|
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 ... |
583-990 |
0e+00 |
|
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: 618.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 583 KRVVITGMGLVSVFGNDVEAYYEKLLSGESGIAPIDRFDASKFPTRFGGQIRGFKSEGYIDGKNDRRLDDCLRYCIVAGK 662
Cdd:cd00834 1 RRVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRFDASGFPSRIAGEVPDFDPEDYLDRKELRRMDRFAQFALAAAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 663 KALESADLggeKLNTIDKIRGGVLVGTGMGGLTVFSDGVQALIEKGHRKITPFFIPYAITNMGSALLAIDLGLMGPNYSI 742
Cdd:cd00834 81 EALADAGL---DPEELDPERIGVVIGSGIGGLATIEEAYRALLEKGPRRVSPFFVPMALPNMAAGQVAIRLGLRGPNYTV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 743 STACATSNYCFYAAANHIRRGEADLMLAGGTEAAIIPIGLGGFVACRALSQRNDDPQTASRPWDKDRDGFVMGEGAGVLV 822
Cdd:cd00834 158 STACASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALRALSTRNDDPEKASRPFDKDRDGFVLGEGAGVLV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 823 MESLEHAMKRGAPIIAEYLGGAVNCDAYHMTDPRADGLGVSSCIHSALEDAGVSPEEVNYINAHATSTIVGDLAELNAIK 902
Cdd:cd00834 238 LESLEHAKARGAKIYAEILGYGASSDAYHITAPDPDGEGAARAMRAALADAGLSPEDIDYINAHGTSTPLNDAAESKAIK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 903 KVFKNTSE-IKINATKSMIGHCLGAAGGLEAIATVKAITTGWLHPTINQFNPEPSVEFDTVANKKQQHEVNVAISNSFGF 981
Cdd:cd00834 318 RVFGEHAKkVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPECDLDYVPNEAREAPIRYALSNSFGF 397
|
....*....
gi 2074720092 982 GGHNSVVAF 990
Cdd:cd00834 398 GGHNASLVF 406
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
583-993 |
0e+00 |
|
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: 613.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 583 KRVVITGMGLVSVFGNDVEAYYEKLLSGESGIAPIDRFDASKFPTRFGGQIRGFKSEGYIDGKNDRRLDDCLRYCIVAGK 662
Cdd:COG0304 1 RRVVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITRFDASGLPVRIAGEVKDFDPEEYLDRKELRRMDRFTQYALAAAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 663 KALESADLggeKLNTIDKIRGGVLVGTGMGGLTVFSDGVQALIEKGHRKITPFFIPYAITNMGSALLAIDLGLMGPNYSI 742
Cdd:COG0304 81 EALADAGL---DLDEVDPDRTGVIIGSGIGGLDTLEEAYRALLEKGPRRVSPFFVPMMMPNMAAGHVSIRFGLKGPNYTV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 743 STACATSNYCFYAAANHIRRGEADLMLAGGTEAAIIPIGLGGFVACRALSQRNDDPQTASRPWDKDRDGFVMGEGAGVLV 822
Cdd:COG0304 158 STACASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLAGFDALGALSTRNDDPEKASRPFDKDRDGFVLGEGAGVLV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 823 MESLEHAMKRGAPIIAEYLGGAVNCDAYHMTDPRADGLGVSSCIHSALEDAGVSPEEVNYINAHATSTIVGDLAELNAIK 902
Cdd:COG0304 238 LEELEHAKARGAKIYAEVVGYGASSDAYHITAPAPDGEGAARAMRAALKDAGLSPEDIDYINAHGTSTPLGDAAETKAIK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 903 KVFKNT-SEIKINATKSMIGHCLGAAGGLEAIATVKAITTGWLHPTINQFNPEPSVEFDTVANKKQQHEVNVAISNSFGF 981
Cdd:COG0304 318 RVFGDHaYKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPECDLDYVPNEAREAKIDYALSNSFGF 397
|
410
....*....|..
gi 2074720092 982 GGHNSVVAFSAF 993
Cdd:COG0304 398 GGHNASLVFKRY 409
|
|
| PRK06333 |
PRK06333 |
beta-ketoacyl-ACP synthase; |
581-995 |
0e+00 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235781 [Multi-domain] Cd Length: 424 Bit Score: 605.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 581 PKKRVVITGMGLVSVFGNDVEAYYEKLLSGESGIAPIDRFDASKFPTRFGGQIR--------GFKSEGYIDGKNDRRLDD 652
Cdd:PRK06333 2 NKKRIVVTGMGAVSPLGCGVETFWQRLLAGQSGIRTLTDFPVGDLATKIGGQVPdlaedaeaGFDPDRYLDPKDQRKMDR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 653 CLRYCIVAGKKALESADLGGEKLNtiDKIRGGVLVGTGMGGLTVFSDGVQALIEKGHRKITPFFIPYAITNMGSALLAID 732
Cdd:PRK06333 82 FILFAMAAAKEALAQAGWDPDTLE--DRERTATIIGSGVGGFPAIAEAVRTLDSRGPRRLSPFTIPSFLTNMAAGHVSIR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 733 LGLMGPNYSISTACATSNYCFYAAANHIRRGEADLMLAGGTEAAIIPIGLGGFVACRALSQR-NDDPQTASRPWDKDRDG 811
Cdd:PRK06333 160 YGFKGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGGTEAAIDRVSLAGFAAARALSTRfNDAPEQASRPFDRDRDG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 812 FVMGEGAGVLVMESLEHAMKRGAPIIAEYLGGAVNCDAYHMTDPRADGLGVSSCIHSALEDAGVSPEEVNYINAHATSTI 891
Cdd:PRK06333 240 FVMGEGAGILVIETLEHALARGAPPLAELVGYGTSADAYHMTAGPEDGEGARRAMLIALRQAGIPPEEVQHLNAHATSTP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 892 VGDLAELNAIKKVFKNTSEIKINATKSMIGHCLGAAGGLEAIATVKAITTGWLHPTINQFNPEPSVE-FDTVANKKQQHE 970
Cdd:PRK06333 320 VGDLGEVAAIKKVFGHVSGLAVSSTKSATGHLLGAAGGVEAIFTILALRDQIAPPTLNLENPDPAAEgLDVVANKARPMD 399
|
410 420
....*....|....*....|....*
gi 2074720092 971 VNVAISNSFGFGGHNSVVAFSAFKP 995
Cdd:PRK06333 400 MDYALSNGFGFGGVNASILFRRWEP 424
|
|
| fabF |
TIGR03150 |
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 ... |
583-990 |
0e+00 |
|
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 (KAS-II, FabF) is involved in the condensation step of fatty acid biosynthesis in which the malonyl donor group is decarboxylated and the resulting carbanion used to attack and extend the acyl group attached to the acyl carrier protein. Most genomes encoding fatty acid biosynthesis contain a number of condensing enzymes, often of all three types: 1, 2 and 3. Synthase 2 is mechanistically related to synthase 1 (KAS-I, FabB) containing a number of absolutely conserved catalytic residues in common. This model is based primarily on genes which are found in apparent operons with other essential genes of fatty acid biosynthesis (GenProp0681). The large gap between the trusted cutoff and the noise cutoff contains many genes which are not found adjacent to genes of the fatty acid pathway in genomes that often also contain a better hit to this model. These genes may be involved in other processes such as polyketide biosyntheses. Some genomes contain more than one above-trusted hit to this model which may result from recent paralogous expansions. Second hits to this model which are not next to other fatty acid biosynthesis genes may be involved in other processes. FabB sequences should fall well below the noise cutoff of this model. [Fatty acid and phospholipid metabolism, Biosynthesis]
Pssm-ID: 274452 [Multi-domain] Cd Length: 407 Bit Score: 599.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 583 KRVVITGMGLVSVFGNDVEAYYEKLLSGESGIAPIDRFDASKFPTRFGGQIRGFKSEGYIDGKNDRRLDDCLRYCIVAGK 662
Cdd:TIGR03150 1 RRVVVTGLGAVTPLGNGVEEFWENLLAGKSGIGPITRFDASDLPVKIAGEVKDFDPEDYIDKKEARRMDRFIQYALAAAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 663 KALESADLggeKLNTIDKIRGGVLVGTGMGGLTVFSDGVQALIEKGHRKITPFFIPYAITNMGSALLAIDLGLMGPNYSI 742
Cdd:TIGR03150 81 EAVEDSGL---DIEEEDAERVGVIIGSGIGGLETIEEQHIVLLEKGPRRVSPFFIPMSIINMAAGQISIRYGAKGPNHAV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 743 STACATSNYCFYAAANHIRRGEADLMLAGGTEAAIIPIGLGGFVACRALSQRNDDPQTASRPWDKDRDGFVMGEGAGVLV 822
Cdd:TIGR03150 158 VTACATGTHAIGDAFRLIQRGDADVMIAGGAEAAITPLGIAGFAAMKALSTRNDDPEKASRPFDKDRDGFVMGEGAGVLV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 823 MESLEHAMKRGAPIIAEYLGGAVNCDAYHMTDPRADGLGVSSCIHSALEDAGVSPEEVNYINAHATSTIVGDLAELNAIK 902
Cdd:TIGR03150 238 LEELEHAKARGAKIYAEIVGYGMSGDAYHITAPAPEGEGAARAMRAALKDAGINPEDVDYINAHGTSTPLGDKAETKAIK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 903 KVFKN-TSEIKINATKSMIGHCLGAAGGLEAIATVKAITTGWLHPTINQFNPEPSVEFDTVANKKQQHEVNVAISNSFGF 981
Cdd:TIGR03150 318 KVFGDhAYKLAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVPPTINLDNPDPECDLDYVPNEAREAKIDYALSNSFGF 397
|
....*....
gi 2074720092 982 GGHNSVVAF 990
Cdd:TIGR03150 398 GGTNASLVF 406
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
583-829 |
1.32e-61 |
|
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: 209.80 E-value: 1.32e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 583 KRVVITGMGLVSVFGNDVEAYYEKLLSGESGIAPI--DRFDASKF---PTRFGGQIRG--------FKSEGYIDGKNDR- 648
Cdd:pfam00109 1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIpaDRWDPDKLydpPSRIAGKIYTkwgglddiFDFDPLFFGISPRe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 649 --RLDDCLRYCIVAGKKALESAdlgGEKLNTIDKIRGGVLVGTGMGGLtvfsDGVQALIEKG-HRKITPFFIPYaITNMG 725
Cdd:pfam00109 81 aeRMDPQQRLLLEAAWEALEDA---GITPDSLDGSRTGVFIGSGIGDY----AALLLLDEDGgPRRGSPFAVGT-MPSVI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 726 SALLAIDLGLMGPNYSISTACATSNYCFYAAANHIRRGEADLMLAGGTEAAIIPIGLGGFVACRALSQrnDDPQTASRPW 805
Cdd:pfam00109 153 AGRISYFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSP--DGPCKAFDPF 230
|
250 260
....*....|....*....|....
gi 2074720092 806 DkdrDGFVMGEGAGVLVMESLEHA 829
Cdd:pfam00109 231 A---DGFVRGEGVGAVVLKRLSDA 251
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
734-985 |
4.13e-24 |
|
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: 103.56 E-value: 4.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 734 GLMGPNYSIS--TACATSNYCFYAAANHIRRGEADLMLAGGTEAAIIPIGLGGFVACRALSqrnddPQTASRPWDKDRDG 811
Cdd:smart00825 83 GVSSSDYSVTvdTACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLS-----PDGRCKTFDASADG 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 812 FVMGEGAGVLVMESLEHAMKRGAPIIAEYLGGAVNCDAyhmtdpRADGL----GVSSCihsaledagvspeevnyinaha 887
Cdd:smart00825 158 YVRGEGVGVVVLKRLSDALRDGDPILAVIRGSAVNQDG------RSNGItapsGPAQL---------------------- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 888 tstIVGdlaelnaikkvfkntseikinATKSMIGHCLGAAG--GLeaIATVKAITTGWLHPTINQFNPEPSVEFDT---- 961
Cdd:smart00825 210 ---LIG---------------------SVKSNIGHLEAAAGvaGL--IKVVLALKHGVIPPTLHFETPNPHIDLEEsplr 263
|
250 260
....*....|....*....|....*....
gi 2074720092 962 VANKKQQHEVN-----VAIsNSFGFGGHN 985
Cdd:smart00825 264 VPTELTPWPPPgrprrAGV-SSFGFGGTN 291
|
|
| DUF4283 |
pfam14111 |
Domain of unknown function (DUF4283); This domain family is found in plants, and is ... |
32-165 |
1.80e-17 |
|
Domain of unknown function (DUF4283); This domain family is found in plants, and is approximately 100 amino acids in length. Considering the very diverse range of other domains it is associated with it is possible that this domain is a binding/guiding region. There are two highly conserved tryptophan residues.
Pssm-ID: 464086 Cd Length: 145 Bit Score: 80.00 E-value: 1.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 32 VVGRIlSGSRFNFNALKETMLTAFKPRKQIDFEKLDNGRFLLNFESPNDLDKVLEGGPWCYDNDLVILKLLLENDDPLSV 111
Cdd:pfam14111 13 LVGRF-TGKVPSLGAIRRVLARQWGLGGGVKIKELGDGYFLFRFPSEEDLERVLSKGPWLIGNVPMLLQRWSPDFKPTPE 91
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2074720092 112 PLWWVDFYVLAKGLPISKMTKDMASFIGNSLGQFRSVDLARNGVAGGSTLRIRV 165
Cdd:pfam14111 92 ELTTIPIWVQLPGLPLHLWSREVLSKIASAVGKPLETDENTENKTRLSFARVKV 145
|
|
| zf-CCHC_4 |
pfam14392 |
Zinc knuckle; The zinc knuckle is a zinc binding motif composed of the the following ... |
167-212 |
2.74e-09 |
|
Zinc knuckle; The zinc knuckle is a zinc binding motif composed of the the following CX2CX4HX4C where X can be any amino acid. This particular family is found in plant proteins.
Pssm-ID: 433930 Cd Length: 49 Bit Score: 53.49 E-value: 2.74e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2074720092 167 LDVSKPLRRVSFFRAGSN-NFNISYTYERLPNFCYICGIMGHIFQFC 212
Cdd:pfam14392 1 IDITKPLRFFRRIRFPSGeWALIRFKYERLRRFCFICGRLGHSDKFC 47
|
|
| |
|
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 ... |
583-990 |
0e+00 |
|
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: 618.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 583 KRVVITGMGLVSVFGNDVEAYYEKLLSGESGIAPIDRFDASKFPTRFGGQIRGFKSEGYIDGKNDRRLDDCLRYCIVAGK 662
Cdd:cd00834 1 RRVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRFDASGFPSRIAGEVPDFDPEDYLDRKELRRMDRFAQFALAAAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 663 KALESADLggeKLNTIDKIRGGVLVGTGMGGLTVFSDGVQALIEKGHRKITPFFIPYAITNMGSALLAIDLGLMGPNYSI 742
Cdd:cd00834 81 EALADAGL---DPEELDPERIGVVIGSGIGGLATIEEAYRALLEKGPRRVSPFFVPMALPNMAAGQVAIRLGLRGPNYTV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 743 STACATSNYCFYAAANHIRRGEADLMLAGGTEAAIIPIGLGGFVACRALSQRNDDPQTASRPWDKDRDGFVMGEGAGVLV 822
Cdd:cd00834 158 STACASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALRALSTRNDDPEKASRPFDKDRDGFVLGEGAGVLV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 823 MESLEHAMKRGAPIIAEYLGGAVNCDAYHMTDPRADGLGVSSCIHSALEDAGVSPEEVNYINAHATSTIVGDLAELNAIK 902
Cdd:cd00834 238 LESLEHAKARGAKIYAEILGYGASSDAYHITAPDPDGEGAARAMRAALADAGLSPEDIDYINAHGTSTPLNDAAESKAIK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 903 KVFKNTSE-IKINATKSMIGHCLGAAGGLEAIATVKAITTGWLHPTINQFNPEPSVEFDTVANKKQQHEVNVAISNSFGF 981
Cdd:cd00834 318 RVFGEHAKkVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPECDLDYVPNEAREAPIRYALSNSFGF 397
|
....*....
gi 2074720092 982 GGHNSVVAF 990
Cdd:cd00834 398 GGHNASLVF 406
|
|
| FabB |
COG0304 |
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ... |
583-993 |
0e+00 |
|
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: 613.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 583 KRVVITGMGLVSVFGNDVEAYYEKLLSGESGIAPIDRFDASKFPTRFGGQIRGFKSEGYIDGKNDRRLDDCLRYCIVAGK 662
Cdd:COG0304 1 RRVVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITRFDASGLPVRIAGEVKDFDPEEYLDRKELRRMDRFTQYALAAAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 663 KALESADLggeKLNTIDKIRGGVLVGTGMGGLTVFSDGVQALIEKGHRKITPFFIPYAITNMGSALLAIDLGLMGPNYSI 742
Cdd:COG0304 81 EALADAGL---DLDEVDPDRTGVIIGSGIGGLDTLEEAYRALLEKGPRRVSPFFVPMMMPNMAAGHVSIRFGLKGPNYTV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 743 STACATSNYCFYAAANHIRRGEADLMLAGGTEAAIIPIGLGGFVACRALSQRNDDPQTASRPWDKDRDGFVMGEGAGVLV 822
Cdd:COG0304 158 STACASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLAGFDALGALSTRNDDPEKASRPFDKDRDGFVLGEGAGVLV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 823 MESLEHAMKRGAPIIAEYLGGAVNCDAYHMTDPRADGLGVSSCIHSALEDAGVSPEEVNYINAHATSTIVGDLAELNAIK 902
Cdd:COG0304 238 LEELEHAKARGAKIYAEVVGYGASSDAYHITAPAPDGEGAARAMRAALKDAGLSPEDIDYINAHGTSTPLGDAAETKAIK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 903 KVFKNT-SEIKINATKSMIGHCLGAAGGLEAIATVKAITTGWLHPTINQFNPEPSVEFDTVANKKQQHEVNVAISNSFGF 981
Cdd:COG0304 318 RVFGDHaYKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPECDLDYVPNEAREAKIDYALSNSFGF 397
|
410
....*....|..
gi 2074720092 982 GGHNSVVAFSAF 993
Cdd:COG0304 398 GGHNASLVFKRY 409
|
|
| PRK06333 |
PRK06333 |
beta-ketoacyl-ACP synthase; |
581-995 |
0e+00 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235781 [Multi-domain] Cd Length: 424 Bit Score: 605.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 581 PKKRVVITGMGLVSVFGNDVEAYYEKLLSGESGIAPIDRFDASKFPTRFGGQIR--------GFKSEGYIDGKNDRRLDD 652
Cdd:PRK06333 2 NKKRIVVTGMGAVSPLGCGVETFWQRLLAGQSGIRTLTDFPVGDLATKIGGQVPdlaedaeaGFDPDRYLDPKDQRKMDR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 653 CLRYCIVAGKKALESADLGGEKLNtiDKIRGGVLVGTGMGGLTVFSDGVQALIEKGHRKITPFFIPYAITNMGSALLAID 732
Cdd:PRK06333 82 FILFAMAAAKEALAQAGWDPDTLE--DRERTATIIGSGVGGFPAIAEAVRTLDSRGPRRLSPFTIPSFLTNMAAGHVSIR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 733 LGLMGPNYSISTACATSNYCFYAAANHIRRGEADLMLAGGTEAAIIPIGLGGFVACRALSQR-NDDPQTASRPWDKDRDG 811
Cdd:PRK06333 160 YGFKGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGGTEAAIDRVSLAGFAAARALSTRfNDAPEQASRPFDRDRDG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 812 FVMGEGAGVLVMESLEHAMKRGAPIIAEYLGGAVNCDAYHMTDPRADGLGVSSCIHSALEDAGVSPEEVNYINAHATSTI 891
Cdd:PRK06333 240 FVMGEGAGILVIETLEHALARGAPPLAELVGYGTSADAYHMTAGPEDGEGARRAMLIALRQAGIPPEEVQHLNAHATSTP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 892 VGDLAELNAIKKVFKNTSEIKINATKSMIGHCLGAAGGLEAIATVKAITTGWLHPTINQFNPEPSVE-FDTVANKKQQHE 970
Cdd:PRK06333 320 VGDLGEVAAIKKVFGHVSGLAVSSTKSATGHLLGAAGGVEAIFTILALRDQIAPPTLNLENPDPAAEgLDVVANKARPMD 399
|
410 420
....*....|....*....|....*
gi 2074720092 971 VNVAISNSFGFGGHNSVVAFSAFKP 995
Cdd:PRK06333 400 MDYALSNGFGFGGVNASILFRRWEP 424
|
|
| fabF |
TIGR03150 |
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 ... |
583-990 |
0e+00 |
|
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 (KAS-II, FabF) is involved in the condensation step of fatty acid biosynthesis in which the malonyl donor group is decarboxylated and the resulting carbanion used to attack and extend the acyl group attached to the acyl carrier protein. Most genomes encoding fatty acid biosynthesis contain a number of condensing enzymes, often of all three types: 1, 2 and 3. Synthase 2 is mechanistically related to synthase 1 (KAS-I, FabB) containing a number of absolutely conserved catalytic residues in common. This model is based primarily on genes which are found in apparent operons with other essential genes of fatty acid biosynthesis (GenProp0681). The large gap between the trusted cutoff and the noise cutoff contains many genes which are not found adjacent to genes of the fatty acid pathway in genomes that often also contain a better hit to this model. These genes may be involved in other processes such as polyketide biosyntheses. Some genomes contain more than one above-trusted hit to this model which may result from recent paralogous expansions. Second hits to this model which are not next to other fatty acid biosynthesis genes may be involved in other processes. FabB sequences should fall well below the noise cutoff of this model. [Fatty acid and phospholipid metabolism, Biosynthesis]
Pssm-ID: 274452 [Multi-domain] Cd Length: 407 Bit Score: 599.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 583 KRVVITGMGLVSVFGNDVEAYYEKLLSGESGIAPIDRFDASKFPTRFGGQIRGFKSEGYIDGKNDRRLDDCLRYCIVAGK 662
Cdd:TIGR03150 1 RRVVVTGLGAVTPLGNGVEEFWENLLAGKSGIGPITRFDASDLPVKIAGEVKDFDPEDYIDKKEARRMDRFIQYALAAAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 663 KALESADLggeKLNTIDKIRGGVLVGTGMGGLTVFSDGVQALIEKGHRKITPFFIPYAITNMGSALLAIDLGLMGPNYSI 742
Cdd:TIGR03150 81 EAVEDSGL---DIEEEDAERVGVIIGSGIGGLETIEEQHIVLLEKGPRRVSPFFIPMSIINMAAGQISIRYGAKGPNHAV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 743 STACATSNYCFYAAANHIRRGEADLMLAGGTEAAIIPIGLGGFVACRALSQRNDDPQTASRPWDKDRDGFVMGEGAGVLV 822
Cdd:TIGR03150 158 VTACATGTHAIGDAFRLIQRGDADVMIAGGAEAAITPLGIAGFAAMKALSTRNDDPEKASRPFDKDRDGFVMGEGAGVLV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 823 MESLEHAMKRGAPIIAEYLGGAVNCDAYHMTDPRADGLGVSSCIHSALEDAGVSPEEVNYINAHATSTIVGDLAELNAIK 902
Cdd:TIGR03150 238 LEELEHAKARGAKIYAEIVGYGMSGDAYHITAPAPEGEGAARAMRAALKDAGINPEDVDYINAHGTSTPLGDKAETKAIK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 903 KVFKN-TSEIKINATKSMIGHCLGAAGGLEAIATVKAITTGWLHPTINQFNPEPSVEFDTVANKKQQHEVNVAISNSFGF 981
Cdd:TIGR03150 318 KVFGDhAYKLAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVPPTINLDNPDPECDLDYVPNEAREAKIDYALSNSFGF 397
|
....*....
gi 2074720092 982 GGHNSVVAF 990
Cdd:TIGR03150 398 GGTNASLVF 406
|
|
| PLN02787 |
PLN02787 |
3-oxoacyl-[acyl-carrier-protein] synthase II |
575-994 |
0e+00 |
|
3-oxoacyl-[acyl-carrier-protein] synthase II
Pssm-ID: 215421 [Multi-domain] Cd Length: 540 Bit Score: 598.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 575 PKRETDPKK-------RVVITGMGLVSVFGNDVEAYYEKLLSGESGIAPIDRFDASKFPTRFGGQIRGFKSEGYIDGKND 647
Cdd:PLN02787 114 PEKEVETKKkpltkqrRVVVTGMGVVSPLGHDPDVFYNNLLEGVSGISEIERFDCSQFPTRIAGEIKSFSTDGWVAPKLS 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 648 RRLDDCLRYCIVAGKKALESADLGGEKLNTIDKIRGGVLVGTGMGGLTVFSDGVQALiEKGHRKITPFFIPYAITNMGSA 727
Cdd:PLN02787 194 KRMDKFMLYLLTAGKKALADGGITEDVMKELDKTKCGVLIGSAMGGMKVFNDAIEAL-RISYRKMNPFCVPFATTNMGSA 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 728 LLAIDLGLMGPNYSISTACATSNYCFYAAANHIRRGEADLMLAGGTEAAIIPIGLGGFVACRALSQRNDDPQTASRPWDK 807
Cdd:PLN02787 273 MLAMDLGWMGPNYSISTACATSNFCILNAANHIIRGEADVMLCGGSDAAIIPIGLGGFVACRALSQRNDDPTKASRPWDM 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 808 DRDGFVMGEGAGVLVMESLEHAMKRGAPIIAEYLGGAVNCDAYHMTDPRADGLGVSSCIHSALEDAGVSPEEVNYINAHA 887
Cdd:PLN02787 353 NRDGFVMGEGAGVLLLEELEHAKKRGANIYAEFLGGSFTCDAYHMTEPHPEGAGVILCIEKALAQSGVSKEDVNYINAHA 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 888 TSTIVGDLAELNAIKKVFKNTSEIKINATKSMIGHCLGAAGGLEAIATVKAITTGWLHPTINQFNPEPSVEFDT-VANKK 966
Cdd:PLN02787 433 TSTKAGDLKEYQALMRCFGQNPELRVNSTKSMIGHLLGAAGAVEAIATVQAIRTGWVHPNINLENPESGVDTKVlVGPKK 512
|
410 420
....*....|....*....|....*...
gi 2074720092 967 QQHEVNVAISNSFGFGGHNSVVAFSAFK 994
Cdd:PLN02787 513 ERLDIKVALSNSFGFGGHNSSILFAPYK 540
|
|
| PRK07314 |
PRK07314 |
beta-ketoacyl-ACP synthase II; |
582-990 |
0e+00 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 235987 [Multi-domain] Cd Length: 411 Bit Score: 589.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 582 KKRVVITGMGLVSVFGNDVEAYYEKLLSGESGIAPIDRFDASKFPTRFGGQIRGFKSEGYIDGKNDRRLDDCLRYCIVAG 661
Cdd:PRK07314 1 KRRVVVTGLGAVSPLGNDVESTWKNLLAGKSGIGPITHFDTSDLAVKIAGEVKDFNPDDYMSRKEARRMDRFIQYGIAAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 662 KKALESADLggeKLNTIDKIRGGVLVGTGMGGLTVFSDGVQALIEKGHRKITPFFIPYAITNMGSALLAIDLGLMGPNYS 741
Cdd:PRK07314 81 KQAVEDAGL---EITEENADRIGVIIGSGIGGLETIEEQHITLLEKGPRRVSPFFVPMAIINMAAGHVSIRYGAKGPNHS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 742 ISTACATSNYCFYAAANHIRRGEADLMLAGGTEAAIIPIGLGGFVACRALSQRNDDPQTASRPWDKDRDGFVMGEGAGVL 821
Cdd:PRK07314 158 IVTACATGAHAIGDAARLIAYGDADVMVAGGAEAAITPLGIAGFAAARALSTRNDDPERASRPFDKDRDGFVMGEGAGIL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 822 VMESLEHAMKRGAPIIAEYLGGAVNCDAYHMTDPRADGLGVSSCIHSALEDAGVSPEEVNYINAHATSTIVGDLAELNAI 901
Cdd:PRK07314 238 VLEELEHAKARGAKIYAEVVGYGMTGDAYHMTAPAPDGEGAARAMKLALKDAGINPEDIDYINAHGTSTPAGDKAETQAI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 902 KKVFKN-TSEIKINATKSMIGHCLGAAGGLEAIATVKAITTGWLHPTINQFNPEPSVEFDTVANKKQQHEVNVAISNSFG 980
Cdd:PRK07314 318 KRVFGEhAYKVAVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPTINLDNPDEECDLDYVPNEARERKIDYALSNSFG 397
|
410
....*....|
gi 2074720092 981 FGGHNSVVAF 990
Cdd:PRK07314 398 FGGTNASLVF 407
|
|
| PTZ00050 |
PTZ00050 |
3-oxoacyl-acyl carrier protein synthase; Provisional |
592-993 |
2.56e-141 |
|
3-oxoacyl-acyl carrier protein synthase; Provisional
Pssm-ID: 240245 [Multi-domain] Cd Length: 421 Bit Score: 429.11 E-value: 2.56e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 592 LVSVFGNDVEAYYEKLLSGESGIAPIDRFDA----------------SKFPTRFGGQIRGfKSEGYIDGKNDRRLDDCLR 655
Cdd:PTZ00050 1 VVTPLGVGAESTWEALIAGKSGIRKLTEFPKflpdcipeqkalenlvAAMPCQIAAEVDQ-SEFDPSDFAPTKRESRATH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 656 YCIVAGKKALESADLggEKLNTIDKIRGGVLVGTGMGGLTVFSDGVQALIEKGHRKITPFFIPYAITNMGSALLAIDLGL 735
Cdd:PTZ00050 80 FAMAAAREALADAKL--DILSEKDQERIGVNIGSGIGSLADLTDEMKTLYEKGHSRVSPYFIPKILGNMAAGLVAIKHKL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 736 MGPNYSISTACATSNYCFYAAANHIRRGEADLMLAGGTEAAIIPIGLGGFVACRALSQR-NDDPQTASRPWDKDRDGFVM 814
Cdd:PTZ00050 158 KGPSGSAVTACATGAHCIGEAFRWIKYGEADIMICGGTEASITPVSFAGFSRMRALCTKyNDDPQRASRPFDKDRAGFVM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 815 GEGAGVLVMESLEHAMKRGAPIIAEYLGGAVNCDAYHMTDPRADGLGVSSCIHSALEDAG-VSPEEVNYINAHATSTIVG 893
Cdd:PTZ00050 238 GEGAGILVLEELEHALRRGAKIYAEIRGYGSSSDAHHITAPHPDGRGARRCMENALKDGAnININDVDYVNAHATSTPIG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 894 DLAELNAIKKVFKN--TSEIKINATKSMIGHCLGAAGGLEAIATVKAITTGWLHPTINQFNPEPSVEFDTVANKKQQHEV 971
Cdd:PTZ00050 318 DKIELKAIKKVFGDsgAPKLYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINLENPDAECDLNLVQGKTAHPLQ 397
|
410 420
....*....|....*....|....
gi 2074720092 972 NV--AISNSFGFGGHNSVVAFSAF 993
Cdd:PTZ00050 398 SIdaVLSTSFGFGGVNTALLFTKY 421
|
|
| PRK08722 |
PRK08722 |
beta-ketoacyl-ACP synthase II; |
582-993 |
3.32e-136 |
|
beta-ketoacyl-ACP synthase II;
Pssm-ID: 181539 [Multi-domain] Cd Length: 414 Bit Score: 415.56 E-value: 3.32e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 582 KKRVVITGMGLVSVFGNDVEAYYEKLLSGESGIAPIDRFDASKFPTRFGGQIRGFKSEGYIDGKNDRRLDDCLRYCIVAG 661
Cdd:PRK08722 3 KRRVVVTGMGMLSPVGNTVESSWKALLAGQSGIVNIEHFDTTNFSTRFAGLVKDFNCEEYMSKKDARKMDLFIQYGIAAG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 662 KKALESAdlgGEKLNTIDKIRGGVLVGTGMGGLTVFSDGVQALIEKGHRKITPFFIPYAITNMGSALLAIDLGLMGPNYS 741
Cdd:PRK08722 83 IQALDDS---GLEVTEENAHRIGVAIGSGIGGLGLIEAGHQALVEKGPRKVSPFFVPSTIVNMIAGNLSIMRGLRGPNIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 742 ISTACATSNYCFYAAANHIRRGEADLMLAGGTEAAIIPIGLGGFVACRALSQRNDDPQTASRPWDKDRDGFVMGEGAGVL 821
Cdd:PRK08722 160 ISTACTTGLHNIGHAARMIAYGDADAMVAGGAEKASTPLGMAGFGAAKALSTRNDEPQKASRPWDKDRDGFVLGDGAGMM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 822 VMESLEHAMKRGAPIIAEYLGGAVNCDAYHMTDPRADGLGVSSCIHSALEDAGVSPEEVNYINAHATSTIVGDLAELNAI 901
Cdd:PRK08722 240 VLEEYEHAKARGAKIYAELVGFGMSGDAYHMTSPSEDGSGGALAMEAAMRDAGVTGEQIGYVNAHGTSTPAGDVAEIKGI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 902 KKVF--KNTSEIKINATKSMIGHCLGAAGGLEAIATVKAITTGWLHPTINQFNPEPSVEFDTVANKKQQHE-VNVAISNS 978
Cdd:PRK08722 320 KRALgeAGSKQVLVSSTKSMTGHLLGAAGSVEAIITVMSLVDQIVPPTINLDDPEEGLDIDLVPHTARKVEsMEYAICNS 399
|
410
....*....|....*
gi 2074720092 979 FGFGGHNSVVAFSAF 993
Cdd:PRK08722 400 FGFGGTNGSLIFKKM 414
|
|
| PRK08439 |
PRK08439 |
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed |
583-991 |
6.17e-133 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
Pssm-ID: 236265 [Multi-domain] Cd Length: 406 Bit Score: 406.81 E-value: 6.17e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 583 KRVVITGMGLVSVFGNDVEAYYEKLLSGESGIAPIDRFDASKFPTRFGGQIRGFKSEGYIDGKNDRRLDDCLRYCIVAGK 662
Cdd:PRK08439 2 KRVVVTGIGMINSLGLNKESSFKAICNGECGIKKITLFDASDFPVQIAGEITDFDPTEVMDPKEVKKADRFIQLGLKAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 663 KALESADLGGEklnTIDKIRGGVLVGTGMGGLTVFSDGVQALIEKGHRKITPFFIPYAITNMGSALLAIDLGLMGPNYSI 742
Cdd:PRK08439 82 EAMKDAGFLPE---ELDAERFGVSSASGIGGLPNIEKNSIICFEKGPRKISPFFIPSALVNMLGGFISIEHGLKGPNLSS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 743 STACATSNYCFYAAANHIRRGEADLMLAGGTEAAIIPIGLGGFVACRALSQRNDDPQTASRPWDKDRDGFVMGEGAGVLV 822
Cdd:PRK08439 159 VTACAAGTHAIIEAVKTIMLGGADKMLVVGAESAICPVGIGGFAAMKALSTRNDDPKKASRPFDKDRDGFVMGEGAGALV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 823 MESLEHAMKRGAPIIAEYLGGAVNCDAYHMTDPRADglGVSSCIHSALEDAGVSpeEVNYINAHATSTIVGDLAELNAIK 902
Cdd:PRK08439 239 LEEYESAKKRGAKIYAEIIGFGESGDANHITSPAPE--GPLRAMKAALEMAGNP--KIDYINAHGTSTPYNDKNETAALK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 903 KVFKNTSEI-KINATKSMIGHCLGAAGGLEAIATVKAITTGWLHPTINQFNPEPSVEFDTVANKKQQHEVNVAISNSFGF 981
Cdd:PRK08439 315 ELFGSKEKVpPVSSTKGQIGHCLGAAGAIEAVISIMAMRDGILPPTINQETPDPECDLDYIPNVARKAELNVVMSNSFGF 394
|
410
....*....|
gi 2074720092 982 GGHNSVVAFS 991
Cdd:PRK08439 395 GGTNGVVIFK 404
|
|
| PLN02836 |
PLN02836 |
3-oxoacyl-[acyl-carrier-protein] synthase |
581-992 |
1.37e-111 |
|
3-oxoacyl-[acyl-carrier-protein] synthase
Pssm-ID: 215449 [Multi-domain] Cd Length: 437 Bit Score: 351.79 E-value: 1.37e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 581 PKKRVVITGMGLVSVFGNDVEAYYEKLLSGESGI--------------APIDRFDASKFPTRFGGQIRGFKSEGYIDGK- 645
Cdd:PLN02836 4 PTRRVVVTGLGLVTPLGCGVETTWRRLIAGECGVraltqddlkmksedEETQLYTLDQLPSRVAALVPRGTGPGDFDEEl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 646 --NDRRLDDCLRYCIVAGKKALESADLG-GEKLntiDKIRGGVLVGTGMGGLTVFSDGVQALIEKGHRKITPFFIPYAIT 722
Cdd:PLN02836 84 wlNSRSSSRFIGYALCAADEALSDARWLpSEDE---AKERTGVSIGGGIGSITDILEAAQLICEKRLRRLSPFFVPRILI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 723 NMGSALLAIDLGLMGPNYSISTACATSNYCFYAAANHIRRGEADLMLAGGTEAAIIPIGLGGFVACRALSQR-NDDPQTA 801
Cdd:PLN02836 161 NMAAGHVSIRYGFQGPNHAAVTACATGAHSIGDAFRMIQFGDADVMVAGGTESSIDALSIAGFSRSRALSTKfNSCPTEA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 802 SRPWDKDRDGFVMGEGAGVLVMESLEHAMKRGAPIIAEYLGGAVNCDAYHMTDPRADGLGVSSCIHSALEDAGVSPEEVN 881
Cdd:PLN02836 241 SRPFDCDRDGFVIGEGAGVLVLEELEHAKRRGAKIYAEVRGYGMSGDAHHITQPHEDGRGAVLAMTRALQQSGLHPNQVD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 882 YINAHATSTIVGDLAELNAIKKVFKN---TSEIKINATKSMIGHCLGAAGGLEAIATVKAITTGWLHPTINQFNPEPSve 958
Cdd:PLN02836 321 YVNAHATSTPLGDAVEARAIKTVFSEhatSGGLAFSSTKGATGHLLGAAGAVEAIFSVLAIHHGIAPPTLNLERPDPI-- 398
|
410 420 430
....*....|....*....|....*....|....*....
gi 2074720092 959 FDT-----VANKKQQheVNVAISNSFGFGGHNSVVAFSA 992
Cdd:PLN02836 399 FDDgfvplTASKAML--IRAALSNSFGFGGTNASLLFTS 435
|
|
| PRK07910 |
PRK07910 |
beta-ketoacyl-ACP synthase; |
585-993 |
7.15e-92 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236129 [Multi-domain] Cd Length: 418 Bit Score: 298.95 E-value: 7.15e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 585 VVITGMGLVSVFGNDVEAYYEKLLSGESGIAPIDRFDASKF--PTRFGGQIRGfKSEGYIDGKNDRRLDDCLRYCIVAGK 662
Cdd:PRK07910 14 VVVTGIAMTTALATDAETTWKLLLDGQSGIRTLDDPFVEEFdlPVRIGGHLLE-EFDHQLTRVELRRMSYLQRMSTVLGR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 663 KALESAdlGGEKlntIDKIRGGVLVGTGMGGLTVFSDGVQALIEKGHRKITPFFIPYAITNMGSALLAIDLGLMGPNYSI 742
Cdd:PRK07910 93 RVWENA--GSPE---VDTNRLMVSIGTGLGSAEELVFAYDDMRARGLRAVSPLAVQMYMPNGPAAAVGLERHAKAGVITP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 743 STACATSNYCFYAAANHIRRGEADLMLAGGTEAAIIPIGLGGFVACRA-LSQRNDDPQTASRPWDKDRDGFVMGEGAGVL 821
Cdd:PRK07910 168 VSACASGSEAIAQAWRQIVLGEADIAICGGVETRIEAVPIAGFAQMRIvMSTNNDDPAGACRPFDKDRDGFVFGEGGALM 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 822 VMESLEHAMKRGAPIIAEYLGGAVNCDAYHMTDPRADGLGVSSCIHSALEDAGVSPEEVNYINAHATSTIVGDLAELNAI 901
Cdd:PRK07910 248 VIETEEHAKARGANILARIMGASITSDGFHMVAPDPNGERAGHAMTRAIELAGLTPGDIDHVNAHATGTSVGDVAEGKAI 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 902 KKVFKNtSEIKINATKSMIGHCLGAAGGLEAIATVKAITTGWLHPTINQFNPEPSVEFDTVANKKQQHEVNVAISNSFGF 981
Cdd:PRK07910 328 NNALGG-HRPAVYAPKSALGHSVGAVGAVESILTVLALRDGVIPPTLNLENLDPEIDLDVVAGEPRPGNYRYAINNSFGF 406
|
410
....*....|..
gi 2074720092 982 GGHNSVVAFSAF 993
Cdd:PRK07910 407 GGHNVALAFGRY 418
|
|
| PRK07967 |
PRK07967 |
beta-ketoacyl-ACP synthase I; |
583-994 |
8.62e-86 |
|
beta-ketoacyl-ACP synthase I;
Pssm-ID: 181184 [Multi-domain] Cd Length: 406 Bit Score: 281.94 E-value: 8.62e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 583 KRVVITGMGLVSVFGNDVEAYYEKLLSGESGIAPIDRFDASKFPTRFGGQIRgFKSEGYIDGKNDRRLDDCLRYCIVAGK 662
Cdd:PRK07967 2 RRVVITGLGIVSSIGNNQQEVLASLREGRSGITFSPEFAEMGMRSQVWGNVK-LDPTGLIDRKVMRFMGDASAYAYLAME 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 663 KALESADLGGEKlntIDKIRGGVLVGTGmGGLTVF----SDGVQAliEKGHRKITPFFIPYAITNMGSALLAIDLGLMGP 738
Cdd:PRK07967 81 QAIADAGLSEEQ---VSNPRTGLIAGSG-GGSTRNqveaADAMRG--PRGPKRVGPYAVTKAMASTVSACLATPFKIKGV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 739 NYSISTACATSNYCFYAAANHIRRGEADLMLAGGTE------AAIipiglggFVACRALS-QRNDDPQTASRPWDKDRDG 811
Cdd:PRK07967 155 NYSISSACATSAHCIGNAVEQIQLGKQDIVFAGGGEeldwemSCL-------FDAMGALStKYNDTPEKASRAYDANRDG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 812 FVMGEGAGVLVMESLEHAMKRGAPIIAEYLGGAVNCDAYHMTDPraDGLGVSSCIHSALedAGVSpEEVNYINAHATSTI 891
Cdd:PRK07967 228 FVIAGGGGVVVVEELEHALARGAKIYAEIVGYGATSDGYDMVAP--SGEGAVRCMQMAL--ATVD-TPIDYINTHGTSTP 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 892 VGDLAELNAIKKVFKNTSEiKINATKSMIGHCLGAAGGLEAIATVKAITTGWLHPTINQFNPEPSVE-FDTVANKKQQHE 970
Cdd:PRK07967 303 VGDVKELGAIREVFGDKSP-AISATKSLTGHSLGAAGVQEAIYSLLMMEHGFIAPSANIEELDPQAAgMPIVTETTDNAE 381
|
410 420
....*....|....*....|....
gi 2074720092 971 VNVAISNSFGFGGHNSVVAFSAFK 994
Cdd:PRK07967 382 LTTVMSNSFGFGGTNATLVFRRYK 405
|
|
| PRK06501 |
PRK06501 |
beta-ketoacyl-ACP synthase; |
579-992 |
4.01e-85 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235817 [Multi-domain] Cd Length: 425 Bit Score: 280.75 E-value: 4.01e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 579 TDPKKR--VVITGMGLVSVFGNDVEAYYEKLLSGESGIAPIDRFDASKFPTRFGGQIRGFKSEGYIDGKNDRRLDDclry 656
Cdd:PRK06501 5 RDHLGRpiVAVTGMGVVTSLGQGKADNWAALTAGESGIHTITRFPTEGLRTRIAGTVDFLPESPFGASALSEALAR---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 657 ciVAGKKALESADLGGEKLNtidkirGGVLVGT--------------GMGGLTVFSDGVQALIEKGHRKITPFFipyAIT 722
Cdd:PRK06501 81 --LAAEEALAQAGIGKGDFP------GPLFLAAppvelewparfalaAAVGDNDAPSYDRLLRAARGGRFDALH---ERF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 723 NMGS--ALLAIDLGLMGPNYSISTACATSNYCFYAAANHIRRGEADLMLAGGTEAAIIPIGLGGFVACRALSQRNDDPQT 800
Cdd:PRK06501 150 QFGSiaDRLADRFGTRGLPISLSTACASGATAIQLGVEAIRRGETDRALCIATDGSVSAEALIRFSLLSALSTQNDPPEK 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 801 ASRPWDKDRDGFVMGEGAGVLVMESLEHAMKRGAPIIAEYLGGAVNCDAYHMTDPRADGLGVSSCIHSALEDAGVSPEEV 880
Cdd:PRK06501 230 ASKPFSKDRDGFVMAEGAGALVLESLESAVARGAKILGIVAGCGEKADSFHRTRSSPDGSPAIGAIRAALADAGLTPEQI 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 881 NYINAHATSTIVGDLAELNAIKKVF-KNTSEIKINATKSMIGHCLGAAGGLEAIATVKAITTGWLHPTINQFNPEPSVEF 959
Cdd:PRK06501 310 DYINAHGTSTPENDKMEYLGLSAVFgERLASIPVSSNKSMIGHTLTAAGAVEAVFSLLTIQTGRLPPTINYDNPDPAIPL 389
|
410 420 430
....*....|....*....|....*....|...
gi 2074720092 960 DTVANKKQQHEVNVAISNSFGFGGHNSVVAFSA 992
Cdd:PRK06501 390 DVVPNVARDARVTAVLSNSFGFGGQNASLVLTA 422
|
|
| PRK09116 |
PRK09116 |
beta-ketoacyl-ACP synthase; |
583-990 |
1.31e-82 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 181657 [Multi-domain] Cd Length: 405 Bit Score: 273.40 E-value: 1.31e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 583 KRVVITGMGLVSVFGNDVEAYYEKLLSGESGIAPIDRFDasKFP---TRFGGQIRGFKSEGYIDGKNDRRLDDCLRYCIV 659
Cdd:PRK09116 2 RRVVVTGMGGVTALGEDWQTIAARLKAGRNAVRRMPEWD--RYDglnTRLAAPIDDFELPAHYTRKKIRSMGRVSLMATR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 660 AGKKALESADLGGEKlnTIDKIRGGVLVGTGMGGLTVFSDGVQALIEKGHRKITPF----FIPY-AITNMGsallaIDLG 734
Cdd:PRK09116 80 ASELALEDAGLLGDP--ILTDGRMGIAYGSSTGSTDPIGAFGTMLLEGSMSGITATtyvrMMPHtTAVNVG-----LFFG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 735 LMGPNYSISTACATSNYCFYAAANHIRRGEADLMLAGG------TEAAIipiglggFVACRALSQRNDDPQTASRPWDKD 808
Cdd:PRK09116 153 LKGRVIPTSSACTSGSQGIGYAYEAIKYGYQTVMLAGGaeelcpTEAAV-------FDTLFATSTRNDAPELTPRPFDAN 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 809 RDGFVMGEGAGVLVMESLEHAMKRGAPIIAEYLGGAVNCDAYHMTDPRADGLGVssCIHSALEDAGVSPEEVNYINAHAT 888
Cdd:PRK09116 226 RDGLVIGEGAGTLVLEELEHAKARGATIYAEIVGFGTNSDGAHVTQPQAETMQI--AMELALKDAGLAPEDIGYVNAHGT 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 889 STIVGDLAELNAIKKVFKNTseIKINATKSMIGHCLGAAGGLEAIATVKAITTGWLHPTINQFNPEPSV-EFDTVANKKQ 967
Cdd:PRK09116 304 ATDRGDIAESQATAAVFGAR--MPISSLKSYFGHTLGACGALEAWMSIEMMNEGWFAPTLNLTQVDPACgALDYIMGEAR 381
|
410 420
....*....|....*....|...
gi 2074720092 968 QHEVNVAISNSFGFGGHNSVVAF 990
Cdd:PRK09116 382 EIDTEYVMSNNFAFGGINTSLIF 404
|
|
| elong_cond_enzymes |
cd00828 |
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ... |
584-988 |
6.06e-82 |
|
"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: 271.62 E-value: 6.06e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 584 RVVITGMGLVS---VFGNDVEAYYEKLLSGESGIAPIDRFDaSKFPTRFGGQIRGFKSEGYiDGKNDRRLDDCLRYCIVA 660
Cdd:cd00828 2 RVVITGIGVVSphgEGCDEVEEFWEALREGRSGIAPVARLK-SRFDRGVAGQIPTGDIPGW-DAKRTGIVDRTTLLALVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 661 GKKALESADLGGEKLNTIDKIrgGVLVGTGMGGLTVFSDGVQALiekgHRKITPFFIPYAI--TNMGSALLAIDLGLM-G 737
Cdd:cd00828 80 TEEALADAGITDPYEVHPSEV--GVVVGSGMGGLRFLRRGGKLD----ARAVNPYVSPKWMlsPNTVAGWVNILLLSShG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 738 PNYSISTACATSNYCFYAAANHIRRGEADLMLAGGTEAaIIPIGLGGFVACRALSQRNDDPQTASRPWDKDRDGFVMGEG 817
Cdd:cd00828 154 PIKTPVGACATALEALDLAVEAIRSGKADIVVVGGVED-PLEEGLSGFANMGALSTAEEEPEEMSRPFDETRDGFVEAEG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 818 AGVLVMESLEHAMKRGAPIIAEYLGGAVNCDAYHMTDPrADGLGVSSCIHSALEDAGVSPEEVNYINAHATSTIVGDLAE 897
Cdd:cd00828 233 AGVLVLERAELALARGAPIYGRVAGTASTTDGAGRSVP-AGGKGIARAIRTALAKAGLSLDDLDVISAHGTSTPANDVAE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 898 LNAIKKVFKN-TSEIKINATKSMIGHCLGAAGGLEAIATVKAITTGWLHPTIN--QFNPEPSVEFDTVANKKQQHEVNVA 974
Cdd:cd00828 312 SRAIAEVAGAlGAPLPVTAQKALFGHSKGAAGALQLIGALQSLEHGLIPPTANldDVDPDVEHLSVVGLSRDLNLKVRAA 391
|
410
....*....|....
gi 2074720092 975 ISNSFGFGGHNSVV 988
Cdd:cd00828 392 LVNAFGFGGSNAAL 405
|
|
| PRK14691 |
PRK14691 |
3-oxoacyl-(acyl carrier protein) synthase II; Provisional |
655-988 |
5.30e-81 |
|
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
Pssm-ID: 173154 [Multi-domain] Cd Length: 342 Bit Score: 266.98 E-value: 5.30e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 655 RYCIVAGKKALESADlggeklNTIDKIRGGVLVGTGMGGLTVFSDGVQALIEKGHRKITPFFIPYAITNMGSALLAIDLG 734
Cdd:PRK14691 6 RYKWITFHPSLTHAD------NTEKQERTATIIGAGIGGFPAIAHAVRTSDSRGPKRLSPFTVPSFLVNLAAGHVSIKHH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 735 LMGPNYSISTACATSNYCFYAAANHIRRGEADLMLAGGTEAAIIPIGLGGFVACRALSQR-NDDPQTASRPWDKDRDGFV 813
Cdd:PRK14691 80 FKGPIGAPVTACAAGVQAIGDAVRMIRNNEADVALCGGAEAVIDTVSLAGFAAARALSTHfNSTPEKASRPFDTARDGFV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 814 MGEGAGVLVMESLEHAMKRGAPIIAEYLGGAVNCDAYHMTDPRADGLGVSSCIHSALEDAGVSPEEVNYINAHATSTIVG 893
Cdd:PRK14691 160 MGEGAGLLIIEELEHALARGAKPLAEIVGYGTSADAYHMTSGAEDGDGAYRAMKIALRQAGITPEQVQHLNAHATSTPVG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 894 DLAELNAIKKVFKNTSEIKINATKSMIGHCLGAAGGLEAIATVKAITTGWLHPTINQFNPEPSVE-FDTVANKKQQHEVN 972
Cdd:PRK14691 240 DLGEINAIKHLFGESNALAITSTKSATGHLLGAAGGLETIFTVLALRDQIVPATLNLENPDPAAKgLNIIAGNAQPHDMT 319
|
330
....*....|....*.
gi 2074720092 973 VAISNSFGFGGHNSVV 988
Cdd:PRK14691 320 YALSNGFGFAGVNASI 335
|
|
| PRK07103 |
PRK07103 |
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated |
582-988 |
8.56e-73 |
|
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
Pssm-ID: 180839 [Multi-domain] Cd Length: 410 Bit Score: 246.87 E-value: 8.56e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 582 KKRVVITGMGLVSVFGNDVEAYYEKLLSGESGIAPIDR--------FDASKFPTRFGGQIRGFKSEGYIDGKNDRRLDDC 653
Cdd:PRK07103 1 MDEVVVTGVGVVSAIGQGRPSFAAALLAGRHAFGVMRRpgrqvpddAGAGLASAFIGAELDSLALPERLDAKLLRRASLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 654 LRYCIVAGKKALESADLGGeklntIDKIRGGVLVGtgmgGLTVFSDgVQALIEKGHRKiTPFFIP--YAITNMGSALLAI 731
Cdd:PRK07103 81 AQAALAAAREAWRDAALGP-----VDPDRIGLVVG----GSNLQQR-EQALVHETYRD-RPAFLRpsYGLSFMDTDLVGL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 732 ---DLGLMGPNYSISTACATSNYCFYAAANHIRRGEADLMLAGGTEAAIIPIGLGGFVACRAL-SQRN-DDPQTASRPWD 806
Cdd:PRK07103 150 cseQFGIRGEGFTVGGASASGQLAVIQAARLVQSGSVDACIAVGALMDLSYWECQALRSLGAMgSDRFaDEPEAACRPFD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 807 KDRDGFVMGEGAGVLVMESLEHAMKRGAPIIAEYLGGAVNCDAYHMTDPraDGLGVSSCIHSALEDAGVSPEEVNYINAH 886
Cdd:PRK07103 230 QDRDGFIYGEACGAVVLESAESARRRGARPYAKLLGWSMRLDANRGPDP--SLEGEMRVIRAALRRAGLGPEDIDYVNPH 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 887 ATSTIVGDLAELNAIKKVfkNTSEIKINATKSMIGHCLGAAGGLEAIATVKAITTGWLHPTINQFNP-EPSveFDTVANK 965
Cdd:PRK07103 308 GTGSPLGDETELAALFAS--GLAHAWINATKSLTGHGLSAAGIVELIATLLQMRAGFLHPSRNLDEPiDER--FRWVGST 383
|
410 420
....*....|....*....|...
gi 2074720092 966 KQQHEVNVAISNSFGFGGHNSVV 988
Cdd:PRK07103 384 AESARIRYALSLSFGFGGINTAL 406
|
|
| PKS |
cd00833 |
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ... |
584-986 |
6.21e-63 |
|
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: 219.74 E-value: 6.21e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 584 RVVITGMGLVsvF--GNDVEAYYEKLLSGESGIAPI--DRFDASKFPTRFGGQIRGF-KSEGYIDGKND----------- 647
Cdd:cd00833 2 PIAIVGMACR--FpgAADPDEFWENLLEGRDAISEIpeDRWDADGYYPDPGKPGKTYtRRGGFLDDVDAfdaaffgispr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 648 --RRLDDCLRYCIVAGKKALESAdlgGEKLNTIDKIRGGVLVGtgmggltVFSDGVQALIEKGHRKITPFFIPYAITNMG 725
Cdd:cd00833 80 eaEAMDPQQRLLLEVAWEALEDA---GYSPESLAGSRTGVFVG-------ASSSDYLELLARDPDEIDAYAATGTSRAFL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 726 SALLAIDLGLMGPNYSISTACATSNYCFYAAANHIRRGEADLMLAGGTEAAIIPIGLGGFVACRALSqrnDDPQtaSRPW 805
Cdd:cd00833 150 ANRISYFFDLRGPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLS---PDGR--CRPF 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 806 DKDRDGFVMGEGAGVLVMESLEHAMKRGAPIIAEYLGGAVNCDAY--HMTDPRADGLgvSSCIHSALEDAGVSPEEVNYI 883
Cdd:cd00833 225 DADADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRtkGITAPSGEAQ--AALIRRAYARAGVDPSDIDYV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 884 NAHATSTIVGDLAELNAIKKVFKNTSE----IKINATKSMIGHCLGAAGGLEAIATVKAITTGWLHPTINQFNPEPSVEF 959
Cdd:cd00833 303 EAHGTGTPLGDPIEVEALAKVFGGSRSadqpLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKIDF 382
|
410 420 430
....*....|....*....|....*....|....*
gi 2074720092 960 D----TVANKKQQHEVNVAIS----NSFGFGGHNS 986
Cdd:cd00833 383 EesplRVPTEARPWPAPAGPRragvSSFGFGGTNA 417
|
|
| ketoacyl-synt |
pfam00109 |
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
583-829 |
1.32e-61 |
|
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: 209.80 E-value: 1.32e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 583 KRVVITGMGLVSVFGNDVEAYYEKLLSGESGIAPI--DRFDASKF---PTRFGGQIRG--------FKSEGYIDGKNDR- 648
Cdd:pfam00109 1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIpaDRWDPDKLydpPSRIAGKIYTkwgglddiFDFDPLFFGISPRe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 649 --RLDDCLRYCIVAGKKALESAdlgGEKLNTIDKIRGGVLVGTGMGGLtvfsDGVQALIEKG-HRKITPFFIPYaITNMG 725
Cdd:pfam00109 81 aeRMDPQQRLLLEAAWEALEDA---GITPDSLDGSRTGVFIGSGIGDY----AALLLLDEDGgPRRGSPFAVGT-MPSVI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 726 SALLAIDLGLMGPNYSISTACATSNYCFYAAANHIRRGEADLMLAGGTEAAIIPIGLGGFVACRALSQrnDDPQTASRPW 805
Cdd:pfam00109 153 AGRISYFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSP--DGPCKAFDPF 230
|
250 260
....*....|....*....|....
gi 2074720092 806 DkdrDGFVMGEGAGVLVMESLEHA 829
Cdd:pfam00109 231 A---DGFVRGEGVGAVVLKRLSDA 251
|
|
| PRK05952 |
PRK05952 |
beta-ketoacyl-ACP synthase; |
584-991 |
2.51e-60 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235653 [Multi-domain] Cd Length: 381 Bit Score: 211.06 E-value: 2.51e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 584 RVVITGMGLVSVFGnDVEAYYEKLLSGESGIAPIDRFdaSKFPTRFGGQIrgfksegyidGKNDRRLDDCLRYCIVAgkk 663
Cdd:PRK05952 3 KVVVTGIGLVSALG-DLEQSWQRLLQGKSGIKLHQPF--PELPPLPLGLI----------GNQPSSLEDLTKTVVTA--- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 664 ALESADLggeklnTIDKIRGGVLVGTgmggltvfSDGVQALIEKGHRKITPFFIPYAIT-----------NMGSALLAID 732
Cdd:PRK05952 67 ALKDAGL------TPPLTDCGVVIGS--------SRGCQGQWEKLARQMYQGDDSPDEEldlenwldtlpHQAAIAAARQ 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 733 LGLMGPNYSISTACATSNYCFYAAANHIRRGEADLMLAGGTEAAIIPIGLGGFVACRALSQrnddpqTASRPWDKDRDGF 812
Cdd:PRK05952 133 IGTQGPVLAPMAACATGLWAIAQGVELIQTGQCQRVIAGAVEAPITPLTLAGFQQMGALAK------TGAYPFDRQREGL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 813 VMGEGAGVLVMESLEHAMKRGAPIIAEYLGGAVNCDAYHMTDPRADGLGVSSCIHSALEDAGVSPEEVNYINAHATSTIV 892
Cdd:PRK05952 207 VLGEGGAILVLESAELAQKRGAKIYGQILGFGLTCDAYHMSAPEPDGKSAIAAIQQCLARSGLTPEDIDYIHAHGTATRL 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 893 GDLAELNAIKKVFknTSEIKINATKSMIGHCLGAAGGLEAIATVKAITTGWLHPTINQFNPEPSVEFDTVAnkkQQHEVN 972
Cdd:PRK05952 287 NDQREANLIQALF--PHRVAVSSTKGATGHTLGASGALGVAFSLLALRHQQLPPCVGLQEPEFDLNFVRQA---QQSPLQ 361
|
410
....*....|....*....
gi 2074720092 973 VAISNSFGFGGHNSVVAFS 991
Cdd:PRK05952 362 NVLCLSFGFGGQNAAIALG 380
|
|
| CLF |
cd00832 |
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ... |
583-988 |
4.06e-57 |
|
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: 202.59 E-value: 4.06e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 583 KRVVITGMGLVSVFGNDVEAYYEKLLSGESGIAPIDRFDASKFPTRFGGQIRGFKSEGYIDGKNDRRLDDCLRYCIVAGK 662
Cdd:cd00832 1 RRAVVTGIGVVAPNGLGVEEYWKAVLDGRSGLGPITRFDPSGYPARLAGEVPDFDAAEHLPGRLLPQTDRMTRLALAAAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 663 KALESADLGGEKLNTIDKirgGVLVGTGMGGLTVFSDGVQALIEKGHRKITPF-----FipYAITnmgSALLAIDLGLMG 737
Cdd:cd00832 81 WALADAGVDPAALPPYDM---GVVTASAAGGFEFGQRELQKLWSKGPRHVSAYqsfawF--YAVN---TGQISIRHGMRG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 738 PNYSISTACATSNYCFYAAANHIRRGeADLMLAGGTEAAIIPIGLGGFVACRALSqRNDDPQTASRPWDKDRDGFVMGEG 817
Cdd:cd00832 153 PSGVVVAEQAGGLDALAQARRLVRRG-TPLVVSGGVDSALCPWGWVAQLSSGRLS-TSDDPARAYLPFDAAAAGYVPGEG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 818 AGVLVMESLEHAMKRGAPIIAEYLGGAVNcdayhMTDPRADGL--GVSSCIHSALEDAGVSPEEVNYINAHATSTIVGDL 895
Cdd:cd00832 231 GAILVLEDAAAARERGARVYGEIAGYAAT-----FDPPPGSGRppGLARAIRLALADAGLTPEDVDVVFADAAGVPELDR 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 896 AELNAIKKVFkNTSEIKINATKSMIGHCLGAAGGLEAIATVKAITTGWLHPTINQFNPEPSVEFDTVANKKQQHEVNVAI 975
Cdd:cd00832 306 AEAAALAAVF-GPRGVPVTAPKTMTGRLYAGGAPLDVATALLALRDGVIPPTVNVTDVPPAYGLDLVTGRPRPAALRTAL 384
|
410
....*....|...
gi 2074720092 976 SNSFGFGGHNSVV 988
Cdd:cd00832 385 VLARGRGGFNSAL 397
|
|
| decarbox_cond_enzymes |
cd00825 |
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ... |
655-989 |
1.61e-54 |
|
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: 192.85 E-value: 1.61e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 655 RYCIVAGKKALESADLGGEKLNTIdkiRGGVLVGTGMGGLTVFSDGVQALIEKGHRKITPFFIPYAitnmgSALLAIDLG 734
Cdd:cd00825 13 ILGFEAAERAIADAGLSREYQKNP---IVGVVVGTGGGSPRFQVFGADAMRAVGPYVVTKAMFPGA-----SGQIATPLG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 735 LMGPNYSISTACATSNYCFYAAANHIRRGEADLMLAGGTEAAIIPIGLGGFVACRALSqrnddPQTASRPWDKDRDGFVM 814
Cdd:cd00825 85 IHGPAYDVSAACAGSLHALSLAADAVQNGKQDIVLAGGSEELAAPMDCEFDAMGALST-----PEKASRTFDAAADGFVF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 815 GEGAGVLVMESLEHAMKRGAPIIAEYLGGAVNCDAYHMTDPRADGLGVSSCIHSALEDAGVSPEEVNYINAHATSTIVGD 894
Cdd:cd00825 160 GDGAGALVVEELEHALARGAHIYAEIVGTAATIDGAGMGAFAPSAEGLARAAKEALAVAGLTVWDIDYLVAHGTGTPIGD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 895 LAELNAIKKVFKNTSeIKINATKSMIGHCLGAAGGLEAIATVKAITTGWLHPTINQFNPEPSVefDTVANKKQQHEVNVA 974
Cdd:cd00825 240 VKELKLLRSEFGDKS-PAVSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIPPSIHIEELDEAG--LNIVTETTPRELRTA 316
|
330
....*....|....*
gi 2074720092 975 ISNSFGFGGHNSVVA 989
Cdd:cd00825 317 LLNGFGLGGTNATLV 331
|
|
| PRK09185 |
PRK09185 |
beta-ketoacyl-ACP synthase; |
682-985 |
8.63e-48 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 236398 [Multi-domain] Cd Length: 392 Bit Score: 175.42 E-value: 8.63e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 682 RGGVLVGTGMGGLtvfSDGVQALiekGHRKITPFFIP----YAITNMGSA--LLAIDLGLMGPNYSISTACATSNYCFYA 755
Cdd:PRK09185 96 RIGVVLGTSTSGI---LEGELAY---RRRDPAHGALPadyhYAQQELGSLadFLRAYLGLSGPAYTISTACSSSAKVFAS 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 756 AANHIRRGEADLMLAGG-------TeaaiipigLGGFVACRALSQrnddpqTASRPWDKDRDGFVMGEGAGVLVMEsleh 828
Cdd:PRK09185 170 ARRLLEAGLCDAAIVGGvdslcrlT--------LNGFNSLESLSP------QPCRPFSANRDGINIGEAAAFFLLE---- 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 829 amkRGAPIIAEYLGGAVNCDAYHMTDPRADGLGVSSCIHSALEDAGVSPEEVNYINAHATSTIVGDLAELNAIKKVFKNT 908
Cdd:PRK09185 232 ---REDDAAVALLGVGESSDAHHMSAPHPEGLGAILAMQQALADAGLAPADIGYINLHGTATPLNDAMESRAVAAVFGDG 308
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2074720092 909 seIKINATKSMIGHCLGAAGGLEAIATVKAITTGWLHPTINQFNPEPSVEFDTVANKKQQHEVNVAISNSFGFGGHN 985
Cdd:PRK09185 309 --VPCSSTKGLTGHTLGAAGAVEAAICWLALRHGLPPHGWNTGQPDPALPPLYLVENAQALAIRYVLSNSFAFGGNN 383
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
585-985 |
8.05e-44 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 173.52 E-value: 8.05e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 585 VVITGMGlvSVF--GNDVEAYYEKLLSGESGIAPI--DRFDASKF-----------PTRFGG---QIRGFksegyidgkn 646
Cdd:COG3321 6 IAIIGMA--CRFpgADDPEEFWRNLRAGRDAITEVpaDRWDADAYydpdpdapgktYVRWGGfldDVDEF---------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 647 drrldDCLRYCI-----------------VAgKKALESADLGGEKLntiDKIRGGVLVGTGMGGLTVFSDGVQALIEkgh 709
Cdd:COG3321 74 -----DALFFGIspreaeamdpqqrllleVA-WEALEDAGYDPESL---AGSRTGVFVGASSNDYALLLLADPEAID--- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 710 rkitpffiPYAIT-NMGSAL---LAIDLGLMGPNYSISTACATSNYCFYAAANHIRRGEADLMLAGGTeAAIIPIGLG-G 784
Cdd:COG3321 142 --------AYALTgNAKSVLagrISYKLDLRGPSVTVDTACSSSLVAVHLACQSLRSGECDLALAGGV-NLMLTPESFiL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 785 FVACRALSqrnddPQTASRPWDKDRDGFVMGEGAGVLVMESLEHAMKRGAPIIAEYLGGAVNCD-AYH-MTDPRadGLGV 862
Cdd:COG3321 213 FSKGGMLS-----PDGRCRAFDADADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDgRSNgLTAPN--GPAQ 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 863 SSCIHSALEDAGVSPEEVNYINAHATSTIVGDLAELNAIKKVF-KNTSE---IKINATKSMIGHCLGAAG--GLeaIATV 936
Cdd:COG3321 286 AAVIRRALADAGVDPATVDYVEAHGTGTPLGDPIEAAALTAAFgQGRPAdqpCAIGSVKSNIGHLEAAAGvaGL--IKAV 363
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2074720092 937 KAITTGWLHPTINQFNPEPSVEFDT----VAN-----KKQQHEVNVAISnSFGFGGHN 985
Cdd:COG3321 364 LALRHGVLPPTLHFETPNPHIDFENspfyVNTelrpwPAGGGPRRAGVS-SFGFGGTN 420
|
|
| Ketoacyl-synt_C |
pfam02801 |
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ... |
838-949 |
1.64e-41 |
|
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: 147.71 E-value: 1.64e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 838 AEYLGGAVNCDAYHMTDPRADGLGVSSCIHSALEDAGVSPEEVNYINAHATSTIVGDLAELNAIKKVF---KNTSEIKIN 914
Cdd:pfam02801 2 AVIKGSAVNHDGRHNGLTAPNGEGQARAIRRALADAGVDPEDVDYVEAHGTGTPLGDPIEAEALKRVFgsgARKQPLAIG 81
|
90 100 110
....*....|....*....|....*....|....*
gi 2074720092 915 ATKSMIGHCLGAAGGLEAIATVKAITTGWLHPTIN 949
Cdd:pfam02801 82 SVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLN 116
|
|
| cond_enzymes |
cd00327 |
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ... |
729-988 |
2.70e-31 |
|
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) Claisen-like condensation reaction. Members are share strong structural similarity, and are involved in the synthesis and degradation of fatty acids, and the production of polyketides, a diverse group of natural products.
Pssm-ID: 238201 [Multi-domain] Cd Length: 254 Bit Score: 123.32 E-value: 2.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 729 LAIDLGLM-GPNYSISTACATSNYCFYAAANHIRRGEADLMLAGGTEAaiipiglggfvacralsqrnddpqtasrpwdk 807
Cdd:cd00327 50 LAYHLGISgGPAYSVNQACATGLTALALAVQQVQNGKADIVLAGGSEE-------------------------------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 808 drdgFVMGEGAGVLVMESLEHAMKRGAPIIAEYLGGAVNCD-AYHMTDPRADGLgvSSCIHSALEDAGVSPEEVNYINAH 886
Cdd:cd00327 98 ----FVFGDGAAAAVVESEEHALRRGAHPQAEIVSTAATFDgASMVPAVSGEGL--ARAARKALEGAGLTPSDIDYVEAH 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 887 ATSTIVGDLAELNAIKKVFkNTSEIKINATKSMIGHCLGAAGGLEAIATVKAITTGWLHPTinqfnpepsvefdtvankk 966
Cdd:cd00327 172 GTGTPIGDAVELALGLDPD-GVRSPAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIPPT------------------- 231
|
250 260
....*....|....*....|..
gi 2074720092 967 qQHEVNVAISNSFGFGGHNSVV 988
Cdd:cd00327 232 -PREPRTVLLLGFGLGGTNAAV 252
|
|
| PKS_KS |
smart00825 |
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ... |
734-985 |
4.13e-24 |
|
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: 103.56 E-value: 4.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 734 GLMGPNYSIS--TACATSNYCFYAAANHIRRGEADLMLAGGTEAAIIPIGLGGFVACRALSqrnddPQTASRPWDKDRDG 811
Cdd:smart00825 83 GVSSSDYSVTvdTACSSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLS-----PDGRCKTFDASADG 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 812 FVMGEGAGVLVMESLEHAMKRGAPIIAEYLGGAVNCDAyhmtdpRADGL----GVSSCihsaledagvspeevnyinaha 887
Cdd:smart00825 158 YVRGEGVGVVVLKRLSDALRDGDPILAVIRGSAVNQDG------RSNGItapsGPAQL---------------------- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 888 tstIVGdlaelnaikkvfkntseikinATKSMIGHCLGAAG--GLeaIATVKAITTGWLHPTINQFNPEPSVEFDT---- 961
Cdd:smart00825 210 ---LIG---------------------SVKSNIGHLEAAAGvaGL--IKVVLALKHGVIPPTLHFETPNPHIDLEEsplr 263
|
250 260
....*....|....*....|....*....
gi 2074720092 962 VANKKQQHEVN-----VAIsNSFGFGGHN 985
Cdd:smart00825 264 VPTELTPWPPPgrprrAGV-SSFGFGGTN 291
|
|
| omega_3_PfaA |
TIGR02813 |
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ... |
718-995 |
4.77e-23 |
|
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: 106.63 E-value: 4.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 718 PYAITNMGSALLAIDLGLMGPNYSISTACATSNYCFYAAANHIRRGEADLMLAGGTEAAIIPIGLGGFVACRALSQRNDd 797
Cdd:TIGR02813 178 PGSLGNVISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGGVCTDNSPFMYMSFSKTPAFTTNED- 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 798 pqtaSRPWDKDRDGFVMGEGAGVLVMESLEHAMKRGAPIIAEYLGGAVNCDAYHMT--DPRADGLgvSSCIHSALEDAGV 875
Cdd:TIGR02813 257 ----IQPFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGKFKSiyAPRPEGQ--AKALKRAYDDAGF 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 876 SPEEVNYINAHATSTIVGDLAELNAIKKVFKNTSE----IKINATKSMIGHCLGAAGGLEAIATVKAITTGWLHPTINQF 951
Cdd:TIGR02813 331 APHTCGLIEAHGTGTAAGDVAEFGGLVSVFSQDNDqkqhIALGSVKSQIGHTKSTAGTAGMIKAVLALHHKVLPPTINVD 410
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2074720092 952 NPEPSVEFD-------TVANKKQQHEVNV---AISNSFGFGGHNSVVAFSAFKP 995
Cdd:TIGR02813 411 QPNPKLDIEnspfylnTETRPWMQREDGTprrAGISSFGFGGTNFHMVLEEYSP 464
|
|
| DUF4283 |
pfam14111 |
Domain of unknown function (DUF4283); This domain family is found in plants, and is ... |
32-165 |
1.80e-17 |
|
Domain of unknown function (DUF4283); This domain family is found in plants, and is approximately 100 amino acids in length. Considering the very diverse range of other domains it is associated with it is possible that this domain is a binding/guiding region. There are two highly conserved tryptophan residues.
Pssm-ID: 464086 Cd Length: 145 Bit Score: 80.00 E-value: 1.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 32 VVGRIlSGSRFNFNALKETMLTAFKPRKQIDFEKLDNGRFLLNFESPNDLDKVLEGGPWCYDNDLVILKLLLENDDPLSV 111
Cdd:pfam14111 13 LVGRF-TGKVPSLGAIRRVLARQWGLGGGVKIKELGDGYFLFRFPSEEDLERVLSKGPWLIGNVPMLLQRWSPDFKPTPE 91
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2074720092 112 PLWWVDFYVLAKGLPISKMTKDMASFIGNSLGQFRSVDLARNGVAGGSTLRIRV 165
Cdd:pfam14111 92 ELTTIPIWVQLPGLPLHLWSREVLSKIASAVGKPLETDENTENKTRLSFARVKV 145
|
|
| zf-CCHC_4 |
pfam14392 |
Zinc knuckle; The zinc knuckle is a zinc binding motif composed of the the following ... |
167-212 |
2.74e-09 |
|
Zinc knuckle; The zinc knuckle is a zinc binding motif composed of the the following CX2CX4HX4C where X can be any amino acid. This particular family is found in plant proteins.
Pssm-ID: 433930 Cd Length: 49 Bit Score: 53.49 E-value: 2.74e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2074720092 167 LDVSKPLRRVSFFRAGSN-NFNISYTYERLPNFCYICGIMGHIFQFC 212
Cdd:pfam14392 1 IDITKPLRFFRRIRFPSGeWALIRFKYERLRRFCFICGRLGHSDKFC 47
|
|
| PRK06519 |
PRK06519 |
beta-ketoacyl-ACP synthase; |
585-932 |
2.31e-08 |
|
beta-ketoacyl-ACP synthase;
Pssm-ID: 235819 [Multi-domain] Cd Length: 398 Bit Score: 57.27 E-value: 2.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 585 VVITGMGLVSVFGNDVEAYYEKLLSGesgiAPIDRFDASKF---------PTRFGGQI--RGfksegyidgkNDRRLDDC 653
Cdd:PRK06519 8 VVITGIGLVSSLGEGLDAHWNALSAG----RPQPNVDTETFapypvhplpEIDWSQQIpkRG----------DQRQMETW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 654 LRYCIVAGKKALESADLGG--EKLNTIDKIrggVLVGTGMGGLTVfsDGvQALIEKGHRKITPFFIPYAITNmgsAL--- 728
Cdd:PRK06519 74 QRLGTYAAGLALDDAGIKGneELLSTMDMI---VAAGGGERDIAV--DT-AILNEARKRNDRGVLLNERLMT---ELrpt 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 729 --LAIDLGLMGPNYSISTACATSNYCFYA-----------AANHIRRGEADLMLAGGTEAA-----IIPIGLGGFVA--- 787
Cdd:PRK06519 145 lfLAQLSNLLAGNISIVHKVTGSSRTFMGeesagvsaieiAFARIASGQSDHALVGGAYNAerpdmLLLYELGGLLLkgg 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 788 CRALSQRNDDpqtasrpwdkDRDGFVMGEGAGVLVMESLEHAMKRGAPIIAEyLGGAVNCDAyhmtdPRADGlGVSSCIH 867
Cdd:PRK06519 225 WAPVWSRGGE----------DGGGFILGSGGAFLVLESREHAEARGARPYAR-ISGVESDRA-----RRAPG-DLEASLE 287
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2074720092 868 SALEDAGVSPEEVNYIN----AHATSTivgdlAELNAIKKVFKntseIKINATKSMIGHclgaagGLEA 932
Cdd:PRK06519 288 RLLKPAGGLAAPTAVISgatgAHPATA-----EEKAALEAALA----GPVRGIGTLFGH------TMEA 341
|
|
| PLN02287 |
PLN02287 |
3-ketoacyl-CoA thiolase |
816-928 |
1.65e-04 |
|
3-ketoacyl-CoA thiolase
Pssm-ID: 215161 [Multi-domain] Cd Length: 452 Bit Score: 45.14 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 816 EGAGVLVMESLEHAMKRGAPIIAEYLG-GAVNCdayhmtDPRADGLGVSSCIHSALEDAGVSPEEVnyinahatstivgD 894
Cdd:PLN02287 292 DGAGAVLLMKRSVAMQKGLPILGVFRSfAAVGV------DPAVMGIGPAVAIPAAVKAAGLELDDI-------------D 352
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2074720092 895 LAELN---------AIKKVFKNTSEIKINATKSMIGHCLGAAG 928
Cdd:PLN02287 353 LFEINeafasqfvyCCKKLGLDPEKVNVNGGAIALGHPLGATG 395
|
|
| PaaJ |
COG0183 |
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ... |
738-818 |
2.56e-04 |
|
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 439953 [Multi-domain] Cd Length: 391 Bit Score: 44.67 E-value: 2.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 738 PNYSISTACATSNYCFYAAANHIRRGEADLMLAGGTEAA-IIPIGLGGFVACRALSQRNDDPQTASRPWDkDRDGFVMGE 816
Cdd:COG0183 80 PAVTVNRVCGSGLQAVALAAQAIAAGDADVVIAGGVESMsRAPMLLPKARWGYRMNAKLVDPMINPGLTD-PYTGLSMGE 158
|
..
gi 2074720092 817 GA 818
Cdd:COG0183 159 TA 160
|
|
| PRK06147 |
PRK06147 |
3-oxoacyl-(acyl carrier protein) synthase; Validated |
765-883 |
2.38e-03 |
|
3-oxoacyl-(acyl carrier protein) synthase; Validated
Pssm-ID: 235715 [Multi-domain] Cd Length: 348 Bit Score: 41.16 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 765 ADLMLAGGTEAAIIpIGLGGFVACRALSQRNDDPQ--TASRPwdkdrDGFVMGEGAGVLVMESLEHAMKRGAPIIAeyLG 842
Cdd:PRK06147 144 RRLIAAGGCPRVLV-AGVDSLLTGPTLAHYEARDRllTSQNS-----NGFIPGEAAAAVLLGRPAGGEAPGLPLLG--LG 215
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2074720092 843 GAVNCDAYHMTDP---RADGLgvSSCIHSALEDAGVSPEEVNYI 883
Cdd:PRK06147 216 LGREPAPVGESEDlplRGDGL--TQAIRAALAEAGCGLEDMDYR 257
|
|
| PRK06064 |
PRK06064 |
thiolase domain-containing protein; |
660-774 |
9.03e-03 |
|
thiolase domain-containing protein;
Pssm-ID: 235688 [Multi-domain] Cd Length: 389 Bit Score: 39.49 E-value: 9.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074720092 660 AGKKALESADLGGEKlntIDkirgGVLVGTGMGGLtvFSDgvQALIekghrkitpffipyaitnmgSALLAIDLGLMG-P 738
Cdd:PRK06064 29 AGLEALEDAGIDGKD---ID----AMYVGNMSAGL--FVS--QEHI--------------------AALIADYAGLAPiP 77
|
90 100 110
....*....|....*....|....*....|....*.
gi 2074720092 739 NYSISTACATSNYCFYAAANHIRRGEADLMLAGGTE 774
Cdd:PRK06064 78 ATRVEAACASGGAALRQAYLAVASGEADVVLAAGVE 113
|
|
| |
