|
Name |
Accession |
Description |
Interval |
E-value |
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
7-373 |
6.36e-103 |
|
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: 309.85 E-value: 6.36e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 7 EVWVTGMAWSTALGDDLEVVWQSLLAGRSGIRSVDFPVA--LRSPLASPLPDLDPALPLPERQHR-------LTVATLRR 77
Cdd:cd00834 2 RVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRFDAsgFPSRIAGEVPDFDPEDYLDRKELRrmdrfaqFALAAAEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 78 ALQDAGLAKAT---EEVVPVLATSYG--------------------HHLDVPETESlSRWAVEAAREAGCQHAPITVSTA 134
Cdd:cd00834 82 ALADAGLDPEEldpERIGVVIGSGIGglatieeayrallekgprrvSPFFVPMALP-NMAAGQVAIRLGLRGPNYTVSTA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 135 CSAGADALLLGLSLIRRGFTDTCLCGGAD-ILTPAKRLGHSQLGTLSADGL------RAFDRAHSGTVLGEGAGFLVLET 207
Cdd:cd00834 161 CASGAHAIGDAARLIRLGRADVVIAGGAEaLITPLTLAGFAALRALSTRNDdpekasRPFDKDRDGFVLGEGAGVLVLES 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 208 RAAALARGARPYGILAGAGSANDAVSAVAPDLSGDCLALAVRRALCDAGLTAHEVGCISTHGTGTRLNDEVETKTYSDLF 287
Cdd:cd00834 241 LEHAKARGAKIYAEILGYGASSDAYHITAPDPDGEGAARAMRAALADAGLSPEDIDYINAHGTSTPLNDAAESKAIKRVF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 288 ASSPRLPLLFGTKGAFGHTLGATGALEAISLLLALGNQQVPPIVGLENPLTGIALPLAMRTALACPAEVGISVTLGFGGF 367
Cdd:cd00834 321 GEHAKKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPECDLDYVPNEAREAPIRYALSNSFGFGGH 400
|
....*.
gi 28855065 368 DTCLVF 373
Cdd:cd00834 401 NASLVF 406
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
8-376 |
2.26e-87 |
|
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: 270.04 E-value: 2.26e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 8 VWVTGMAWSTALGDDLEVVWQSLLAGRSGIRSVDFPVA--LRSPLASPLPDLDPALPLPERQHR-------LTVATLRRA 78
Cdd:COG0304 3 VVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITRFDAsgLPVRIAGEVKDFDPEEYLDRKELRrmdrftqYALAAAREA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 79 LQDAGLAKATEE-----VVpvLATSYG------HHLDVPETESLSRW-------------AVEAAREAGCQHAPITVSTA 134
Cdd:COG0304 83 LADAGLDLDEVDpdrtgVI--IGSGIGgldtleEAYRALLEKGPRRVspffvpmmmpnmaAGHVSIRFGLKGPNYTVSTA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 135 CSAGADALLLGLSLIRRGFTDTCLCGGADI-LTPAKRLGHSQLGTLS------ADGLRAFDRAHSGTVLGEGAGFLVLET 207
Cdd:COG0304 161 CASGAHAIGEAYRLIRRGRADVMIAGGAEAaITPLGLAGFDALGALStrnddpEKASRPFDKDRDGFVLGEGAGVLVLEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 208 RAAALARGARPYGILAGAGSANDAVSAVAPDLSGDCLALAVRRALCDAGLTAHEVGCISTHGTGTRLNDEVETKTYSDLF 287
Cdd:COG0304 241 LEHAKARGAKIYAEVVGYGASSDAYHITAPAPDGEGAARAMRAALKDAGLSPEDIDYINAHGTSTPLGDAAETKAIKRVF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 288 ASSPRLPLLFGTKGAFGHTLGATGALEAISLLLALGNQQVPPIVGLENPLTGIALPLAMRTALACPAEVGISVTLGFGGF 367
Cdd:COG0304 321 GDHAYKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPECDLDYVPNEAREAKIDYALSNSFGFGGH 400
|
....*....
gi 28855065 368 DTCLVFQRA 376
Cdd:COG0304 401 NASLVFKRY 409
|
|
| PRK05952 |
PRK05952 |
beta-ketoacyl-ACP synthase; |
6-375 |
2.43e-61 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 201.82 E-value: 2.43e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 6 VEVWVTGMAWSTALGDdLEVVWQSLLAGRSGIRsvdfpvalrspLASPLPDLdPALPL------PERQHRLTVATLRRAL 79
Cdd:PRK05952 2 MKVVVTGIGLVSALGD-LEQSWQRLLQGKSGIK-----------LHQPFPEL-PPLPLglignqPSSLEDLTKTVVTAAL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 80 QDAGLAKATEEVVPVLATSYGH--------------HLDVPETESLSRW--------AVEAAREAGCQHAPITVSTACSA 137
Cdd:PRK05952 69 KDAGLTPPLTDCGVVIGSSRGCqgqweklarqmyqgDDSPDEELDLENWldtlphqaAIAAARQIGTQGPVLAPMAACAT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 138 GADALLLGLSLIRRGFTDTCLCGGADI-LTPAKRLGHSQLGTLSADGLRAFDRAHSGTVLGEGAGFLVLETRAAALARGA 216
Cdd:PRK05952 149 GLWAIAQGVELIQTGQCQRVIAGAVEApITPLTLAGFQQMGALAKTGAYPFDRQREGLVLGEGGAILVLESAELAQKRGA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 217 RPYGILAGAGSANDAVSAVAPDLSGDCLALAVRRALCDAGLTAHEVGCISTHGTGTRLNDEVETKTYSDLFassPRLPLL 296
Cdd:PRK05952 229 KIYGQILGFGLTCDAYHMSAPEPDGKSAIAAIQQCLARSGLTPEDIDYIHAHGTATRLNDQREANLIQALF---PHRVAV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 297 FGTKGAFGHTLGATGALEAISLLLALGNQQVPPIVGLENPltgiALPLAM-RTALACPAEVGISVTLGFGGFDTCLVFQR 375
Cdd:PRK05952 306 SSTKGATGHTLGASGALGVAFSLLALRHQQLPPCVGLQEP----EFDLNFvRQAQQSPLQNVLCLSFGFGGQNAAIALGK 381
|
|
| Ketoacyl-synt_C |
pfam02801 |
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
219-334 |
2.22e-24 |
|
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: 96.48 E-value: 2.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 219 YGILAGAGSANDAVSAVAPDLSGDCLALAVRRALCDAGLTAHEVGCISTHGTGTRLNDEVETKTYSDLFASSPR-LPLLF 297
Cdd:pfam02801 1 YAVIKGSAVNHDGRHNGLTAPNGEGQARAIRRALADAGVDPEDVDYVEAHGTGTPLGDPIEAEALKRVFGSGARkQPLAI 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 28855065 298 G-TKGAFGHTLGATGALEAISLLLALGNQQVPPIVGLE 334
Cdd:pfam02801 81 GsVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLNLE 118
|
|
| omega_3_PfaA |
TIGR02813 |
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ... |
131-377 |
7.55e-15 |
|
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: 76.58 E-value: 7.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 131 VSTACSAGADALLLGLSLIRRGFTDTCLCGGADI-LTPAKRLGHSQLGTLSA-DGLRAFDRAHSGTVLGEGAGFLVLETR 208
Cdd:TIGR02813 202 VDAACAGSLAAIRMALSELLEGRSEMMITGGVCTdNSPFMYMSFSKTPAFTTnEDIQPFDIDSKGMMIGEGIGMMALKRL 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 209 AAALARGARPYGILAGAGSANDA--VSAVAPDLSGDclALAVRRALCDAGLTAHEVGCISTHGTGTRLNDEVETKTYSDL 286
Cdd:TIGR02813 282 EDAERDGDRIYAVIKGVGASSDGkfKSIYAPRPEGQ--AKALKRAYDDAGFAPHTCGLIEAHGTGTAAGDVAEFGGLVSV 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 287 FA--SSPRLPLLFGT-KGAFGHTLGATGALEAISLLLALGNQQVPPIVGLENPLTGIAL---PLAMRTAL--------AC 352
Cdd:TIGR02813 360 FSqdNDQKQHIALGSvKSQIGHTKSTAGTAGMIKAVLALHHKVLPPTINVDQPNPKLDIensPFYLNTETrpwmqredGT 439
|
250 260
....*....|....*....|....*
gi 28855065 353 PAEVGISvTLGFGGFDTCLVFQRAR 377
Cdd:TIGR02813 440 PRRAGIS-SFGFGGTNFHMVLEEYS 463
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
21-206 |
2.45e-12 |
|
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: 66.97 E-value: 2.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 21 DDLEVVWQSLLAGRSGIRSVD---FPVALRSPLAsplpdLDPalplperQHRLTVATLRRALQDAGLakateevvpvlat 97
Cdd:smart00825 14 DDPEEFWDLLLAGLDDVDLFDaafFGISPREAEA-----MDP-------QQRLLLEVAWEALEDAGI------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 98 syghhldVPETESLSRWAVEAAreAGCQHAPITVSTACSAGADALLLGLSLIRRGFTDTCLCGGAD-ILTPAKRLGHSQL 176
Cdd:smart00825 69 -------DPESLRGSRTGVFVG--VSSSDYSVTVDTACSSSLVALHLACQSLRSGECDMALAGGVNlILSPDTFVGLSRA 139
|
170 180 190
....*....|....*....|....*....|.
gi 28855065 177 GTLSADGL-RAFDRAHSGTVLGEGAGFLVLE 206
Cdd:smart00825 140 GMLSPDGRcKTFDASADGYVRGEGVGVVVLK 170
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| KAS_I_II |
cd00834 |
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ... |
7-373 |
6.36e-103 |
|
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: 309.85 E-value: 6.36e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 7 EVWVTGMAWSTALGDDLEVVWQSLLAGRSGIRSVDFPVA--LRSPLASPLPDLDPALPLPERQHR-------LTVATLRR 77
Cdd:cd00834 2 RVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRFDAsgFPSRIAGEVPDFDPEDYLDRKELRrmdrfaqFALAAAEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 78 ALQDAGLAKAT---EEVVPVLATSYG--------------------HHLDVPETESlSRWAVEAAREAGCQHAPITVSTA 134
Cdd:cd00834 82 ALADAGLDPEEldpERIGVVIGSGIGglatieeayrallekgprrvSPFFVPMALP-NMAAGQVAIRLGLRGPNYTVSTA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 135 CSAGADALLLGLSLIRRGFTDTCLCGGAD-ILTPAKRLGHSQLGTLSADGL------RAFDRAHSGTVLGEGAGFLVLET 207
Cdd:cd00834 161 CASGAHAIGDAARLIRLGRADVVIAGGAEaLITPLTLAGFAALRALSTRNDdpekasRPFDKDRDGFVLGEGAGVLVLES 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 208 RAAALARGARPYGILAGAGSANDAVSAVAPDLSGDCLALAVRRALCDAGLTAHEVGCISTHGTGTRLNDEVETKTYSDLF 287
Cdd:cd00834 241 LEHAKARGAKIYAEILGYGASSDAYHITAPDPDGEGAARAMRAALADAGLSPEDIDYINAHGTSTPLNDAAESKAIKRVF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 288 ASSPRLPLLFGTKGAFGHTLGATGALEAISLLLALGNQQVPPIVGLENPLTGIALPLAMRTALACPAEVGISVTLGFGGF 367
Cdd:cd00834 321 GEHAKKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPECDLDYVPNEAREAPIRYALSNSFGFGGH 400
|
....*.
gi 28855065 368 DTCLVF 373
Cdd:cd00834 401 NASLVF 406
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
8-376 |
2.26e-87 |
|
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: 270.04 E-value: 2.26e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 8 VWVTGMAWSTALGDDLEVVWQSLLAGRSGIRSVDFPVA--LRSPLASPLPDLDPALPLPERQHR-------LTVATLRRA 78
Cdd:COG0304 3 VVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITRFDAsgLPVRIAGEVKDFDPEEYLDRKELRrmdrftqYALAAAREA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 79 LQDAGLAKATEE-----VVpvLATSYG------HHLDVPETESLSRW-------------AVEAAREAGCQHAPITVSTA 134
Cdd:COG0304 83 LADAGLDLDEVDpdrtgVI--IGSGIGgldtleEAYRALLEKGPRRVspffvpmmmpnmaAGHVSIRFGLKGPNYTVSTA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 135 CSAGADALLLGLSLIRRGFTDTCLCGGADI-LTPAKRLGHSQLGTLS------ADGLRAFDRAHSGTVLGEGAGFLVLET 207
Cdd:COG0304 161 CASGAHAIGEAYRLIRRGRADVMIAGGAEAaITPLGLAGFDALGALStrnddpEKASRPFDKDRDGFVLGEGAGVLVLEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 208 RAAALARGARPYGILAGAGSANDAVSAVAPDLSGDCLALAVRRALCDAGLTAHEVGCISTHGTGTRLNDEVETKTYSDLF 287
Cdd:COG0304 241 LEHAKARGAKIYAEVVGYGASSDAYHITAPAPDGEGAARAMRAALKDAGLSPEDIDYINAHGTSTPLGDAAETKAIKRVF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 288 ASSPRLPLLFGTKGAFGHTLGATGALEAISLLLALGNQQVPPIVGLENPLTGIALPLAMRTALACPAEVGISVTLGFGGF 367
Cdd:COG0304 321 GDHAYKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPECDLDYVPNEAREAKIDYALSNSFGFGGH 400
|
....*....
gi 28855065 368 DTCLVFQRA 376
Cdd:COG0304 401 NASLVFKRY 409
|
|
| PRK05952 |
PRK05952 |
beta-ketoacyl-ACP synthase; |
6-375 |
2.43e-61 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 201.82 E-value: 2.43e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 6 VEVWVTGMAWSTALGDdLEVVWQSLLAGRSGIRsvdfpvalrspLASPLPDLdPALPL------PERQHRLTVATLRRAL 79
Cdd:PRK05952 2 MKVVVTGIGLVSALGD-LEQSWQRLLQGKSGIK-----------LHQPFPEL-PPLPLglignqPSSLEDLTKTVVTAAL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 80 QDAGLAKATEEVVPVLATSYGH--------------HLDVPETESLSRW--------AVEAAREAGCQHAPITVSTACSA 137
Cdd:PRK05952 69 KDAGLTPPLTDCGVVIGSSRGCqgqweklarqmyqgDDSPDEELDLENWldtlphqaAIAAARQIGTQGPVLAPMAACAT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 138 GADALLLGLSLIRRGFTDTCLCGGADI-LTPAKRLGHSQLGTLSADGLRAFDRAHSGTVLGEGAGFLVLETRAAALARGA 216
Cdd:PRK05952 149 GLWAIAQGVELIQTGQCQRVIAGAVEApITPLTLAGFQQMGALAKTGAYPFDRQREGLVLGEGGAILVLESAELAQKRGA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 217 RPYGILAGAGSANDAVSAVAPDLSGDCLALAVRRALCDAGLTAHEVGCISTHGTGTRLNDEVETKTYSDLFassPRLPLL 296
Cdd:PRK05952 229 KIYGQILGFGLTCDAYHMSAPEPDGKSAIAAIQQCLARSGLTPEDIDYIHAHGTATRLNDQREANLIQALF---PHRVAV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 297 FGTKGAFGHTLGATGALEAISLLLALGNQQVPPIVGLENPltgiALPLAM-RTALACPAEVGISVTLGFGGFDTCLVFQR 375
Cdd:PRK05952 306 SSTKGATGHTLGASGALGVAFSLLALRHQQLPPCVGLQEP----EFDLNFvRQAQQSPLQNVLCLSFGFGGQNAAIALGK 381
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
8-375 |
5.85e-51 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 175.75 E-value: 5.85e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 8 VWVTGMAWSTALGDDLEVVWQSLLAGRSGIRSVD--FPVALRSPLASPLPDLDPALPLPERQHR-------LTVATLRRA 78
Cdd:PRK07314 4 VVVTGLGAVSPLGNDVESTWKNLLAGKSGIGPIThfDTSDLAVKIAGEVKDFNPDDYMSRKEARrmdrfiqYGIAAAKQA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 79 LQDAGLAKATEE-----VV--------PVLATSYGHHLD----------VPeteslSRWAVEAAREAGCQH---AP-ITV 131
Cdd:PRK07314 84 VEDAGLEITEENadrigVIigsgigglETIEEQHITLLEkgprrvspffVP-----MAIINMAAGHVSIRYgakGPnHSI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 132 STACSAGADALLLGLSLIRRGFTDTCLCGGADilTPAKRLGHS------QLGTLSADGLRA---FDRAHSGTVLGEGAGF 202
Cdd:PRK07314 159 VTACATGAHAIGDAARLIAYGDADVMVAGGAE--AAITPLGIAgfaaarALSTRNDDPERAsrpFDKDRDGFVMGEGAGI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 203 LVLETRAAALARGARPYGILAGAGSANDAVSAVAPDLSGDCLALAVRRALCDAGLTAHEVGCISTHGTGTRLNDEVETKT 282
Cdd:PRK07314 237 LVLEELEHAKARGAKIYAEVVGYGMTGDAYHMTAPAPDGEGAARAMKLALKDAGINPEDIDYINAHGTSTPAGDKAETQA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 283 YSDLF-ASSPRLPlLFGTKGAFGHTLGATGALEAISLLLALGNQQVPPIVGLENPLTGIALPLAMRTALACPAEVGISVT 361
Cdd:PRK07314 317 IKRVFgEHAYKVA-VSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPTINLDNPDEECDLDYVPNEARERKIDYALSNS 395
|
410
....*....|....
gi 28855065 362 LGFGGFDTCLVFQR 375
Cdd:PRK07314 396 FGFGGTNASLVFKR 409
|
|
| PRK06333 |
PRK06333 |
beta-ketoacyl-ACP synthase; |
10-375 |
8.19e-49 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235781 [Multi-domain] Cd Length: 424 Bit Score: 170.18 E-value: 8.19e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 10 VTGMAWSTALGDDLEVVWQSLLAGRSGIRSV-DFPVA-LRSPLASPLPDL--------DPALPLPERQHR-------LTV 72
Cdd:PRK06333 8 VTGMGAVSPLGCGVETFWQRLLAGQSGIRTLtDFPVGdLATKIGGQVPDLaedaeagfDPDRYLDPKDQRkmdrfilFAM 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 73 ATLRRALQDAGLAKATEEVVPVLATSYG-------------HHLDVPETESLSRWAVE------AAREAGCQH---API- 129
Cdd:PRK06333 88 AAAKEALAQAGWDPDTLEDRERTATIIGsgvggfpaiaeavRTLDSRGPRRLSPFTIPsfltnmAAGHVSIRYgfkGPLg 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 130 TVSTACSAGADALLLGLSLIRRGFTDTCLCGGA----DILTPAKRLGHSQLGTLSAD----GLRAFDRAHSGTVLGEGAG 201
Cdd:PRK06333 168 APVTACAAGVQAIGDAARLIRSGEADVAVCGGTeaaiDRVSLAGFAAARALSTRFNDapeqASRPFDRDRDGFVMGEGAG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 202 FLVLETRAAALARGARPYGILAGAGSANDAVSAVAPDLSGDCLALAVRRALCDAGLTAHEVGCISTHGTGTRLNDEVETK 281
Cdd:PRK06333 248 ILVIETLEHALARGAPPLAELVGYGTSADAYHMTAGPEDGEGARRAMLIALRQAGIPPEEVQHLNAHATSTPVGDLGEVA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 282 TYSDLFAsSPRLPLLFGTKGAFGHTLGATGALEAISLLLALGNQQVPPIVGLENPLTGIA-LPLAMRTALACPAEVGISV 360
Cdd:PRK06333 328 AIKKVFG-HVSGLAVSSTKSATGHLLGAAGGVEAIFTILALRDQIAPPTLNLENPDPAAEgLDVVANKARPMDMDYALSN 406
|
410
....*....|....*
gi 28855065 361 TLGFGGFDTCLVFQR 375
Cdd:PRK06333 407 GFGFGGVNASILFRR 421
|
|
| PRK06501 |
PRK06501 |
beta-ketoacyl-ACP synthase; |
4-375 |
2.95e-46 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235817 [Multi-domain] Cd Length: 425 Bit Score: 163.65 E-value: 2.95e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 4 RPVeVWVTGMAWSTALGDDLEVVWQSLLAGRSGIRSVD-FPV-ALRSPLASPLPDLD-PALPLPERQHRLTVATLRRALQ 80
Cdd:PRK06501 10 RPI-VAVTGMGVVTSLGQGKADNWAALTAGESGIHTITrFPTeGLRTRIAGTVDFLPeSPFGASALSEALARLAAEEALA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 81 DAGLAKA-----------------------TEEVVPVLATSYGHHLDVPETESLSRW---------AVEAAREAGCQHAP 128
Cdd:PRK06501 89 QAGIGKGdfpgplflaappvelewparfalAAAVGDNDAPSYDRLLRAARGGRFDALherfqfgsiADRLADRFGTRGLP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 129 ITVSTACSAGADALLLGLSLIRRGFTDTCLCGGAD-ILTPAKRLGHSQLGTLS------ADGLRAFDRAHSGTVLGEGAG 201
Cdd:PRK06501 169 ISLSTACASGATAIQLGVEAIRRGETDRALCIATDgSVSAEALIRFSLLSALStqndppEKASKPFSKDRDGFVMAEGAG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 202 FLVLETRAAALARGARPYGILAGAGSANDAV--SAVAPDlsGDCLALAVRRALCDAGLTAHEVGCISTHGTGTRLNDEVE 279
Cdd:PRK06501 249 ALVLESLESAVARGAKILGIVAGCGEKADSFhrTRSSPD--GSPAIGAIRAALADAGLTPEQIDYINAHGTSTPENDKME 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 280 TKTYSDLFAS-SPRLPlLFGTKGAFGHTLGATGALEAISLLLALGNQQVPPIVGLENPLTGIALPLAMRTALACPAEVGI 358
Cdd:PRK06501 327 YLGLSAVFGErLASIP-VSSNKSMIGHTLTAAGAVEAVFSLLTIQTGRLPPTINYDNPDPAIPLDVVPNVARDARVTAVL 405
|
410
....*....|....*..
gi 28855065 359 SVTLGFGGFDTCLVFQR 375
Cdd:PRK06501 406 SNSFGFGGQNASLVLTA 422
|
|
| PTZ00050 |
PTZ00050 |
3-oxoacyl-acyl carrier protein synthase; Provisional |
17-375 |
7.94e-46 |
|
3-oxoacyl-acyl carrier protein synthase; Provisional
Pssm-ID: 240245 [Multi-domain] Cd Length: 421 Bit Score: 162.17 E-value: 7.94e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 17 TALGDDLEVVWQSLLAGRSGIRSV-DFPVALRSPL-----------------ASPL--PDLDPALPLPE----RQHRLTV 72
Cdd:PTZ00050 3 TPLGVGAESTWEALIAGKSGIRKLtEFPKFLPDCIpeqkalenlvaampcqiAAEVdqSEFDPSDFAPTkresRATHFAM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 73 ATLRRALQDAGLAKATE------------------EVVPVLATSYG-HHLDVPETESLSRWAVEAAREAGCQH---API- 129
Cdd:PTZ00050 83 AAAREALADAKLDILSEkdqerigvnigsgigslaDLTDEMKTLYEkGHSRVSPYFIPKILGNMAAGLVAIKHklkGPSg 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 130 TVSTACSAGADALLLGLSLIRRGFTDTCLCGGA-DILTPAKRLGHSQLGTLSA-------DGLRAFDRAHSGTVLGEGAG 201
Cdd:PTZ00050 163 SAVTACATGAHCIGEAFRWIKYGEADIMICGGTeASITPVSFAGFSRMRALCTkynddpqRASRPFDKDRAGFVMGEGAG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 202 FLVLETRAAALARGARPYGILAGAGSANDAVSAVAPDLSGDCLALAVRRALCDAG-LTAHEVGCISTHGTGTRLNDEVET 280
Cdd:PTZ00050 243 ILVLEELEHALRRGAKIYAEIRGYGSSSDAHHITAPHPDGRGARRCMENALKDGAnININDVDYVNAHATSTPIGDKIEL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 281 KTYSDLFASSPRLPLLF-GTKGAFGHTLGATGALEAISLLLALGNQQVPPIVGLENPLTGIALPLAMRTALAC--PAEVG 357
Cdd:PTZ00050 323 KAIKKVFGDSGAPKLYVsSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINLENPDAECDLNLVQGKTAHPlqSIDAV 402
|
410
....*....|....*...
gi 28855065 358 ISVTLGFGGFDTCLVFQR 375
Cdd:PTZ00050 403 LSTSFGFGGVNTALLFTK 420
|
|
| PRK09185 |
PRK09185 |
beta-ketoacyl-ACP synthase; |
8-377 |
4.45e-41 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236398 [Multi-domain] Cd Length: 392 Bit Score: 148.84 E-value: 4.45e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 8 VWVTGMAWSTALGDDLEVVWQSLLAGR-SGIRSVDFPVALRSPLASPLPDLD-PALP--LPE---RQHRLTVATLRRALQ 80
Cdd:PRK09185 4 VYISAFGATSALGRGLDAILAALRAGRaSGMRPCDFWLVDLPTWVGEVVGVElPALPaaLAAfdcRNNRLALLALQQIEP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 81 DAGLAKAT---EEVVPVLATS----------YGHHLdvPETESLSRWAVEAAREAGC-----QHA-----P-ITVSTACS 136
Cdd:PRK09185 84 AVEAAIARygaDRIGVVLGTStsgilegelaYRRRD--PAHGALPADYHYAQQELGSladflRAYlglsgPaYTISTACS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 137 AGADALLLGLSLIRRGFTDTCLCGGADILTPAKRLGHSQLGTLSADGLRAFDRAHSGTVLGEGAGFLVLETRAAALArga 216
Cdd:PRK09185 162 SSAKVFASARRLLEAGLCDAAIVGGVDSLCRLTLNGFNSLESLSPQPCRPFSANRDGINIGEAAAFFLLEREDDAAV--- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 217 rpygILAGAGSANDAVSAVAPDLSGDCLALAVRRALCDAGLTAHEVGCISTHGTGTRLNDEVETKTYSDLFASSPRLPll 296
Cdd:PRK09185 239 ----ALLGVGESSDAHHMSAPHPEGLGAILAMQQALADAGLAPADIGYINLHGTATPLNDAMESRAVAAVFGDGVPCS-- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 297 fGTKGAFGHTLGATGALEAISLLLALGNQQVPPIVGLENPLTGIALPLAMRTALACPAEVGISVTLGFGGFDTCLVFQRA 376
Cdd:PRK09185 313 -STKGLTGHTLGAAGAVEAAICWLALRHGLPPHGWNTGQPDPALPPLYLVENAQALAIRYVLSNSFAFGGNNCSLIFGRA 391
|
.
gi 28855065 377 R 377
Cdd:PRK09185 392 D 392
|
|
| PRK07103 |
PRK07103 |
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated |
7-375 |
3.06e-39 |
|
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
Pssm-ID: 180839 [Multi-domain] Cd Length: 410 Bit Score: 144.40 E-value: 3.06e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 7 EVWVTGMAWSTALGDDLEVVWQSLLAGRSGIRSVDFP-----VALRSPLASPLPDLD-PALPLPERQH-----------R 69
Cdd:PRK07103 3 EVVVTGVGVVSAIGQGRPSFAAALLAGRHAFGVMRRPgrqvpDDAGAGLASAFIGAElDSLALPERLDakllrraslsaQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 70 LTVATLRRALQDAGLAKA---------------TEEVVPVLATSYGHHLDVPETESLSRW---AVEAAREA-GCQHAPIT 130
Cdd:PRK07103 83 AALAAAREAWRDAALGPVdpdriglvvggsnlqQREQALVHETYRDRPAFLRPSYGLSFMdtdLVGLCSEQfGIRGEGFT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 131 VSTACSAGADALLLGLSLIRRGFTDTCLCGGADI-LTPAKRLGHSQLGTLSADGL--------RAFDRAHSGTVLGEGAG 201
Cdd:PRK07103 163 VGGASASGQLAVIQAARLVQSGSVDACIAVGALMdLSYWECQALRSLGAMGSDRFadepeaacRPFDQDRDGFIYGEACG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 202 FLVLETRAAALARGARPYGILAGAGSANDAVSAVAPDLSGDclALAVRRALCDAGLTAHEVGCISTHGTGTRLNDEVETK 281
Cdd:PRK07103 243 AVVLESAESARRRGARPYAKLLGWSMRLDANRGPDPSLEGE--MRVIRAALRRAGLGPEDIDYVNPHGTGSPLGDETELA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 282 TysdLFASSPRLPLLFGTKGAFGHTLGATGALEAISLLLALGNQQVPPIVGLENPLT-------GIALPLAMRTALacpa 354
Cdd:PRK07103 321 A---LFASGLAHAWINATKSLTGHGLSAAGIVELIATLLQMRAGFLHPSRNLDEPIDerfrwvgSTAESARIRYAL---- 393
|
410 420
....*....|....*....|.
gi 28855065 355 evgiSVTLGFGGFDTCLVFQR 375
Cdd:PRK07103 394 ----SLSFGFGGINTALVLER 410
|
|
| PRK07910 |
PRK07910 |
beta-ketoacyl-ACP synthase; |
8-376 |
7.13e-39 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236129 [Multi-domain] Cd Length: 418 Bit Score: 143.72 E-value: 7.13e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 8 VWVTGMAWSTALGDDLEVVWQSLLAGRSGIRSV--------DFPVALRSPLaspLPDLDPALPlPERQHRLT----VATL 75
Cdd:PRK07910 14 VVVTGIAMTTALATDAETTWKLLLDGQSGIRTLddpfveefDLPVRIGGHL---LEEFDHQLT-RVELRRMSylqrMSTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 76 --RRALQDAGlakaTEEVVPV-LATSYGHHLDVPET-------------ESLSRWAVE------AAREAGCQHAP----I 129
Cdd:PRK07910 90 lgRRVWENAG----SPEVDTNrLMVSIGTGLGSAEElvfayddmrarglRAVSPLAVQmympngPAAAVGLERHAkagvI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 130 TVSTACSAGADALLLGLSLIRRGFTDTCLCGGADILTPAKRL-GHSQLG-TLS------ADGLRAFDRAHSGTVLGEGAG 201
Cdd:PRK07910 166 TPVSACASGSEAIAQAWRQIVLGEADIAICGGVETRIEAVPIaGFAQMRiVMStnnddpAGACRPFDKDRDGFVFGEGGA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 202 FLVLETRAAALARGARPYGILAGAGSANDAVSAVAPDLSGDCLALAVRRALCDAGLTAHEVGCISTHGTGTRLNDEVETK 281
Cdd:PRK07910 246 LMVIETEEHAKARGANILARIMGASITSDGFHMVAPDPNGERAGHAMTRAIELAGLTPGDIDHVNAHATGTSVGDVAEGK 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 282 TYSDlfASSPRLPLLFGTKGAFGHTLGATGALEAISLLLALGNQQVPPIVGLENPLTGIALPLAMRTALACPAEVGISVT 361
Cdd:PRK07910 326 AINN--ALGGHRPAVYAPKSALGHSVGAVGAVESILTVLALRDGVIPPTLNLENLDPEIDLDVVAGEPRPGNYRYAINNS 403
|
410
....*....|....*
gi 28855065 362 LGFGGFDTCLVFQRA 376
Cdd:PRK07910 404 FGFGGHNVALAFGRY 418
|
|
| PRK08722 |
PRK08722 |
beta-ketoacyl-ACP synthase II; |
8-375 |
5.31e-37 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 181539 [Multi-domain] Cd Length: 414 Bit Score: 138.60 E-value: 5.31e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 8 VWVTGMAWSTALGDDLEVVWQSLLAGRSGIRSVD-FPVALRSP-LASPLPDLDPALPLPERQHR-------LTVATLRRA 78
Cdd:PRK08722 6 VVVTGMGMLSPVGNTVESSWKALLAGQSGIVNIEhFDTTNFSTrFAGLVKDFNCEEYMSKKDARkmdlfiqYGIAAGIQA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 79 LQDAGLaKATEEVVPVLATSYGHHLD------------------------VPETeSLSRWAVEAAREAGCQHAPITVSTA 134
Cdd:PRK08722 86 LDDSGL-EVTEENAHRIGVAIGSGIGglglieaghqalvekgprkvspffVPST-IVNMIAGNLSIMRGLRGPNIAISTA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 135 CSAGADALLLGLSLIRRGFTDTCLCGGAD-ILTPAKRLGHSQLGTLSAD------GLRAFDRAHSGTVLGEGAGFLVLET 207
Cdd:PRK08722 164 CTTGLHNIGHAARMIAYGDADAMVAGGAEkASTPLGMAGFGAAKALSTRndepqkASRPWDKDRDGFVLGDGAGMMVLEE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 208 RAAALARGARPYGILAGAGSANDAVSAVAPDLSGDCLALAVRRALCDAGLTAHEVGCISTHGTGTRLNDEVETKTYSD-L 286
Cdd:PRK08722 244 YEHAKARGAKIYAELVGFGMSGDAYHMTSPSEDGSGGALAMEAAMRDAGVTGEQIGYVNAHGTSTPAGDVAEIKGIKRaL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 287 FASSPRLPLLFGTKGAFGHTLGATGALEAISLLLALGNQQVPPIVGLENPLTGIALPLAMRTALACPA-EVGISVTLGFG 365
Cdd:PRK08722 324 GEAGSKQVLVSSTKSMTGHLLGAAGSVEAIITVMSLVDQIVPPTINLDDPEEGLDIDLVPHTARKVESmEYAICNSFGFG 403
|
410
....*....|
gi 28855065 366 GFDTCLVFQR 375
Cdd:PRK08722 404 GTNGSLIFKK 413
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
20-372 |
5.94e-37 |
|
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: 138.46 E-value: 5.94e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 20 GDDLEVVWQSLLAGRSGIRSVDFPVALRSPLASPLPDLDPALP------------------LPER-------QHRLTVAT 74
Cdd:cd00833 15 AADPDEFWENLLEGRDAISEIPEDRWDADGYYPDPGKPGKTYTrrggflddvdafdaaffgISPReaeamdpQQRLLLEV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 75 LRRALQDAGLAKATEE------VVPVLATSYGHHLDvPETESLSRWAVeaareAGCQHAPI---------------TVST 133
Cdd:cd00833 95 AWEALEDAGYSPESLAgsrtgvFVGASSSDYLELLA-RDPDEIDAYAA-----TGTSRAFLanrisyffdlrgpslTVDT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 134 ACSAGADALLLGLSLIRRGFTDTCLCGGAD-ILTPAKRLGHSQLGTLSADGL-RAFDRAHSGTVLGEGAGFLVLETRAAA 211
Cdd:cd00833 169 ACSSSLVALHLACQSLRSGECDLALVGGVNlILSPDMFVGFSKAGMLSPDGRcRPFDADADGYVRGEGVGVVVLKRLSDA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 212 LARGARPYGILAGAGSANDAVSA--VAPdlSGDCLALAVRRALCDAGLTAHEVGCISTHGTGTRLNDEVETKTYSDLFA- 288
Cdd:cd00833 249 LRDGDRIYAVIRGSAVNQDGRTKgiTAP--SGEAQAALIRRAYARAGVDPSDIDYVEAHGTGTPLGDPIEVEALAKVFGg 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 289 -SSPRLPLLFG-TKGAFGHTLGATGALEAISLLLALGNQQVPPIVGLENPLTGIAL---PLAMRT-ALACPAE-----VG 357
Cdd:cd00833 327 sRSADQPLLIGsVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKIDFeesPLRVPTeARPWPAPagprrAG 406
|
410
....*....|....*
gi 28855065 358 ISVtLGFGGFDTCLV 372
Cdd:cd00833 407 VSS-FGFGGTNAHVI 420
|
|
| PRK08439 |
PRK08439 |
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed |
8-375 |
7.47e-36 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
Pssm-ID: 236265 [Multi-domain] Cd Length: 406 Bit Score: 135.25 E-value: 7.47e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 8 VWVTGMAWSTALGDDLEVVWQSLLAGRSGIRSV------DFPVALrsplASPLPDLDPALPL-------PERQHRLTVAT 74
Cdd:PRK08439 4 VVVTGIGMINSLGLNKESSFKAICNGECGIKKItlfdasDFPVQI----AGEITDFDPTEVMdpkevkkADRFIQLGLKA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 75 LRRALQDAGLAKAT--EEVVPVLATSYGHHLDVPETESL----------SRWAVEAAR----------EAGCQHAPITVS 132
Cdd:PRK08439 80 AREAMKDAGFLPEEldAERFGVSSASGIGGLPNIEKNSIicfekgprkiSPFFIPSALvnmlggfisiEHGLKGPNLSSV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 133 TACSAGADALLLGLSLIRRGFTDTCLCGGAD-ILTPAKRLGHSQLGTLS------ADGLRAFDRAHSGTVLGEGAGFLVL 205
Cdd:PRK08439 160 TACAAGTHAIIEAVKTIMLGGADKMLVVGAEsAICPVGIGGFAAMKALStrnddpKKASRPFDKDRDGFVMGEGAGALVL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 206 ETRAAALARGARPYGILAGAGSANDAVSAVAPDLSGDclALAVRRALCDAGLTahEVGCISTHGTGTRLNDEVETKTYSD 285
Cdd:PRK08439 240 EEYESAKKRGAKIYAEIIGFGESGDANHITSPAPEGP--LRAMKAALEMAGNP--KIDYINAHGTSTPYNDKNETAALKE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 286 LFASSPRLPLLFGTKGAFGHTLGATGALEAISLLLALGNQQVPPIVGLENPLTGIALPLAMRTALACPAEVGISVTLGFG 365
Cdd:PRK08439 316 LFGSKEKVPPVSSTKGQIGHCLGAAGAIEAVISIMAMRDGILPPTINQETPDPECDLDYIPNVARKAELNVVMSNSFGFG 395
|
410
....*....|
gi 28855065 366 GFDTCLVFQR 375
Cdd:PRK08439 396 GTNGVVIFKK 405
|
|
| PRK09116 |
PRK09116 |
beta-ketoacyl-ACP synthase; |
8-373 |
1.17e-35 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 181657 [Multi-domain] Cd Length: 405 Bit Score: 134.73 E-value: 1.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 8 VWVTGMAWSTALGDDLEVVWQSLLAGRSGIRSVD----FPvALRSPLASPLPDLDPALPLPERQHR-------LTVATLR 76
Cdd:PRK09116 4 VVVTGMGGVTALGEDWQTIAARLKAGRNAVRRMPewdrYD-GLNTRLAAPIDDFELPAHYTRKKIRsmgrvslMATRASE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 77 RALQDAGLA---------------KATEEVVPVLAtsYGHHLDVPETESLS----------RWAVEAAREAGCQHAPITV 131
Cdd:PRK09116 83 LALEDAGLLgdpiltdgrmgiaygSSTGSTDPIGA--FGTMLLEGSMSGITattyvrmmphTTAVNVGLFFGLKGRVIPT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 132 STACSAGADALLLGLSLIRRGFTDTCLCGGADILTPAkrlGHSQLGTLSADGL---------RAFDRAHSGTVLGEGAGF 202
Cdd:PRK09116 161 SSACTSGSQGIGYAYEAIKYGYQTVMLAGGAEELCPT---EAAVFDTLFATSTrndapeltpRPFDANRDGLVIGEGAGT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 203 LVLETRAAALARGARPYGILAGAGSANDAVSAVAPDlsGDCLALAVRRALCDAGLTAHEVGCISTHGTGTRLNDEVETKT 282
Cdd:PRK09116 238 LVLEELEHAKARGATIYAEIVGFGTNSDGAHVTQPQ--AETMQIAMELALKDAGLAPEDIGYVNAHGTATDRGDIAESQA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 283 YSDLFasSPRLPLLfGTKGAFGHTLGATGALEAISLLLALGNQQVPPIVGLEN--PLTGiALPLAMRTALACPAEVGISV 360
Cdd:PRK09116 316 TAAVF--GARMPIS-SLKSYFGHTLGACGALEAWMSIEMMNEGWFAPTLNLTQvdPACG-ALDYIMGEAREIDTEYVMSN 391
|
410
....*....|...
gi 28855065 361 TLGFGGFDTCLVF 373
Cdd:PRK09116 392 NFAFGGINTSLIF 404
|
|
| PLN02836 |
PLN02836 |
3-oxoacyl-[acyl-carrier-protein] synthase |
5-373 |
3.44e-31 |
|
3-oxoacyl-[acyl-carrier-protein] synthase
Pssm-ID: 215449 [Multi-domain] Cd Length: 437 Bit Score: 122.98 E-value: 3.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 5 PVEVWVTGMAWSTALGDDLEVVWQSLLAGRSGIRSV---DFP-------------------VALRSPLASPLPDLDPALP 62
Cdd:PLN02836 5 TRRVVVTGLGLVTPLGCGVETTWRRLIAGECGVRALtqdDLKmksedeetqlytldqlpsrVAALVPRGTGPGDFDEELW 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 63 LPERQHR----LTVATLRRALQDAGLAKATEEVVPVLATSYGHHL----DVPETESL--------------SRWAVEAAR 120
Cdd:PLN02836 85 LNSRSSSrfigYALCAADEALSDARWLPSEDEAKERTGVSIGGGIgsitDILEAAQLicekrlrrlspffvPRILINMAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 121 EA--------GCQHAPitvSTACSAGADALLLGLSLIRRGFTDTCLCGGADILTPAKRL-GHSQLGTLSA-------DGL 184
Cdd:PLN02836 165 GHvsirygfqGPNHAA---VTACATGAHSIGDAFRMIQFGDADVMVAGGTESSIDALSIaGFSRSRALSTkfnscptEAS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 185 RAFDRAHSGTVLGEGAGFLVLETRAAALARGARPYGILAGAGSANDAVSAVAPDLSGDCLALAVRRALCDAGLTAHEVGC 264
Cdd:PLN02836 242 RPFDCDRDGFVIGEGAGVLVLEELEHAKRRGAKIYAEVRGYGMSGDAHHITQPHEDGRGAVLAMTRALQQSGLHPNQVDY 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 265 ISTHGTGTRLNDEVETKTYSDLF---ASSPRLPlLFGTKGAFGHTLGATGALEAISLLLALGNQQVPPIVGLENP---LT 338
Cdd:PLN02836 322 VNAHATSTPLGDAVEARAIKTVFsehATSGGLA-FSSTKGATGHLLGAAGAVEAIFSVLAIHHGIAPPTLNLERPdpiFD 400
|
410 420 430
....*....|....*....|....*....|....*
gi 28855065 339 GIALPLAmrTALACPAEVGISVTLGFGGFDTCLVF 373
Cdd:PLN02836 401 DGFVPLT--ASKAMLIRAALSNSFGFGGTNASLLF 433
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
21-372 |
5.75e-31 |
|
"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: 121.78 E-value: 5.75e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 21 DDLEVVWQSLLAGRSGIR-SVDFPVALRSPLASPLPDLDPA------LPLPERQHRLTVATLRRALQDAGLAKATEEVVP 93
Cdd:cd00828 19 DEVEEFWEALREGRSGIApVARLKSRFDRGVAGQIPTGDIPgwdakrTGIVDRTTLLALVATEEALADAGITDPYEVHPS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 94 VLATSYG---------------HHLDVPETESLsRWAVEAAREAGC-------QHAPI-TVSTACSAGADALLLGLSLIR 150
Cdd:cd00828 99 EVGVVVGsgmgglrflrrggklDARAVNPYVSP-KWMLSPNTVAGWvnilllsSHGPIkTPVGACATALEALDLAVEAIR 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 151 RGFTDTCLCGGADILTPAKRLGHSQLGTLSADG------LRAFDRAHSGTVLGEGAGFLVLETRAAALARGARPYGILAG 224
Cdd:cd00828 178 SGKADIVVVGGVEDPLEEGLSGFANMGALSTAEeepeemSRPFDETRDGFVEAEGAGVLVLERAELALARGAPIYGRVAG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 225 AGSANDAVSAVAPDLsGDCLALAVRRALCDAGLTAHEVGCISTHGTGTRLNDEVETKTYSDLFASSPRLPLLFGTKGAFG 304
Cdd:cd00828 258 TASTTDGAGRSVPAG-GKGIARAIRTALAKAGLSLDDLDVISAHGTSTPANDVAESRAIAEVAGALGAPLPVTAQKALFG 336
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 305 HTLGATGALEAISLLLALGNQQVPPIVGLE--NPLTGIALPLAMRTALACPAEVGISVTLGFGGFDTCLV 372
Cdd:cd00828 337 HSKGAAGALQLIGALQSLEHGLIPPTANLDdvDPDVEHLSVVGLSRDLNLKVRAALVNAFGFGGSNAALV 406
|
|
| PLN02787 |
PLN02787 |
3-oxoacyl-[acyl-carrier-protein] synthase II |
3-373 |
3.65e-30 |
|
3-oxoacyl-[acyl-carrier-protein] synthase II
Pssm-ID: 215421 [Multi-domain] Cd Length: 540 Bit Score: 121.24 E-value: 3.65e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 3 SRPVEVWVTGMAWSTALGDDLEVVWQSLLAGRSGIRSV------DFPVALRSPLASPLPDLDPALPLPERQHRLTVATL- 75
Cdd:PLN02787 126 TKQRRVVVTGMGVVSPLGHDPDVFYNNLLEGVSGISEIerfdcsQFPTRIAGEIKSFSTDGWVAPKLSKRMDKFMLYLLt 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 76 --RRALQDAGLakaTEEVVPVLATSYGHHLDVPETESLSRW--AVEAAREAGCQHAPITV-------------------- 131
Cdd:PLN02787 206 agKKALADGGI---TEDVMKELDKTKCGVLIGSAMGGMKVFndAIEALRISYRKMNPFCVpfattnmgsamlamdlgwmg 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 132 -----STACSAGADALLLGLSLIRRGFTDTCLCGGADILTPAKRLGH-------SQLGTLSADGLRAFDRAHSGTVLGEG 199
Cdd:PLN02787 283 pnysiSTACATSNFCILNAANHIIRGEADVMLCGGSDAAIIPIGLGGfvacralSQRNDDPTKASRPWDMNRDGFVMGEG 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 200 AGFLVLETRAAALARGARPYGILAGAGSANDAVSAVAPDLSGDCLALAVRRALCDAGLTAHEVGCISTHGTGTRLNDEVE 279
Cdd:PLN02787 363 AGVLLLEELEHAKKRGANIYAEFLGGSFTCDAYHMTEPHPEGAGVILCIEKALAQSGVSKEDVNYINAHATSTKAGDLKE 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 280 TKTYSDLFASSPRLPlLFGTKGAFGHTLGATGALEAISLLLALGNQQVPPIVGLENPLTGIALPLAMRTALA-CPAEVGI 358
Cdd:PLN02787 443 YQALMRCFGQNPELR-VNSTKSMIGHLLGAAGAVEAIATVQAIRTGWVHPNINLENPESGVDTKVLVGPKKErLDIKVAL 521
|
410
....*....|....*
gi 28855065 359 SVTLGFGGFDTCLVF 373
Cdd:PLN02787 522 SNSFGFGGHNSSILF 536
|
|
| PRK14691 |
PRK14691 |
3-oxoacyl-(acyl carrier protein) synthase II; Provisional |
127-375 |
3.95e-30 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
Pssm-ID: 173154 [Multi-domain] Cd Length: 342 Bit Score: 118.29 E-value: 3.95e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 127 APITvstACSAGADALLLGLSLIRRGFTDTCLCGGADILT--------PAKRLGHSQLGTLSADGLRAFDRAHSGTVLGE 198
Cdd:PRK14691 86 APVT---ACAAGVQAIGDAVRMIRNNEADVALCGGAEAVIdtvslagfAAARALSTHFNSTPEKASRPFDTARDGFVMGE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 199 GAGFLVLETRAAALARGARPYGILAGAGSANDAVSAVAPDLSGDCLALAVRRALCDAGLTAHEVGCISTHGTGTRLNDEV 278
Cdd:PRK14691 163 GAGLLIIEELEHALARGAKPLAEIVGYGTSADAYHMTSGAEDGDGAYRAMKIALRQAGITPEQVQHLNAHATSTPVGDLG 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 279 ETKTYSDLFASSPRLPLLfGTKGAFGHTLGATGALEAISLLLALGNQQVPPIVGLENP---------LTGIALPLAMRTA 349
Cdd:PRK14691 243 EINAIKHLFGESNALAIT-STKSATGHLLGAAGGLETIFTVLALRDQIVPATLNLENPdpaakglniIAGNAQPHDMTYA 321
|
250 260
....*....|....*....|....*.
gi 28855065 350 LacpaevgiSVTLGFGGFDTCLVFQR 375
Cdd:PRK14691 322 L--------SNGFGFAGVNASILLKR 339
|
|
| Ketoacyl-synt_C |
pfam02801 |
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
219-334 |
2.22e-24 |
|
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: 96.48 E-value: 2.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 219 YGILAGAGSANDAVSAVAPDLSGDCLALAVRRALCDAGLTAHEVGCISTHGTGTRLNDEVETKTYSDLFASSPR-LPLLF 297
Cdd:pfam02801 1 YAVIKGSAVNHDGRHNGLTAPNGEGQARAIRRALADAGVDPEDVDYVEAHGTGTPLGDPIEAEALKRVFGSGARkQPLAI 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 28855065 298 G-TKGAFGHTLGATGALEAISLLLALGNQQVPPIVGLE 334
Cdd:pfam02801 81 GsVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLNLE 118
|
|
| CLF |
cd00832 |
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ... |
10-372 |
2.24e-24 |
|
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: 103.21 E-value: 2.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 10 VTGMAWSTALGDDLEVVWQSLLAGRSGIRSVDF--PVALRSPLASPLPDLDPA-------LPLPERQHRLTVATLRRALQ 80
Cdd:cd00832 5 VTGIGVVAPNGLGVEEYWKAVLDGRSGLGPITRfdPSGYPARLAGEVPDFDAAehlpgrlLPQTDRMTRLALAAADWALA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 81 DAGLAKATE---EVVPVLATS-----YGHHldvpETESL----SRW-----------AVEAAREA---GCQHAPITVSTA 134
Cdd:cd00832 85 DAGVDPAALppyDMGVVTASAaggfeFGQR----ELQKLwskgPRHvsayqsfawfyAVNTGQISirhGMRGPSGVVVAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 135 CSAGADALLLGLSLIRRGfTDTCLCGGAD-ILTPAKRLGHSQLGTLS-----ADGLRAFDRAHSGTVLGEGAGFLVLETR 208
Cdd:cd00832 161 QAGGLDALAQARRLVRRG-TPLVVSGGVDsALCPWGWVAQLSSGRLStsddpARAYLPFDAAAAGYVPGEGGAILVLEDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 209 AAALARGARPYGILAGAGSANDAVSAVApdlSGDCLALAVRRALCDAGLTAHEVGCISTHGTGTRLNDEVETKTYSDLFA 288
Cdd:cd00832 240 AAARERGARVYGEIAGYAATFDPPPGSG---RPPGLARAIRLALADAGLTPEDVDVVFADAAGVPELDRAEAAALAAVFG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 289 ssPRLPLLFGTKGAFGHTLGATGALEAISLLLALGNQQVPPIVGLENPLTGIALPLAMRTALACPAEVGISVTLGFGGFD 368
Cdd:cd00832 317 --PRGVPVTAPKTMTGRLYAGGAPLDVATALLALRDGVIPPTVNVTDVPPAYGLDLVTGRPRPAALRTALVLARGRGGFN 394
|
....
gi 28855065 369 TCLV 372
Cdd:cd00832 395 SALV 398
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
7-207 |
1.60e-22 |
|
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: 95.39 E-value: 1.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 7 EVWVTGMAWSTALGDDLEVVWQSLLAGRSGIRSVD---FPVALRSPLASPLP--------------DLDPAL---PLPE- 65
Cdd:pfam00109 2 PVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIPadrWDPDKLYDPPSRIAgkiytkwgglddifDFDPLFfgiSPREa 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 66 ----RQHRLTVATLRRALQDAGLAKATEE------VVPVLATSYGHHLDVPETESLSRW---------AVEAAREA---G 123
Cdd:pfam00109 82 ermdPQQRLLLEAAWEALEDAGITPDSLDgsrtgvFIGSGIGDYAALLLLDEDGGPRRGspfavgtmpSVIAGRISyflG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 124 CQHAPITVSTACSAGADALLLGLSLIRRGFTDTCLCGGAD-ILTPAKRLGHSQLGTLSADG-LRAFDRAHSGTVLGEGAG 201
Cdd:pfam00109 162 LRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNlLLTPLGFAGFSAAGMLSPDGpCKAFDPFADGFVRGEGVG 241
|
....*.
gi 28855065 202 FLVLET 207
Cdd:pfam00109 242 AVVLKR 247
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
129-336 |
1.41e-21 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 96.87 E-value: 1.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 129 ITVSTACSAGADALLLGLSLIRRGFTDTCLCGGADI-LTPAKRLGHSQLGTLSADGL-RAFDRAHSGTVLGEGAGFLVLE 206
Cdd:COG3321 168 VTVDTACSSSLVAVHLACQSLRSGECDLALAGGVNLmLTPESFILFSKGGMLSPDGRcRAFDADADGYVRGEGVGVVVLK 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 207 TRAAALARGARPYGILAGAGSAND--AVSAVAPdlSGDCLALAVRRALCDAGLTAHEVGCISTHGTGTRLNDEVE----T 280
Cdd:COG3321 248 RLSDALRDGDRIYAVIRGSAVNQDgrSNGLTAP--NGPAQAAVIRRALADAGVDPATVDYVEAHGTGTPLGDPIEaaalT 325
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 28855065 281 KTYSDlfASSPRLPLLFGT-KGAFGHTLGATGALEAISLLLALGNQQVPPIVGLENP 336
Cdd:COG3321 326 AAFGQ--GRPADQPCAIGSvKSNIGHLEAAAGVAGLIKAVLALRHGVLPPTLHFETP 380
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
66-366 |
1.10e-20 |
|
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: 91.93 E-value: 1.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 66 RQHRLTVATLRRALQDAGLAKATEE----VVPVLATSYGHHLDVPETESLsrWAVEAAREAGCQHAPIT----------- 130
Cdd:cd00825 10 YVSILGFEAAERAIADAGLSREYQKnpivGVVVGTGGGSPRFQVFGADAM--RAVGPYVVTKAMFPGASgqiatplgihg 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 131 ----VSTACSAGADALLLGLSLIRRGFTDTCLCGGADILT-PAKRLGHSQLGTLSADG-LRAFDRAHSGTVLGEGAGFLV 204
Cdd:cd00825 88 paydVSAACAGSLHALSLAADAVQNGKQDIVLAGGSEELAaPMDCEFDAMGALSTPEKaSRTFDAAADGFVFGDGAGALV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 205 LETRAAALARGARPYGILAGAGSANDAVSAVAPDLSGDCLALAVRRALCDAGLTAHEVGCISTHGTGTRLNDEVETKTYS 284
Cdd:cd00825 168 VEELEHALARGAHIYAEIVGTAATIDGAGMGAFAPSAEGLARAAKEALAVAGLTVWDIDYLVAHGTGTPIGDVKELKLLR 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 285 DLFAssPRLPLLFGTKGAFGHTLGATGALEAISLLLALGNQQVPPIVGLENpLTGIALPLAMRTAlacPAEVGISVTLGF 364
Cdd:cd00825 248 SEFG--DKSPAVSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIPPSIHIEE-LDEAGLNIVTETT---PRELRTALLNGF 321
|
..
gi 28855065 365 GG 366
Cdd:cd00825 322 GL 323
|
|
| PRK07967 |
PRK07967 |
beta-ketoacyl-ACP synthase I; |
8-375 |
4.15e-19 |
|
beta-ketoacyl-ACP synthase I;
Pssm-ID: 181184 [Multi-domain] Cd Length: 406 Bit Score: 88.19 E-value: 4.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 8 VWVTGMAWSTALGDDLEVVWQSLLAGRSGI-RSVDFP-VALRSPLASPlPDLDPALPLPERQHR-LTVAT------LRRA 78
Cdd:PRK07967 4 VVITGLGIVSSIGNNQQEVLASLREGRSGItFSPEFAeMGMRSQVWGN-VKLDPTGLIDRKVMRfMGDASayaylaMEQA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 79 LQDAGLAK--ATEEVVPVLATSYGhhldvPETeslsRWAVEAA---RE--------------------AGCQHAPI---- 129
Cdd:PRK07967 83 IADAGLSEeqVSNPRTGLIAGSGG-----GST----RNQVEAAdamRGprgpkrvgpyavtkamastvSACLATPFkikg 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 130 ---TVSTACSAGADALLLGLSLIRRGFTDTCLCGGADILTPAKRLGHSQLGTLS-------ADGLRAFDRAHSGTVLGEG 199
Cdd:PRK07967 154 vnySISSACATSAHCIGNAVEQIQLGKQDIVFAGGGEELDWEMSCLFDAMGALStkyndtpEKASRAYDANRDGFVIAGG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 200 AGFLVLETRAAALARGARPYGILAGAGSANDAVSAVAPdlSGDCLALAVRRALCDaglTAHEVGCISTHGTGTRLNDEVE 279
Cdd:PRK07967 234 GGVVVVEELEHALARGAKIYAEIVGYGATSDGYDMVAP--SGEGAVRCMQMALAT---VDTPIDYINTHGTSTPVGDVKE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 280 TKTYSDLFASspRLPLLFGTKGAFGHTLGATGALEAISLLLALGNQQVPPIVGLENPLTGIA-LPLAMRTALACPAEVGI 358
Cdd:PRK07967 309 LGAIREVFGD--KSPAISATKSLTGHSLGAAGVQEAIYSLLMMEHGFIAPSANIEELDPQAAgMPIVTETTDNAELTTVM 386
|
410
....*....|....*..
gi 28855065 359 SVTLGFGGFDTCLVFQR 375
Cdd:PRK07967 387 SNSFGFGGTNATLVFRR 403
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
66-329 |
1.13e-15 |
|
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: 75.94 E-value: 1.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 66 RQHRLTVATLRRALQDAGLAKATEEVVpVLATSYGHHLdvpetesLSRWAVEAAREAGCQHAP-ITVSTACSAGADALLL 144
Cdd:cd00327 6 TASELGFEAAEQAIADAGLSKGPIVGV-IVGTTGGSGE-------FSGAAGQLAYHLGISGGPaYSVNQACATGLTALAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 145 GLSLIRRGFTDTCLCGGADILtpakrlghsqlgtlsadglrafdrahsgtVLGEGAGFLVLETRAAALARGARPYGILAG 224
Cdd:cd00327 78 AVQQVQNGKADIVLAGGSEEF-----------------------------VFGDGAAAAVVESEEHALRRGAHPQAEIVS 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 225 AGSANDAVSAVaPDLSGDCLALAVRRALCDAGLTAHEVGCISTHGTGTRLNDEVETKtySDLFASSPRLPLLFGTKGAFG 304
Cdd:cd00327 129 TAATFDGASMV-PAVSGEGLARAARKALEGAGLTPSDIDYVEAHGTGTPIGDAVELA--LGLDPDGVRSPAVSATLIMTG 205
|
250 260
....*....|....*....|....*
gi 28855065 305 HTLGATGALEAISLLLALGNQQVPP 329
Cdd:cd00327 206 HPLGAAGLAILDELLLMLEHEFIPP 230
|
|
| omega_3_PfaA |
TIGR02813 |
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ... |
131-377 |
7.55e-15 |
|
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: 76.58 E-value: 7.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 131 VSTACSAGADALLLGLSLIRRGFTDTCLCGGADI-LTPAKRLGHSQLGTLSA-DGLRAFDRAHSGTVLGEGAGFLVLETR 208
Cdd:TIGR02813 202 VDAACAGSLAAIRMALSELLEGRSEMMITGGVCTdNSPFMYMSFSKTPAFTTnEDIQPFDIDSKGMMIGEGIGMMALKRL 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 209 AAALARGARPYGILAGAGSANDA--VSAVAPDLSGDclALAVRRALCDAGLTAHEVGCISTHGTGTRLNDEVETKTYSDL 286
Cdd:TIGR02813 282 EDAERDGDRIYAVIKGVGASSDGkfKSIYAPRPEGQ--AKALKRAYDDAGFAPHTCGLIEAHGTGTAAGDVAEFGGLVSV 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 287 FA--SSPRLPLLFGT-KGAFGHTLGATGALEAISLLLALGNQQVPPIVGLENPLTGIAL---PLAMRTAL--------AC 352
Cdd:TIGR02813 360 FSqdNDQKQHIALGSvKSQIGHTKSTAGTAGMIKAVLALHHKVLPPTINVDQPNPKLDIensPFYLNTETrpwmqredGT 439
|
250 260
....*....|....*....|....*
gi 28855065 353 PAEVGISvTLGFGGFDTCLVFQRAR 377
Cdd:TIGR02813 440 PRRAGIS-SFGFGGTNFHMVLEEYS 463
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
21-206 |
2.45e-12 |
|
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: 66.97 E-value: 2.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 21 DDLEVVWQSLLAGRSGIRSVD---FPVALRSPLAsplpdLDPalplperQHRLTVATLRRALQDAGLakateevvpvlat 97
Cdd:smart00825 14 DDPEEFWDLLLAGLDDVDLFDaafFGISPREAEA-----MDP-------QQRLLLEVAWEALEDAGI------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 98 syghhldVPETESLSRWAVEAAreAGCQHAPITVSTACSAGADALLLGLSLIRRGFTDTCLCGGAD-ILTPAKRLGHSQL 176
Cdd:smart00825 69 -------DPESLRGSRTGVFVG--VSSSDYSVTVDTACSSSLVALHLACQSLRSGECDMALAGGVNlILSPDTFVGLSRA 139
|
170 180 190
....*....|....*....|....*....|.
gi 28855065 177 GTLSADGL-RAFDRAHSGTVLGEGAGFLVLE 206
Cdd:smart00825 140 GMLSPDGRcKTFDASADGYVRGEGVGVVVLK 170
|
|
| SCP-x_thiolase |
cd00829 |
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ... |
70-168 |
7.12e-05 |
|
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: 44.56 E-value: 7.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 70 LTVATLRRALQDAGLAKATEEVVpVLATSYGHhldvpetESLSRWAVEAAREAGCQHAPIT-VSTACSAGADALLLGLSL 148
Cdd:cd00829 19 LAAEAARAALDDAGLEPADIDAV-VVGNAAGG-------RFQSFPGALIAEYLGLLGKPATrVEAAGASGSAAVRAAAAA 90
|
90 100
....*....|....*....|
gi 28855065 149 IRRGFTDTCLCGGADILTPA 168
Cdd:cd00829 91 IASGLADVVLVVGAEKMSDV 110
|
|
| thiolase |
cd00751 |
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of ... |
68-200 |
1.56e-03 |
|
Thiolase are ubiquitous enzymes that catalyze the reversible thiolytic cleavage of 3-ketoacyl-CoA into acyl-CoA and acetyl-CoA, a 2-step reaction involving a covalent intermediate formed with a catalytic cysteine. They are found in prokaryotes and eukaryotes (cytosol, microbodies and mitochondria). There are 2 functional different classes: thiolase-I (3-ketoacyl-CoA thiolase) and thiolase-II (acetoacetyl-CoA thiolase). Thiolase-I can cleave longer fatty acid molecules and plays an important role in the beta-oxidative degradation of fatty acids. Thiolase-II has a high substrate specificity. Although it can cleave acetoacyl-CoA, its main function is the synthesis of acetoacyl-CoA from two molecules of acetyl-CoA, which gives it importance in several biosynthetic pathways.
Pssm-ID: 238383 [Multi-domain] Cd Length: 386 Bit Score: 40.15 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 68 HRLTVATLRRALQDAGLAKAT-EEVVpvlatsYGHHLDVPETESLSRWAveaAREAGC-QHAP-ITVSTACSAGADALLL 144
Cdd:cd00751 23 DDLGAAVIKALLERAGLDPEEvDDVI------MGNVLQAGEGQNPARQA---ALLAGLpESVPaTTVNRVCGSGLQAVAL 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28855065 145 GLSLIRRGFTDTCLCGGADILTPA----------KRLGHSQLGTLSADGLRAfdrAHSGTVLGEGA 200
Cdd:cd00751 94 AAQSIAAGEADVVVAGGVESMSRApyllpkarrgGRLGLNTLDGMLDDGLTD---PFTGLSMGITA 156
|
|
| PRK06519 |
PRK06519 |
beta-ketoacyl-ACP synthase; |
1-89 |
5.04e-03 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235819 [Multi-domain] Cd Length: 398 Bit Score: 38.78 E-value: 5.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28855065 1 MVSRPVEVWVTGMAWSTALGDDLEVVWQsLLAGRSGIRSVD------FPValrsplaSPLPDLDPALPLP----ERQ--- 67
Cdd:PRK06519 1 MRMQPNDVVITGIGLVSSLGEGLDAHWN-ALSAGRPQPNVDtetfapYPV-------HPLPEIDWSQQIPkrgdQRQmet 72
|
90 100
....*....|....*....|...
gi 28855065 68 -HRLTVATLRRALQDAGLAKATE 89
Cdd:PRK06519 73 wQRLGTYAAGLALDDAGIKGNEE 95
|
|
| |
