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Conserved domains on  [gi|1440740089|emb|STZ33584|]
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MaoC-like dehydratase [Mycolicibacterium smegmatis]

Protein Classification

hotdog family protein( domain architecture ID 107)

hotdog family protein may have metabolic roles such as thioester hydrolysis in fatty acid metabolism and degradation of phenylacetic acid and the environmental pollutant 4-chlorobenzoate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HadA super family cl48912
(3R)-hydroxyacyl-ACP dehydratase subunit HadA;
8-150 1.87e-62

(3R)-hydroxyacyl-ACP dehydratase subunit HadA;


The actual alignment was detected with superfamily member NF040624:

Pssm-ID: 468596 [Multi-domain]  Cd Length: 144  Bit Score: 189.43  E-value: 1.87e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440740089   8 IGTHYRYPDYFEVGREKVREFSAAVKDDHPAHFDEAAAKECGHDNLIAPLTFLAVAGRRVQLDLFDKFDVPINLERVLHR 87
Cdd:NF040624    1 VGMHYRYPDYYEVGREKVREYARAVQNDHPAHHDEEAARELGYDGLVAPLTFISIIGIIAQRALFEEANVGYDLSQIVQT 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1440740089  88 DQKLIFHRPIVVGDKLWFDSYLDSVIESHGTVICEIRAEVTDDDGKPVATSIVTMLGEAEIDE 150
Cdd:NF040624   81 DQRLKFHRPIVAGDRLTCDVYVDSFRQMAGTDIIVTKNIITDQDGEPVLTTYTTLVGRTGEDG 143
 
Name Accession Description Interval E-value
HadA NF040624
(3R)-hydroxyacyl-ACP dehydratase subunit HadA;
8-150 1.87e-62

(3R)-hydroxyacyl-ACP dehydratase subunit HadA;


Pssm-ID: 468596 [Multi-domain]  Cd Length: 144  Bit Score: 189.43  E-value: 1.87e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440740089   8 IGTHYRYPDYFEVGREKVREFSAAVKDDHPAHFDEAAAKECGHDNLIAPLTFLAVAGRRVQLDLFDKFDVPINLERVLHR 87
Cdd:NF040624    1 VGMHYRYPDYYEVGREKVREYARAVQNDHPAHHDEEAARELGYDGLVAPLTFISIIGIIAQRALFEEANVGYDLSQIVQT 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1440740089  88 DQKLIFHRPIVVGDKLWFDSYLDSVIESHGTVICEIRAEVTDDDGKPVATSIVTMLGEAEIDE 150
Cdd:NF040624   81 DQRLKFHRPIVAGDRLTCDVYVDSFRQMAGTDIIVTKNIITDQDGEPVLTTYTTLVGRTGEDG 143
fused_HadA_HadB NF040620
fused (3R)-hydroxyacyl-ACP dehydratase subunits HadA/HadB;
8-155 6.53e-52

fused (3R)-hydroxyacyl-ACP dehydratase subunits HadA/HadB;


Pssm-ID: 468592 [Multi-domain]  Cd Length: 329  Bit Score: 168.48  E-value: 6.53e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440740089   8 IGTHYRYPDYFEVGREKVREFSAAVKDDHPAHFDEAAAKECGHDNLIAPLTFLAVAGRRVQLDLFDKFDVPINLERVLHR 87
Cdd:NF040620    1 VGRHYRVDDYYEVGREKIREFARAVQDFHPAHWDEAAAAELGYDGLVAPPTFASIVGMLAQRALFETVLTGYDLSQILQT 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1440740089  88 DQKLIFHRPIVVGDKLWFDSYLDSVIESHGTVICEIRAEVTDDDGKPVATSIVTMLGEAEIDEADEIS 155
Cdd:NF040620   81 DQVFEFHRPILAGDRLTCDVSLESFRQFAGGDLIVVKNVLTDQHGEVVQTGHTTLVARTGAEVDPGIA 148
PRK13692 PRK13692
(3R)-hydroxyacyl-ACP dehydratase subunit HadA; Provisional
 1-149 2.14e-50

(3R)-hydroxyacyl-ACP dehydratase subunit HadA; Provisional


Pssm-ID: 237473  Cd Length: 159  Bit Score: 159.58  E-value: 2.14e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440740089   1 MSIAANIIGTHYRYPDYFEVGREKVREFSAAVKDDHPAHFDEAAAKECGHDNLIAPLTFLAVAGRRVQLDLFDKFDVPIN 80
Cdd:PRK13692    1 MALSADIVGMHYRYPDHYEVEREKIREYAVAVQNDDAAYFEEDAAAELGYKGLLAPLTFICVFGYKAQSAFFKHANIAVA 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1440740089  81 LERVLHRDQKLIFHRPIVVGDKLWFDSYLDSVIESHGTVICEIRAEVTDDDGKPVATSIVTMLGEAEID 149
Cdd:PRK13692   81 DAQIVQVDQVLKFEKPIVAGDKLYCDVYVDSVREAHGTQIIVTKNIVTNEEGDVVQETYTTLAGRAGED 149
MaoC_dehydrat_N pfam13452
N-terminal half of MaoC dehydratase; It is clear from the structures of bacterial members of ...
 8-137 1.02e-31

N-terminal half of MaoC dehydratase; It is clear from the structures of bacterial members of MaoC dehydratase, pfam01575, that the full-length functional dehydratase enzyme is made up of two structures that dimerize to form a whole. Divergence of the N- and C- monomers in higher eukaryotes has led to two distinct domains, this one and MaoC_dehydratas. However, in order to function as an enzyme both are required together.


Pssm-ID: 433220 [Multi-domain]  Cd Length: 132  Bit Score: 110.86  E-value: 1.02e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440740089   8 IGTHYRyPDYFEVGREKVREFSAAVKDDHPAHFDEAAAKECGHDNLIAPLTFLAVAGRRVQLDLfdkFDVPINLERVLHR 87
Cdd:pfam13452   3 IGVEFG-PVKYEVERGAIREFARAIGETNPAYWDEAAARAAGYGDLPAPPTFLFVLGWDAPGFM---EQLGIDLSRLLHG 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1440740089  88 DQKLIFHRPIVVGDKLWFDSYLDSVIESHGT-VIC--EIRAEVTDDDGKPVAT 137
Cdd:pfam13452  79 EQRFTYHRPLRAGDELTCRSQIADVYDKKGNgALCfvVVETEVTNQRGEPVAT 131
MaoC COG2030
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];
8-143 2.26e-22

Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];


Pssm-ID: 441633 [Multi-domain]  Cd Length: 140  Bit Score: 87.25  E-value: 2.26e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440740089   8 IGTHYRyPDYFEVGREKVREFSAAVKDDHPAHFDEAAAKECGHDNLIAPLTFLAVAGRRVQLDLFDkFDVPINLervlhR 87
Cdd:COG2030     7 VGDVLP-HGGRTVTEEDIVLFAGATGDPNPIHLDEEAAAATGFGGRIAHGMLTLSLASGLLVDDLP-GTAVANL-----G 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1440740089  88 DQKLIFHRPIVVGDKLWFDSYLDSVIESHGTVICEIRAEVTDDDGKPVATSIVTML 143
Cdd:COG2030    80 LQEVRFLRPVRVGDTLRARVEVLEKRESKSRGIVTLRTTVTNQDGEVVLTGEATVL 135
R_hydratase_like cd03441
(R)-hydratase [(R)-specific enoyl-CoA hydratase]. Catalyzes the hydration of trans-2-enoyl ...
 19-143 4.33e-14

(R)-hydratase [(R)-specific enoyl-CoA hydratase]. Catalyzes the hydration of trans-2-enoyl CoA to (R)-3-hydroxyacyl-CoA as part of the PHA (polyhydroxyalkanoate) biosynthetic pathway. The structure of the monomer includes a five-strand antiparallel beta-sheet wrapped around a central alpha helix, referred to as a hot dog fold. The active site lies within a substrate-binding tunnel formed by the homodimer. Other enzymes with this fold include MaoC dehydratase, Hydratase-Dehydrogenase-Epimerase protein (HDE), and the fatty acid synthase beta subunit.


Pssm-ID: 239525 [Multi-domain]  Cd Length: 127  Bit Score: 65.36  E-value: 4.33e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440740089  19 EVGREKVREFSAAVKDDHPAHFDEAAAKECGHDNLIAPLTFLAVAGRRVQLDLFDKFDVPInlervlHRDQKLIFHRPIV 98
Cdd:cd03441     9 TVTEADIALFARLSGDPNPIHVDPEYAKAAGFGGRIAHGMLTLSLASGLLVQWLPGTDGAN------LGSQSVRFLAPVF 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1440740089  99 VGDKLWFDSYLDSVIESHGTVICEIRAEVTDDDGKPVATSIVTML 143
Cdd:cd03441    83 PGDTLRVEVEVLGKRPSKGRGVVTVRTEARNQGGEVVLSGEATVL 127
 
Name Accession Description Interval E-value
HadA NF040624
(3R)-hydroxyacyl-ACP dehydratase subunit HadA;
8-150 1.87e-62

(3R)-hydroxyacyl-ACP dehydratase subunit HadA;


Pssm-ID: 468596 [Multi-domain]  Cd Length: 144  Bit Score: 189.43  E-value: 1.87e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440740089   8 IGTHYRYPDYFEVGREKVREFSAAVKDDHPAHFDEAAAKECGHDNLIAPLTFLAVAGRRVQLDLFDKFDVPINLERVLHR 87
Cdd:NF040624    1 VGMHYRYPDYYEVGREKVREYARAVQNDHPAHHDEEAARELGYDGLVAPLTFISIIGIIAQRALFEEANVGYDLSQIVQT 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1440740089  88 DQKLIFHRPIVVGDKLWFDSYLDSVIESHGTVICEIRAEVTDDDGKPVATSIVTMLGEAEIDE 150
Cdd:NF040624   81 DQRLKFHRPIVAGDRLTCDVYVDSFRQMAGTDIIVTKNIITDQDGEPVLTTYTTLVGRTGEDG 143
fused_HadA_HadB NF040620
fused (3R)-hydroxyacyl-ACP dehydratase subunits HadA/HadB;
8-155 6.53e-52

fused (3R)-hydroxyacyl-ACP dehydratase subunits HadA/HadB;


Pssm-ID: 468592 [Multi-domain]  Cd Length: 329  Bit Score: 168.48  E-value: 6.53e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440740089   8 IGTHYRYPDYFEVGREKVREFSAAVKDDHPAHFDEAAAKECGHDNLIAPLTFLAVAGRRVQLDLFDKFDVPINLERVLHR 87
Cdd:NF040620    1 VGRHYRVDDYYEVGREKIREFARAVQDFHPAHWDEAAAAELGYDGLVAPPTFASIVGMLAQRALFETVLTGYDLSQILQT 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1440740089  88 DQKLIFHRPIVVGDKLWFDSYLDSVIESHGTVICEIRAEVTDDDGKPVATSIVTMLGEAEIDEADEIS 155
Cdd:NF040620   81 DQVFEFHRPILAGDRLTCDVSLESFRQFAGGDLIVVKNVLTDQHGEVVQTGHTTLVARTGAEVDPGIA 148
PRK13692 PRK13692
(3R)-hydroxyacyl-ACP dehydratase subunit HadA; Provisional
 1-149 2.14e-50

(3R)-hydroxyacyl-ACP dehydratase subunit HadA; Provisional


Pssm-ID: 237473  Cd Length: 159  Bit Score: 159.58  E-value: 2.14e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440740089   1 MSIAANIIGTHYRYPDYFEVGREKVREFSAAVKDDHPAHFDEAAAKECGHDNLIAPLTFLAVAGRRVQLDLFDKFDVPIN 80
Cdd:PRK13692    1 MALSADIVGMHYRYPDHYEVEREKIREYAVAVQNDDAAYFEEDAAAELGYKGLLAPLTFICVFGYKAQSAFFKHANIAVA 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1440740089  81 LERVLHRDQKLIFHRPIVVGDKLWFDSYLDSVIESHGTVICEIRAEVTDDDGKPVATSIVTMLGEAEID 149
Cdd:PRK13692   81 DAQIVQVDQVLKFEKPIVAGDKLYCDVYVDSVREAHGTQIIVTKNIVTNEEGDVVQETYTTLAGRAGED 149
PRK13691 PRK13691
(3R)-hydroxyacyl-ACP dehydratase subunit HadC; Provisional
 1-145 3.50e-44

(3R)-hydroxyacyl-ACP dehydratase subunit HadC; Provisional


Pssm-ID: 139768 [Multi-domain]  Cd Length: 166  Bit Score: 143.81  E-value: 3.50e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440740089   1 MSIAANIIGTHYRYPDYFEVGREKVREFSAAVKDDHPAHFDEAAAKECGHDNLIAPLTFLAVAGRRVQLDLFDKFDVPIN 80
Cdd:PRK13691    1 MALKTDIRGMVWRYPDYFVVGREQIRQFARAVKCDHPAFFSEDAAAELGYDALVAPLTFVTIFAKYVQLDFFRHVDVGME 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1440740089  81 LERVLHRDQKLIFHRPIVVGDKLWFDSYLDSVIESHGTVICEIRAEVTDDDGKPVATSIVTMLGE 145
Cdd:PRK13691   81 TMQIVQVDQRFVFHKPVLAGDKLWARMDIHSVDERFGADIVVTRNVCTNDDGELVMEAYTTLMGQ 145
MaoC_dehydrat_N pfam13452
N-terminal half of MaoC dehydratase; It is clear from the structures of bacterial members of ...
 8-137 1.02e-31

N-terminal half of MaoC dehydratase; It is clear from the structures of bacterial members of MaoC dehydratase, pfam01575, that the full-length functional dehydratase enzyme is made up of two structures that dimerize to form a whole. Divergence of the N- and C- monomers in higher eukaryotes has led to two distinct domains, this one and MaoC_dehydratas. However, in order to function as an enzyme both are required together.


Pssm-ID: 433220 [Multi-domain]  Cd Length: 132  Bit Score: 110.86  E-value: 1.02e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440740089   8 IGTHYRyPDYFEVGREKVREFSAAVKDDHPAHFDEAAAKECGHDNLIAPLTFLAVAGRRVQLDLfdkFDVPINLERVLHR 87
Cdd:pfam13452   3 IGVEFG-PVKYEVERGAIREFARAIGETNPAYWDEAAARAAGYGDLPAPPTFLFVLGWDAPGFM---EQLGIDLSRLLHG 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1440740089  88 DQKLIFHRPIVVGDKLWFDSYLDSVIESHGT-VIC--EIRAEVTDDDGKPVAT 137
Cdd:pfam13452  79 EQRFTYHRPLRAGDELTCRSQIADVYDKKGNgALCfvVVETEVTNQRGEPVAT 131
MaoC COG2030
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];
8-143 2.26e-22

Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];


Pssm-ID: 441633 [Multi-domain]  Cd Length: 140  Bit Score: 87.25  E-value: 2.26e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440740089   8 IGTHYRyPDYFEVGREKVREFSAAVKDDHPAHFDEAAAKECGHDNLIAPLTFLAVAGRRVQLDLFDkFDVPINLervlhR 87
Cdd:COG2030     7 VGDVLP-HGGRTVTEEDIVLFAGATGDPNPIHLDEEAAAATGFGGRIAHGMLTLSLASGLLVDDLP-GTAVANL-----G 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1440740089  88 DQKLIFHRPIVVGDKLWFDSYLDSVIESHGTVICEIRAEVTDDDGKPVATSIVTML 143
Cdd:COG2030    80 LQEVRFLRPVRVGDTLRARVEVLEKRESKSRGIVTLRTTVTNQDGEVVLTGEATVL 135
R_hydratase_like cd03441
(R)-hydratase [(R)-specific enoyl-CoA hydratase]. Catalyzes the hydration of trans-2-enoyl ...
 19-143 4.33e-14

(R)-hydratase [(R)-specific enoyl-CoA hydratase]. Catalyzes the hydration of trans-2-enoyl CoA to (R)-3-hydroxyacyl-CoA as part of the PHA (polyhydroxyalkanoate) biosynthetic pathway. The structure of the monomer includes a five-strand antiparallel beta-sheet wrapped around a central alpha helix, referred to as a hot dog fold. The active site lies within a substrate-binding tunnel formed by the homodimer. Other enzymes with this fold include MaoC dehydratase, Hydratase-Dehydrogenase-Epimerase protein (HDE), and the fatty acid synthase beta subunit.


Pssm-ID: 239525 [Multi-domain]  Cd Length: 127  Bit Score: 65.36  E-value: 4.33e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440740089  19 EVGREKVREFSAAVKDDHPAHFDEAAAKECGHDNLIAPLTFLAVAGRRVQLDLFDKFDVPInlervlHRDQKLIFHRPIV 98
Cdd:cd03441     9 TVTEADIALFARLSGDPNPIHVDPEYAKAAGFGGRIAHGMLTLSLASGLLVQWLPGTDGAN------LGSQSVRFLAPVF 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1440740089  99 VGDKLWFDSYLDSVIESHGTVICEIRAEVTDDDGKPVATSIVTML 143
Cdd:cd03441    83 PGDTLRVEVEVLGKRPSKGRGVVTVRTEARNQGGEVVLSGEATVL 127
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 83-143 1.75e-04

The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl carrier protein (ACP)-dehydratase) structure and subsequently in 4HBT (4-hydroxybenzoyl-CoA thioesterase) from Pseudomonas. A number of other seemingly unrelated proteins also share the hotdog fold. These proteins have related, but distinct, catalytic activities that include metabolic roles such as thioester hydrolysis in fatty acid metabolism, and degradation of phenylacetic acid and the environmental pollutant 4-chlorobenzoate. This superfamily also includes the PaaI-like protein FapR, a non-catalytic bacterial homolog involved in transcriptional regulation of fatty acid biosynthesis.


Pssm-ID: 239524 [Multi-domain]  Cd Length: 100  Bit Score: 39.00  E-value: 1.75e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1440740089  83 RVLHRDQKLIFHRPIVVGDKLwfdsYLDSVIESHGTVICEIRAEVTDDDGKPVATSIVTML 143
Cdd:cd03440    44 GAVTLSLDVRFLRPVRPGDTL----TVEAEVVRVGRSSVTVEVEVRNEDGKLVATATATFV 100
R_hydratase cd03449
(R)-hydratase [(R)-specific enoyl-CoA hydratase] catalyzes the hydration of trans-2-enoyl CoA ...
 25-148 2.61e-03

(R)-hydratase [(R)-specific enoyl-CoA hydratase] catalyzes the hydration of trans-2-enoyl CoA to (R)-3-hydroxyacyl-CoA as part of the PHA (polyhydroxyalkanoate) biosynthetic pathway. (R)-hydratase contains a hot-dog fold similar to those of thioesterase II, and beta-hydroxydecanoyl-ACP dehydratase, MaoC dehydratase, Hydratase-Dehydrogenase-Epimerase protein (HDE), and the fatty acid synthase beta subunit. The active site lies within a substrate-binding tunnel formed by the (R)-hydratase homodimer. A subset of the bacterial (R)-hydratases contain a C-terminal phosphotransacetylase (PTA) domain.


Pssm-ID: 239533 [Multi-domain]  Cd Length: 128  Bit Score: 36.37  E-value: 2.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440740089  25 VREFSAAVKDDHPAHFDEAAAKECGHDNLIAPLTFLAVAGRRVqldLFDKFDVPinleRVLHRDQKLIFHRPIVVGDKLW 104
Cdd:cd03449    18 VELFAELSGDFNPIHLDEEYAKKTRFGGRIAHGMLTASLISAV---LGTLLPGP----GTIYLSQSLRFLRPVFIGDTVT 90

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1440740089 105 FDSYLDSVIESHGTVICEIRaeVTDDDGKPVatsivtMLGEAEI 148
Cdd:cd03449    91 ATVTVTEKREDKKRVTLETV--CTNQNGEVV------IEGEAVV 126
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 93-143 3.33e-03

Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 36.07  E-value: 3.33e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1440740089  93 FHRPIVVGDKLwfdsYLDSVIESHGTVICEIRAEVTDDDGKPVATSIVTML 143
Cdd:COG2050    86 FLRPARLGDRL----TAEARVVRRGRRLAVVEVEVTDEDGKLVATATGTFA 132
 
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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