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Conserved domains on  [gi|29653839|ref|NP_819531|]
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3-oxoacyl-[acyl-carrier-protein] synthase [Coxiella burnetii RSA 493]

Protein Classification

beta-ketoacyl-[acyl-carrier-protein] synthase II( domain architecture ID 11496422)

beta-ketoacyl-[acyl-carrier-protein] synthase II catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP, part of the dissociated (or type II) fatty acid biosynthesis system

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
fabF TIGR03150
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 ...
4-409 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: 762.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839     4 RRVVITGLGVVSPLGNKVSDMWQALLAGKSGVKPITRFDASSFPTQIAAEVRDFDPALVLDLKSIRKTDVFVQFAMESAR 83
Cdd:TIGR03150   1 RRVVVTGLGAVTPLGNGVEEFWENLLAGKSGIGPITRFDASDLPVKIAGEVKDFDPEDYIDKKEARRMDRFIQYALAAAK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839    84 QAWEDSGLEINETNAPRVGVAIGSGIGGMPWIEKNYDALLTSGPRKISPFFIPGAIINMASGMVSIKYDLKGPNISIVTA 163
Cdd:TIGR03150  81 EAVEDSGLDIEEEDAERVGVIIGSGIGGLETIEEQHIVLLEKGPRRVSPFFIPMSIINMAAGQISIRYGAKGPNHAVVTA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839   164 CTTGLHNIGHAARMIAHNDADAMIAGGTEMASTPLGIGGFAAVRALSTRNDEPEKASRPWDKGRDGFVLGEGAACVVVEE 243
Cdd:TIGR03150 161 CATGTHAIGDAFRLIQRGDADVMIAGGAEAAITPLGIAGFAAMKALSTRNDDPEKASRPFDKDRDGFVMGEGAGVLVLEE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839   244 LEHAKKRNATIYAEIIGFGMSGDAYHMTRPDPEAEGFTTCMKNSLRDAGIAPERVDYINAHGTSTPAADPLEARAIKKTF 323
Cdd:TIGR03150 241 LEHAKARGAKIYAEIVGYGMSGDAYHITAPAPEGEGAARAMRAALKDAGINPEDVDYINAHGTSTPLGDKAETKAIKKVF 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839   324 GDHAYKLAVSSTKSMTGHMLGAAGALETVISVLAIRDNTAPPTINLENPDEGCDLDFVPNEAREMKIDTVMSNSFGFGGT 403
Cdd:TIGR03150 321 GDHAYKLAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVPPTINLDNPDPECDLDYVPNEAREAKIDYALSNSFGFGGT 400

                  ....*.
gi 29653839   404 NGTLVL 409
Cdd:TIGR03150 401 NASLVF 406
 
Name Accession Description Interval E-value
fabF TIGR03150
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 ...
4-409 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: 762.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839     4 RRVVITGLGVVSPLGNKVSDMWQALLAGKSGVKPITRFDASSFPTQIAAEVRDFDPALVLDLKSIRKTDVFVQFAMESAR 83
Cdd:TIGR03150   1 RRVVVTGLGAVTPLGNGVEEFWENLLAGKSGIGPITRFDASDLPVKIAGEVKDFDPEDYIDKKEARRMDRFIQYALAAAK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839    84 QAWEDSGLEINETNAPRVGVAIGSGIGGMPWIEKNYDALLTSGPRKISPFFIPGAIINMASGMVSIKYDLKGPNISIVTA 163
Cdd:TIGR03150  81 EAVEDSGLDIEEEDAERVGVIIGSGIGGLETIEEQHIVLLEKGPRRVSPFFIPMSIINMAAGQISIRYGAKGPNHAVVTA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839   164 CTTGLHNIGHAARMIAHNDADAMIAGGTEMASTPLGIGGFAAVRALSTRNDEPEKASRPWDKGRDGFVLGEGAACVVVEE 243
Cdd:TIGR03150 161 CATGTHAIGDAFRLIQRGDADVMIAGGAEAAITPLGIAGFAAMKALSTRNDDPEKASRPFDKDRDGFVMGEGAGVLVLEE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839   244 LEHAKKRNATIYAEIIGFGMSGDAYHMTRPDPEAEGFTTCMKNSLRDAGIAPERVDYINAHGTSTPAADPLEARAIKKTF 323
Cdd:TIGR03150 241 LEHAKARGAKIYAEIVGYGMSGDAYHITAPAPEGEGAARAMRAALKDAGINPEDVDYINAHGTSTPLGDKAETKAIKKVF 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839   324 GDHAYKLAVSSTKSMTGHMLGAAGALETVISVLAIRDNTAPPTINLENPDEGCDLDFVPNEAREMKIDTVMSNSFGFGGT 403
Cdd:TIGR03150 321 GDHAYKLAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVPPTINLDNPDPECDLDYVPNEAREAKIDYALSNSFGFGGT 400

                  ....*.
gi 29653839   404 NGTLVL 409
Cdd:TIGR03150 401 NASLVF 406
PRK07314 PRK07314
beta-ketoacyl-ACP synthase II;
3-412 0e+00

beta-ketoacyl-ACP synthase II;


Pssm-ID: 235987 [Multi-domain]  Cd Length: 411  Bit Score: 739.29  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839    3 KRRVVITGLGVVSPLGNKVSDMWQALLAGKSGVKPITRFDASSFPTQIAAEVRDFDPALVLDLKSIRKTDVFVQFAMESA 82
Cdd:PRK07314   1 KRRVVVTGLGAVSPLGNDVESTWKNLLAGKSGIGPITHFDTSDLAVKIAGEVKDFNPDDYMSRKEARRMDRFIQYGIAAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839   83 RQAWEDSGLEINETNAPRVGVAIGSGIGGMPWIEKNYDALLTSGPRKISPFFIPGAIINMASGMVSIKYDLKGPNISIVT 162
Cdd:PRK07314  81 KQAVEDAGLEITEENADRIGVIIGSGIGGLETIEEQHITLLEKGPRRVSPFFVPMAIINMAAGHVSIRYGAKGPNHSIVT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839  163 ACTTGLHNIGHAARMIAHNDADAMIAGGTEMASTPLGIGGFAAVRALSTRNDEPEKASRPWDKGRDGFVLGEGAACVVVE 242
Cdd:PRK07314 161 ACATGAHAIGDAARLIAYGDADVMVAGGAEAAITPLGIAGFAAARALSTRNDDPERASRPFDKDRDGFVMGEGAGILVLE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839  243 ELEHAKKRNATIYAEIIGFGMSGDAYHMTRPDPEAEGFTTCMKNSLRDAGIAPERVDYINAHGTSTPAADPLEARAIKKT 322
Cdd:PRK07314 241 ELEHAKARGAKIYAEVVGYGMTGDAYHMTAPAPDGEGAARAMKLALKDAGINPEDIDYINAHGTSTPAGDKAETQAIKRV 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839  323 FGDHAYKLAVSSTKSMTGHMLGAAGALETVISVLAIRDNTAPPTINLENPDEGCDLDFVPNEAREMKIDTVMSNSFGFGG 402
Cdd:PRK07314 321 FGEHAYKVAVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPTINLDNPDEECDLDYVPNEARERKIDYALSNSFGFGG 400
                        410
                 ....*....|
gi 29653839  403 TNGTLVLSRV 412
Cdd:PRK07314 401 TNASLVFKRY 410
FabB COG0304
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...
4-412 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: 713.79  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839   4 RRVVITGLGVVSPLGNKVSDMWQALLAGKSGVKPITRFDASSFPTQIAAEVRDFDPALVLDLKSIRKTDVFVQFAMESAR 83
Cdd:COG0304   1 RRVVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITRFDASGLPVRIAGEVKDFDPEEYLDRKELRRMDRFTQYALAAAR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839  84 QAWEDSGLEINETNAPRVGVAIGSGIGGMPWIEKNYDALLTSGPRKISPFFIPGAIINMASGMVSIKYDLKGPNISIVTA 163
Cdd:COG0304  81 EALADAGLDLDEVDPDRTGVIIGSGIGGLDTLEEAYRALLEKGPRRVSPFFVPMMMPNMAAGHVSIRFGLKGPNYTVSTA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839 164 CTTGLHNIGHAARMIAHNDADAMIAGGTEMASTPLGIGGFAAVRALSTRNDEPEKASRPWDKGRDGFVLGEGAACVVVEE 243
Cdd:COG0304 161 CASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLAGFDALGALSTRNDDPEKASRPFDKDRDGFVLGEGAGVLVLEE 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839 244 LEHAKKRNATIYAEIIGFGMSGDAYHMTRPDPEAEGFTTCMKNSLRDAGIAPERVDYINAHGTSTPAADPLEARAIKKTF 323
Cdd:COG0304 241 LEHAKARGAKIYAEVVGYGASSDAYHITAPAPDGEGAARAMRAALKDAGLSPEDIDYINAHGTSTPLGDAAETKAIKRVF 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839 324 GDHAYKLAVSSTKSMTGHMLGAAGALETVISVLAIRDNTAPPTINLENPDEGCDLDFVPNEAREMKIDTVMSNSFGFGGT 403
Cdd:COG0304 321 GDHAYKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPECDLDYVPNEAREAKIDYALSNSFGFGGH 400

                ....*....
gi 29653839 404 NGTLVLSRV 412
Cdd:COG0304 401 NASLVFKRY 409
KAS_I_II cd00834
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...
4-409 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: 659.23  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839   4 RRVVITGLGVVSPLGNKVSDMWQALLAGKSGVKPITRFDASSFPTQIAAEVRDFDPALVLDLKSIRKTDVFVQFAMESAR 83
Cdd:cd00834   1 RRVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRFDASGFPSRIAGEVPDFDPEDYLDRKELRRMDRFAQFALAAAE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839  84 QAWEDSGLEINETNAPRVGVAIGSGIGGMPWIEKNYDALLTSGPRKISPFFIPGAIINMASGMVSIKYDLKGPNISIVTA 163
Cdd:cd00834  81 EALADAGLDPEELDPERIGVVIGSGIGGLATIEEAYRALLEKGPRRVSPFFVPMALPNMAAGQVAIRLGLRGPNYTVSTA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839 164 CTTGLHNIGHAARMIAHNDADAMIAGGTEMASTPLGIGGFAAVRALSTRNDEPEKASRPWDKGRDGFVLGEGAACVVVEE 243
Cdd:cd00834 161 CASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALRALSTRNDDPEKASRPFDKDRDGFVLGEGAGVLVLES 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839 244 LEHAKKRNATIYAEIIGFGMSGDAYHMTRPDPEAEGFTTCMKNSLRDAGIAPERVDYINAHGTSTPAADPLEARAIKKTF 323
Cdd:cd00834 241 LEHAKARGAKIYAEILGYGASSDAYHITAPDPDGEGAARAMRAALADAGLSPEDIDYINAHGTSTPLNDAAESKAIKRVF 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839 324 GDHAYKLAVSSTKSMTGHMLGAAGALETVISVLAIRDNTAPPTINLENPDEGCDLDFVPNEAREMKIDTVMSNSFGFGGT 403
Cdd:cd00834 321 GEHAKKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPECDLDYVPNEAREAPIRYALSNSFGFGGH 400

                ....*.
gi 29653839 404 NGTLVL 409
Cdd:cd00834 401 NASLVF 406
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
4-247 1.20e-68

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: 217.50  E-value: 1.20e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839     4 RRVVITGLGVVSPLGNKVSDMWQALLAGKSGVKPI--TRFDASSF---PTQIAAEVR----------DFDPALV-LDLKS 67
Cdd:pfam00109   1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIpaDRWDPDKLydpPSRIAGKIYtkwgglddifDFDPLFFgISPRE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839    68 IRKTDVFVQFAMESARQAWEDSGLEINETNAPRVGVAIGSGIGGmpwiEKNYDAL-LTSGPRKISPFFIpGAIINMASGM 146
Cdd:pfam00109  81 AERMDPQQRLLLEAAWEALEDAGITPDSLDGSRTGVFIGSGIGD----YAALLLLdEDGGPRRGSPFAV-GTMPSVIAGR 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839   147 VSIKYDLKGPNISIVTACTTGLHNIGHAARMIAHNDADAMIAGGTEMASTPLGIGGFAAVRALSTrnDEPEKASRPWDkg 226
Cdd:pfam00109 156 ISYFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSP--DGPCKAFDPFA-- 231
                         250       260
                  ....*....|....*....|.
gi 29653839   227 rDGFVLGEGAACVVVEELEHA 247
Cdd:pfam00109 232 -DGFVRGEGVGAVVLKRLSDA 251
PKS_KS smart00825
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ...
6-409 2.13e-23

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: 99.33  E-value: 2.13e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839      6 VVITGLGVVSPLGNKVSDMWQALLAGKSGVKpitRFDASSFptQI-AAEVRDFDPALVLdlksirktdvfvqfAMESARQ 84
Cdd:smart00825   1 IAIVGMSCRFPGADDPEEFWDLLLAGLDDVD---LFDAAFF--GIsPREAEAMDPQQRL--------------LLEVAWE 61
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839     85 AWEDSGLEINETNAPRVGVAIGSGIGGmpwieknydalltsgprkispffipgaiinmasgmvsikYdlkgpNISIVTAC 164
Cdd:smart00825  62 ALEDAGIDPESLRGSRTGVFVGVSSSD---------------------------------------Y-----SVTVDTAC 97
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839    165 TTGLHNIGHAARMIAHNDADAMIAGGTEMASTPLGIGGFAAVRALStrndePEKASRPWDKGRDGFVLGEGAACVVVEEL 244
Cdd:smart00825  98 SSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLS-----PDGRCKTFDASADGYVRGEGVGVVVLKRL 172
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839    245 EHAKKRNATIYAEIIGFGM--SGDAYHMTRPDPEAEgfttcmknslrdagiapervdyinahgtstpaadplearaikkt 322
Cdd:smart00825 173 SDALRDGDPILAVIRGSAVnqDGRSNGITAPSGPAQ-------------------------------------------- 208
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839    323 fgdhaykLAVSSTKSMTGHMLGAAGaLETVI-SVLAIRDNTAPPTINLENPDEGCDLD----FVPNEAREMKIDT----V 393
Cdd:smart00825 209 -------LLIGSVKSNIGHLEAAAG-VAGLIkVVLALKHGVIPPTLHFETPNPHIDLEesplRVPTELTPWPPPGrprrA 280
                          410
                   ....*....|....*.
gi 29653839    394 MSNSFGFGGTNGTLVL 409
Cdd:smart00825 281 GVSSFGFGGTNAHVIL 296
 
Name Accession Description Interval E-value
fabF TIGR03150
beta-ketoacyl-acyl-carrier-protein synthase II; 3-oxoacyl-[acyl-carrier-protein] synthase 2 ...
4-409 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: 762.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839     4 RRVVITGLGVVSPLGNKVSDMWQALLAGKSGVKPITRFDASSFPTQIAAEVRDFDPALVLDLKSIRKTDVFVQFAMESAR 83
Cdd:TIGR03150   1 RRVVVTGLGAVTPLGNGVEEFWENLLAGKSGIGPITRFDASDLPVKIAGEVKDFDPEDYIDKKEARRMDRFIQYALAAAK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839    84 QAWEDSGLEINETNAPRVGVAIGSGIGGMPWIEKNYDALLTSGPRKISPFFIPGAIINMASGMVSIKYDLKGPNISIVTA 163
Cdd:TIGR03150  81 EAVEDSGLDIEEEDAERVGVIIGSGIGGLETIEEQHIVLLEKGPRRVSPFFIPMSIINMAAGQISIRYGAKGPNHAVVTA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839   164 CTTGLHNIGHAARMIAHNDADAMIAGGTEMASTPLGIGGFAAVRALSTRNDEPEKASRPWDKGRDGFVLGEGAACVVVEE 243
Cdd:TIGR03150 161 CATGTHAIGDAFRLIQRGDADVMIAGGAEAAITPLGIAGFAAMKALSTRNDDPEKASRPFDKDRDGFVMGEGAGVLVLEE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839   244 LEHAKKRNATIYAEIIGFGMSGDAYHMTRPDPEAEGFTTCMKNSLRDAGIAPERVDYINAHGTSTPAADPLEARAIKKTF 323
Cdd:TIGR03150 241 LEHAKARGAKIYAEIVGYGMSGDAYHITAPAPEGEGAARAMRAALKDAGINPEDVDYINAHGTSTPLGDKAETKAIKKVF 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839   324 GDHAYKLAVSSTKSMTGHMLGAAGALETVISVLAIRDNTAPPTINLENPDEGCDLDFVPNEAREMKIDTVMSNSFGFGGT 403
Cdd:TIGR03150 321 GDHAYKLAVSSTKSMTGHLLGAAGAIEAIFTVLAIRDGIVPPTINLDNPDPECDLDYVPNEAREAKIDYALSNSFGFGGT 400

                  ....*.
gi 29653839   404 NGTLVL 409
Cdd:TIGR03150 401 NASLVF 406
PRK07314 PRK07314
beta-ketoacyl-ACP synthase II;
3-412 0e+00

beta-ketoacyl-ACP synthase II;


Pssm-ID: 235987 [Multi-domain]  Cd Length: 411  Bit Score: 739.29  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839    3 KRRVVITGLGVVSPLGNKVSDMWQALLAGKSGVKPITRFDASSFPTQIAAEVRDFDPALVLDLKSIRKTDVFVQFAMESA 82
Cdd:PRK07314   1 KRRVVVTGLGAVSPLGNDVESTWKNLLAGKSGIGPITHFDTSDLAVKIAGEVKDFNPDDYMSRKEARRMDRFIQYGIAAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839   83 RQAWEDSGLEINETNAPRVGVAIGSGIGGMPWIEKNYDALLTSGPRKISPFFIPGAIINMASGMVSIKYDLKGPNISIVT 162
Cdd:PRK07314  81 KQAVEDAGLEITEENADRIGVIIGSGIGGLETIEEQHITLLEKGPRRVSPFFVPMAIINMAAGHVSIRYGAKGPNHSIVT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839  163 ACTTGLHNIGHAARMIAHNDADAMIAGGTEMASTPLGIGGFAAVRALSTRNDEPEKASRPWDKGRDGFVLGEGAACVVVE 242
Cdd:PRK07314 161 ACATGAHAIGDAARLIAYGDADVMVAGGAEAAITPLGIAGFAAARALSTRNDDPERASRPFDKDRDGFVMGEGAGILVLE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839  243 ELEHAKKRNATIYAEIIGFGMSGDAYHMTRPDPEAEGFTTCMKNSLRDAGIAPERVDYINAHGTSTPAADPLEARAIKKT 322
Cdd:PRK07314 241 ELEHAKARGAKIYAEVVGYGMTGDAYHMTAPAPDGEGAARAMKLALKDAGINPEDIDYINAHGTSTPAGDKAETQAIKRV 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839  323 FGDHAYKLAVSSTKSMTGHMLGAAGALETVISVLAIRDNTAPPTINLENPDEGCDLDFVPNEAREMKIDTVMSNSFGFGG 402
Cdd:PRK07314 321 FGEHAYKVAVSSTKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPTINLDNPDEECDLDYVPNEARERKIDYALSNSFGFGG 400
                        410
                 ....*....|
gi 29653839  403 TNGTLVLSRV 412
Cdd:PRK07314 401 TNASLVFKRY 410
FabB COG0304
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...
4-412 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: 713.79  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839   4 RRVVITGLGVVSPLGNKVSDMWQALLAGKSGVKPITRFDASSFPTQIAAEVRDFDPALVLDLKSIRKTDVFVQFAMESAR 83
Cdd:COG0304   1 RRVVITGLGAVSPLGNGVEEFWEALLAGRSGIRPITRFDASGLPVRIAGEVKDFDPEEYLDRKELRRMDRFTQYALAAAR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839  84 QAWEDSGLEINETNAPRVGVAIGSGIGGMPWIEKNYDALLTSGPRKISPFFIPGAIINMASGMVSIKYDLKGPNISIVTA 163
Cdd:COG0304  81 EALADAGLDLDEVDPDRTGVIIGSGIGGLDTLEEAYRALLEKGPRRVSPFFVPMMMPNMAAGHVSIRFGLKGPNYTVSTA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839 164 CTTGLHNIGHAARMIAHNDADAMIAGGTEMASTPLGIGGFAAVRALSTRNDEPEKASRPWDKGRDGFVLGEGAACVVVEE 243
Cdd:COG0304 161 CASGAHAIGEAYRLIRRGRADVMIAGGAEAAITPLGLAGFDALGALSTRNDDPEKASRPFDKDRDGFVLGEGAGVLVLEE 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839 244 LEHAKKRNATIYAEIIGFGMSGDAYHMTRPDPEAEGFTTCMKNSLRDAGIAPERVDYINAHGTSTPAADPLEARAIKKTF 323
Cdd:COG0304 241 LEHAKARGAKIYAEVVGYGASSDAYHITAPAPDGEGAARAMRAALKDAGLSPEDIDYINAHGTSTPLGDAAETKAIKRVF 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839 324 GDHAYKLAVSSTKSMTGHMLGAAGALETVISVLAIRDNTAPPTINLENPDEGCDLDFVPNEAREMKIDTVMSNSFGFGGT 403
Cdd:COG0304 321 GDHAYKVPVSSTKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPECDLDYVPNEAREAKIDYALSNSFGFGGH 400

                ....*....
gi 29653839 404 NGTLVLSRV 412
Cdd:COG0304 401 NASLVFKRY 409
KAS_I_II cd00834
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...
4-409 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: 659.23  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839   4 RRVVITGLGVVSPLGNKVSDMWQALLAGKSGVKPITRFDASSFPTQIAAEVRDFDPALVLDLKSIRKTDVFVQFAMESAR 83
Cdd:cd00834   1 RRVVITGLGAVTPLGNGVEEFWEALLAGRSGIRPITRFDASGFPSRIAGEVPDFDPEDYLDRKELRRMDRFAQFALAAAE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839  84 QAWEDSGLEINETNAPRVGVAIGSGIGGMPWIEKNYDALLTSGPRKISPFFIPGAIINMASGMVSIKYDLKGPNISIVTA 163
Cdd:cd00834  81 EALADAGLDPEELDPERIGVVIGSGIGGLATIEEAYRALLEKGPRRVSPFFVPMALPNMAAGQVAIRLGLRGPNYTVSTA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839 164 CTTGLHNIGHAARMIAHNDADAMIAGGTEMASTPLGIGGFAAVRALSTRNDEPEKASRPWDKGRDGFVLGEGAACVVVEE 243
Cdd:cd00834 161 CASGAHAIGDAARLIRLGRADVVIAGGAEALITPLTLAGFAALRALSTRNDDPEKASRPFDKDRDGFVLGEGAGVLVLES 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839 244 LEHAKKRNATIYAEIIGFGMSGDAYHMTRPDPEAEGFTTCMKNSLRDAGIAPERVDYINAHGTSTPAADPLEARAIKKTF 323
Cdd:cd00834 241 LEHAKARGAKIYAEILGYGASSDAYHITAPDPDGEGAARAMRAALADAGLSPEDIDYINAHGTSTPLNDAAESKAIKRVF 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839 324 GDHAYKLAVSSTKSMTGHMLGAAGALETVISVLAIRDNTAPPTINLENPDEGCDLDFVPNEAREMKIDTVMSNSFGFGGT 403
Cdd:cd00834 321 GEHAKKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPECDLDYVPNEAREAPIRYALSNSFGFGGH 400

                ....*.
gi 29653839 404 NGTLVL 409
Cdd:cd00834 401 NASLVF 406
PRK08722 PRK08722
beta-ketoacyl-ACP synthase II;
1-412 0e+00

beta-ketoacyl-ACP synthase II;


Pssm-ID: 181539 [Multi-domain]  Cd Length: 414  Bit Score: 548.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839    1 MEKRRVVITGLGVVSPLGNKVSDMWQALLAGKSGVKPITRFDASSFPTQIAAEVRDFDPALVLDLKSIRKTDVFVQFAME 80
Cdd:PRK08722   1 MSKRRVVVTGMGMLSPVGNTVESSWKALLAGQSGIVNIEHFDTTNFSTRFAGLVKDFNCEEYMSKKDARKMDLFIQYGIA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839   81 SARQAWEDSGLEINETNAPRVGVAIGSGIGGMPWIEKNYDALLTSGPRKISPFFIPGAIINMASGMVSIKYDLKGPNISI 160
Cdd:PRK08722  81 AGIQALDDSGLEVTEENAHRIGVAIGSGIGGLGLIEAGHQALVEKGPRKVSPFFVPSTIVNMIAGNLSIMRGLRGPNIAI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839  161 VTACTTGLHNIGHAARMIAHNDADAMIAGGTEMASTPLGIGGFAAVRALSTRNDEPEKASRPWDKGRDGFVLGEGAACVV 240
Cdd:PRK08722 161 STACTTGLHNIGHAARMIAYGDADAMVAGGAEKASTPLGMAGFGAAKALSTRNDEPQKASRPWDKDRDGFVLGDGAGMMV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839  241 VEELEHAKKRNATIYAEIIGFGMSGDAYHMTRPDPEAEGFTTCMKNSLRDAGIAPERVDYINAHGTSTPAADPLEARAIK 320
Cdd:PRK08722 241 LEEYEHAKARGAKIYAELVGFGMSGDAYHMTSPSEDGSGGALAMEAAMRDAGVTGEQIGYVNAHGTSTPAGDVAEIKGIK 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839  321 KTFGDH-AYKLAVSSTKSMTGHMLGAAGALETVISVLAIRDNTAPPTINLENPDEGCDLDFVPNEAREMK-IDTVMSNSF 398
Cdd:PRK08722 321 RALGEAgSKQVLVSSTKSMTGHLLGAAGSVEAIITVMSLVDQIVPPTINLDDPEEGLDIDLVPHTARKVEsMEYAICNSF 400
                        410
                 ....*....|....
gi 29653839  399 GFGGTNGTLVLSRV 412
Cdd:PRK08722 401 GFGGTNGSLIFKKM 414
PRK06333 PRK06333
beta-ketoacyl-ACP synthase;
1-411 0e+00

beta-ketoacyl-ACP synthase;


Pssm-ID: 235781 [Multi-domain]  Cd Length: 424  Bit Score: 542.28  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839    1 MEKRRVVITGLGVVSPLGNKVSDMWQALLAGKSGVKPITRFDASSFPTQIAAEVRD--------FDPALVLDLKSIRKTD 72
Cdd:PRK06333   1 MNKKRIVVTGMGAVSPLGCGVETFWQRLLAGQSGIRTLTDFPVGDLATKIGGQVPDlaedaeagFDPDRYLDPKDQRKMD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839   73 VFVQFAMESARQAWEDSGLEINETNAP-RVGVAIGSGIGGMPWIEKNYDALLTSGPRKISPFFIPGAIINMASGMVSIKY 151
Cdd:PRK06333  81 RFILFAMAAAKEALAQAGWDPDTLEDReRTATIIGSGVGGFPAIAEAVRTLDSRGPRRLSPFTIPSFLTNMAAGHVSIRY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839  152 DLKGPNISIVTACTTGLHNIGHAARMIAHNDADAMIAGGTEMASTPLGIGGFAAVRALSTR-NDEPEKASRPWDKGRDGF 230
Cdd:PRK06333 161 GFKGPLGAPVTACAAGVQAIGDAARLIRSGEADVAVCGGTEAAIDRVSLAGFAAARALSTRfNDAPEQASRPFDRDRDGF 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839  231 VLGEGAACVVVEELEHAKKRNATIYAEIIGFGMSGDAYHMTRPDPEAEGFTTCMKNSLRDAGIAPERVDYINAHGTSTPA 310
Cdd:PRK06333 241 VMGEGAGILVIETLEHALARGAPPLAELVGYGTSADAYHMTAGPEDGEGARRAMLIALRQAGIPPEEVQHLNAHATSTPV 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839  311 ADPLEARAIKKTFGdHAYKLAVSSTKSMTGHMLGAAGALETVISVLAIRDNTAPPTINLENPDEGCD-LDFVPNEAREMK 389
Cdd:PRK06333 321 GDLGEVAAIKKVFG-HVSGLAVSSTKSATGHLLGAAGGVEAIFTILALRDQIAPPTLNLENPDPAAEgLDVVANKARPMD 399
                        410       420
                 ....*....|....*....|..
gi 29653839  390 IDTVMSNSFGFGGTNGTLVLSR 411
Cdd:PRK06333 400 MDYALSNGFGFGGVNASILFRR 421
PRK08439 PRK08439
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
4-412 0e+00

3-oxoacyl-(acyl carrier protein) synthase II; Reviewed


Pssm-ID: 236265 [Multi-domain]  Cd Length: 406  Bit Score: 542.02  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839    4 RRVVITGLGVVSPLGNKVSDMWQALLAGKSGVKPITRFDASSFPTQIAAEVRDFDPALVLDLKSIRKTDVFVQFAMESAR 83
Cdd:PRK08439   2 KRVVVTGIGMINSLGLNKESSFKAICNGECGIKKITLFDASDFPVQIAGEITDFDPTEVMDPKEVKKADRFIQLGLKAAR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839   84 QAWEDSGLEINETNAPRVGVAIGSGIGGMPWIEKNYDALLTSGPRKISPFFIPGAIINMASGMVSIKYDLKGPNISIVTA 163
Cdd:PRK08439  82 EAMKDAGFLPEELDAERFGVSSASGIGGLPNIEKNSIICFEKGPRKISPFFIPSALVNMLGGFISIEHGLKGPNLSSVTA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839  164 CTTGLHNIGHAARMIAHNDADAMIAGGTEMASTPLGIGGFAAVRALSTRNDEPEKASRPWDKGRDGFVLGEGAACVVVEE 243
Cdd:PRK08439 162 CAAGTHAIIEAVKTIMLGGADKMLVVGAESAICPVGIGGFAAMKALSTRNDDPKKASRPFDKDRDGFVMGEGAGALVLEE 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839  244 LEHAKKRNATIYAEIIGFGMSGDAYHMTRPDPeaEGFTTCMKNSLRDAGiaPERVDYINAHGTSTPAADPLEARAIKKTF 323
Cdd:PRK08439 242 YESAKKRGAKIYAEIIGFGESGDANHITSPAP--EGPLRAMKAALEMAG--NPKIDYINAHGTSTPYNDKNETAALKELF 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839  324 GDHAYKLAVSSTKSMTGHMLGAAGALETVISVLAIRDNTAPPTINLENPDEGCDLDFVPNEAREMKIDTVMSNSFGFGGT 403
Cdd:PRK08439 318 GSKEKVPPVSSTKGQIGHCLGAAGAIEAVISIMAMRDGILPPTINQETPDPECDLDYIPNVARKAELNVVMSNSFGFGGT 397

                 ....*....
gi 29653839  404 NGTLVLSRV 412
Cdd:PRK08439 398 NGVVIFKKV 406
PTZ00050 PTZ00050
3-oxoacyl-acyl carrier protein synthase; Provisional
13-412 1.54e-169

3-oxoacyl-acyl carrier protein synthase; Provisional


Pssm-ID: 240245 [Multi-domain]  Cd Length: 421  Bit Score: 481.11  E-value: 1.54e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839   13 VVSPLGNKVSDMWQALLAGKSGVKPITRFDA----------------SSFPTQIAAEVR--DFDPalvLDLKSIRKTDVF 74
Cdd:PTZ00050   1 VVTPLGVGAESTWEALIAGKSGIRKLTEFPKflpdcipeqkalenlvAAMPCQIAAEVDqsEFDP---SDFAPTKRESRA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839   75 VQFAMESARQAWEDSGLEI-NETNAPRVGVAIGSGIGGMPWIEKNYDALLTSGPRKISPFFIPGAIINMASGMVSIKYDL 153
Cdd:PTZ00050  78 THFAMAAAREALADAKLDIlSEKDQERIGVNIGSGIGSLADLTDEMKTLYEKGHSRVSPYFIPKILGNMAAGLVAIKHKL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839  154 KGPNISIVTACTTGLHNIGHAARMIAHNDADAMIAGGTEMASTPLGIGGFAAVRALSTR-NDEPEKASRPWDKGRDGFVL 232
Cdd:PTZ00050 158 KGPSGSAVTACATGAHCIGEAFRWIKYGEADIMICGGTEASITPVSFAGFSRMRALCTKyNDDPQRASRPFDKDRAGFVM 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839  233 GEGAACVVVEELEHAKKRNATIYAEIIGFGMSGDAYHMTRPDPEAEGFTTCMKNSLRDAGIAPER-VDYINAHGTSTPAA 311
Cdd:PTZ00050 238 GEGAGILVLEELEHALRRGAKIYAEIRGYGSSSDAHHITAPHPDGRGARRCMENALKDGANININdVDYVNAHATSTPIG 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839  312 DPLEARAIKKTFGDH-AYKLAVSSTKSMTGHMLGAAGALETVISVLAIRDNTAPPTINLENPDEGCDLDFVPNEAR--EM 388
Cdd:PTZ00050 318 DKIELKAIKKVFGDSgAPKLYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINLENPDAECDLNLVQGKTAhpLQ 397
                        410       420
                 ....*....|....*....|....
gi 29653839  389 KIDTVMSNSFGFGGTNGTLVLSRV 412
Cdd:PTZ00050 398 SIDAVLSTSFGFGGVNTALLFTKY 421
PLN02836 PLN02836
3-oxoacyl-[acyl-carrier-protein] synthase
4-412 3.18e-153

3-oxoacyl-[acyl-carrier-protein] synthase


Pssm-ID: 215449 [Multi-domain]  Cd Length: 437  Bit Score: 440.38  E-value: 3.18e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839    4 RRVVITGLGVVSPLGNKVSDMWQALLAGKSGVKPITRFDA--------------SSFPTQIAAEV------RDFDPALVL 63
Cdd:PLN02836   6 RRVVVTGLGLVTPLGCGVETTWRRLIAGECGVRALTQDDLkmksedeetqlytlDQLPSRVAALVprgtgpGDFDEELWL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839   64 DLKSIRKtdvFVQFAMESARQAWEDSG-LEINETNAPRVGVAIGSGIGGMPWIEKNYDALLTSGPRKISPFFIPGAIINM 142
Cdd:PLN02836  86 NSRSSSR---FIGYALCAADEALSDARwLPSEDEAKERTGVSIGGGIGSITDILEAAQLICEKRLRRLSPFFVPRILINM 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839  143 ASGMVSIKYDLKGPNISIVTACTTGLHNIGHAARMIAHNDADAMIAGGTEMASTPLGIGGFAAVRALSTR-NDEPEKASR 221
Cdd:PLN02836 163 AAGHVSIRYGFQGPNHAAVTACATGAHSIGDAFRMIQFGDADVMVAGGTESSIDALSIAGFSRSRALSTKfNSCPTEASR 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839  222 PWDKGRDGFVLGEGAACVVVEELEHAKKRNATIYAEIIGFGMSGDAYHMTRPDPEAEGFTTCMKNSLRDAGIAPERVDYI 301
Cdd:PLN02836 243 PFDCDRDGFVIGEGAGVLVLEELEHAKRRGAKIYAEVRGYGMSGDAHHITQPHEDGRGAVLAMTRALQQSGLHPNQVDYV 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839  302 NAHGTSTPAADPLEARAIKKTFGDHAY--KLAVSSTKSMTGHMLGAAGALETVISVLAIRDNTAPPTINLENPDEGCDLD 379
Cdd:PLN02836 323 NAHATSTPLGDAVEARAIKTVFSEHATsgGLAFSSTKGATGHLLGAAGAVEAIFSVLAIHHGIAPPTLNLERPDPIFDDG 402
                        410       420       430
                 ....*....|....*....|....*....|....
gi 29653839  380 FVP-NEAREMKIDTVMSNSFGFGGTNGTLVLSRV 412
Cdd:PLN02836 403 FVPlTASKAMLIRAALSNSFGFGGTNASLLFTSP 436
PLN02787 PLN02787
3-oxoacyl-[acyl-carrier-protein] synthase II
1-410 6.70e-137

3-oxoacyl-[acyl-carrier-protein] synthase II


Pssm-ID: 215421 [Multi-domain]  Cd Length: 540  Bit Score: 402.43  E-value: 6.70e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839    1 MEKRRVVITGLGVVSPLGNKVSDMWQALLAGKSGVKPITRFDASSFPTQIAAEVRDFDPALVLDLKSIRKTDVFVQFAME 80
Cdd:PLN02787 126 TKQRRVVVTGMGVVSPLGHDPDVFYNNLLEGVSGISEIERFDCSQFPTRIAGEIKSFSTDGWVAPKLSKRMDKFMLYLLT 205
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839   81 SARQAWEDSGLE---INETNAPRVGVAIGSGIGGMPWIEKNYDALLTSgPRKISPFFIPGAIINMASGMVSIKYDLKGPN 157
Cdd:PLN02787 206 AGKKALADGGITedvMKELDKTKCGVLIGSAMGGMKVFNDAIEALRIS-YRKMNPFCVPFATTNMGSAMLAMDLGWMGPN 284
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839  158 ISIVTACTTGLHNIGHAARMIAHNDADAMIAGGTEMASTPLGIGGFAAVRALSTRNDEPEKASRPWDKGRDGFVLGEGAA 237
Cdd:PLN02787 285 YSISTACATSNFCILNAANHIIRGEADVMLCGGSDAAIIPIGLGGFVACRALSQRNDDPTKASRPWDMNRDGFVMGEGAG 364
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839  238 CVVVEELEHAKKRNATIYAEIIGFGMSGDAYHMTRPDPEAEGFTTCMKNSLRDAGIAPERVDYINAHGTSTPAADPLEAR 317
Cdd:PLN02787 365 VLLLEELEHAKKRGANIYAEFLGGSFTCDAYHMTEPHPEGAGVILCIEKALAQSGVSKEDVNYINAHATSTKAGDLKEYQ 444
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839  318 AIKKTFGDHAyKLAVSSTKSMTGHMLGAAGALETVISVLAIRDNTAPPTINLENPDEGCDLD-FVPNEAREMKIDTVMSN 396
Cdd:PLN02787 445 ALMRCFGQNP-ELRVNSTKSMIGHLLGAAGAVEAIATVQAIRTGWVHPNINLENPESGVDTKvLVGPKKERLDIKVALSN 523
                        410
                 ....*....|....
gi 29653839  397 SFGFGGTNGTLVLS 410
Cdd:PLN02787 524 SFGFGGHNSSILFA 537
PRK07967 PRK07967
beta-ketoacyl-ACP synthase I;
4-412 5.45e-114

beta-ketoacyl-ACP synthase I;


Pssm-ID: 181184 [Multi-domain]  Cd Length: 406  Bit Score: 339.34  E-value: 5.45e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839    4 RRVVITGLGVVSPLGNKVSDMWQALLAGKSGVKPITRFDASSFPTQIAAEVrDFDPALVLDLKSIR---KTDVFVQFAME 80
Cdd:PRK07967   2 RRVVITGLGIVSSIGNNQQEVLASLREGRSGITFSPEFAEMGMRSQVWGNV-KLDPTGLIDRKVMRfmgDASAYAYLAME 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839   81 sarQAWEDSGLEINETNAPRVGVAIGSGIGGMPWIEKNYDALLTS-GPRKISPFFIPGAIINMASGMVSIKYDLKGPNIS 159
Cdd:PRK07967  81 ---QAIADAGLSEEQVSNPRTGLIAGSGGGSTRNQVEAADAMRGPrGPKRVGPYAVTKAMASTVSACLATPFKIKGVNYS 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839  160 IVTACTTGLHNIGHAARMIAHNDADAMIAGGTEMASTPLGIGgFAAVRALSTR-NDEPEKASRPWDKGRDGFVLGEGAAC 238
Cdd:PRK07967 158 ISSACATSAHCIGNAVEQIQLGKQDIVFAGGGEELDWEMSCL-FDAMGALSTKyNDTPEKASRAYDANRDGFVIAGGGGV 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839  239 VVVEELEHAKKRNATIYAEIIGFGMSGDAYHMTRpdPEAEGFTTCMKNSLRDAGiapERVDYINAHGTSTPAADPLEARA 318
Cdd:PRK07967 237 VVVEELEHALARGAKIYAEIVGYGATSDGYDMVA--PSGEGAVRCMQMALATVD---TPIDYINTHGTSTPVGDVKELGA 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839  319 IKKTFGDHAykLAVSSTKSMTGHMLGAAGALETVISVLAIRDNTAPPTINLENPDEG-CDLDFVPNEAREMKIDTVMSNS 397
Cdd:PRK07967 312 IREVFGDKS--PAISATKSLTGHSLGAAGVQEAIYSLLMMEHGFIAPSANIEELDPQaAGMPIVTETTDNAELTTVMSNS 389
                        410
                 ....*....|....*
gi 29653839  398 FGFGGTNGTLVLSRV 412
Cdd:PRK07967 390 FGFGGTNATLVFRRY 404
PRK06501 PRK06501
beta-ketoacyl-ACP synthase;
6-411 7.40e-113

beta-ketoacyl-ACP synthase;


Pssm-ID: 235817 [Multi-domain]  Cd Length: 425  Bit Score: 336.99  E-value: 7.40e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839    6 VVITGLGVVSPLGNKVSDMWQALLAGKSGVKPITRFDASSFPTQIAAEVrDFdpalvLDLKSIRKTDVFVQFAMESARQA 85
Cdd:PRK06501  13 VAVTGMGVVTSLGQGKADNWAALTAGESGIHTITRFPTEGLRTRIAGTV-DF-----LPESPFGASALSEALARLAAEEA 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839   86 WEDSGLEINETNAP--------------RVGVAIGSGIGGMPwiekNYDALLT-SGPRKISPF---FIPGAIinmaSGMV 147
Cdd:PRK06501  87 LAQAGIGKGDFPGPlflaappvelewpaRFALAAAVGDNDAP----SYDRLLRaARGGRFDALherFQFGSI----ADRL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839  148 SIKYDLKGPNISIVTACTTGLHNIGHAARMIAHNDADAMIAGGTEMASTPLGIGGFAAVRALSTRNDEPEKASRPWDKGR 227
Cdd:PRK06501 159 ADRFGTRGLPISLSTACASGATAIQLGVEAIRRGETDRALCIATDGSVSAEALIRFSLLSALSTQNDPPEKASKPFSKDR 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839  228 DGFVLGEGAACVVVEELEHAKKRNATIYAEIIGFGMSGDAYHMTRPDPEAEGFTTCMKNSLRDAGIAPERVDYINAHGTS 307
Cdd:PRK06501 239 DGFVMAEGAGALVLESLESAVARGAKILGIVAGCGEKADSFHRTRSSPDGSPAIGAIRAALADAGLTPEQIDYINAHGTS 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839  308 TPAADPLEARAIKKTFGDHAYKLAVSSTKSMTGHMLGAAGALETVISVLAIRDNTAPPTINLENPDEGCDLDFVPNEARE 387
Cdd:PRK06501 319 TPENDKMEYLGLSAVFGERLASIPVSSNKSMIGHTLTAAGAVEAVFSLLTIQTGRLPPTINYDNPDPAIPLDVVPNVARD 398
                        410       420
                 ....*....|....*....|....
gi 29653839  388 MKIDTVMSNSFGFGGTNGTLVLSR 411
Cdd:PRK06501 399 ARVTAVLSNSFGFGGQNASLVLTA 422
PRK09116 PRK09116
beta-ketoacyl-ACP synthase;
4-409 2.47e-106

beta-ketoacyl-ACP synthase;


Pssm-ID: 181657 [Multi-domain]  Cd Length: 405  Bit Score: 319.63  E-value: 2.47e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839    4 RRVVITGLGVVSPLGNKVSDMWQALLAGKSGVKPITRFD-ASSFPTQIAAEVRDFDPALVLDLKSIRKTDVFVQFAMESA 82
Cdd:PRK09116   2 RRVVVTGMGGVTALGEDWQTIAARLKAGRNAVRRMPEWDrYDGLNTRLAAPIDDFELPAHYTRKKIRSMGRVSLMATRAS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839   83 RQAWEDSGLEINE--TNApRVGVAIGSGIGGMPWIEKNYDALLTSGPRKISPffipGAIINM----ASGMVSIKYDLKGP 156
Cdd:PRK09116  82 ELALEDAGLLGDPilTDG-RMGIAYGSSTGSTDPIGAFGTMLLEGSMSGITA----TTYVRMmphtTAVNVGLFFGLKGR 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839  157 NISIVTACTTGLHNIGHAARMIAHNDADAMIAGGTEMAStPLGIGGFAAVRALSTRNDEPEKASRPWDKGRDGFVLGEGA 236
Cdd:PRK09116 157 VIPTSSACTSGSQGIGYAYEAIKYGYQTVMLAGGAEELC-PTEAAVFDTLFATSTRNDAPELTPRPFDANRDGLVIGEGA 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839  237 ACVVVEELEHAKKRNATIYAEIIGFGMSGDAYHMTRPDPEAEGftTCMKNSLRDAGIAPERVDYINAHGTSTPAADPLEA 316
Cdd:PRK09116 236 GTLVLEELEHAKARGATIYAEIVGFGTNSDGAHVTQPQAETMQ--IAMELALKDAGLAPEDIGYVNAHGTATDRGDIAES 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839  317 RAIKKTFGDhayKLAVSSTKSMTGHMLGAAGALETVISVLAIRDNTAPPTINLENPDEGC-DLDFVPNEAREMKIDTVMS 395
Cdd:PRK09116 314 QATAAVFGA---RMPISSLKSYFGHTLGACGALEAWMSIEMMNEGWFAPTLNLTQVDPACgALDYIMGEAREIDTEYVMS 390
                        410
                 ....*....|....
gi 29653839  396 NSFGFGGTNGTLVL 409
Cdd:PRK09116 391 NNFAFGGINTSLIF 404
PRK07910 PRK07910
beta-ketoacyl-ACP synthase;
6-411 4.20e-105

beta-ketoacyl-ACP synthase;


Pssm-ID: 236129 [Multi-domain]  Cd Length: 418  Bit Score: 317.06  E-value: 4.20e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839    6 VVITGLGVVSPLGNKVSDMWQALLAGKSGVKP-----ITRFDassFPTQIAAE-VRDFDPALVLdlKSIRKTDVFVQFAM 79
Cdd:PRK07910  14 VVVTGIAMTTALATDAETTWKLLLDGQSGIRTlddpfVEEFD---LPVRIGGHlLEEFDHQLTR--VELRRMSYLQRMST 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839   80 ESARQAWEDSGLEinETNAPRVGVAIGSGIGGMPWIEKNYDALLTSGPRKISPFFIPGAIINMASGMVSIKYDLKGPNIS 159
Cdd:PRK07910  89 VLGRRVWENAGSP--EVDTNRLMVSIGTGLGSAEELVFAYDDMRARGLRAVSPLAVQMYMPNGPAAAVGLERHAKAGVIT 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839  160 IVTACTTGLHNIGHAARMIAHNDADAMIAGGTEMASTPLGIGGFAAVRA-LSTRNDEPEKASRPWDKGRDGFVLGEGAAC 238
Cdd:PRK07910 167 PVSACASGSEAIAQAWRQIVLGEADIAICGGVETRIEAVPIAGFAQMRIvMSTNNDDPAGACRPFDKDRDGFVFGEGGAL 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839  239 VVVEELEHAKKRNATIYAEIIGFGMSGDAYHMTRPDPEAEGFTTCMKNSLRDAGIAPERVDYINAHGTSTPAADPLEARA 318
Cdd:PRK07910 247 MVIETEEHAKARGANILARIMGASITSDGFHMVAPDPNGERAGHAMTRAIELAGLTPGDIDHVNAHATGTSVGDVAEGKA 326
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839  319 IKKTFGDHayKLAVSSTKSMTGHMLGAAGALETVISVLAIRDNTAPPTINLENPDEGCDLDFVPNEAREMKIDTVMSNSF 398
Cdd:PRK07910 327 INNALGGH--RPAVYAPKSALGHSVGAVGAVESILTVLALRDGVIPPTLNLENLDPEIDLDVVAGEPRPGNYRYAINNSF 404
                        410
                 ....*....|...
gi 29653839  399 GFGGTNGTLVLSR 411
Cdd:PRK07910 405 GFGGHNVALAFGR 417
PRK14691 PRK14691
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
94-414 7.53e-105

3-oxoacyl-(acyl carrier protein) synthase II; Provisional


Pssm-ID: 173154 [Multi-domain]  Cd Length: 342  Bit Score: 313.97  E-value: 7.53e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839   94 NETNAPRVGVAIGSGIGGMPWIEKNYDALLTSGPRKISPFFIPGAIINMASGMVSIKYDLKGPNISIVTACTTGLHNIGH 173
Cdd:PRK14691  21 NTEKQERTATIIGAGIGGFPAIAHAVRTSDSRGPKRLSPFTVPSFLVNLAAGHVSIKHHFKGPIGAPVTACAAGVQAIGD 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839  174 AARMIAHNDADAMIAGGTEMASTPLGIGGFAAVRALSTR-NDEPEKASRPWDKGRDGFVLGEGAACVVVEELEHAKKRNA 252
Cdd:PRK14691 101 AVRMIRNNEADVALCGGAEAVIDTVSLAGFAAARALSTHfNSTPEKASRPFDTARDGFVMGEGAGLLIIEELEHALARGA 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839  253 TIYAEIIGFGMSGDAYHMTRPDPEAEGFTTCMKNSLRDAGIAPERVDYINAHGTSTPAADPLEARAIKKTFGDhAYKLAV 332
Cdd:PRK14691 181 KPLAEIVGYGTSADAYHMTSGAEDGDGAYRAMKIALRQAGITPEQVQHLNAHATSTPVGDLGEINAIKHLFGE-SNALAI 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839  333 SSTKSMTGHMLGAAGALETVISVLAIRDNTAPPTINLENPDEGCD-LDFVPNEAREMKIDTVMSNSFGFGGTNGTLVLSR 411
Cdd:PRK14691 260 TSTKSATGHLLGAAGGLETIFTVLALRDQIVPATLNLENPDPAAKgLNIIAGNAQPHDMTYALSNGFGFAGVNASILLKR 339

                 ...
gi 29653839  412 VFD 414
Cdd:PRK14691 340 WVD 342
elong_cond_enzymes cd00828
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ...
4-409 3.45e-94

"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: 288.57  E-value: 3.45e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839   4 RRVVITGLGVVSPLGNK---VSDMWQALLAGKSGVKPITRFDaSSFPTQIAAEVRDFDPAlVLDLKSIRKTDVFVQFAME 80
Cdd:cd00828   1 SRVVITGIGVVSPHGEGcdeVEEFWEALREGRSGIAPVARLK-SRFDRGVAGQIPTGDIP-GWDAKRTGIVDRTTLLALV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839  81 SARQAWEDSGLEINETNAP-RVGVAIGSGIGGMPWIEKNYDALLtsgpRKISPFFIPGAI--INMASGMVSIKYDLK-GP 156
Cdd:cd00828  79 ATEEALADAGITDPYEVHPsEVGVVVGSGMGGLRFLRRGGKLDA----RAVNPYVSPKWMlsPNTVAGWVNILLLSShGP 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839 157 NISIVTACTTGLHNIGHAARMIAHNDADAMIAGGTEmASTPLGIGGFAAVRALSTRNDEPEKASRPWDKGRDGFVLGEGA 236
Cdd:cd00828 155 IKTPVGACATALEALDLAVEAIRSGKADIVVVGGVE-DPLEEGLSGFANMGALSTAEEEPEEMSRPFDETRDGFVEAEGA 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839 237 ACVVVEELEHAKKRNATIYAEIIGFGMSGDAYHMTRPDPeAEGFTTCMKNSLRDAGIAPERVDYINAHGTSTPAADPLEA 316
Cdd:cd00828 234 GVLVLERAELALARGAPIYGRVAGTASTTDGAGRSVPAG-GKGIARAIRTALAKAGLSLDDLDVISAHGTSTPANDVAES 312
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839 317 RAIKKTFGDHAYKLAVSSTKSMTGHMLGAAGALETVISVLAIRDNTAPPTINLENPDEGCDLDFVPNEAR--EMKIDTVM 394
Cdd:cd00828 313 RAIAEVAGALGAPLPVTAQKALFGHSKGAAGALQLIGALQSLEHGLIPPTANLDDVDPDVEHLSVVGLSRdlNLKVRAAL 392
                       410
                ....*....|....*
gi 29653839 395 SNSFGFGGTNGTLVL 409
Cdd:cd00828 393 VNAFGFGGSNAALVL 407
PRK05952 PRK05952
beta-ketoacyl-ACP synthase;
5-411 7.72e-88

beta-ketoacyl-ACP synthase;


Pssm-ID: 235653 [Multi-domain]  Cd Length: 381  Bit Score: 271.54  E-value: 7.72e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839    5 RVVITGLGVVSPLGNkVSDMWQALLAGKSGVKPITRFdassfptqiaAEVRDFDPALV----LDLKSIRKTDVfvqfame 80
Cdd:PRK05952   3 KVVVTGIGLVSALGD-LEQSWQRLLQGKSGIKLHQPF----------PELPPLPLGLIgnqpSSLEDLTKTVV------- 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839   81 saRQAWEDSGLEINETNAprvGVAIGS--GIGGM--PWIEKNYDALLTSGPRKISPFFI---PgaiiNMASGMVSIKYDL 153
Cdd:PRK05952  65 --TAALKDAGLTPPLTDC---GVVIGSsrGCQGQweKLARQMYQGDDSPDEELDLENWLdtlP----HQAAIAAARQIGT 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839  154 KGPNISIVTACTTGLHNIGHAARMIAHNDADAMIAGGTEMASTPLGIGGFAAVRALSTrndepeKASRPWDKGRDGFVLG 233
Cdd:PRK05952 136 QGPVLAPMAACATGLWAIAQGVELIQTGQCQRVIAGAVEAPITPLTLAGFQQMGALAK------TGAYPFDRQREGLVLG 209
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839  234 EGAACVVVEELEHAKKRNATIYAEIIGFGMSGDAYHMTRPDPEAEGFTTCMKNSLRDAGIAPERVDYINAHGTSTPAADP 313
Cdd:PRK05952 210 EGGAILVLESAELAQKRGAKIYGQILGFGLTCDAYHMSAPEPDGKSAIAAIQQCLARSGLTPEDIDYIHAHGTATRLNDQ 289
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839  314 LEARAIKKTFGdhaYKLAVSSTKSMTGHMLGAAGALETVISVLAIRDNTAPPTINLENPDegCDLDFVpNEAREMKIDTV 393
Cdd:PRK05952 290 REANLIQALFP---HRVAVSSTKGATGHTLGASGALGVAFSLLALRHQQLPPCVGLQEPE--FDLNFV-RQAQQSPLQNV 363
                        410
                 ....*....|....*...
gi 29653839  394 MSNSFGFGGTNGTLVLSR 411
Cdd:PRK05952 364 LCLSFGFGGQNAAIALGK 381
CLF cd00832
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ...
4-409 2.56e-86

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: 268.07  E-value: 2.56e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839   4 RRVVITGLGVVSPLGNKVSDMWQALLAGKSGVKPITRFDASSFPTQIAAEVRDFDPALVLDLKSIRKTDVFVQFAMESAR 83
Cdd:cd00832   1 RRAVVTGIGVVAPNGLGVEEYWKAVLDGRSGLGPITRFDPSGYPARLAGEVPDFDAAEHLPGRLLPQTDRMTRLALAAAD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839  84 QAWEDSGLEINETNAPRVGVAIGSGIGGMPWIEKNYDALLTSGPRKISPFFIPGAIINMASGMVSIKYDLKGPNISIVTA 163
Cdd:cd00832  81 WALADAGVDPAALPPYDMGVVTASAAGGFEFGQRELQKLWSKGPRHVSAYQSFAWFYAVNTGQISIRHGMRGPSGVVVAE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839 164 CTTGLHNIGHAARMIAhNDADAMIAGGTEMASTPLGIGGFAAVRALSTrNDEPEKASRPWDKGRDGFVLGEGAACVVVEE 243
Cdd:cd00832 161 QAGGLDALAQARRLVR-RGTPLVVSGGVDSALCPWGWVAQLSSGRLST-SDDPARAYLPFDAAAAGYVPGEGGAILVLED 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839 244 LEHAKKRNATIYAEIIGFGMSGDAyhmtRPDP-EAEGFTTCMKNSLRDAGIAPERVDYINAHGTSTPAADPLEARAIKKT 322
Cdd:cd00832 239 AAAARERGARVYGEIAGYAATFDP----PPGSgRPPGLARAIRLALADAGLTPEDVDVVFADAAGVPELDRAEAAALAAV 314
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839 323 FGDHAykLAVSSTKSMTGHMLGAAGALETVISVLAIRDNTAPPTINLENPDEGCDLDFVPNEAREMKIDTVMSNSFGFGG 402
Cdd:cd00832 315 FGPRG--VPVTAPKTMTGRLYAGGAPLDVATALLALRDGVIPPTVNVTDVPPAYGLDLVTGRPRPAALRTALVLARGRGG 392

                ....*..
gi 29653839 403 TNGTLVL 409
Cdd:cd00832 393 FNSALVV 399
PRK07103 PRK07103
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
5-411 8.33e-83

polyketide beta-ketoacyl:acyl carrier protein synthase; Validated


Pssm-ID: 180839 [Multi-domain]  Cd Length: 410  Bit Score: 259.58  E-value: 8.33e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839    5 RVVITGLGVVSPLGNKVSDMWQALLAGKSGVKPITRFDASSFPTQ--------IAAEVRDFDPALVLDLKSIRKTDVFVQ 76
Cdd:PRK07103   3 EVVVTGVGVVSAIGQGRPSFAAALLAGRHAFGVMRRPGRQVPDDAgaglasafIGAELDSLALPERLDAKLLRRASLSAQ 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839   77 FAMESARQAWEDSGLEinETNAPRVGVAIGSGIggmpwIEKNYDALL----TSGPRKISPFFIPGAIINMASGMVSIKYD 152
Cdd:PRK07103  83 AALAAAREAWRDAALG--PVDPDRIGLVVGGSN-----LQQREQALVhetyRDRPAFLRPSYGLSFMDTDLVGLCSEQFG 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839  153 LKGPNISIVTACTTGLHNIGHAARMIAHNDADAMIAGGTEMASTPLGIGGFAAVRALSTRN--DEPEKASRPWDKGRDGF 230
Cdd:PRK07103 156 IRGEGFTVGGASASGQLAVIQAARLVQSGSVDACIAVGALMDLSYWECQALRSLGAMGSDRfaDEPEAACRPFDQDRDGF 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839  231 VLGEGAACVVVEELEHAKKRNATIYAEIIGFGMSGDAyhmTR-PDPEAEGFTTCMKNSLRDAGIAPERVDYINAHGTSTP 309
Cdd:PRK07103 236 IYGEACGAVVLESAESARRRGARPYAKLLGWSMRLDA---NRgPDPSLEGEMRVIRAALRRAGLGPEDIDYVNPHGTGSP 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839  310 AADPLEARAIKKTFGDHAYklaVSSTKSMTGHMLGAAGALETVISVLAIRDNTAPPTINLENP-DEGCdlDFVPNEAREM 388
Cdd:PRK07103 313 LGDETELAALFASGLAHAW---INATKSLTGHGLSAAGIVELIATLLQMRAGFLHPSRNLDEPiDERF--RWVGSTAESA 387
                        410       420
                 ....*....|....*....|...
gi 29653839  389 KIDTVMSNSFGFGGTNGTLVLSR 411
Cdd:PRK07103 388 RIRYALSLSFGFGGINTALVLER 410
PKS cd00833
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ...
5-409 1.14e-73

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: 236.30  E-value: 1.14e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839   5 RVVITGLGVVSPLGNKVSDMWQALLAGKSGVKPIT--RFDASSFPTQIAA-------------EVRDFDP---------A 60
Cdd:cd00833   2 PIAIVGMACRFPGAADPDEFWENLLEGRDAISEIPedRWDADGYYPDPGKpgktytrrggfldDVDAFDAaffgispreA 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839  61 LVLDLksirktdvfvQF--AMESARQAWEDSGLEINETNAPRVGVAIGSGIGgmpwiekNYDALLTSGPRKISPFFIPGA 138
Cdd:cd00833  82 EAMDP----------QQrlLLEVAWEALEDAGYSPESLAGSRTGVFVGASSS-------DYLELLARDPDEIDAYAATGT 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839 139 IINMASGMVSIKYDLKGPNISIVTACTTGLHNIGHAARMIAHNDADAMIAGGTEMASTPLGIGGFAAVRALStrndePEK 218
Cdd:cd00833 145 SRAFLANRISYFFDLRGPSLTVDTACSSSLVALHLACQSLRSGECDLALVGGVNLILSPDMFVGFSKAGMLS-----PDG 219
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839 219 ASRPWDKGRDGFVLGEGAACVVVEELEHAKKRNATIYAEIIGFGMSGDAY--HMTRPDPEAegFTTCMKNSLRDAGIAPE 296
Cdd:cd00833 220 RCRPFDADADGYVRGEGVGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRtkGITAPSGEA--QAALIRRAYARAGVDPS 297
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839 297 RVDYINAHGTSTPAADPLEARAIKKTFG---DHAYKLAVSSTKSMTGHMLGAAGALETVISVLAIRDNTAPPTINLENPD 373
Cdd:cd00833 298 DIDYVEAHGTGTPLGDPIEVEALAKVFGgsrSADQPLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPN 377
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....
gi 29653839 374 EGCDLD----FVPNEAREMKIDTVMS----NSFGFGGTNGTLVL 409
Cdd:cd00833 378 PKIDFEesplRVPTEARPWPAPAGPRragvSSFGFGGTNAHVIL 421
PRK09185 PRK09185
beta-ketoacyl-ACP synthase;
6-411 1.99e-73

beta-ketoacyl-ACP synthase;


Pssm-ID: 236398 [Multi-domain]  Cd Length: 392  Bit Score: 234.74  E-value: 1.99e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839    6 VVITGLGVVSPLGNKVSDMWQALLAGK-SGVKPITRFDASSfPTQIAAEVRDFDPALVLDLKSIR-KTDVFVQFAMESAR 83
Cdd:PRK09185   4 VYISAFGATSALGRGLDAILAALRAGRaSGMRPCDFWLVDL-PTWVGEVVGVELPALPAALAAFDcRNNRLALLALQQIE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839   84 QAWEDSgleINETNAPRVGVAIG---SGIGGMpwiEKNYDALLTSGPRKISPFFIPGAIINMASGMVSIKYDLKGPNISI 160
Cdd:PRK09185  83 PAVEAA---IARYGADRIGVVLGtstSGILEG---ELAYRRRDPAHGALPADYHYAQQELGSLADFLRAYLGLSGPAYTI 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839  161 VTACTTGLHNIGHAARMIAHNDADAMIAGGTE-MASTPLGigGFAAVRALSTRndepekASRPWDKGRDGFVLGEGAACV 239
Cdd:PRK09185 157 STACSSSAKVFASARRLLEAGLCDAAIVGGVDsLCRLTLN--GFNSLESLSPQ------PCRPFSANRDGINIGEAAAFF 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839  240 VVEelehakkRNATIYAEIIGFGMSGDAYHMTRPDPEAEGFTTCMKNSLRDAGIAPERVDYINAHGTSTPAADPLEARAI 319
Cdd:PRK09185 229 LLE-------REDDAAVALLGVGESSDAHHMSAPHPEGLGAILAMQQALADAGLAPADIGYINLHGTATPLNDAMESRAV 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839  320 KKTFGDHaykLAVSSTKSMTGHMLGAAGALETVISVLAIRDNTAPPTINLENPDEGCDLDFVPNEAREMKIDTVMSNSFG 399
Cdd:PRK09185 302 AAVFGDG---VPCSSTKGLTGHTLGAAGAVEAAICWLALRHGLPPHGWNTGQPDPALPPLYLVENAQALAIRYVLSNSFA 378
                        410
                 ....*....|..
gi 29653839  400 FGGTNGTLVLSR 411
Cdd:PRK09185 379 FGGNNCSLIFGR 390
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
4-247 1.20e-68

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: 217.50  E-value: 1.20e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839     4 RRVVITGLGVVSPLGNKVSDMWQALLAGKSGVKPI--TRFDASSF---PTQIAAEVR----------DFDPALV-LDLKS 67
Cdd:pfam00109   1 EPVAIVGMGCRFPGGNDPEEFWENLLEGRDGISEIpaDRWDPDKLydpPSRIAGKIYtkwgglddifDFDPLFFgISPRE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839    68 IRKTDVFVQFAMESARQAWEDSGLEINETNAPRVGVAIGSGIGGmpwiEKNYDAL-LTSGPRKISPFFIpGAIINMASGM 146
Cdd:pfam00109  81 AERMDPQQRLLLEAAWEALEDAGITPDSLDGSRTGVFIGSGIGD----YAALLLLdEDGGPRRGSPFAV-GTMPSVIAGR 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839   147 VSIKYDLKGPNISIVTACTTGLHNIGHAARMIAHNDADAMIAGGTEMASTPLGIGGFAAVRALSTrnDEPEKASRPWDkg 226
Cdd:pfam00109 156 ISYFLGLRGPSVTVDTACSSSLVAIHAAVQSIRSGEADVALAGGVNLLLTPLGFAGFSAAGMLSP--DGPCKAFDPFA-- 231
                         250       260
                  ....*....|....*....|.
gi 29653839   227 rDGFVLGEGAACVVVEELEHA 247
Cdd:pfam00109 232 -DGFVRGEGVGAVVLKRLSDA 251
decarbox_cond_enzymes cd00825
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ...
73-409 2.50e-68

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: 219.81  E-value: 2.50e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839  73 VFVQFAMESARQAWEDSGLEINETNAPRVGVAIGSGIGGMPWIEKNYDALLTSGPRKISPFFIPGAiinmaSGMVSIKYD 152
Cdd:cd00825  10 YVSILGFEAAERAIADAGLSREYQKNPIVGVVVGTGGGSPRFQVFGADAMRAVGPYVVTKAMFPGA-----SGQIATPLG 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839 153 LKGPNISIVTACTTGLHNIGHAARMIAHNDADAMIAGGTEMASTPlgiggFAAVRALSTRNDEPEKASRPWDKGRDGFVL 232
Cdd:cd00825  85 IHGPAYDVSAACAGSLHALSLAADAVQNGKQDIVLAGGSEELAAP-----MDCEFDAMGALSTPEKASRTFDAAADGFVF 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839 233 GEGAACVVVEELEHAKKRNATIYAEIIGFGMSGDAYHMTRPDPEAEGFTTCMKNSLRDAGIAPERVDYINAHGTSTPAAD 312
Cdd:cd00825 160 GDGAGALVVEELEHALARGAHIYAEIVGTAATIDGAGMGAFAPSAEGLARAAKEALAVAGLTVWDIDYLVAHGTGTPIGD 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839 313 PLEARAIKKTFGDHayKLAVSSTKSMTGHMLGAAGALETVISVLAIRDNTAPPTINLENPDEgcDLDFVPNEAREMKIDT 392
Cdd:cd00825 240 VKELKLLRSEFGDK--SPAVSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIPPSIHIEELDE--AGLNIVTETTPRELRT 315
                       330
                ....*....|....*..
gi 29653839 393 VMSNSFGFGGTNGTLVL 409
Cdd:cd00825 316 ALLNGFGLGGTNATLVL 332
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
23-409 5.15e-57

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 202.41  E-value: 5.15e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839   23 DMWQALLAGKSGVKPIT--RFDASSF--PTQIAA------------EVRDFDP---------ALVLDlksirktdvfVQ- 76
Cdd:COG3321   23 EFWRNLRAGRDAITEVPadRWDADAYydPDPDAPgktyvrwggfldDVDEFDAlffgispreAEAMD----------PQq 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839   77 -FAMESARQAWEDSGLEINETNAPRVGVAIGSGIGgmpwiekNYDALLTSGPRKISPFFIPGAIINMASGMVSIKYDLKG 155
Cdd:COG3321   93 rLLLEVAWEALEDAGYDPESLAGSRTGVFVGASSN-------DYALLLLADPEAIDAYALTGNAKSVLAGRISYKLDLRG 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839  156 PNISIVTACTTGLHNIGHAARMIAHNDADAMIAGGTEMASTPLGIGGFAAVRALStrndePEKASRPWDKGRDGFVLGEG 235
Cdd:COG3321  166 PSVTVDTACSSSLVAVHLACQSLRSGECDLALAGGVNLMLTPESFILFSKGGMLS-----PDGRCRAFDADADGYVRGEG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839  236 AACVVVEELEHAKKRNATIYAEIIGFGMS--GDAYHMTRPDPEAEgfTTCMKNSLRDAGIAPERVDYINAHGTSTPAADP 313
Cdd:COG3321  241 VGVVVLKRLSDALRDGDRIYAVIRGSAVNqdGRSNGLTAPNGPAQ--AAVIRRALADAGVDPATVDYVEAHGTGTPLGDP 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839  314 LEARAIKKTFGDHAYK---LAVSSTKSMTGHMLGAAGALeTVI-SVLAIRDNTAPPTINLENPDEGCDLD----FVPNEA 385
Cdd:COG3321  319 IEAAALTAAFGQGRPAdqpCAIGSVKSNIGHLEAAAGVA-GLIkAVLALRHGVLPPTLHFETPNPHIDFEnspfYVNTEL 397
                        410       420       430
                 ....*....|....*....|....*....|
gi 29653839  386 REMKIDT------VmsNSFGFGGTNGTLVL 409
Cdd:COG3321  398 RPWPAGGgprragV--SSFGFGGTNAHVVL 425
Ketoacyl-synt_C pfam02801
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ...
255-370 2.97e-47

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: 157.73  E-value: 2.97e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839   255 YAEIIGFGMSGDAYHMTRPDPEAEGFTTCMKNSLRDAGIAPERVDYINAHGTSTPAADPLEARAIKKTFGDHAYK--LAV 332
Cdd:pfam02801   1 YAVIKGSAVNHDGRHNGLTAPNGEGQARAIRRALADAGVDPEDVDYVEAHGTGTPLGDPIEAEALKRVFGSGARKqpLAI 80
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 29653839   333 SSTKSMTGHMLGAAGALETVISVLAIRDNTAPPTINLE 370
Cdd:pfam02801  81 GSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLNLE 118
cond_enzymes cd00327
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ...
77-409 4.31e-36

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: 132.95  E-value: 4.31e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839  77 FAMESARQAWEDSGLEinetNAPRVGVAIGSGIGGmpwieknyDALLTSGPRKISPFFIPGaiinmasgmvsikydlkGP 156
Cdd:cd00327  10 LGFEAAEQAIADAGLS----KGPIVGVIVGTTGGS--------GEFSGAAGQLAYHLGISG-----------------GP 60
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839 157 NISIVTACTTGLHNIGHAARMIAHNDADAMIAGGTEMastplgiggfaavralstrndepekasrpwdkgrdgFVLGEGA 236
Cdd:cd00327  61 AYSVNQACATGLTALALAVQQVQNGKADIVLAGGSEE------------------------------------FVFGDGA 104
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839 237 ACVVVEELEHAKKRNATIYAEIIGFGMSGDAYHMtRPDPEAEGFTTCMKNSLRDAGIAPERVDYINAHGTSTPAADPLEA 316
Cdd:cd00327 105 AAAVVESEEHALRRGAHPQAEIVSTAATFDGASM-VPAVSGEGLARAARKALEGAGLTPSDIDYVEAHGTGTPIGDAVEL 183
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839 317 RAIKKTFGDHAykLAVSSTKSMTGHMLGAAGALETVISVLAIRDNTAPPTinlenPDEGcdldfvpnearemkiDTVMSN 396
Cdd:cd00327 184 ALGLDPDGVRS--PAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIPPT-----PREP---------------RTVLLL 241
                       330
                ....*....|...
gi 29653839 397 SFGFGGTNGTLVL 409
Cdd:cd00327 242 GFGLGGTNAAVVL 254
omega_3_PfaA TIGR02813
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ...
136-409 2.26e-34

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: 135.90  E-value: 2.26e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839    136 PGAIINMASGMVSIKYDLKGPNISIVTACTTGLHNIGHAARMIAHNDADAMIAGGTEMASTPLGIGGFAAVRALSTRNDe 215
Cdd:TIGR02813  178 PGSLGNVISGRIANRFDLGGMNCVVDAACAGSLAAIRMALSELLEGRSEMMITGGVCTDNSPFMYMSFSKTPAFTTNED- 256
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839    216 pekaSRPWDKGRDGFVLGEGAACVVVEELEHAKKRNATIYAEIIGFGMSGDAYHMTRPDPEAEGFTTCMKNSLRDAGIAP 295
Cdd:TIGR02813  257 ----IQPFDIDSKGMMIGEGIGMMALKRLEDAERDGDRIYAVIKGVGASSDGKFKSIYAPRPEGQAKALKRAYDDAGFAP 332
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839    296 ERVDYINAHGTSTPAADPLEARAIKKTFG---DHAYKLAVSSTKSMTGHMLGAAGALETVISVLAIRDNTAPPTINLENP 372
Cdd:TIGR02813  333 HTCGLIEAHGTGTAAGDVAEFGGLVSVFSqdnDQKQHIALGSVKSQIGHTKSTAGTAGMIKAVLALHHKVLPPTINVDQP 412
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 29653839    373 DEGCDLDFVP----NEARE--MKIDTVMS----NSFGFGGTNGTLVL 409
Cdd:TIGR02813  413 NPKLDIENSPfylnTETRPwmQREDGTPRragiSSFGFGGTNFHMVL 459
PKS_KS smart00825
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ...
6-409 2.13e-23

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: 99.33  E-value: 2.13e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839      6 VVITGLGVVSPLGNKVSDMWQALLAGKSGVKpitRFDASSFptQI-AAEVRDFDPALVLdlksirktdvfvqfAMESARQ 84
Cdd:smart00825   1 IAIVGMSCRFPGADDPEEFWDLLLAGLDDVD---LFDAAFF--GIsPREAEAMDPQQRL--------------LLEVAWE 61
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839     85 AWEDSGLEINETNAPRVGVAIGSGIGGmpwieknydalltsgprkispffipgaiinmasgmvsikYdlkgpNISIVTAC 164
Cdd:smart00825  62 ALEDAGIDPESLRGSRTGVFVGVSSSD---------------------------------------Y-----SVTVDTAC 97
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839    165 TTGLHNIGHAARMIAHNDADAMIAGGTEMASTPLGIGGFAAVRALStrndePEKASRPWDKGRDGFVLGEGAACVVVEEL 244
Cdd:smart00825  98 SSSLVALHLACQSLRSGECDMALAGGVNLILSPDTFVGLSRAGMLS-----PDGRCKTFDASADGYVRGEGVGVVVLKRL 172
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839    245 EHAKKRNATIYAEIIGFGM--SGDAYHMTRPDPEAEgfttcmknslrdagiapervdyinahgtstpaadplearaikkt 322
Cdd:smart00825 173 SDALRDGDPILAVIRGSAVnqDGRSNGITAPSGPAQ-------------------------------------------- 208
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839    323 fgdhaykLAVSSTKSMTGHMLGAAGaLETVI-SVLAIRDNTAPPTINLENPDEGCDLD----FVPNEAREMKIDT----V 393
Cdd:smart00825 209 -------LLIGSVKSNIGHLEAAAG-VAGLIkVVLALKHGVIPPTLHFETPNPHIDLEesplRVPTELTPWPPPGrprrA 280
                          410
                   ....*....|....*.
gi 29653839    394 MSNSFGFGGTNGTLVL 409
Cdd:smart00825 281 GVSSFGFGGTNAHVIL 296
PRK06519 PRK06519
beta-ketoacyl-ACP synthase;
1-365 7.95e-10

beta-ketoacyl-ACP synthase;


Pssm-ID: 235819 [Multi-domain]  Cd Length: 398  Bit Score: 60.35  E-value: 7.95e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839    1 MEKRRVVITGLGVVSPLGNKVSDMWQALLAGKsgvkPITRFDASSF---PTQIAAEVrDFDpalvldlKSI-RKTDvfvQ 76
Cdd:PRK06519   3 MQPNDVVITGIGLVSSLGEGLDAHWNALSAGR----PQPNVDTETFapyPVHPLPEI-DWS-------QQIpKRGD---Q 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839   77 FAMES--------ARQAWEDSGLEINE--TNAPRVGVAIGSGiggmpwiEKNY--DALLTSGPRKISPffiPGAIINMA- 143
Cdd:PRK06519  68 RQMETwqrlgtyaAGLALDDAGIKGNEelLSTMDMIVAAGGG-------ERDIavDTAILNEARKRND---RGVLLNERl 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839  144 -------------SGMvsikydLKGpNISIVTACT-----------TGLHNIGHAARMIAHNDADAMIAGGTEMASTPLG 199
Cdd:PRK06519 138 mtelrptlflaqlSNL------LAG-NISIVHKVTgssrtfmgeesAGVSAIEIAFARIASGQSDHALVGGAYNAERPDM 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839  200 IGGFAAVRALSTRNDEPEKASRPWDKGrdGFVLGEGAACVVVEELEHAKKRNATIYAEIigfgmSGDAYHMTRPDPEAeg 279
Cdd:PRK06519 211 LLLYELGGLLLKGGWAPVWSRGGEDGG--GFILGSGGAFLVLESREHAEARGARPYARI-----SGVESDRARRAPGD-- 281
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839  280 FTTCMKNSLRDAGIAPERVDYInahgTSTPAADPLEARaiKKTFGDHAYKLAVSSTKSMTGHMLGAAGALETVISVLAIR 359
Cdd:PRK06519 282 LEASLERLLKPAGGLAAPTAVI----SGATGAHPATAE--EKAALEAALAGPVRGIGTLFGHTMEAQFPLGLALAALSVS 355

                 ....*.
gi 29653839  360 DNTAPP 365
Cdd:PRK06519 356 KGALFP 361
PRK06147 PRK06147
3-oxoacyl-(acyl carrier protein) synthase; Validated
167-301 2.59e-06

3-oxoacyl-(acyl carrier protein) synthase; Validated


Pssm-ID: 235715 [Multi-domain]  Cd Length: 348  Bit Score: 48.86  E-value: 2.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839  167 GLHNIGHAARMIAHNDADAMIAGGTE-MASTPLGIGGFAAVRALSTRNDEpekasrpwdkgrdGFVLGEGAACVVVEELE 245
Cdd:PRK06147 136 GAVALAQARRLIAAGGCPRVLVAGVDsLLTGPTLAHYEARDRLLTSQNSN-------------GFIPGEAAAAVLLGRPA 202
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 29653839  246 HAKKRNATIYAeiIGFGMSGDAYHMTRPDP-EAEGFTTCMKNSLRDAGIAPERVDYI 301
Cdd:PRK06147 203 GGEAPGLPLLG--LGLGREPAPVGESEDLPlRGDGLTQAIRAALAEAGCGLEDMDYR 257
SCP-x_thiolase cd00829
Thiolase domain associated with sterol carrier protein (SCP)-x isoform and related proteins; ...
74-304 1.21e-03

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: 40.71  E-value: 1.21e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839  74 FVQFAMESARQAWEDSGLEINETNAPRVGVAIGSGIGGMPwieknydalltsgprkispffipGAIINMASGMvsikydL 153
Cdd:cd00829  16 PLELAAEAARAALDDAGLEPADIDAVVVGNAAGGRFQSFP-----------------------GALIAEYLGL------L 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839 154 KGPNISIVTACTTGLHNIGHAARMIAHNDADAMIAGGTEMAST--------------------PLGIGGFAAVRAL---- 209
Cdd:cd00829  67 GKPATRVEAAGASGSAAVRAAAAAIASGLADVVLVVGAEKMSDvptgdeaggrasdlewegpePPGGLTPPALYALaarr 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839 210 ----------------------STRND----------EPEKASRP-WD--KGRDGFVLGEGAACVVVEELEHAKKRNATi 254
Cdd:cd00829 147 ymhrygttredlakvavknhrnAARNPyaqfrkpitvEDVLNSRMiADplRLLDCCPVSDGAAAVVLASEERARELTDR- 225
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 29653839 255 YAEIIGFGMSGDAYHMTRPDPEA--EGFTTCMKNSLRDAGIAPERVDYINAH 304
Cdd:cd00829 226 PVWILGVGAASDTPSLSERDDFLslDAARLAARRAYKMAGITPDDIDVAELY 277
PaaJ COG0183
Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is ...
163-236 1.82e-03

Acetyl-CoA acetyltransferase [Lipid transport and metabolism]; Acetyl-CoA acetyltransferase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 439953 [Multi-domain]  Cd Length: 391  Bit Score: 40.05  E-value: 1.82e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 29653839 163 ACTTGLHNIGHAARMIAHNDADAMIAGGTEMAST-PLGIGGFAAVRALSTRNDEPEKASRPWDKgRDGFVLGEGA 236
Cdd:COG0183  87 VCGSGLQAVALAAQAIAAGDADVVIAGGVESMSRaPMLLPKARWGYRMNAKLVDPMINPGLTDP-YTGLSMGETA 160
PLN02644 PLN02644
acetyl-CoA C-acetyltransferase
232-360 3.30e-03

acetyl-CoA C-acetyltransferase


Pssm-ID: 215347 [Multi-domain]  Cd Length: 394  Bit Score: 39.31  E-value: 3.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839  232 LGEGAACVVVEELEHAKKRNATIYAEIIGFgmsGDAYHmtrpDPEAegFTT----CMKNSLRDAGIAPERVDY--INahg 305
Cdd:PLN02644 250 ISDGAAALVLVSGEKALELGLQVIAKIRGY---ADAAQ----APEL--FTTapalAIPKALKHAGLEASQVDYyeIN--- 317
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 29653839  306 tstpAADPLEARAIKKTFGDHAYKLAVSSTKSMTGHMLGAAGA--LETVISVLAIRD 360
Cdd:PLN02644 318 ----EAFSVVALANQKLLGLDPEKVNVHGGAVSLGHPIGCSGAriLVTLLGVLRSKN 370
PRK12578 PRK12578
thiolase domain-containing protein;
69-202 3.56e-03

thiolase domain-containing protein;


Pssm-ID: 183606 [Multi-domain]  Cd Length: 385  Bit Score: 39.44  E-value: 3.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839   69 RKTDVFVQ-FAMESARQAWEDSGLEINETNAPRVGVAIGSGIGGMPwieknydalltsgprkispffipGAIINMASGMV 147
Cdd:PRK12578  15 RRDDVSVQeLAWESIKEALNDAGVSQTDIELVVVGSTAYRGIELYP-----------------------APIVAEYSGLT 71
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 29653839  148 SikydlKGPnISIVTACTTGLHNIGHAARMIAHNDADAMIAGGTEM-----ASTPLGIGG 202
Cdd:PRK12578  72 G-----KVP-LRVEAMCATGLAASLTAYTAVASGLVDMAIAVGVDKmtevdTSTSLAIGG 125
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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