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Conserved domains on  [gi|712037591|gb|AIW63287|]
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polyketide synthase AS3D903 [Azadinium spinosum]

Protein Classification

PKS_assoc and PKS domain-containing protein( domain architecture ID 10426314)

PKS_assoc and PKS domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PKS cd00833
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ...
 372-783 5.42e-113

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: 351.09  E-value: 5.42e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591 372 LFMAGTDALIDPPYIRFDKEPYYMNDRDAplyGKAYVFHGSFVAHDIliGFDHEFFGYTYEEAEAIAPAQRWVLEVGYIT 451
Cdd:cd00833   24 NLLEGRDAISEIPEDRWDADGYYPDPGKP---GKTYTRRGGFLDDVD--AFDAAFFGISPREAEAMDPQQRLLLEVAWEA 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591 452 LHHAGWTKQSLNKARIGTFSGDSGSEWNDLYWKQDEHVMFC----NHSCVTNTRIAHALGLTGPNVHADTACSASLVAAN 527
Cdd:cd00833   99 LEDAGYSPESLAGSRTGVFVGASSSDYLELLARDPDEIDAYaatgTSRAFLANRISYFFDLRGPSLTVDTACSSSLVALH 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591 528 VATHFLRTytegglkenpdqegceqqNQIDYALCAGILCMVSPAGWIGECASTMLSYRGRCFTYDSSADGFIRGEGsCHA 607
Cdd:cd00833  179 LACQSLRS------------------GECDLALVGGVNLILSPDMFVGFSKAGMLSPDGRCRPFDADADGYVRGEG-VGV 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591 608 FLERRHDDHVSVGSRSLAVLMGTAVNQDGKSASLTAPHGPSQQETIRMSLREAVLKPNDVLLTECHGTGTALGDPIEVGA 687
Cdd:cd00833  240 VVLKRLSDALRDGDRIYAVIRGSAVNQDGRTKGITAPSGEAQAALIRRAYARAGVDPSDIDYVEAHGTGTPLGDPIEVEA 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591 688 NRGVmFGKRERPFFHCT---AKAHVGHEEANAGTCGLLKIVLMLQNGMITPNPHLRALNPHLDTHAYPIYFVNELSTMQR 764
Cdd:cd00833  320 LAKV-FGGSRSADQPLLigsVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKIDFEESPLRVPTEARPWPA 398

                        410       420
                 ....*....|....*....|.
gi 712037591 765 ADD--IYGVSSFGFGGTNSRA 783
Cdd:cd00833  399 PAGprRAGVSSFGFGGTNAHV 419
PKS_assoc super family cl22841
polyketide synthase-associated domain; This model describes a rare domain found as the ...
 100-328 1.54e-50

polyketide synthase-associated domain; This model describes a rare domain found as the N-terminal region of a number of dinoflagellate-specific proteins that resemble type I polyketide synthases.


The actual alignment was detected with superfamily member TIGR04556:

Pssm-ID: 275349  Cd Length: 228  Bit Score: 177.18  E-value: 1.54e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591  100 EDGGFDTLWPAANDTSygVFGSTVIDCLATKGYCVVQMFGSKVLRETALEEAAETP---IYEGLRAEMEEAFLGKENNSR 176
Cdd:TIGR04556   1 DLDGFDIVLGPKSDPD--VVGEEIADCLATKGFCVMKLFVASEDLDSAVDVAKKLEdagQFFRLAVEFEEGYLGKEGSAK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591  177 VGLIEKDTPER---LLDNALAFCDRDITNLSMLLMQAGPDCFGFEIQSRTNAIARTPYPEGQVVTSPNFS-EDDMGEKFv 252
Cdd:TIGR04556  79 VAWLDPSSPDApdaVKDSPLKKMDANFSSIAQMLQPYSQESLGFEVYSRTNALLRLPLPDGDEEEYPPAEaDDGEAEKY- 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 712037591  253 eatIEFISRKKFCVMYLIENNGGLIEFYPKEHlgMGEKVELPIQKNRMVIFRSDLMNYSYKPQGTSVSIQAWLLDE 328
Cdd:TIGR04556 158 ---LHTMCRRKLTVLVFMGPTGGTLTLQPKEE--GGDSVEVPAEPGTVVLIRSDAYEYSYEPTGESLTLSSFLMQD 228
 
Name Accession Description Interval E-value
PKS cd00833
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ...
 372-783 5.42e-113

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: 351.09  E-value: 5.42e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591 372 LFMAGTDALIDPPYIRFDKEPYYMNDRDAplyGKAYVFHGSFVAHDIliGFDHEFFGYTYEEAEAIAPAQRWVLEVGYIT 451
Cdd:cd00833   24 NLLEGRDAISEIPEDRWDADGYYPDPGKP---GKTYTRRGGFLDDVD--AFDAAFFGISPREAEAMDPQQRLLLEVAWEA 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591 452 LHHAGWTKQSLNKARIGTFSGDSGSEWNDLYWKQDEHVMFC----NHSCVTNTRIAHALGLTGPNVHADTACSASLVAAN 527
Cdd:cd00833   99 LEDAGYSPESLAGSRTGVFVGASSSDYLELLARDPDEIDAYaatgTSRAFLANRISYFFDLRGPSLTVDTACSSSLVALH 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591 528 VATHFLRTytegglkenpdqegceqqNQIDYALCAGILCMVSPAGWIGECASTMLSYRGRCFTYDSSADGFIRGEGsCHA 607
Cdd:cd00833  179 LACQSLRS------------------GECDLALVGGVNLILSPDMFVGFSKAGMLSPDGRCRPFDADADGYVRGEG-VGV 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591 608 FLERRHDDHVSVGSRSLAVLMGTAVNQDGKSASLTAPHGPSQQETIRMSLREAVLKPNDVLLTECHGTGTALGDPIEVGA 687
Cdd:cd00833  240 VVLKRLSDALRDGDRIYAVIRGSAVNQDGRTKGITAPSGEAQAALIRRAYARAGVDPSDIDYVEAHGTGTPLGDPIEVEA 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591 688 NRGVmFGKRERPFFHCT---AKAHVGHEEANAGTCGLLKIVLMLQNGMITPNPHLRALNPHLDTHAYPIYFVNELSTMQR 764
Cdd:cd00833  320 LAKV-FGGSRSADQPLLigsVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKIDFEESPLRVPTEARPWPA 398

                        410       420
                 ....*....|....*....|.
gi 712037591 765 ADD--IYGVSSFGFGGTNSRA 783
Cdd:cd00833  399 PAGprRAGVSSFGFGGTNAHV 419
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
 358-780 2.50e-96

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


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 328.76  E-value: 2.50e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591  358 RFPanceGCDMTAALF---MAGTDALIDPPYIRFDKEPYYMNDRDAPlyGKAYVFHGSFVaHDILiGFDHEFFGYTYEEA 434
Cdd:COG3321    14 RFP----GADDPEEFWrnlRAGRDAITEVPADRWDADAYYDPDPDAP--GKTYVRWGGFL-DDVD-EFDALFFGISPREA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591  435 EAIAPAQRWVLEVGYITLHHAGWTKQSLNKARIGTFSGDSGSEWNDL----YWKQDEHVMFCNHSCVTNTRIAHALGLTG 510
Cdd:COG3321    86 EAMDPQQRLLLEVAWEALEDAGYDPESLAGSRTGVFVGASSNDYALLlladPEAIDAYALTGNAKSVLAGRISYKLDLRG 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591  511 PNVHADTACSASLVAANVATHFLRTYtegglkenpdqegceqqnQIDYALCAGILCMVSPAGWIGECASTMLSYRGRCFT 590
Cdd:COG3321   166 PSVTVDTACSSSLVAVHLACQSLRSG------------------ECDLALAGGVNLMLTPESFILFSKGGMLSPDGRCRA 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591  591 YDSSADGFIRGEGsCHAFLERRHDDHVSVGSRSLAVLMGTAVNQDGKSASLTAPHGPSQQETIRMSLREAVLKPNDVLLT 670
Cdd:COG3321   228 FDADADGYVRGEG-VGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRSNGLTAPNGPAQAAVIRRALADAGVDPATVDYV 306

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591  671 ECHGTGTALGDPIEVGANRGVmFGKRERPFFHC---TAKAHVGHEEANAGTCGLLKIVLMLQNGMITPNPHLRALNPHLD 747
Cdd:COG3321   307 EAHGTGTPLGDPIEAAALTAA-FGQGRPADQPCaigSVKSNIGHLEAAAGVAGLIKAVLALRHGVLPPTLHFETPNPHID 385

                         410       420       430
                  ....*....|....*....|....*....|....*
gi 712037591  748 THAYPIYFVNELSTMQRADD--IYGVSSFGFGGTN 780
Cdd:COG3321   386 FENSPFYVNTELRPWPAGGGprRAGVSSFGFGGTN 420
PKS_KS smart00825
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ...
 421-780 2.62e-65

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: 220.28  E-value: 2.62e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591   421 GFDHEFFGYTYEEAEAIAPAQRWVLEVGYITLHHAGWTKQSLNKARIGTFSGDSGSEWndlywkqdehvmfcnhsCVTnt 500
Cdd:smart00825  32 LFDAAFFGISPREAEAMDPQQRLLLEVAWEALEDAGIDPESLRGSRTGVFVGVSSSDY-----------------SVT-- 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591   501 riahalgltgpnVhaDTACSASLVAANVATHFLRtytegglkenpdqegceqQNQIDYALCAGILCMVSPAGWIGECAST 580
Cdd:smart00825  93 ------------V--DTACSSSLVALHLACQSLR------------------SGECDMALAGGVNLILSPDTFVGLSRAG 140

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591   581 MLSYRGRCFTYDSSADGFIRGEGSCHAFLER-----RHDDHVsvgsrsLAVLMGTAVNQDGKSASLTAPHGPSQqetirm 655
Cdd:smart00825 141 MLSPDGRCKTFDASADGYVRGEGVGVVVLKRlsdalRDGDPI------LAVIRGSAVNQDGRSNGITAPSGPAQ------ 208

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591   656 slreavlkpndvllteChgtgtALGdpievganrgvmfgkrerpffhcTAKAHVGHEEANAGTCGLLKIVLMLQNGMITP 735
Cdd:smart00825 209 ----------------L-----LIG-----------------------SVKSNIGHLEAAAGVAGLIKVVLALKHGVIPP 244

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*..
gi 712037591   736 NPHLRALNPHLDTHAYPIYFVNELSTMQRADD--IYGVSSFGFGGTN 780
Cdd:smart00825 245 TLHFETPNPHIDLEESPLRVPTELTPWPPPGRprRAGVSSFGFGGTN 291
PKS_assoc TIGR04556
polyketide synthase-associated domain; This model describes a rare domain found as the ...
 100-328 1.54e-50

polyketide synthase-associated domain; This model describes a rare domain found as the N-terminal region of a number of dinoflagellate-specific proteins that resemble type I polyketide synthases.


Pssm-ID: 275349  Cd Length: 228  Bit Score: 177.18  E-value: 1.54e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591  100 EDGGFDTLWPAANDTSygVFGSTVIDCLATKGYCVVQMFGSKVLRETALEEAAETP---IYEGLRAEMEEAFLGKENNSR 176
Cdd:TIGR04556   1 DLDGFDIVLGPKSDPD--VVGEEIADCLATKGFCVMKLFVASEDLDSAVDVAKKLEdagQFFRLAVEFEEGYLGKEGSAK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591  177 VGLIEKDTPER---LLDNALAFCDRDITNLSMLLMQAGPDCFGFEIQSRTNAIARTPYPEGQVVTSPNFS-EDDMGEKFv 252
Cdd:TIGR04556  79 VAWLDPSSPDApdaVKDSPLKKMDANFSSIAQMLQPYSQESLGFEVYSRTNALLRLPLPDGDEEEYPPAEaDDGEAEKY- 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 712037591  253 eatIEFISRKKFCVMYLIENNGGLIEFYPKEHlgMGEKVELPIQKNRMVIFRSDLMNYSYKPQGTSVSIQAWLLDE 328
Cdd:TIGR04556 158 ---LHTMCRRKLTVLVFMGPTGGTLTLQPKEE--GGDSVEVPAEPGTVVLIRSDAYEYSYEPTGESLTLSSFLMQD 228
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
 348-614 6.45e-40

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: 147.78  E-value: 6.45e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591  348 NRVHVTAIHERFPaNCEGCDMTAALFMAGTDALIDPPYIRFDKEPYYMNDRDAPlyGKAYVFHGSFVAHDiliGFDHEFF 427
Cdd:pfam00109   1 EPVAIVGMGCRFP-GGNDPEEFWENLLEGRDGISEIPADRWDPDKLYDPPSRIA--GKIYTKWGGLDDIF---DFDPLFF 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591  428 GYTYEEAEAIAPAQRWVLEVGYITLHHAGWTKQSLNKARIGTFSGDSGSEWNDlYWKQDE---------HVMFCNHSCVT 498
Cdd:pfam00109  75 GISPREAERMDPQQRLLLEAAWEALEDAGITPDSLDGSRTGVFIGSGIGDYAA-LLLLDEdggprrgspFAVGTMPSVIA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591  499 NtRIAHALGLTGPNVHADTACSASLVAANVATHFLRtytegglkenpdqegceqQNQIDYALCAGILCMVSPAGWIGECA 578
Cdd:pfam00109 154 G-RISYFLGLRGPSVTVDTACSSSLVAIHAAVQSIR------------------SGEADVALAGGVNLLLTPLGFAGFSA 214

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 712037591  579 STMLSYRGRCFTYDSSADGFIRGEGSCHAFLERRHD 614
Cdd:pfam00109 215 AGMLSPDGPCKAFDPFADGFVRGEGVGAVVLKRLSD 250
omega_3_PfaA TIGR02813
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ...
 378-780 1.11e-29

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: 127.43  E-value: 1.11e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591   378 DALIDPPYIRFDKEPYYMNDRDAPlyGKAYVFHGSFVAHdilIGFDHEFFGYTYEEAEAIAPAQRWVLEV---------- 447
Cdd:TIGR02813   36 DAITDVPSDHWAKDDYYDSDKSEA--DKSYCKRGGFLPE---VDFNPMEFGLPPNILELTDISQLLSLVVakevlndagl 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591   448 --GY------ITLHHAGWTK--QSLNkARI------------GTFSGDSG---SEWNDLYWKQDEHVMFCNHSCVTNTRI 502
Cdd:TIGR02813  111 pdGYdrdkigITLGVGGGQKqsSSLN-ARLqypvlkkvfkasGVEDEDSEmliKKFQDQYIHWEENSFPGSLGNVISGRI 189

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591   503 AHALGLTGPNVHADTACSASLVAANVAthfLRTYTEGglkenpdqegceqqnQIDYALCAGILCMVSPAGWIGECASTML 582
Cdd:TIGR02813  190 ANRFDLGGMNCVVDAACAGSLAAIRMA---LSELLEG---------------RSEMMITGGVCTDNSPFMYMSFSKTPAF 251

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591   583 SYRGRCFTYDSSADGFIRGEGSCHAFLeRRHDDHVSVGSRSLAVLMGTAVNQDGKSASLTAPHGPSQQETIRMSLREAVL 662
Cdd:TIGR02813  252 TTNEDIQPFDIDSKGMMIGEGIGMMAL-KRLEDAERDGDRIYAVIKGVGASSDGKFKSIYAPRPEGQAKALKRAYDDAGF 330

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591   663 KPNDVLLTECHGTGTALGDPIEVGANRGVmFGKRERPFFHC---TAKAHVGHEEANAGTCGLLKIVLMLQNGMITPNPHL 739
Cdd:TIGR02813  331 APHTCGLIEAHGTGTAAGDVAEFGGLVSV-FSQDNDQKQHIalgSVKSQIGHTKSTAGTAGMIKAVLALHHKVLPPTINV 409

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*
gi 712037591   740 RALNPHLDTHAYPIYFVNELST-MQRADDI---YGVSSFGFGGTN 780
Cdd:TIGR02813  410 DQPNPKLDIENSPFYLNTETRPwMQREDGTprrAGISSFGFGGTN 454
PRK07103 PRK07103
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
 588-781 2.85e-19

polyketide beta-ketoacyl:acyl carrier protein synthase; Validated


Pssm-ID: 180839 [Multi-domain]  Cd Length: 410  Bit Score: 91.25  E-value: 2.85e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591 588 CFTYDSSADGFIRGEgSCHAFLERRHDDHVSVGSRSLAVLMGTAVNQDGKSasLTAPHGPSQQETIRMSLREAVLKPNDV 667
Cdd:PRK07103 225 CRPFDQDRDGFIYGE-ACGAVVLESAESARRRGARPYAKLLGWSMRLDANR--GPDPSLEGEMRVIRAALRRAGLGPEDI 301

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591 668 LLTECHGTGTALGDPIEVGANRGVMFGkreRPFFHCTaKAHVGHEEANAGTCGLLKIVLMLQNGMITPNPHL-RALNPHL 746
Cdd:PRK07103 302 DYVNPHGTGSPLGDETELAALFASGLA---HAWINAT-KSLTGHGLSAAGIVELIATLLQMRAGFLHPSRNLdEPIDERF 377

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 712037591 747 DthaypiyFVNElsTMQRADDIYGVS-SFGFGGTNS 781
Cdd:PRK07103 378 R-------WVGS--TAESARIRYALSlSFGFGGINT 404
 
Name Accession Description Interval E-value
PKS cd00833
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ...
 372-783 5.42e-113

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: 351.09  E-value: 5.42e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591 372 LFMAGTDALIDPPYIRFDKEPYYMNDRDAplyGKAYVFHGSFVAHDIliGFDHEFFGYTYEEAEAIAPAQRWVLEVGYIT 451
Cdd:cd00833   24 NLLEGRDAISEIPEDRWDADGYYPDPGKP---GKTYTRRGGFLDDVD--AFDAAFFGISPREAEAMDPQQRLLLEVAWEA 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591 452 LHHAGWTKQSLNKARIGTFSGDSGSEWNDLYWKQDEHVMFC----NHSCVTNTRIAHALGLTGPNVHADTACSASLVAAN 527
Cdd:cd00833   99 LEDAGYSPESLAGSRTGVFVGASSSDYLELLARDPDEIDAYaatgTSRAFLANRISYFFDLRGPSLTVDTACSSSLVALH 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591 528 VATHFLRTytegglkenpdqegceqqNQIDYALCAGILCMVSPAGWIGECASTMLSYRGRCFTYDSSADGFIRGEGsCHA 607
Cdd:cd00833  179 LACQSLRS------------------GECDLALVGGVNLILSPDMFVGFSKAGMLSPDGRCRPFDADADGYVRGEG-VGV 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591 608 FLERRHDDHVSVGSRSLAVLMGTAVNQDGKSASLTAPHGPSQQETIRMSLREAVLKPNDVLLTECHGTGTALGDPIEVGA 687
Cdd:cd00833  240 VVLKRLSDALRDGDRIYAVIRGSAVNQDGRTKGITAPSGEAQAALIRRAYARAGVDPSDIDYVEAHGTGTPLGDPIEVEA 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591 688 NRGVmFGKRERPFFHCT---AKAHVGHEEANAGTCGLLKIVLMLQNGMITPNPHLRALNPHLDTHAYPIYFVNELSTMQR 764
Cdd:cd00833  320 LAKV-FGGSRSADQPLLigsVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPKIDFEESPLRVPTEARPWPA 398

                        410       420
                 ....*....|....*....|.
gi 712037591 765 ADD--IYGVSSFGFGGTNSRA 783
Cdd:cd00833  399 PAGprRAGVSSFGFGGTNAHV 419
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
 358-780 2.50e-96

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


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 328.76  E-value: 2.50e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591  358 RFPanceGCDMTAALF---MAGTDALIDPPYIRFDKEPYYMNDRDAPlyGKAYVFHGSFVaHDILiGFDHEFFGYTYEEA 434
Cdd:COG3321    14 RFP----GADDPEEFWrnlRAGRDAITEVPADRWDADAYYDPDPDAP--GKTYVRWGGFL-DDVD-EFDALFFGISPREA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591  435 EAIAPAQRWVLEVGYITLHHAGWTKQSLNKARIGTFSGDSGSEWNDL----YWKQDEHVMFCNHSCVTNTRIAHALGLTG 510
Cdd:COG3321    86 EAMDPQQRLLLEVAWEALEDAGYDPESLAGSRTGVFVGASSNDYALLlladPEAIDAYALTGNAKSVLAGRISYKLDLRG 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591  511 PNVHADTACSASLVAANVATHFLRTYtegglkenpdqegceqqnQIDYALCAGILCMVSPAGWIGECASTMLSYRGRCFT 590
Cdd:COG3321   166 PSVTVDTACSSSLVAVHLACQSLRSG------------------ECDLALAGGVNLMLTPESFILFSKGGMLSPDGRCRA 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591  591 YDSSADGFIRGEGsCHAFLERRHDDHVSVGSRSLAVLMGTAVNQDGKSASLTAPHGPSQQETIRMSLREAVLKPNDVLLT 670
Cdd:COG3321   228 FDADADGYVRGEG-VGVVVLKRLSDALRDGDRIYAVIRGSAVNQDGRSNGLTAPNGPAQAAVIRRALADAGVDPATVDYV 306

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591  671 ECHGTGTALGDPIEVGANRGVmFGKRERPFFHC---TAKAHVGHEEANAGTCGLLKIVLMLQNGMITPNPHLRALNPHLD 747
Cdd:COG3321   307 EAHGTGTPLGDPIEAAALTAA-FGQGRPADQPCaigSVKSNIGHLEAAAGVAGLIKAVLALRHGVLPPTLHFETPNPHID 385

                         410       420       430
                  ....*....|....*....|....*....|....*
gi 712037591  748 THAYPIYFVNELSTMQRADD--IYGVSSFGFGGTN 780
Cdd:COG3321   386 FENSPFYVNTELRPWPAGGGprRAGVSSFGFGGTN 420
PKS_KS smart00825
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ...
 421-780 2.62e-65

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: 220.28  E-value: 2.62e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591   421 GFDHEFFGYTYEEAEAIAPAQRWVLEVGYITLHHAGWTKQSLNKARIGTFSGDSGSEWndlywkqdehvmfcnhsCVTnt 500
Cdd:smart00825  32 LFDAAFFGISPREAEAMDPQQRLLLEVAWEALEDAGIDPESLRGSRTGVFVGVSSSDY-----------------SVT-- 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591   501 riahalgltgpnVhaDTACSASLVAANVATHFLRtytegglkenpdqegceqQNQIDYALCAGILCMVSPAGWIGECAST 580
Cdd:smart00825  93 ------------V--DTACSSSLVALHLACQSLR------------------SGECDMALAGGVNLILSPDTFVGLSRAG 140

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591   581 MLSYRGRCFTYDSSADGFIRGEGSCHAFLER-----RHDDHVsvgsrsLAVLMGTAVNQDGKSASLTAPHGPSQqetirm 655
Cdd:smart00825 141 MLSPDGRCKTFDASADGYVRGEGVGVVVLKRlsdalRDGDPI------LAVIRGSAVNQDGRSNGITAPSGPAQ------ 208

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591   656 slreavlkpndvllteChgtgtALGdpievganrgvmfgkrerpffhcTAKAHVGHEEANAGTCGLLKIVLMLQNGMITP 735
Cdd:smart00825 209 ----------------L-----LIG-----------------------SVKSNIGHLEAAAGVAGLIKVVLALKHGVIPP 244

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*..
gi 712037591   736 NPHLRALNPHLDTHAYPIYFVNELSTMQRADD--IYGVSSFGFGGTN 780
Cdd:smart00825 245 TLHFETPNPHIDLEESPLRVPTELTPWPPPGRprRAGVSSFGFGGTN 291
PKS_assoc TIGR04556
polyketide synthase-associated domain; This model describes a rare domain found as the ...
 100-328 1.54e-50

polyketide synthase-associated domain; This model describes a rare domain found as the N-terminal region of a number of dinoflagellate-specific proteins that resemble type I polyketide synthases.


Pssm-ID: 275349  Cd Length: 228  Bit Score: 177.18  E-value: 1.54e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591  100 EDGGFDTLWPAANDTSygVFGSTVIDCLATKGYCVVQMFGSKVLRETALEEAAETP---IYEGLRAEMEEAFLGKENNSR 176
Cdd:TIGR04556   1 DLDGFDIVLGPKSDPD--VVGEEIADCLATKGFCVMKLFVASEDLDSAVDVAKKLEdagQFFRLAVEFEEGYLGKEGSAK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591  177 VGLIEKDTPER---LLDNALAFCDRDITNLSMLLMQAGPDCFGFEIQSRTNAIARTPYPEGQVVTSPNFS-EDDMGEKFv 252
Cdd:TIGR04556  79 VAWLDPSSPDApdaVKDSPLKKMDANFSSIAQMLQPYSQESLGFEVYSRTNALLRLPLPDGDEEEYPPAEaDDGEAEKY- 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 712037591  253 eatIEFISRKKFCVMYLIENNGGLIEFYPKEHlgMGEKVELPIQKNRMVIFRSDLMNYSYKPQGTSVSIQAWLLDE 328
Cdd:TIGR04556 158 ---LHTMCRRKLTVLVFMGPTGGTLTLQPKEE--GGDSVEVPAEPGTVVLIRSDAYEYSYEPTGESLTLSSFLMQD 228
ketoacyl-synt pfam00109
Beta-ketoacyl synthase, N-terminal domain; The structure of beta-ketoacyl synthase is similar ...
 348-614 6.45e-40

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: 147.78  E-value: 6.45e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591  348 NRVHVTAIHERFPaNCEGCDMTAALFMAGTDALIDPPYIRFDKEPYYMNDRDAPlyGKAYVFHGSFVAHDiliGFDHEFF 427
Cdd:pfam00109   1 EPVAIVGMGCRFP-GGNDPEEFWENLLEGRDGISEIPADRWDPDKLYDPPSRIA--GKIYTKWGGLDDIF---DFDPLFF 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591  428 GYTYEEAEAIAPAQRWVLEVGYITLHHAGWTKQSLNKARIGTFSGDSGSEWNDlYWKQDE---------HVMFCNHSCVT 498
Cdd:pfam00109  75 GISPREAERMDPQQRLLLEAAWEALEDAGITPDSLDGSRTGVFIGSGIGDYAA-LLLLDEdggprrgspFAVGTMPSVIA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591  499 NtRIAHALGLTGPNVHADTACSASLVAANVATHFLRtytegglkenpdqegceqQNQIDYALCAGILCMVSPAGWIGECA 578
Cdd:pfam00109 154 G-RISYFLGLRGPSVTVDTACSSSLVAIHAAVQSIR------------------SGEADVALAGGVNLLLTPLGFAGFSA 214

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 712037591  579 STMLSYRGRCFTYDSSADGFIRGEGSCHAFLERRHD 614
Cdd:pfam00109 215 AGMLSPDGPCKAFDPFADGFVRGEGVGAVVLKRLSD 250
Ketoacyl-synt_C pfam02801
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ...
 624-740 1.39e-33

Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar to that of the thiolase family (pfam00108) and also chalcone synthase. The active site of beta-ketoacyl synthase is located between the N and C-terminal domains.


Pssm-ID: 426989  Cd Length: 118  Bit Score: 124.99  E-value: 1.39e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591  624 LAVLMGTAVNQDGKSASLTAPHGPSQQETIRMSLREAVLKPNDVLLTECHGTGTALGDPIEVGANRGVM-FGKRERPFFH 702
Cdd:pfam02801   1 YAVIKGSAVNHDGRHNGLTAPNGEGQARAIRRALADAGVDPEDVDYVEAHGTGTPLGDPIEAEALKRVFgSGARKQPLAI 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 712037591  703 CTAKAHVGHEEANAGTCGLLKIVLMLQNGMITPNPHLR 740
Cdd:pfam02801  81 GSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTLNLE 118
decarbox_cond_enzymes cd00825
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ...
 440-781 3.22e-31

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: 125.06  E-value: 3.22e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591 440 AQRWVLEVGYITLHHAGWTKQSLNKAR----IGTFSGD--SGSEWNDLYWKQDEHVMFCNHSCVTNTRIAHALGLTGPNV 513
Cdd:cd00825   11 VSILGFEAAERAIADAGLSREYQKNPIvgvvVGTGGGSprFQVFGADAMRAVGPYVVTKAMFPGASGQIATPLGIHGPAY 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591 514 HADTACSASLVAANVATHFLrtytegglkenpdqegceQQNQIDYALCAGILCMVSPAGWIGECASTMLSYRGRCFTYDS 593
Cdd:cd00825   91 DVSAACAGSLHALSLAADAV------------------QNGKQDIVLAGGSEELAAPMDCEFDAMGALSTPEKASRTFDA 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591 594 SADGFIRGEGSCHAFLERRhDDHVSVGSRSLAVLMGTAVNQDGKSASLTAPHGPSQQETIRMSLREAVLKPNDVLLTECH 673
Cdd:cd00825  153 AADGFVFGDGAGALVVEEL-EHALARGAHIYAEIVGTAATIDGAGMGAFAPSAEGLARAAKEALAVAGLTVWDIDYLVAH 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591 674 GTGTALGDPIEVGANRGVmFGKRERPFFHctAKAHVGHEEANAGTCGLLKIVLMLQNGMITPNPHLRALNPHLDTHAypi 753
Cdd:cd00825  232 GTGTPIGDVKELKLLRSE-FGDKSPAVSA--TKAMTGNLSSAAVVLAVDEAVLMLEHGFIPPSIHIEELDEAGLNIV--- 305

                        330       340
                 ....*....|....*....|....*...
gi 712037591 754 yfvneLSTMQRADDIYGVSSFGFGGTNS 781
Cdd:cd00825  306 -----TETTPRELRTALLNGFGLGGTNA 328
KAS_I_II cd00834
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...
 452-781 2.18e-30

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: 124.57  E-value: 2.18e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591 452 LHHAGWTKQSLNKARIGTF--SGDSGSEWNDLYWKQ------DEHVMFCNHSCVTNT---RIAHALGLTGPNVHADTACS 520
Cdd:cd00834   83 LADAGLDPEELDPERIGVVigSGIGGLATIEEAYRAllekgpRRVSPFFVPMALPNMaagQVAIRLGLRGPNYTVSTACA 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591 521 ASLVAANVATHFLRtytegglkenpdqegceqQNQIDYALCAGILCMVSPAGWIGECASTMLSYRG-----RCFTYDSSA 595
Cdd:cd00834  163 SGAHAIGDAARLIR------------------LGRADVVIAGGAEALITPLTLAGFAALRALSTRNddpekASRPFDKDR 224

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591 596 DGFIRGEGSCHAFLERRhdDH-VSVGSRSLAVLMGTAVNQDGksASLTAPH--GPSQQETIRMSLREAVLKPNDVLLTEC 672
Cdd:cd00834  225 DGFVLGEGAGVLVLESL--EHaKARGAKIYAEILGYGASSDA--YHITAPDpdGEGAARAMRAALADAGLSPEDIDYINA 300

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591 673 HGTGTALGDPIEVGANRGVmFGKRERPfFHCTA-KAHVGHeeaNAGTCGLLKIV---LMLQNGMITPNPHLRALNPHLDT 748
Cdd:cd00834  301 HGTSTPLNDAAESKAIKRV-FGEHAKK-VPVSStKSMTGH---LLGAAGAVEAIatlLALRDGVLPPTINLEEPDPECDL 375

                        330       340       350
                 ....*....|....*....|....*....|....
gi 712037591 749 HaypiYFVNElstMQRADDIYGVS-SFGFGGTNS 781
Cdd:cd00834  376 D----YVPNE---AREAPIRYALSnSFGFGGHNA 402
omega_3_PfaA TIGR02813
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ...
 378-780 1.11e-29

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: 127.43  E-value: 1.11e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591   378 DALIDPPYIRFDKEPYYMNDRDAPlyGKAYVFHGSFVAHdilIGFDHEFFGYTYEEAEAIAPAQRWVLEV---------- 447
Cdd:TIGR02813   36 DAITDVPSDHWAKDDYYDSDKSEA--DKSYCKRGGFLPE---VDFNPMEFGLPPNILELTDISQLLSLVVakevlndagl 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591   448 --GY------ITLHHAGWTK--QSLNkARI------------GTFSGDSG---SEWNDLYWKQDEHVMFCNHSCVTNTRI 502
Cdd:TIGR02813  111 pdGYdrdkigITLGVGGGQKqsSSLN-ARLqypvlkkvfkasGVEDEDSEmliKKFQDQYIHWEENSFPGSLGNVISGRI 189

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591   503 AHALGLTGPNVHADTACSASLVAANVAthfLRTYTEGglkenpdqegceqqnQIDYALCAGILCMVSPAGWIGECASTML 582
Cdd:TIGR02813  190 ANRFDLGGMNCVVDAACAGSLAAIRMA---LSELLEG---------------RSEMMITGGVCTDNSPFMYMSFSKTPAF 251

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591   583 SYRGRCFTYDSSADGFIRGEGSCHAFLeRRHDDHVSVGSRSLAVLMGTAVNQDGKSASLTAPHGPSQQETIRMSLREAVL 662
Cdd:TIGR02813  252 TTNEDIQPFDIDSKGMMIGEGIGMMAL-KRLEDAERDGDRIYAVIKGVGASSDGKFKSIYAPRPEGQAKALKRAYDDAGF 330

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591   663 KPNDVLLTECHGTGTALGDPIEVGANRGVmFGKRERPFFHC---TAKAHVGHEEANAGTCGLLKIVLMLQNGMITPNPHL 739
Cdd:TIGR02813  331 APHTCGLIEAHGTGTAAGDVAEFGGLVSV-FSQDNDQKQHIalgSVKSQIGHTKSTAGTAGMIKAVLALHHKVLPPTINV 409

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*
gi 712037591   740 RALNPHLDTHAYPIYFVNELST-MQRADDI---YGVSSFGFGGTN 780
Cdd:TIGR02813  410 DQPNPKLDIENSPFYLNTETRPwMQREDGTprrAGISSFGFGGTN 454
FabB COG0304
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...
 452-781 2.27e-28

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: 118.66  E-value: 2.27e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591 452 LHHAGWTKQSLNKARIGTF--SGDSGSEWN----DLYWKQDEHVM--FCNHSCVTNT---RIAHALGLTGPNVHADTACS 520
Cdd:COG0304   83 LADAGLDLDEVDPDRTGVIigSGIGGLDTLeeayRALLEKGPRRVspFFVPMMMPNMaagHVSIRFGLKGPNYTVSTACA 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591 521 ASLVAANVATHFLRtytegglkenpdqegceqQNQIDYALCAGILCMVSPAGWIGECASTMLSYRGR-----CFTYDSSA 595
Cdd:COG0304  163 SGAHAIGEAYRLIR------------------RGRADVMIAGGAEAAITPLGLAGFDALGALSTRNDdpekaSRPFDKDR 224

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591 596 DGFIRGEGSCHAFLERRhdDH-VSVGSRSLAVLMGTAVNQDGKSASLTAPHGPSQQETIRMSLREAVLKPNDVLLTECHG 674
Cdd:COG0304  225 DGFVLGEGAGVLVLEEL--EHaKARGAKIYAEVVGYGASSDAYHITAPAPDGEGAARAMRAALKDAGLSPEDIDYINAHG 302

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591 675 TGTALGDPIEVGANRGVmFGKR-ERPFFHCTaKAHVGHEeanAGTCGLLKIV---LMLQNGMITPNPHLRALNPhldthA 750
Cdd:COG0304  303 TSTPLGDAAETKAIKRV-FGDHaYKVPVSST-KSMTGHL---LGAAGAIEAIasvLALRDGVIPPTINLENPDP-----E 372

                        330       340       350
                 ....*....|....*....|....*....|..
gi 712037591 751 YPIYFVNElsTMQRADDIYGVS-SFGFGGTNS 781
Cdd:COG0304  373 CDLDYVPN--EAREAKIDYALSnSFGFGGHNA 402
elong_cond_enzymes cd00828
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ...
 423-781 4.55e-24

"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: 105.60  E-value: 4.55e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591 423 DHEFFGYTYEEAEAIAPAQRWVLEVGYITLHHAGWTK-QSLNKARIGTFSGDSGSEWNDLY------WKQDEHV----MF 491
Cdd:cd00828   55 TGDIPGWDAKRTGIVDRTTLLALVATEEALADAGITDpYEVHPSEVGVVVGSGMGGLRFLRrggkldARAVNPYvspkWM 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591 492 CNHSCVTNTRIAHALGLTGPNVHADTACSASLVAANVATHFLRtytegglkenpdqegceqQNQIDYALCAG----ILCM 567
Cdd:cd00828  135 LSPNTVAGWVNILLLSSHGPIKTPVGACATALEALDLAVEAIR------------------SGKADIVVVGGvedpLEEG 196

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591 568 VSPAGWIGECASTMLSYRGRCFTYDSSADGFIRGEGSCHAFLERRhDDHVSVGSRSLAVLMGTAVNQDGKSASLTAPhGP 647
Cdd:cd00828  197 LSGFANMGALSTAEEEPEEMSRPFDETRDGFVEAEGAGVLVLERA-ELALARGAPIYGRVAGTASTTDGAGRSVPAG-GK 274

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591 648 SQQETIRMSLREAVLKPNDVLLTECHGTGTALGDPIEVGANRGVmFGKRERPFFHCTAKAHVGHEEANAGTCGLLKIVLM 727
Cdd:cd00828  275 GIARAIRTALAKAGLSLDDLDVISAHGTSTPANDVAESRAIAEV-AGALGAPLPVTAQKALFGHSKGAAGALQLIGALQS 353

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 712037591 728 LQNGMITPNPHLRALNPHLDTHAYPIyfvneLSTMQRADDIYG-VSSFGFGGTNS 781
Cdd:cd00828  354 LEHGLIPPTANLDDVDPDVEHLSVVG-----LSRDLNLKVRAAlVNAFGFGGSNA 403
PRK07103 PRK07103
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
 588-781 2.85e-19

polyketide beta-ketoacyl:acyl carrier protein synthase; Validated


Pssm-ID: 180839 [Multi-domain]  Cd Length: 410  Bit Score: 91.25  E-value: 2.85e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591 588 CFTYDSSADGFIRGEgSCHAFLERRHDDHVSVGSRSLAVLMGTAVNQDGKSasLTAPHGPSQQETIRMSLREAVLKPNDV 667
Cdd:PRK07103 225 CRPFDQDRDGFIYGE-ACGAVVLESAESARRRGARPYAKLLGWSMRLDANR--GPDPSLEGEMRVIRAALRRAGLGPEDI 301

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591 668 LLTECHGTGTALGDPIEVGANRGVMFGkreRPFFHCTaKAHVGHEEANAGTCGLLKIVLMLQNGMITPNPHL-RALNPHL 746
Cdd:PRK07103 302 DYVNPHGTGSPLGDETELAALFASGLA---HAWINAT-KSLTGHGLSAAGIVELIATLLQMRAGFLHPSRNLdEPIDERF 377

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 712037591 747 DthaypiyFVNElsTMQRADDIYGVS-SFGFGGTNS 781
Cdd:PRK07103 378 R-------WVGS--TAESARIRYALSlSFGFGGINT 404
PRK06333 PRK06333
beta-ketoacyl-ACP synthase;
502-781 1.14e-14

beta-ketoacyl-ACP synthase;


Pssm-ID: 235781 [Multi-domain]  Cd Length: 424  Bit Score: 76.96  E-value: 1.14e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591 502 IAHALGLTGPNVHADTACSASLVAANVATHFLRTytegglkenpdqegceqqNQIDYALCAGILCMVSPAGWIGECASTM 581
Cdd:PRK06333 156 VSIRYGFKGPLGAPVTACAAGVQAIGDAARLIRS------------------GEADVAVCGGTEAAIDRVSLAGFAAARA 217

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591 582 LSYR--------GRCFtyDSSADGFIRGEGSCHAFLERRhdDH-VSVGSRSLAVLMGTAVNQDGKSASLTAPHGPSQQET 652
Cdd:PRK06333 218 LSTRfndapeqaSRPF--DRDRDGFVMGEGAGILVIETL--EHaLARGAPPLAELVGYGTSADAYHMTAGPEDGEGARRA 293

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591 653 IRMSLREAVLKPNDVLLTECHGTGTALGDPIEVGANRGVmFGKRERPFFHCTaKAHVGHEEANAGtcGLLKI--VLMLQN 730
Cdd:PRK06333 294 MLIALRQAGIPPEEVQHLNAHATSTPVGDLGEVAAIKKV-FGHVSGLAVSST-KSATGHLLGAAG--GVEAIftILALRD 369

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 712037591 731 GMITPNPHLRalNPhlDTHAYPIYFVNelSTMQRADDIYGVS-SFGFGGTNS 781
Cdd:PRK06333 370 QIAPPTLNLE--NP--DPAAEGLDVVA--NKARPMDMDYALSnGFGFGGVNA 415
PRK07910 PRK07910
beta-ketoacyl-ACP synthase;
586-780 1.50e-13

beta-ketoacyl-ACP synthase;


Pssm-ID: 236129 [Multi-domain]  Cd Length: 418  Bit Score: 73.61  E-value: 1.50e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591 586 GRCFTYDSSADGFIRGEGSCHAFLERrhDDHVSV-GSRSLAVLMGTAVNQDGKSASLTAPHGPSQQETIRMSLREAVLKP 664
Cdd:PRK07910 226 GACRPFDKDRDGFVFGEGGALMVIET--EEHAKArGANILARIMGASITSDGFHMVAPDPNGERAGHAMTRAIELAGLTP 303

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591 665 NDVLLTECHGTGTALGDPIEVGANRGVMFGKRERPFfhcTAKAHVGHEEANAGTCGLLKIVLMLQNGMITPNPHLRALNP 744
Cdd:PRK07910 304 GDIDHVNAHATGTSVGDVAEGKAINNALGGHRPAVY---APKSALGHSVGAVGAVESILTVLALRDGVIPPTLNLENLDP 380

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 712037591 745 HLDthaypiyfVNELSTMQRADDI-YGVS-SFGFGGTN 780
Cdd:PRK07910 381 EID--------LDVVAGEPRPGNYrYAINnSFGFGGHN 410
PTZ00050 PTZ00050
3-oxoacyl-acyl carrier protein synthase; Provisional
 499-781 2.17e-13

3-oxoacyl-acyl carrier protein synthase; Provisional


Pssm-ID: 240245 [Multi-domain]  Cd Length: 421  Bit Score: 73.19  E-value: 2.17e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591 499 NTRIAHalGLTGPNVHADTACSASLVAANVATHFLrtytegglkenpdqegceQQNQIDYALCAGILCMVSPAGWIGECA 578
Cdd:PTZ00050 150 LVAIKH--KLKGPSGSAVTACATGAHCIGEAFRWI------------------KYGEADIMICGGTEASITPVSFAGFSR 209

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591 579 STMLS--YRGR----CFTYDSSADGFIRGEGSCHAFLErrHDDH-VSVGSRSLAVLMGTAVNQDGKSasLTAPH--GPSQ 649
Cdd:PTZ00050 210 MRALCtkYNDDpqraSRPFDKDRAGFVMGEGAGILVLE--ELEHaLRRGAKIYAEIRGYGSSSDAHH--ITAPHpdGRGA 285

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591 650 QETIRMSLREAVLKP-NDVLLTECHGTGTALGDPIEVGANRGVMFGKRERPFFHCTAKAHVGHEEANAGTCGLLKIVLML 728
Cdd:PTZ00050 286 RRCMENALKDGANINiNDVDYVNAHATSTPIGDKIELKAIKKVFGDSGAPKLYVSSTKGGLGHLLGAAGAVESIVTILSL 365

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 712037591 729 QNGMITPNPHLRALNPHLDTHaypiYFVNELSTMQRADDIYGVSSFGFGGTNS 781
Cdd:PTZ00050 366 YEQIIPPTINLENPDAECDLN----LVQGKTAHPLQSIDAVLSTSFGFGGVNT 414
PRK08439 PRK08439
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
 507-780 1.20e-12

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


Pssm-ID: 236265 [Multi-domain]  Cd Length: 406  Bit Score: 70.53  E-value: 1.20e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591 507 GLTGPNVHADTACSASLVAANVAThflRTYTEGGlkenpdqegceqqnqIDYALCAGILCMVSPAGWIGECASTMLSYR- 585
Cdd:PRK08439 150 GLKGPNLSSVTACAAGTHAIIEAV---KTIMLGG---------------ADKMLVVGAESAICPVGIGGFAAMKALSTRn 211

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591 586 ------GRCFtyDSSADGFIRGEGSCHAFLErRHDDHVSVGSRSLAVLMGTAVNQDGKSASLTAPHGPSQqeTIRMSLRE 659
Cdd:PRK08439 212 ddpkkaSRPF--DKDRDGFVMGEGAGALVLE-EYESAKKRGAKIYAEIIGFGESGDANHITSPAPEGPLR--AMKAALEM 286

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591 660 AVLKPNDVLltECHGTGTALGDPIEVGANRGVMFGKRERPFFHCTaKAHVGHEEANAGTCGLLKIVLMLQNGMITPNPHL 739
Cdd:PRK08439 287 AGNPKIDYI--NAHGTSTPYNDKNETAALKELFGSKEKVPPVSST-KGQIGHCLGAAGAIEAVISIMAMRDGILPPTINQ 363

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 712037591 740 RALNPHLDTHAYPiyfvnelSTMQRADDIYGVS-SFGFGGTN 780
Cdd:PRK08439 364 ETPDPECDLDYIP-------NVARKAELNVVMSnSFGFGGTN 398
PRK09185 PRK09185
beta-ketoacyl-ACP synthase;
502-780 4.69e-12

beta-ketoacyl-ACP synthase;


Pssm-ID: 236398 [Multi-domain]  Cd Length: 392  Bit Score: 68.72  E-value: 4.69e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591 502 IAHALGLTGPNVHADTACSASLVAANVATHFLRTytegGLkenpdqegceqqnqIDYALCAGI--LCMVSPAGWigecAS 579
Cdd:PRK09185 143 LRAYLGLSGPAYTISTACSSSAKVFASARRLLEA----GL--------------CDAAIVGGVdsLCRLTLNGF----NS 200

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591 580 TMLSYRGRCFTYDSSADGFIRGEGSCHAFLERRHDDHVsvgsrslaVLMGTAVNQDGKSASltAPH--GPSQQETIRMSL 657
Cdd:PRK09185 201 LESLSPQPCRPFSANRDGINIGEAAAFFLLEREDDAAV--------ALLGVGESSDAHHMS--APHpeGLGAILAMQQAL 270

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591 658 REAVLKPNDVLLTECHGTGTALGDPIEVGANRGVmFGKRerpfFHCTA-KAHVGHEEANAGTCGLLKIVLMLQNGMITPN 736
Cdd:PRK09185 271 ADAGLAPADIGYINLHGTATPLNDAMESRAVAAV-FGDG----VPCSStKGLTGHTLGAAGAVEAAICWLALRHGLPPHG 345

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 712037591 737 PHLRALNPHLDthayPIYFVNELSTMQRAddiYGVS-SFGFGGTN 780
Cdd:PRK09185 346 WNTGQPDPALP----PLYLVENAQALAIR---YVLSnSFAFGGNN 383
PRK07967 PRK07967
beta-ketoacyl-ACP synthase I;
590-781 1.19e-11

beta-ketoacyl-ACP synthase I;


Pssm-ID: 181184 [Multi-domain]  Cd Length: 406  Bit Score: 67.39  E-value: 1.19e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591 590 TYDSSADGF-IRGEGSCHAFLERRHddHVSVGSRSLAVLMGTAVNQDGksASLTAPHGPSQQETIRMSLrEAVLKPNDVL 668
Cdd:PRK07967 220 AYDANRDGFvIAGGGGVVVVEELEH--ALARGAKIYAEIVGYGATSDG--YDMVAPSGEGAVRCMQMAL-ATVDTPIDYI 294

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591 669 LTecHGTGTALGDPIEVGANRGVmFGKReRPFFHCTaKAHVGHEEANAGTCGLLKIVLMLQNGMITPNPHLRALNPHLDt 748
Cdd:PRK07967 295 NT--HGTSTPVGDVKELGAIREV-FGDK-SPAISAT-KSLTGHSLGAAGVQEAIYSLLMMEHGFIAPSANIEELDPQAA- 368

                        170       180       190
                 ....*....|....*....|....*....|....
gi 712037591 749 hAYPIyfVNElsTMQRAD-DIYGVSSFGFGGTNS 781
Cdd:PRK07967 369 -GMPI--VTE--TTDNAElTTVMSNSFGFGGTNA 397
PRK14691 PRK14691
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
 510-781 1.56e-11

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


Pssm-ID: 173154 [Multi-domain]  Cd Length: 342  Bit Score: 66.68  E-value: 1.56e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591 510 GPNVHADTACSASLVAANVATHFLRtytegglkenpdqegceqQNQIDYALCAGILCMVSPAGWIGECASTMLSY----- 584
Cdd:PRK14691  82 GPIGAPVTACAAGVQAIGDAVRMIR------------------NNEADVALCGGAEAVIDTVSLAGFAAARALSThfnst 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591 585 -RGRCFTYDSSADGFIRGEGSCHAFLERRhDDHVSVGSRSLAVLMGTAVNQDGKSASLTAPHGPSQQETIRMSLREAVLK 663
Cdd:PRK14691 144 pEKASRPFDTARDGFVMGEGAGLLIIEEL-EHALARGAKPLAEIVGYGTSADAYHMTSGAEDGDGAYRAMKIALRQAGIT 222

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591 664 PNDVLLTECHGTGTALGDPIEVGANRGvMFGKRERPFFHCTaKAHVGHEEANAGTCGLLKIVLMLQNGMITPNPHLRalN 743
Cdd:PRK14691 223 PEQVQHLNAHATSTPVGDLGEINAIKH-LFGESNALAITST-KSATGHLLGAAGGLETIFTVLALRDQIVPATLNLE--N 298

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 712037591 744 PHLDTHAYPIYFVNElstmQRADDIYGVSS-FGFGGTNS 781
Cdd:PRK14691 299 PDPAAKGLNIIAGNA----QPHDMTYALSNgFGFAGVNA 333
PLN02836 PLN02836
3-oxoacyl-[acyl-carrier-protein] synthase
 507-781 6.25e-11

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


Pssm-ID: 215449 [Multi-domain]  Cd Length: 437  Bit Score: 65.58  E-value: 6.25e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591 507 GLTGPNVHADTACSASLVAANVATHFLrtytegglkenpdqegceQQNQIDYALCAGILCMVSPAGWIGECASTMLSYR- 585
Cdd:PLN02836 172 GFQGPNHAAVTACATGAHSIGDAFRMI------------------QFGDADVMVAGGTESSIDALSIAGFSRSRALSTKf 233

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591 586 -------GRCFtyDSSADGFIRGEGSCHAFLERRhdDHVSV-GSRSLAVLMGTAVNQDGKSasLTAPH--GPSQQETIRM 655
Cdd:PLN02836 234 nscpteaSRPF--DCDRDGFVIGEGAGVLVLEEL--EHAKRrGAKIYAEVRGYGMSGDAHH--ITQPHedGRGAVLAMTR 307

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591 656 SLREAVLKPNDVLLTECHGTGTALGDPIEVGANRGVMFGkrerpffHCTA--------KAHVGHEEANAGTCGLLKIVLM 727
Cdd:PLN02836 308 ALQQSGLHPNQVDYVNAHATSTPLGDAVEARAIKTVFSE-------HATSgglafsstKGATGHLLGAAGAVEAIFSVLA 380

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 712037591 728 LQNGMITPNPHLRALNPHLDTHAYPIyfvnelsTMQRADDIYGV--SSFGFGGTNS 781
Cdd:PLN02836 381 IHHGIAPPTLNLERPDPIFDDGFVPL-------TASKAMLIRAAlsNSFGFGGTNA 429
PRK07314 PRK07314
beta-ketoacyl-ACP synthase II;
506-780 7.88e-11

beta-ketoacyl-ACP synthase II;


Pssm-ID: 235987 [Multi-domain]  Cd Length: 411  Bit Score: 64.81  E-value: 7.88e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591 506 LGLTGPNVHADTACSASLVAANVATHFLrtytegglkenpdqegceQQNQIDYALCAGILCMVSPAGWIGECASTMLSYR 585
Cdd:PRK07314 149 YGAKGPNHSIVTACATGAHAIGDAARLI------------------AYGDADVMVAGGAEAAITPLGIAGFAAARALSTR 210

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591 586 -----GRCFTYDSSADGFIRGEGSC--------HAfLERrhddhvsvGSRSLAVLMGTAVNQDgkSASLTAPH--GPSQQ 650
Cdd:PRK07314 211 nddpeRASRPFDKDRDGFVMGEGAGilvleeleHA-KAR--------GAKIYAEVVGYGMTGD--AYHMTAPApdGEGAA 279

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591 651 ETIRMSLREAVLKPNDVLLTECHGTGTALGDPIEVGANRGVmFGKrerpffHC------TAKAHVGHEEANAGtcGLLKI 724
Cdd:PRK07314 280 RAMKLALKDAGINPEDIDYINAHGTSTPAGDKAETQAIKRV-FGE------HAykvavsSTKSMTGHLLGAAG--AVEAI 350

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 712037591 725 --VLMLQNGMITPNPHLRALNPHLDthaypIYFV-NElstmQRADDI-YGVS-SFGFGGTN 780
Cdd:PRK07314 351 fsVLAIRDQVIPPTINLDNPDEECD-----LDYVpNE----ARERKIdYALSnSFGFGGTN 402
PRK09116 PRK09116
beta-ketoacyl-ACP synthase;
591-780 1.30e-10

beta-ketoacyl-ACP synthase;


Pssm-ID: 181657 [Multi-domain]  Cd Length: 405  Bit Score: 64.24  E-value: 1.30e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591 591 YDSSADGFIRGEGSCHAFLERRhdDH-VSVGSRSLAVLMGTAVNQDGksASLTAPHGPSQQETIRMSLREAVLKPNDVLL 669
Cdd:PRK09116 222 FDANRDGLVIGEGAGTLVLEEL--EHaKARGATIYAEIVGFGTNSDG--AHVTQPQAETMQIAMELALKDAGLAPEDIGY 297

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591 670 TECHGTGTALGDPIEVGANRGVmFGKReRPFfhCTAKAHVGHeeaNAGTCGLLKIVL---MLQNGMITPNPHLRALNPH- 745
Cdd:PRK09116 298 VNAHGTATDRGDIAESQATAAV-FGAR-MPI--SSLKSYFGH---TLGACGALEAWMsieMMNEGWFAPTLNLTQVDPAc 370

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 712037591 746 --LDthaypiYFVNELSTMQRadDIYGVSSFGFGGTN 780
Cdd:PRK09116 371 gaLD------YIMGEAREIDT--EYVMSNNFAFGGIN 399
PRK08722 PRK08722
beta-ketoacyl-ACP synthase II;
507-780 3.09e-10

beta-ketoacyl-ACP synthase II;


Pssm-ID: 181539 [Multi-domain]  Cd Length: 414  Bit Score: 63.10  E-value: 3.09e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591 507 GLTGPNVHADTACSASLvaANVAtHFLRTYTEGglkenpdqegceqqnQIDYALCAGILCMVSPAGWIGECASTMLSYRG 586
Cdd:PRK08722 152 GLRGPNIAISTACTTGL--HNIG-HAARMIAYG---------------DADAMVAGGAEKASTPLGMAGFGAAKALSTRN 213

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591 587 R-----CFTYDSSADGFIRGEGSCHAFLErRHDDHVSVGSRSLAVLMGTAVNQDGKSASLTAPHGPSQQETIRMSLREAV 661
Cdd:PRK08722 214 DepqkaSRPWDKDRDGFVLGDGAGMMVLE-EYEHAKARGAKIYAELVGFGMSGDAYHMTSPSEDGSGGALAMEAAMRDAG 292

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591 662 LKPNDVLLTECHGTGTALGDPIEVGANRGVMFGKRERPFFHCTAKAHVGHEEANAGTCGLLKIVLMLQNGMITPNPHLRA 741
Cdd:PRK08722 293 VTGEQIGYVNAHGTSTPAGDVAEIKGIKRALGEAGSKQVLVSSTKSMTGHLLGAAGSVEAIITVMSLVDQIVPPTINLDD 372

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 712037591 742 LNPHLDTHAYPiYFVNELSTMQRAddiyGVSSFGFGGTN 780
Cdd:PRK08722 373 PEEGLDIDLVP-HTARKVESMEYA----ICNSFGFGGTN 406
PLN02787 PLN02787
3-oxoacyl-[acyl-carrier-protein] synthase II
 443-781 1.70e-09

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


Pssm-ID: 215421 [Multi-domain]  Cd Length: 540  Bit Score: 61.15  E-value: 1.70e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591 443 WVLEVGYITLHHAGWTKQ---SLNKARIGTFSGDS--GSE-WNDL-------YWKQDEhvmFCNHSCVTN---TRIAHAL 506
Cdd:PLN02787 202 YLLTAGKKALADGGITEDvmkELDKTKCGVLIGSAmgGMKvFNDAiealrisYRKMNP---FCVPFATTNmgsAMLAMDL 278

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591 507 GLTGPNVHADTACSAS-LVAANVATHFLRtytegglkenpdqegceqqNQIDYALCAGILCMVSPAGWIGECASTMLSYR 585
Cdd:PLN02787 279 GWMGPNYSISTACATSnFCILNAANHIIR-------------------GEADVMLCGGSDAAIIPIGLGGFVACRALSQR 339

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591 586 GRCFT-----YDSSADGFIRGEGSCHAFLERRhdDHVSV-GSRSLAVLMGTAVNQDGKSASLTAPHGPSQQETIRMSLRE 659
Cdd:PLN02787 340 NDDPTkasrpWDMNRDGFVMGEGAGVLLLEEL--EHAKKrGANIYAEFLGGSFTCDAYHMTEPHPEGAGVILCIEKALAQ 417

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591 660 AVLKPNDVLLTECHGTGTALGDPIEVGAnrgVM--FGKRERPFFHCTaKAHVGHEEANAGTCGLLKIVLMLQNGMITPNP 737
Cdd:PLN02787 418 SGVSKEDVNYINAHATSTKAGDLKEYQA---LMrcFGQNPELRVNST-KSMIGHLLGAAGAVEAIATVQAIRTGWVHPNI 493

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 712037591 738 HLRALNPHLDTHaypiyfVNELSTMQRADDIYGVS-SFGFGGTNS 781
Cdd:PLN02787 494 NLENPESGVDTK------VLVGPKKERLDIKVALSnSFGFGGHNS 532
CLF cd00832
Chain-length factor (CLF) is a factor required for polyketide chain initiation of aromatic ...
 559-747 4.98e-07

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: 52.75  E-value: 4.98e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591 559 ALCAGILCMVSPAGWIGECASTMLS--------YRgrcfTYDSSADGFIRGEGSCHAFLErRHDDHVSVGSRSLAVLMGT 630
Cdd:cd00832  182 VVSGGVDSALCPWGWVAQLSSGRLStsddparaYL----PFDAAAAGYVPGEGGAILVLE-DAAAARERGARVYGEIAGY 256

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591 631 AVNQDGKSASltaPHGPSQQETIRMSLREAVLKPNDVLLTECHGTGTALGDPIEVGANRGVmFGKRERPffhCTA-KAHV 709
Cdd:cd00832  257 AATFDPPPGS---GRPPGLARAIRLALADAGLTPEDVDVVFADAAGVPELDRAEAAALAAV-FGPRGVP---VTApKTMT 329

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 712037591 710 GHEEANAGTCGLLKIVLMLQNGMITPNPHLRALNPHLD 747
Cdd:cd00832  330 GRLYAGGAPLDVATALLALRDGVIPPTVNVTDVPPAYG 367
PRK06501 PRK06501
beta-ketoacyl-ACP synthase;
501-781 1.99e-06

beta-ketoacyl-ACP synthase;


Pssm-ID: 235817 [Multi-domain]  Cd Length: 425  Bit Score: 51.17  E-value: 1.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591 501 RIAHALGLTGPNVHADTACSASLVAAnvathflrtytegglkenpdQEGCE--QQNQIDYALCAGILCMVSPAGWIGECA 578
Cdd:PRK06501 157 RLADRFGTRGLPISLSTACASGATAI--------------------QLGVEaiRRGETDRALCIATDGSVSAEALIRFSL 216

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591 579 STMLSYR-------GRCFTYDSsaDGFIRGEGSCHAFLERrHDDHVSVGSRSLAVLMGTAVNQDGKSASLTAPHGPSQQE 651
Cdd:PRK06501 217 LSALSTQndppekaSKPFSKDR--DGFVMAEGAGALVLES-LESAVARGAKILGIVAGCGEKADSFHRTRSSPDGSPAIG 293

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 712037591 652 TIRMSLREAVLKPNDVLLTECHGTGTALGDPIEVGANRGVmFGKRERPFFHCTAKAHVGHEEANAGTCGLLKIVLMLQNG 731
Cdd:PRK06501 294 AIRAALADAGLTPEQIDYINAHGTSTPENDKMEYLGLSAV-FGERLASIPVSSNKSMIGHTLTAAGAVEAVFSLLTIQTG 372

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 712037591 732 MITPnphlrALNPHLDTHAYPIYFVNELSTMQRADDIYGvSSFGFGGTNS 781
Cdd:PRK06501 373 RLPP-----TINYDNPDPAIPLDVVPNVARDARVTAVLS-NSFGFGGQNA 416
KAsynt_C_assoc pfam16197
Ketoacyl-synthetase C-terminal extension; KAsynt_C_assoc represents the very C-terminus of a ...
 735-781 5.74e-03

Ketoacyl-synthetase C-terminal extension; KAsynt_C_assoc represents the very C-terminus of a subset of proteins from the keto-acyl-synthetase 2 family. It is found in proteins ranging from bacteria to human.


Pssm-ID: 465059 [Multi-domain]  Cd Length: 111  Bit Score: 37.14  E-value: 5.74e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 712037591  735 PNPHLRALnphLDThayPIYFVNElsTMQRADDIYGVSSFGFGGTNS 781
Cdd:pfam16197   1 PNPDIPAL---LDG---RLKVVTE--PTPWPGGIVGVNSFGFGGANA 39
 
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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