGGAPLDVATALLALRDGVIPPTVNVTDVPPAYGLDLVTGRpRPAALRTAL 384
|
250
....*....|....
gi 981242683 381 SNSFGFGGTNCTLV 394
Cdd:cd00832 385 VLARGRGGFNSALV 398
|
|
| omega_3_PfaA |
TIGR02813 |
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ... |
212-401 |
9.11e-19 |
|
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: 88.91 E-value: 9.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 212 RPFDVARDGISIGEAAAFALLERVPAARGTLDDDAILLLGIGESSDAHHMS--SPHPEGLGArlAIEQALASAGLDATDI 289
Cdd:TIGR02813 258 QPFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGKFKSiyAPRPEGQAK--ALKRAYDDAGFAPHTC 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 290 DYVNLHGTATPSNDAAESRAVGALLAR-------TPCSSTKGATGHTLGAAGALEAVITALALREGFVPAGVNTTQPDPA 362
Cdd:TIGR02813 336 GLIEAHGTGTAAGDVAEFGGLVSVFSQdndqkqhIALGSVKSQIGHTKSTAGTAGMIKAVLALHHKVLPPTINVDQPNPK 415
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 981242683 363 LAAD---YVLASRA--------AQMRTALSNSFGFGGTNCTLVFG--RADHA 401
Cdd:TIGR02813 416 LDIEnspFYLNTETrpwmqredGTPRRAGISSFGFGGTNFHMVLEeySPKHQ 467
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
76-238 |
5.64e-18 |
|
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: 82.68 E-value: 5.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 76 ALEQDGFDARVAAAVarygaqRVGVFVGTSTSGILETERAYMRRDPASGalpanFRYTHTHNPYSAAAFVRAYCGLRGPA 155
Cdd:pfam00109 98 ALEDAGITPDSLDGS------RTGVFIGSGIGDYAALLLLDEDGGPRRG-----SPFAVGTMPSVIAGRISYFLGLRGPS 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 156 TAISSACSSGAKVFGSARRMIEAGLIDAAVVGGVDT-LCLTTLYGFNSLELLSR-QPCRPFDVARDGISIGEAAAFALLE 233
Cdd:pfam00109 167 VTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLlLTPLGFAGFSAAGMLSPdGPCKAFDPFADGFVRGEGVGAVVLK 246
|
....*
gi 981242683 234 RVPAA 238
Cdd:pfam00109 247 RLSDA 251
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
150-394 |
4.97e-17 |
|
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: 80.18 E-value: 4.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 150 GLRGPATAISSACSSGAKVFGSARRMIEAGLIDAAVVGGVDTlclttlygfnslellsrqpcrpfdvardgISIGEAAAF 229
Cdd:cd00327 56 ISGGPAYSVNQACATGLTALALAVQQVQNGKADIVLAGGSEE-----------------------------FVFGDGAAA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 230 ALLERVPAARGTLDDDAILLLGIGESSDAHHMSsPHPEGLGARLAIEQALASAGLDATDIDYVNLHGTATPSNDAAEsRA 309
Cdd:cd00327 107 AVVESEEHALRRGAHPQAEIVSTAATFDGASMV-PAVSGEGLARAARKALEGAGLTPSDIDYVEAHGTGTPIGDAVE-LA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 310 VGA---LLARTPCSSTKGATGHTLGAAGALEAVITALALREGFVPAgvnttqpdpalaadyvlasRAAQMRTALSNSFGF 386
Cdd:cd00327 185 LGLdpdGVRSPAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIPP-------------------TPREPRTVLLLGFGL 245
|
....*...
gi 981242683 387 GGTNCTLV 394
Cdd:cd00327 246 GGTNAAVV 253
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
155-394 |
1.48e-15 |
|
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: 76.60 E-value: 1.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 155 ATAISSACSSGAKVFGSARRMIEAGLIDAAVVGGVdTLCLT--TLYGFNSLELLSRQ-PCRPFDVARDGISIGEAAAFAL 231
Cdd:smart00825 90 SVTVDTACSSSLVALHLACQSLRSGECDMALAGGV-NLILSpdTFVGLSRAGMLSPDgRCKTFDASADGYVRGEGVGVVV 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 232 LERVPAARgtLDDDAIL--LLGIGESSDAhhmssphpeglgarlaieqalASAGLdatdidyvnlhgTAtPSNDAaeSRA 309
Cdd:smart00825 169 LKRLSDAL--RDGDPILavIRGSAVNQDG---------------------RSNGI------------TA-PSGPA--QLL 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 310 VGallartpcsSTKGATGHTLGAAGaLEAVI-TALALREGFVPAGVNTTQPDPALAAD----YVLAS-----RAAQMRTA 379
Cdd:smart00825 211 IG---------SVKSNIGHLEAAAG-VAGLIkVVLALKHGVIPPTLHFETPNPHIDLEesplRVPTEltpwpPPGRPRRA 280
|
250
....*....|....*
gi 981242683 380 LSNSFGFGGTNCTLV 394
Cdd:smart00825 281 GVSSFGFGGTNAHVI 295
|
|
| PRK06147 |
PRK06147 |
3-oxoacyl-(acyl carrier protein) synthase; Validated |
164-292 |
5.53e-05 |
|
3-oxoacyl-(acyl carrier protein) synthase; Validated
Pssm-ID: 235715 [Multi-domain] Cd Length: 348 Bit Score: 45.01 E-value: 5.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981242683 164 SGAKVFGSARRMIEAGLIDAAVVGGVDTLCLT-TLYGFNSLELLSRQPCrpfdvaRDGISIGEAAAFALLERVPAARGTl 242
Cdd:PRK06147 135 SGAVALAQARRLIAAGGCPRVLVAGVDSLLTGpTLAHYEARDRLLTSQN------SNGFIPGEAAAAVLLGRPAGGEAP- 207
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 981242683 243 dDDAILLLGIGESSDAHHMSSPHP---EGLGArlAIEQALASAGLDATDIDYV 292
Cdd:PRK06147 208 -GLPLLGLGLGREPAPVGESEDLPlrgDGLTQ--AIRAALAEAGCGLEDMDYR 257
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
223-295 |
2.93e-04 |
|
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: 42.64 E-value: 2.93e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 981242683 223 IGEAAAFALLERVPAARgTLDDDAILLLGIGESSDAHHMSSPHPEGL--GARLAIEQALASAGLDATDIDYVNLH 295
Cdd:cd00829 204 VSDGAAAVVLASEERAR-ELTDRPVWILGVGAASDTPSLSERDDFLSldAARLAARRAYKMAGITPDDIDVAELY 277
|
|
| PRK06064 |
PRK06064 |
thiolase domain-containing protein; |
142-208 |
4.47e-03 |
|
thiolase domain-containing protein;
Pssm-ID: 235688 [Multi-domain] Cd Length: 389 Bit Score: 39.11 E-value: 4.47e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 981242683 142 AAFVRAYCGLRG-PATAISSACSSGAKVFGSARRMIEAGLIDAAVVGGVDTlcLTTLYGFNSLELLSR 208
Cdd:PRK06064 64 AALIADYAGLAPiPATRVEAACASGGAALRQAYLAVASGEADVVLAAGVEK--MTDVPTPDATEAIAR 129
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
154-191 |
7.53e-03 |
|
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: 38.12 E-value: 7.53e-03
10 20 30
....*....|....*....|....*....|....*...
gi 981242683 154 PATAISSACSSGAKVFGSARRMIEAGLIDAAVVGGVDT 191
Cdd:COG0183 80 PAVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVES 117
|
|
| |
