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Conserved domains on  [gi|18414694|ref|NP_567507|]
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histidine triad nucleotide-binding 4 [Arabidopsis thaliana]

Protein Classification

HIT family protein( domain architecture ID 694)

HIT (Histidine triad) family protein, named for a motif related to the sequence HxHxH/Qxx (x, a hydrophobic amino acid), is part of a superfamily of nucleotide hydrolases and transferases, which act on the alpha-phosphate of ribonucleotides

CATH:  3.30.428.10
Gene Ontology:  GO:1904047
PubMed:  1472710|9323207|12504684|12119013
SCOP:  3000223

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
HIT_like super family cl00228
HIT family: HIT (Histidine triad) proteins, named for a motif related to the sequence HxHxH ...
 8-108 7.99e-34

HIT family: HIT (Histidine triad) proteins, named for a motif related to the sequence HxHxH/Qxx (x, a hydrophobic amino acid), are a superfamily of nucleotide hydrolases and transferases, which act on the alpha-phosphate of ribonucleotides. On the basis of sequence, substrate specificity, structure, evolution and mechanism, HIT proteins are classified in the literacture into three major branches: the Hint branch, which consists of adenosine 5' -monophosphoramide hydrolases, the Fhit branch, that consists of diadenosine polyphosphate hydrolases, and the GalT branch consisting of specific nucloside monophosphate transferases. Further sequence analysis reveals several new closely related, yet uncharacterized subgroups.


The actual alignment was detected with superfamily member cd01278:

Pssm-ID: 469672 [Multi-domain]  Cd Length: 104  Bit Score: 114.40  E-value: 7.99e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414694   8 CIFCEIV--RNPTTTRLLHTDEKVIAFQDIKPAAQRHYLVIPKEHIPTVNDLqrRDEDYSLVRHMLSVGQQLLQKDA--P 83
Cdd:cd01278   2 CHFCDIAkrRDPDPEDQVYEDDRVVVFKDIYPKARHHYLVIPKEHIASLKAL--TKEDVPLLEHMETVGREKLLRSDntD 79

                        90       100
                ....*....|....*....|....*
gi 18414694  84 QSIHRFGFHQPPFNSVDHLHLHCFA 108
Cdd:cd01278  80 PSEFRFGFHAPPFTSVSHLHLHVIA 104
 
Name Accession Description Interval E-value
aprataxin_related cd01278
aprataxin related: Aprataxin, a HINT family hydrolase is mutated in ataxia oculomotor apraxia ...
 8-108 7.99e-34

aprataxin related: Aprataxin, a HINT family hydrolase is mutated in ataxia oculomotor apraxia syndrome. All the members of this subgroup have the conserved HxHxHxx (where x is a hydrophobic residue) signature motif. Members of this subgroup are predominantly eukaryotic in origin.


Pssm-ID: 238609 [Multi-domain]  Cd Length: 104  Bit Score: 114.40  E-value: 7.99e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414694   8 CIFCEIV--RNPTTTRLLHTDEKVIAFQDIKPAAQRHYLVIPKEHIPTVNDLqrRDEDYSLVRHMLSVGQQLLQKDA--P 83
Cdd:cd01278   2 CHFCDIAkrRDPDPEDQVYEDDRVVVFKDIYPKARHHYLVIPKEHIASLKAL--TKEDVPLLEHMETVGREKLLRSDntD 79

                        90       100
                ....*....|....*....|....*
gi 18414694  84 QSIHRFGFHQPPFNSVDHLHLHCFA 108
Cdd:cd01278  80 PSEFRFGFHAPPFTSVSHLHLHVIA 104
DcpS_C pfam11969
Scavenger mRNA decapping enzyme C-term binding; This family consists of several scavenger mRNA ...
 7-120 2.09e-33

Scavenger mRNA decapping enzyme C-term binding; This family consists of several scavenger mRNA decapping enzymes (DcpS) and is the C-terminal region. DcpS is a scavenger pyrophosphatase that hydrolyses the residual cap structure following 3' to 5' decay of an mRNA. The association of DcpS with 3' to 5' exonuclease exosome components suggests that these two activities are linked and there is a coupled exonucleolytic decay-dependent decapping pathway. The C-terminal domain contains a histidine triad (HIT) sequence with three histidines separated by hydrophobic residues. The central histidine within the DcpS HIT motif is critical for decapping activity and defines the HIT motif as a new mRNA decapping domain, making DcpS the first member of the HIT family of proteins with a defined biological function.


Pssm-ID: 463415 [Multi-domain]  Cd Length: 114  Bit Score: 113.47  E-value: 2.09e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414694     7 ACIFCEIVRNPTTTRLLHTDEKVIAFQDIKPAAQRHYLVIPKEHIPTVNDLqrRDEDYSLVRHMLSVGQQLLQKDAP--- 83
Cdd:pfam11969   1 KWVFCIIAKGEEPERVVYEDEGFVVFKDIKPKAPLHLLVIPKRHIKSLRDL--TPEHLPLLEHMREVAKKVIEEKYIgvd 78

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 18414694    84 QSIHRFGFHQPPfnSVDHLHLHCFALPYVPRWKAIKY 120
Cdd:pfam11969  79 RDELRLGFHYPP--SVYHLHLHVISPDFESLGLGRKK 113
HinT COG0537
Purine nucleoside phosphoramidase/Ap4A hydrolase, histidine triade (HIT) family [Nucleotide ...
 8-140 6.08e-19

Purine nucleoside phosphoramidase/Ap4A hydrolase, histidine triade (HIT) family [Nucleotide transport and metabolism, General function prediction only];


Pssm-ID: 440303 [Multi-domain]  Cd Length: 133  Bit Score: 76.91  E-value: 6.08e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414694   8 CIFCEIVRNPTTTRLLHTDEKVIAFQDIKPAAQRHYLVIPKEHIPTVNDLqrrDEDysLVRHMLSVGQQLLQkdapqsIH 87
Cdd:COG0537   3 CIFCKIIAGEIPALIVYEDEHVLAFLDINPYAPGHTLVIPKRHVASLFDL---TPE--ELAELMRLAQKVAK------AL 71

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18414694  88 RFGFHQPPFN-----------SVDHLHLHCfalpyVPRWK--AIKYKSLGPLGGFIEAETLLEKIR 140
Cdd:COG0537  72 RKALGPDGFNlginngeaagqTVPHLHVHV-----IPRYEgdDNFMPVIGTKVDPEELEETARKLR 132
PRK10687 PRK10687
purine nucleoside phosphoramidase; Provisional
 9-81 5.84e-09

purine nucleoside phosphoramidase; Provisional


Pssm-ID: 182648 [Multi-domain]  Cd Length: 119  Bit Score: 50.66  E-value: 5.84e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18414694    9 IFCEIVRNPTTTRLLHTDEKVIAFQDIKPAAQRHYLVIPKEHIPTVNDLQRRDEdySLVRHMLSVGQQLLQKD 81
Cdd:PRK10687   6 IFSKIIRREIPSDIVYQDELVTAFRDISPQAPTHILIIPNILIPTVNDVSAEHE--QALGRMITVAAKIAEQE 76
galT_1 TIGR00209
galactose-1-phosphate uridylyltransferase, family 1; This enzyme is involved in glucose and ...
 44-142 2.12e-03

galactose-1-phosphate uridylyltransferase, family 1; This enzyme is involved in glucose and galactose interconversion. This model describes one of two extremely distantly related branches of the model pfam01087. [Energy metabolism, Sugars]


Pssm-ID: 129313 [Multi-domain]  Cd Length: 347  Bit Score: 36.86  E-value: 2.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414694    44 LVIPKEHIPTVNDL-QRRDEDYSLVRHMLSVG-QQLLQKDAPQSIhrfGFHQPPFNSVD--HLHLHCFALPYVPRWKAIK 119
Cdd:TIGR00209 234 LLLPKAHVLRITDLtDAQRSDLALILKKLTSKyDNLFETSFPYSM---GWHGAPFNGEEnqHWQLHAHFYPPLLRSATVR 310

                          90       100
                  ....*....|....*....|....*...
gi 18414694   120 -----YKSLGPLGGFIEAETLLEKIRPL 142
Cdd:TIGR00209 311 kfmvgYEMLGETQRDLTAEQAAERLRAL 338
 
Name Accession Description Interval E-value
aprataxin_related cd01278
aprataxin related: Aprataxin, a HINT family hydrolase is mutated in ataxia oculomotor apraxia ...
 8-108 7.99e-34

aprataxin related: Aprataxin, a HINT family hydrolase is mutated in ataxia oculomotor apraxia syndrome. All the members of this subgroup have the conserved HxHxHxx (where x is a hydrophobic residue) signature motif. Members of this subgroup are predominantly eukaryotic in origin.


Pssm-ID: 238609 [Multi-domain]  Cd Length: 104  Bit Score: 114.40  E-value: 7.99e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414694   8 CIFCEIV--RNPTTTRLLHTDEKVIAFQDIKPAAQRHYLVIPKEHIPTVNDLqrRDEDYSLVRHMLSVGQQLLQKDA--P 83
Cdd:cd01278   2 CHFCDIAkrRDPDPEDQVYEDDRVVVFKDIYPKARHHYLVIPKEHIASLKAL--TKEDVPLLEHMETVGREKLLRSDntD 79

                        90       100
                ....*....|....*....|....*
gi 18414694  84 QSIHRFGFHQPPFNSVDHLHLHCFA 108
Cdd:cd01278  80 PSEFRFGFHAPPFTSVSHLHLHVIA 104
DcpS_C pfam11969
Scavenger mRNA decapping enzyme C-term binding; This family consists of several scavenger mRNA ...
 7-120 2.09e-33

Scavenger mRNA decapping enzyme C-term binding; This family consists of several scavenger mRNA decapping enzymes (DcpS) and is the C-terminal region. DcpS is a scavenger pyrophosphatase that hydrolyses the residual cap structure following 3' to 5' decay of an mRNA. The association of DcpS with 3' to 5' exonuclease exosome components suggests that these two activities are linked and there is a coupled exonucleolytic decay-dependent decapping pathway. The C-terminal domain contains a histidine triad (HIT) sequence with three histidines separated by hydrophobic residues. The central histidine within the DcpS HIT motif is critical for decapping activity and defines the HIT motif as a new mRNA decapping domain, making DcpS the first member of the HIT family of proteins with a defined biological function.


Pssm-ID: 463415 [Multi-domain]  Cd Length: 114  Bit Score: 113.47  E-value: 2.09e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414694     7 ACIFCEIVRNPTTTRLLHTDEKVIAFQDIKPAAQRHYLVIPKEHIPTVNDLqrRDEDYSLVRHMLSVGQQLLQKDAP--- 83
Cdd:pfam11969   1 KWVFCIIAKGEEPERVVYEDEGFVVFKDIKPKAPLHLLVIPKRHIKSLRDL--TPEHLPLLEHMREVAKKVIEEKYIgvd 78

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 18414694    84 QSIHRFGFHQPPfnSVDHLHLHCFALPYVPRWKAIKY 120
Cdd:pfam11969  79 RDELRLGFHYPP--SVYHLHLHVISPDFESLGLGRKK 113
PKCI_related cd01276
Protein Kinase C Interacting protein related (PKCI): PKCI and related proteins belong to the ...
 8-105 5.24e-19

Protein Kinase C Interacting protein related (PKCI): PKCI and related proteins belong to the ubiquitous HIT family of hydrolases that act on alpha-phosphates of ribonucleotides. The members of this subgroup have a conserved HxHxHxx motif (x is a hydrophobic residue) that is a signature for this family. No enzymatic activity has been reported however, for PKCI and its related members.


Pssm-ID: 238607 [Multi-domain]  Cd Length: 104  Bit Score: 76.45  E-value: 5.24e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414694   8 CIFCEIVRNPTTTRLLHTDEKVIAFQDIKPAAQRHYLVIPKEHIPTVNDLQRRDEDysLVRHMLSVGQQLLQKdapqsih 87
Cdd:cd01276   2 CIFCKIIRGEIPAKKVYEDDEVLAFHDINPQAPVHILVIPKKHIASLSDATEEDEE--LLGHLLSAAAKVAKD------- 72

                        90       100
                ....*....|....*....|....*....
gi 18414694  88 rFGFHQPPF-----------NSVDHLHLH 105
Cdd:cd01276  73 -LGIAEDGYrlvincgkdggQEVFHLHLH 100
HinT COG0537
Purine nucleoside phosphoramidase/Ap4A hydrolase, histidine triade (HIT) family [Nucleotide ...
 8-140 6.08e-19

Purine nucleoside phosphoramidase/Ap4A hydrolase, histidine triade (HIT) family [Nucleotide transport and metabolism, General function prediction only];


Pssm-ID: 440303 [Multi-domain]  Cd Length: 133  Bit Score: 76.91  E-value: 6.08e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414694   8 CIFCEIVRNPTTTRLLHTDEKVIAFQDIKPAAQRHYLVIPKEHIPTVNDLqrrDEDysLVRHMLSVGQQLLQkdapqsIH 87
Cdd:COG0537   3 CIFCKIIAGEIPALIVYEDEHVLAFLDINPYAPGHTLVIPKRHVASLFDL---TPE--ELAELMRLAQKVAK------AL 71

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18414694  88 RFGFHQPPFN-----------SVDHLHLHCfalpyVPRWK--AIKYKSLGPLGGFIEAETLLEKIR 140
Cdd:COG0537  72 RKALGPDGFNlginngeaagqTVPHLHVHV-----IPRYEgdDNFMPVIGTKVDPEELEETARKLR 132
HIT_like cd00468
HIT family: HIT (Histidine triad) proteins, named for a motif related to the sequence HxHxH ...
 24-105 4.61e-13

HIT family: HIT (Histidine triad) proteins, named for a motif related to the sequence HxHxH/Qxx (x, a hydrophobic amino acid), are a superfamily of nucleotide hydrolases and transferases, which act on the alpha-phosphate of ribonucleotides. On the basis of sequence, substrate specificity, structure, evolution and mechanism, HIT proteins are classified in the literacture into three major branches: the Hint branch, which consists of adenosine 5' -monophosphoramide hydrolases, the Fhit branch, that consists of diadenosine polyphosphate hydrolases, and the GalT branch consisting of specific nucloside monophosphate transferases. Further sequence analysis reveals several new closely related, yet uncharacterized subgroups.


Pssm-ID: 238263 [Multi-domain]  Cd Length: 86  Bit Score: 60.56  E-value: 4.61e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414694  24 HTDEKVIAFQDIKPAAQRHYLVIPKEHIPTVNDLqRRDEDYSLVRHMLSVGQQLLQKDAPQSIHRF-GFHQPPFNSVDHL 102
Cdd:cd00468   2 PDDEHSFAFVNLKPAAPGHVLVCPKRHVETLPDL-DEALLADLVITAQRVAAELEKHGNVPSLTVFvNDGAAAGQSVPHV 80


                ...
gi 18414694 103 HLH 105
Cdd:cd00468  81 HLH 83
HINT_subgroup cd01277
HINT (histidine triad nucleotide-binding protein) subgroup: Members of this CD belong to the ...
 8-57 1.31e-10

HINT (histidine triad nucleotide-binding protein) subgroup: Members of this CD belong to the superfamily of histidine triad hydrolases that act on alpha-phosphate of ribonucleotides. This subgroup includes members from all three forms of cellular life. Although the biochemical function has not been characterised for many of the members of this subgroup, the proteins from Yeast have been shown to be involved in secretion, peroxisome formation and gene expression.


Pssm-ID: 238608 [Multi-domain]  Cd Length: 103  Bit Score: 54.54  E-value: 1.31e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 18414694   8 CIFCEIVRNPTTTRLLHTDEKVIAFQDIKPAAQRHYLVIPKEHIPTVNDL 57
Cdd:cd01277   2 CIFCKIIAGEIPSYKVYEDDHVLAFLDINPASKGHTLVIPKKHYENLLDL 51
HIT pfam01230
HIT domain;
19-105 5.40e-10

HIT domain;


Pssm-ID: 395984 [Multi-domain]  Cd Length: 98  Bit Score: 53.08  E-value: 5.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414694    19 TTRLLHTDEKVIAFQDIKPAAQRHYLVIPKEHIPTVNDLQRRDEDY--SLVRHMLSVGQQLLQKDAPQSIHRFGFHQppF 96
Cdd:pfam01230   5 PSTVVYEDDLVLAFLDIDPQAPGHILVIPKKHIRELHDLTPEELGDlmSVAQKVARALGKVFKADGYRIVINNGAHA--G 82


                  ....*....
gi 18414694    97 NSVDHLHLH 105
Cdd:pfam01230  83 QSVPHLHIH 91
PRK10687 PRK10687
purine nucleoside phosphoramidase; Provisional
 9-81 5.84e-09

purine nucleoside phosphoramidase; Provisional


Pssm-ID: 182648 [Multi-domain]  Cd Length: 119  Bit Score: 50.66  E-value: 5.84e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18414694    9 IFCEIVRNPTTTRLLHTDEKVIAFQDIKPAAQRHYLVIPKEHIPTVNDLQRRDEdySLVRHMLSVGQQLLQKD 81
Cdd:PRK10687   6 IFSKIIRREIPSDIVYQDELVTAFRDISPQAPTHILIIPNILIPTVNDVSAEHE--QALGRMITVAAKIAEQE 76
FHIT cd01275
FHIT (fragile histidine family): FHIT proteins, related to the HIT family carry a motif HxHxH ...
 8-116 1.74e-07

FHIT (fragile histidine family): FHIT proteins, related to the HIT family carry a motif HxHxH/Qxx (x, is a hydrophobic amino acid), On the basis of sequence, substrate specificity, structure, evolution and mechanism, HIT proteins are classified into three branches: the Hint branch, which consists of adenosine 5' -monophosphoramide hydrolases, the Fhit branch, that consists of diadenosine polyphosphate hydrolases, and the GalT branch consisting of specific nucloside monophosphate transferases. Fhit plays a very important role in the development of tumours. Infact, Fhit deletions are among the earliest and most frequent genetic alterations in the development of tumours.


Pssm-ID: 238606 [Multi-domain]  Cd Length: 126  Bit Score: 46.90  E-value: 1.74e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414694   8 CIFCEIVRNPTTTRL-LHTDEKVIAFQDIKPAAQRHYLVIPKEHIPTVNDLqrRDEDYSLVRHMLSVGQQLLQK-DAPQS 85
Cdd:cd01275   1 CVFCDIPIKPDEDNLvFYRTKHSFAVVNLYPYNPGHVLVVPYRHVPRLEDL--TPEEIADLFKLVQLAMKALKVvYKPDG 78

                        90       100       110
                ....*....|....*....|....*....|...
gi 18414694  86 IHrFGFHQPPF--NSVDHLHLHcfalpYVPRWK 116
Cdd:cd01275  79 FN-IGINDGKAggGIVPHVHIH-----IVPRWN 105
GalT cd00608
Galactose-1-phosphate uridyl transferase (GalT): This enzyme plays a key role in galactose ...
 8-142 1.75e-04

Galactose-1-phosphate uridyl transferase (GalT): This enzyme plays a key role in galactose metabolism by catalysing the transfer of a uridine 5'-phosphoryl group from UDP-galactose 1-phosphate. The structure of E.coli GalT reveals that the enzyme contains two identical subunits. It also demonstrates that the active site is formed by amino acid residues from both subunits of the dimer.


Pssm-ID: 238341 [Multi-domain]  Cd Length: 329  Bit Score: 39.98  E-value: 1.75e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414694   8 CIFCEIVRNPTTT--RLLHTDEKVIAFqdiKPAAQR---HYLVIPKEHIPTVNDL--QRRDEDYSLVRHMLSVGQQLLQK 80
Cdd:cd00608 186 CLLCDYLKLELESkeRIVVENEHFVAV---VPFWARwpfEVHILPKRHVSRFTDLtdEEREDLAEILKRLLARYDNLFNC 262

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18414694  81 DAPQSihrFGFHQPPFNSVD------HLHLHCFalpyvPRWKAIKYKslgPLGGFieaETL-LEKIRPL 142
Cdd:cd00608 263 SFPYS---MGWHQAPTGGKElenwyyHWHFEIP-----PRRSATVLK---FMAGF---ELGaGEFINDV 317
GalT COG1085
Galactose-1-phosphate uridylyltransferase [Carbohydrate transport and metabolism];
8-129 2.17e-04

Galactose-1-phosphate uridylyltransferase [Carbohydrate transport and metabolism];


Pssm-ID: 440702 [Multi-domain]  Cd Length: 336  Bit Score: 39.82  E-value: 2.17e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414694   8 CIFCEIVRNPTT--TRLLHTDEKVIAFqdiKPAAQR---HYLVIPKEHIP---TVNDLQRRDedysLVRHMLSVGQQL-- 77
Cdd:COG1085 192 CLLCDILAQELAagERVVAENEHFVAF---VPFAARwpfETWILPKRHVSdfeELTDEERDD----LARILKRVLRRLdn 264

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 18414694  78 LQKDAPQSihrFGFHQPPFNSVDHLHLHCFALPYVPRWKAIKyksLGPLGGF 129
Cdd:COG1085 265 LLGDFPYN---MGLHQAPVDGEERDHYHWHLEIYPRLRSATV---LKFLAGF 310
galT_1 TIGR00209
galactose-1-phosphate uridylyltransferase, family 1; This enzyme is involved in glucose and ...
 44-142 2.12e-03

galactose-1-phosphate uridylyltransferase, family 1; This enzyme is involved in glucose and galactose interconversion. This model describes one of two extremely distantly related branches of the model pfam01087. [Energy metabolism, Sugars]


Pssm-ID: 129313 [Multi-domain]  Cd Length: 347  Bit Score: 36.86  E-value: 2.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18414694    44 LVIPKEHIPTVNDL-QRRDEDYSLVRHMLSVG-QQLLQKDAPQSIhrfGFHQPPFNSVD--HLHLHCFALPYVPRWKAIK 119
Cdd:TIGR00209 234 LLLPKAHVLRITDLtDAQRSDLALILKKLTSKyDNLFETSFPYSM---GWHGAPFNGEEnqHWQLHAHFYPPLLRSATVR 310

                          90       100
                  ....*....|....*....|....*...
gi 18414694   120 -----YKSLGPLGGFIEAETLLEKIRPL 142
Cdd:TIGR00209 311 kfmvgYEMLGETQRDLTAEQAAERLRAL 338
 
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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