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Conserved domains on  [gi|512154917|gb|EPD97364|]
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hypothetical protein HMPREF1486_00004, partial [Streptomyces sp. HPH0547]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PksD super family cl43841
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
 1-177 7.91e-73

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


The actual alignment was detected with superfamily member COG3321:

Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 237.85  E-value: 7.91e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512154917    1 DLLEAHGTGTRLGDPIEAQALINTYGTAHTPDRPLHLGSLKSNIGHTQAAAGVAGVIKAVQAIRHRTMPASLYADNPTAE 80
Cdd:COG3321   304 DYVEAHGTGTPLGDPIEAAALTAAFGQGRPADQPCAIGSVKSNIGHLEAAAGVAGLIKAVLALRHGVLPPTLHFETPNPH 383

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512154917   81 VDWSAGTVRLLAQARPWEAAAYPRRAGVSSFGMSGTNAHLIVEEYRPDPERGEPPAEAPawsdvaVPLVLSAKSPQALRE 160
Cdd:COG3321   384 IDFENSPFYVNTELRPWPAGGGPRRAGVSSFGFGGTNAHVVLEEAPAAAPAAAAAARPP------QLLVLSAKTEEALRA 457

                         170
                  ....*....|....*..
gi 512154917  161 QASALSRHLRDHPEEPL 177
Cdd:COG3321   458 LAARLAAFLEAHPDLDL 474
 
Name Accession Description Interval E-value
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
 1-177 7.91e-73

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


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 237.85  E-value: 7.91e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512154917    1 DLLEAHGTGTRLGDPIEAQALINTYGTAHTPDRPLHLGSLKSNIGHTQAAAGVAGVIKAVQAIRHRTMPASLYADNPTAE 80
Cdd:COG3321   304 DYVEAHGTGTPLGDPIEAAALTAAFGQGRPADQPCAIGSVKSNIGHLEAAAGVAGLIKAVLALRHGVLPPTLHFETPNPH 383

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512154917   81 VDWSAGTVRLLAQARPWEAAAYPRRAGVSSFGMSGTNAHLIVEEYRPDPERGEPPAEAPawsdvaVPLVLSAKSPQALRE 160
Cdd:COG3321   384 IDFENSPFYVNTELRPWPAGGGPRRAGVSSFGFGGTNAHVVLEEAPAAAPAAAAAARPP------QLLVLSAKTEEALRA 457

                         170
                  ....*....|....*..
gi 512154917  161 QASALSRHLRDHPEEPL 177
Cdd:COG3321   458 LAARLAAFLEAHPDLDL 474
PKS cd00833
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ...
 1-122 1.97e-56

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: 182.76  E-value: 1.97e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512154917   1 DLLEAHGTGTRLGDPIEAQALINTYGTAHTPDRPLHLGSLKSNIGHTQAAAGVAGVIKAVQAIRHRTMPASLYADNPTAE 80
Cdd:cd00833  300 DYVEAHGTGTPLGDPIEVEALAKVFGGSRSADQPLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPK 379

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 512154917  81 VDWSAGTVRLLAQARPWEAAAYPRRAGVSSFGMSGTNAHLIV 122
Cdd:cd00833  380 IDFEESPLRVPTEARPWPAPAGPRRAGVSSFGFGGTNAHVIL 421
PKS_KS smart00825
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ...
 11-124 4.83e-48

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: 157.88  E-value: 4.83e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512154917    11 RLGDPIEAqaLINtyGTA----------HTPDRP--LHLGSLKSNIGHTQAAAGVAGVIKAVQAIRHRTMPASLYADNPT 78
Cdd:smart00825 177 RDGDPILA--VIR--GSAvnqdgrsngiTAPSGPaqLLIGSVKSNIGHLEAAAGVAGLIKVVLALKHGVIPPTLHFETPN 252

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 512154917    79 AEVDWSAGTVRLLAQARPWEAAAYPRRAGVSSFGMSGTNAHLIVEE 124
Cdd:smart00825 253 PHIDLEESPLRVPTELTPWPPPGRPRRAGVSSFGFGGTNAHVILEE 298
omega_3_PfaA TIGR02813
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ...
 2-158 1.05e-35

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: 131.67  E-value: 1.05e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512154917     2 LLEAHGTGTRLGDPIEAQALINTYGTAHTPDRPLHLGSLKSNIGHTQAAAGVAGVIKAVQAIRHRTMPASLYADNPTAEV 81
Cdd:TIGR02813  337 LIEAHGTGTAAGDVAEFGGLVSVFSQDNDQKQHIALGSVKSQIGHTKSTAGTAGMIKAVLALHHKVLPPTINVDQPNPKL 416

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 512154917    82 DWSAGTVRLLAQARPWEAAA--YPRRAGVSSFGMSGTNAHLIVEEYRPDPERGeppaEAPAWSDVAVPLVLSAKSPQAL 158
Cdd:TIGR02813  417 DIENSPFYLNTETRPWMQREdgTPRRAGISSFGFGGTNFHMVLEEYSPKHQRD----DQYRQRAVAQTLLFTAANEKAL 491
Ketoacyl-synt_C pfam02801
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ...
 1-72 8.93e-29

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: 103.03  E-value: 8.93e-29
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 512154917    1 DLLEAHGTGTRLGDPIEAQALINTYGtAHTPDRPLHLGSLKSNIGHTQAAAGVAGVIKAVQAIRHRTMPASL 72
Cdd:pfam02801  45 DYVEAHGTGTPLGDPIEAEALKRVFG-SGARKQPLAIGSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTL 115
PTZ00050 PTZ00050
3-oxoacyl-acyl carrier protein synthase; Provisional
 1-125 8.04e-13

3-oxoacyl-acyl carrier protein synthase; Provisional


Pssm-ID: 240245 [Multi-domain]  Cd Length: 421  Bit Score: 65.48  E-value: 8.04e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512154917   1 DLLEAHGTGTRLGDPIEAQALINTYGtaHTPDRPLHLGSLKSNIGHTQAAAGVAGVIKAVQAIRHRTMPASLYADNPTAE 80
Cdd:PTZ00050 305 DYVNAHATSTPIGDKIELKAIKKVFG--DSGAPKLYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINLENPDAE 382

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 512154917  81 VDwsagtvrLLAQARPWEAAAYPRRAGVS-SFGMSGTNAHLIVEEY 125
Cdd:PTZ00050 383 CD-------LNLVQGKTAHPLQSIDAVLStSFGFGGVNTALLFTKY 421
 
Name Accession Description Interval E-value
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
 1-177 7.91e-73

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


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 237.85  E-value: 7.91e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512154917    1 DLLEAHGTGTRLGDPIEAQALINTYGTAHTPDRPLHLGSLKSNIGHTQAAAGVAGVIKAVQAIRHRTMPASLYADNPTAE 80
Cdd:COG3321   304 DYVEAHGTGTPLGDPIEAAALTAAFGQGRPADQPCAIGSVKSNIGHLEAAAGVAGLIKAVLALRHGVLPPTLHFETPNPH 383

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512154917   81 VDWSAGTVRLLAQARPWEAAAYPRRAGVSSFGMSGTNAHLIVEEYRPDPERGEPPAEAPawsdvaVPLVLSAKSPQALRE 160
Cdd:COG3321   384 IDFENSPFYVNTELRPWPAGGGPRRAGVSSFGFGGTNAHVVLEEAPAAAPAAAAAARPP------QLLVLSAKTEEALRA 457

                         170
                  ....*....|....*..
gi 512154917  161 QASALSRHLRDHPEEPL 177
Cdd:COG3321   458 LAARLAAFLEAHPDLDL 474
PKS cd00833
polyketide synthases (PKSs) polymerize simple fatty acids into a large variety of different ...
 1-122 1.97e-56

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: 182.76  E-value: 1.97e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512154917   1 DLLEAHGTGTRLGDPIEAQALINTYGTAHTPDRPLHLGSLKSNIGHTQAAAGVAGVIKAVQAIRHRTMPASLYADNPTAE 80
Cdd:cd00833  300 DYVEAHGTGTPLGDPIEVEALAKVFGGSRSADQPLLIGSVKSNIGHLEAAAGLAGLIKVVLALEHGVIPPNLHFETPNPK 379

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 512154917  81 VDWSAGTVRLLAQARPWEAAAYPRRAGVSSFGMSGTNAHLIV 122
Cdd:cd00833  380 IDFEESPLRVPTEARPWPAPAGPRRAGVSSFGFGGTNAHVIL 421
PKS_KS smart00825
Beta-ketoacyl synthase; The structure of beta-ketoacyl synthase is similar to that of the ...
 11-124 4.83e-48

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: 157.88  E-value: 4.83e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512154917    11 RLGDPIEAqaLINtyGTA----------HTPDRP--LHLGSLKSNIGHTQAAAGVAGVIKAVQAIRHRTMPASLYADNPT 78
Cdd:smart00825 177 RDGDPILA--VIR--GSAvnqdgrsngiTAPSGPaqLLIGSVKSNIGHLEAAAGVAGLIKVVLALKHGVIPPTLHFETPN 252

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 512154917    79 AEVDWSAGTVRLLAQARPWEAAAYPRRAGVSSFGMSGTNAHLIVEE 124
Cdd:smart00825 253 PHIDLEESPLRVPTELTPWPPPGRPRRAGVSSFGFGGTNAHVILEE 298
omega_3_PfaA TIGR02813
polyketide-type polyunsaturated fatty acid synthase PfaA; Members of the seed for this ...
 2-158 1.05e-35

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: 131.67  E-value: 1.05e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512154917     2 LLEAHGTGTRLGDPIEAQALINTYGTAHTPDRPLHLGSLKSNIGHTQAAAGVAGVIKAVQAIRHRTMPASLYADNPTAEV 81
Cdd:TIGR02813  337 LIEAHGTGTAAGDVAEFGGLVSVFSQDNDQKQHIALGSVKSQIGHTKSTAGTAGMIKAVLALHHKVLPPTINVDQPNPKL 416

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 512154917    82 DWSAGTVRLLAQARPWEAAA--YPRRAGVSSFGMSGTNAHLIVEEYRPDPERGeppaEAPAWSDVAVPLVLSAKSPQAL 158
Cdd:TIGR02813  417 DIENSPFYLNTETRPWMQREdgTPRRAGISSFGFGGTNFHMVLEEYSPKHQRD----DQYRQRAVAQTLLFTAANEKAL 491
Ketoacyl-synt_C pfam02801
Beta-ketoacyl synthase, C-terminal domain; The structure of beta-ketoacyl synthase is similar ...
 1-72 8.93e-29

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: 103.03  E-value: 8.93e-29
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 512154917    1 DLLEAHGTGTRLGDPIEAQALINTYGtAHTPDRPLHLGSLKSNIGHTQAAAGVAGVIKAVQAIRHRTMPASL 72
Cdd:pfam02801  45 DYVEAHGTGTPLGDPIEAEALKRVFG-SGARKQPLAIGSVKSNIGHLEGAAGAAGLIKVVLALRHGVIPPTL 115
KAS_I_II cd00834
Beta-ketoacyl-acyl carrier protein (ACP) synthase (KAS), type I and II. KASs are responsible ...
 5-122 1.67e-16

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: 75.65  E-value: 1.67e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512154917   5 AHGTGTRLGDPIEAQALINTYGTAhtpDRPLHLGSLKSNIGHTQAAAGVAGVIKAVQAIRHRTMPASLYADNPTAEVDws 84
Cdd:cd00834  300 AHGTSTPLNDAAESKAIKRVFGEH---AKKVPVSSTKSMTGHLLGAAGAVEAIATLLALRDGVLPPTINLEEPDPECD-- 374

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 512154917  85 agtVRLLaqarPWEAAAYPRRAGVS-SFGMSGTNAHLIV 122
Cdd:cd00834  375 ---LDYV----PNEAREAPIRYALSnSFGFGGHNASLVF 406
FabB COG0304
3-oxoacyl-(acyl-carrier-protein) synthase [Lipid transport and metabolism, Secondary ...
 5-125 3.55e-15

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: 72.05  E-value: 3.55e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512154917   5 AHGTGTRLGDPIEAQALINTYGtAHTPDRPLHlgSLKSNIGHTQAAAGVAGVIKAVQAIRHRTMPASLYADNPTAEVDws 84
Cdd:COG0304  300 AHGTSTPLGDAAETKAIKRVFG-DHAYKVPVS--STKSMTGHLLGAAGAIEAIASVLALRDGVIPPTINLENPDPECD-- 374

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 512154917  85 agtVRLLAQarpwEAAAYPRRAGVS-SFGMSGTNAHLIVEEY 125
Cdd:COG0304  375 ---LDYVPN----EAREAKIDYALSnSFGFGGHNASLVFKRY 409
KAsynt_C_assoc pfam16197
Ketoacyl-synthetase C-terminal extension; KAsynt_C_assoc represents the very C-terminus of a ...
 77-174 1.72e-13

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: 63.33  E-value: 1.72e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512154917   77 PTAEVD-WSAGTVRLLAQARPWEaaayPRRAGVSSFGMSGTNAHLIVEEYRPDPERGEPPAEAPawsdvaVPLVLSAKSP 155
Cdd:pfam16197   1 PNPDIPaLLDGRLKVVTEPTPWP----GGIVGVNSFGFGGANAHVILKSNPKPKIPPESPDNLP------RLVLLSGRTE 70

                          90
                  ....*....|....*....
gi 512154917  156 QALREQASALSRHLRDHPE 174
Cdd:pfam16197  71 EAVKALLEKLENHLDDAEF 89
decarbox_cond_enzymes cd00825
decarboxylating condensing enzymes; Family of enzymes that catalyze the formation of a new ...
 1-122 3.51e-13

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: 66.12  E-value: 3.51e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512154917   1 DLLEAHGTGTRLGDPIEAQALINTYGtahtpDRPLHLGSLKSNIGHTQAAAGVAGVIKAVQAIRHRTMPASLYadnpTAE 80
Cdd:cd00825  226 DYLVAHGTGTPIGDVKELKLLRSEFG-----DKSPAVSATKAMTGNLSSAAVVLAVDEAVLMLEHGFIPPSIH----IEE 296

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 512154917  81 VDWSAGTVRLLAQARPweaaayPRRAGVSSFGMSGTNAHLIV 122
Cdd:cd00825  297 LDEAGLNIVTETTPRE------LRTALLNGFGLGGTNATLVL 332
PTZ00050 PTZ00050
3-oxoacyl-acyl carrier protein synthase; Provisional
 1-125 8.04e-13

3-oxoacyl-acyl carrier protein synthase; Provisional


Pssm-ID: 240245 [Multi-domain]  Cd Length: 421  Bit Score: 65.48  E-value: 8.04e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512154917   1 DLLEAHGTGTRLGDPIEAQALINTYGtaHTPDRPLHLGSLKSNIGHTQAAAGVAGVIKAVQAIRHRTMPASLYADNPTAE 80
Cdd:PTZ00050 305 DYVNAHATSTPIGDKIELKAIKKVFG--DSGAPKLYVSSTKGGLGHLLGAAGAVESIVTILSLYEQIIPPTINLENPDAE 382

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 512154917  81 VDwsagtvrLLAQARPWEAAAYPRRAGVS-SFGMSGTNAHLIVEEY 125
Cdd:PTZ00050 383 CD-------LNLVQGKTAHPLQSIDAVLStSFGFGGVNTALLFTKY 421
PLN02836 PLN02836
3-oxoacyl-[acyl-carrier-protein] synthase
 1-121 9.87e-12

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


Pssm-ID: 215449 [Multi-domain]  Cd Length: 437  Bit Score: 62.12  E-value: 9.87e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512154917   1 DLLEAHGTGTRLGDPIEAQAlINTYGTAHTPDRPLHLGSLKSNIGHTQAAAGVAGVIKAVQAIRHRTMPASLYADNPTAE 80
Cdd:PLN02836 320 DYVNAHATSTPLGDAVEARA-IKTVFSEHATSGGLAFSSTKGATGHLLGAAGAVEAIFSVLAIHHGIAPPTLNLERPDPI 398

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 512154917  81 VDwsAGTVRLLAqarpweAAAYPRRAGVS-SFGMSGTNAHLI 121
Cdd:PLN02836 399 FD--DGFVPLTA------SKAMLIRAALSnSFGFGGTNASLL 432
PRK07314 PRK07314
beta-ketoacyl-ACP synthase II;
1-126 5.76e-11

beta-ketoacyl-ACP synthase II;


Pssm-ID: 235987 [Multi-domain]  Cd Length: 411  Bit Score: 59.80  E-value: 5.76e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512154917   1 DLLEAHGTGTRLGDPIEAQALINTYGtAHTPDRPLHlgSLKSNIGHTQAAAGVAGVIKAVQAIRHRTMPASLYADNPTAE 80
Cdd:PRK07314 297 DYINAHGTSTPAGDKAETQAIKRVFG-EHAYKVAVS--STKSMTGHLLGAAGAVEAIFSVLAIRDQVIPPTINLDNPDEE 373

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 512154917  81 VDwsAGTVRLLAQARPWEAAayprragVS-SFGMSGTNAHLIVEEYR 126
Cdd:PRK07314 374 CD--LDYVPNEARERKIDYA-------LSnSFGFGGTNASLVFKRYE 411
PRK06333 PRK06333
beta-ketoacyl-ACP synthase;
3-127 1.29e-10

beta-ketoacyl-ACP synthase;


Pssm-ID: 235781 [Multi-domain]  Cd Length: 424  Bit Score: 58.86  E-value: 1.29e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512154917   3 LEAHGTGTRLGDPIEAQALINTYGTahtpDRPLHLGSLKSNIGHTQAAAGVAGVIKAVQAIRHRTMPASLYADNPTAEVD 82
Cdd:PRK06333 311 LNAHATSTPVGDLGEVAAIKKVFGH----VSGLAVSSTKSATGHLLGAAGGVEAIFTILALRDQIAPPTLNLENPDPAAE 386

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 512154917  83 wsaGTVRLLAQARPWEAaaypRRAGVSSFGMSGTNAHLIVEEYRP 127
Cdd:PRK06333 387 ---GLDVVANKARPMDM----DYALSNGFGFGGVNASILFRRWEP 424
elong_cond_enzymes cd00828
"elongating" condensing enzymes are a subclass of decarboxylating condensing enzymes, ...
 1-122 2.39e-10

"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: 58.22  E-value: 2.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512154917   1 DLLEAHGTGTRLGDPIEAQAlINTYGTAHTpdRPLHLGSLKSNIGHTQAAAGVAGVIKAVQAIRHRTMPASLYADNPTAE 80
Cdd:cd00828  295 DVISAHGTSTPANDVAESRA-IAEVAGALG--APLPVTAQKALFGHSKGAAGALQLIGALQSLEHGLIPPTANLDDVDPD 371

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 512154917  81 VDWSAGTvrllAQARPWEAAayPRRAGVSSFGMSGTNAHLIV 122
Cdd:cd00828  372 VEHLSVV----GLSRDLNLK--VRAALVNAFGFGGSNAALVL 407
cond_enzymes cd00327
Condensing enzymes; Family of enzymes that catalyze a (decarboxylating or non-decarboxylating) ...
 1-122 1.32e-08

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: 52.45  E-value: 1.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512154917   1 DLLEAHGTGTRLGDPIEAQALINTYGtahtpDRPLHLGSLKSNIGHTQAAAGVAGVIKAVQAIRHRTMPaslyadnPTAE 80
Cdd:cd00327  166 DYVEAHGTGTPIGDAVELALGLDPDG-----VRSPAVSATLIMTGHPLGAAGLAILDELLLMLEHEFIP-------PTPR 233

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 512154917  81 VdwsagtvrllaqarpweaaayPRRAGVSSFGMSGTNAHLIV 122
Cdd:cd00327  234 E---------------------PRTVLLLGFGLGGTNAAVVL 254
PLN02787 PLN02787
3-oxoacyl-[acyl-carrier-protein] synthase II
 3-126 3.84e-08

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


Pssm-ID: 215421 [Multi-domain]  Cd Length: 540  Bit Score: 51.90  E-value: 3.84e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512154917   3 LEAHGTGTRLGDPIEAQALINTYGtaHTPDrpLHLGSLKSNIGHTQAAAGVAGVIKAVQAIRHRTMPASLYADNPTAEVD 82
Cdd:PLN02787 428 INAHATSTKAGDLKEYQALMRCFG--QNPE--LRVNSTKSMIGHLLGAAGAVEAIATVQAIRTGWVHPNINLENPESGVD 503

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 512154917  83 WSagtVRLLAQARPWEAAAyprrAGVSSFGMSGTNAHLIVEEYR 126
Cdd:PLN02787 504 TK---VLVGPKKERLDIKV----ALSNSFGFGGHNSSILFAPYK 540
PRK08722 PRK08722
beta-ketoacyl-ACP synthase II;
3-121 1.54e-07

beta-ketoacyl-ACP synthase II;


Pssm-ID: 181539 [Multi-domain]  Cd Length: 414  Bit Score: 50.00  E-value: 1.54e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512154917   3 LEAHGTGTRLGDPIEAQALINTYGTAHTPDrpLHLGSLKSNIGHTQAAAGVAGVIKAVQAIRHRTMPASLYADNPTA--E 80
Cdd:PRK08722 301 VNAHGTSTPAGDVAEIKGIKRALGEAGSKQ--VLVSSTKSMTGHLLGAAGSVEAIITVMSLVDQIVPPTINLDDPEEglD 378

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 512154917  81 VDWSAGTvrllaqARPWEAAAYprrAGVSSFGMSGTNAHLI 121
Cdd:PRK08722 379 IDLVPHT------ARKVESMEY---AICNSFGFGGTNGSLI 410
PRK09185 PRK09185
beta-ketoacyl-ACP synthase;
1-121 4.61e-07

beta-ketoacyl-ACP synthase;


Pssm-ID: 236398 [Multi-domain]  Cd Length: 392  Bit Score: 48.68  E-value: 4.61e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512154917   1 DLLEAHGTGTRLGDPIEAQALINTYGTAhtpdrpLHLGSLKSNIGHTQAAAGVAGVIKAVQAIRHRTMPASLyadnPTAE 80
Cdd:PRK09185 281 GYINLHGTATPLNDAMESRAVAAVFGDG------VPCSSTKGLTGHTLGAAGAVEAAICWLALRHGLPPHGW----NTGQ 350

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 512154917  81 VDWSAGTVRLLAQARPweaaAYPRRAGVSSFGMSGTNAHLI 121
Cdd:PRK09185 351 PDPALPPLYLVENAQA----LAIRYVLSNSFAFGGNNCSLI 387
PRK14691 PRK14691
3-oxoacyl-(acyl carrier protein) synthase II; Provisional
 3-125 5.27e-07

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


Pssm-ID: 173154 [Multi-domain]  Cd Length: 342  Bit Score: 48.19  E-value: 5.27e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512154917   3 LEAHGTGTRLGDPIEAQALINTYGTAHTpdrpLHLGSLKSNIGHTQAAAGVAGVIKAVQAIRHRTMPASLYADNPtaevD 82
Cdd:PRK14691 229 LNAHATSTPVGDLGEINAIKHLFGESNA----LAITSTKSATGHLLGAAGGLETIFTVLALRDQIVPATLNLENP----D 300

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 512154917  83 WSAGTVRLLA-QARPWEAAayprRAGVSSFGMSGTNAHLIVEEY 125
Cdd:PRK14691 301 PAAKGLNIIAgNAQPHDMT----YALSNGFGFAGVNASILLKRW 340
PRK05952 PRK05952
beta-ketoacyl-ACP synthase;
1-118 1.15e-06

beta-ketoacyl-ACP synthase;


Pssm-ID: 235653 [Multi-domain]  Cd Length: 381  Bit Score: 47.35  E-value: 1.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512154917   1 DLLEAHGTGTRLGDPIEAQaLINTYgtahTPDRPLhLGSLKSNIGHTQAAAGVAGVIKAVQAIRHRTMPASLYADNPTAE 80
Cdd:PRK05952 275 DYIHAHGTATRLNDQREAN-LIQAL----FPHRVA-VSSTKGATGHTLGASGALGVAFSLLALRHQQLPPCVGLQEPEFD 348

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 512154917  81 VDWsagtVRllaqarpweaaaYPRRAGVS-----SFGMSGTNA 118
Cdd:PRK05952 349 LNF----VR------------QAQQSPLQnvlclSFGFGGQNA 375
PRK07103 PRK07103
polyketide beta-ketoacyl:acyl carrier protein synthase; Validated
 1-123 1.17e-06

polyketide beta-ketoacyl:acyl carrier protein synthase; Validated


Pssm-ID: 180839 [Multi-domain]  Cd Length: 410  Bit Score: 47.33  E-value: 1.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512154917   1 DLLEAHGTGTRLGDPIEAQALINTyGTAHTpdrplHLGSLKSNIGHTQAAAGVAGVIKAVQAIRHRTMPASLYADNP-TA 79
Cdd:PRK07103 302 DYVNPHGTGSPLGDETELAALFAS-GLAHA-----WINATKSLTGHGLSAAGIVELIATLLQMRAGFLHPSRNLDEPiDE 375

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 512154917  80 EVDWSAGTVRllaqarpweaAAYPRRAGVSSFGMSGTNAHLIVE 123
Cdd:PRK07103 376 RFRWVGSTAE----------SARIRYALSLSFGFGGINTALVLE 409
PRK07910 PRK07910
beta-ketoacyl-ACP synthase;
1-125 1.89e-06

beta-ketoacyl-ACP synthase;


Pssm-ID: 236129 [Multi-domain]  Cd Length: 418  Bit Score: 46.65  E-value: 1.89e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512154917   1 DLLEAHGTGTRLGDPIEAQALINTYGTAHTPdrplhLGSLKSNIGHTQAAAGVAGVIKAVQAIRHRTMPASLYADNPTAE 80
Cdd:PRK07910 307 DHVNAHATGTSVGDVAEGKAINNALGGHRPA-----VYAPKSALGHSVGAVGAVESILTVLALRDGVIPPTLNLENLDPE 381

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 512154917  81 VDWSAGTvrllAQARPWEAaaypRRAGVSSFGMSGTNAHLIVEEY 125
Cdd:PRK07910 382 IDLDVVA----GEPRPGNY----RYAINNSFGFGGHNVALAFGRY 418
PRK06501 PRK06501
beta-ketoacyl-ACP synthase;
1-121 2.12e-06

beta-ketoacyl-ACP synthase;


Pssm-ID: 235817 [Multi-domain]  Cd Length: 425  Bit Score: 46.55  E-value: 2.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512154917   1 DLLEAHGTGTRLGDPIEAQALINTYG--TAHTPdrplhLGSLKSNIGHTQAAAGVAGVIKAVQAIRHRTMPASLYADNP- 77
Cdd:PRK06501 310 DYINAHGTSTPENDKMEYLGLSAVFGerLASIP-----VSSNKSMIGHTLTAAGAVEAVFSLLTIQTGRLPPTINYDNPd 384

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 512154917  78 -TAEVDWSAGTVRllaqarpweaAAYPRRAGVSSFGMSGTNAHLI 121
Cdd:PRK06501 385 pAIPLDVVPNVAR----------DARVTAVLSNSFGFGGQNASLV 419
PRK07967 PRK07967
beta-ketoacyl-ACP synthase I;
1-125 1.79e-05

beta-ketoacyl-ACP synthase I;


Pssm-ID: 181184 [Multi-domain]  Cd Length: 406  Bit Score: 43.89  E-value: 1.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512154917   1 DLLEAHGTGTRLGDPIEAQALINTYGtahtpDRPLHLGSLKSNIGHTQAAAGVAGVIKAVQAIRHRTMPASLYADnptaE 80
Cdd:PRK07967 292 DYINTHGTSTPVGDVKELGAIREVFG-----DKSPAISATKSLTGHSLGAAGVQEAIYSLLMMEHGFIAPSANIE----E 362

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 512154917  81 VDWSAGTVRLLAQARpweaaaypRRAGV-----SSFGMSGTNAHLIVEEY 125
Cdd:PRK07967 363 LDPQAAGMPIVTETT--------DNAELttvmsNSFGFGGTNATLVFRRY 404
PRK09116 PRK09116
beta-ketoacyl-ACP synthase;
5-52 4.02e-05

beta-ketoacyl-ACP synthase;


Pssm-ID: 181657 [Multi-domain]  Cd Length: 405  Bit Score: 42.67  E-value: 4.02e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 512154917   5 AHGTGTRLGDPIEAQALINTYGtAHTPdrplhLGSLKSNIGHTQAAAG 52
Cdd:PRK09116 300 AHGTATDRGDIAESQATAAVFG-ARMP-----ISSLKSYFGHTLGACG 341
PRK08439 PRK08439
3-oxoacyl-(acyl carrier protein) synthase II; Reviewed
 1-121 2.73e-04

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


Pssm-ID: 236265 [Multi-domain]  Cd Length: 406  Bit Score: 40.49  E-value: 2.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512154917   1 DLLEAHGTGTRLGDPIEAQALINTYGTahTPDRPLhLGSLKSNIGHTQAAAGVAGVIKAVQAIRHRTMPASLYADNPTAE 80
Cdd:PRK08439 293 DYINAHGTSTPYNDKNETAALKELFGS--KEKVPP-VSSTKGQIGHCLGAAGAIEAVISIMAMRDGILPPTINQETPDPE 369

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 512154917  81 VDwsagtvrllAQARPWEAaaypRRAGV-----SSFGMSGTNAHLI 121
Cdd:PRK08439 370 CD---------LDYIPNVA----RKAELnvvmsNSFGFGGTNGVVI 402
 
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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