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Conserved domains on  [gi|42573622|ref|NP_974907|]
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histidine triad nucleotide-binding 3 [Arabidopsis thaliana]

Protein Classification

HIT family protein( domain architecture ID 10101098)

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

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List of domain hits

 Name Accession Description Interval E-value
HINT_subgroup cd01277
HINT (histidine triad nucleotide-binding protein) subgroup: Members of this CD belong to the ...
 49-151 7.79e-46

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: 146.60  E-value: 7.79e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573622  49 DCVFCKIIRGESPCLKLYEDDMCLCILDTNPLSHGHSLIIPKLHYPTLEETPPSVVAAMCSKVPLISNAIVKATGSDSFN 128
Cdd:cd01277   1 DCIFCKIIAGEIPSYKVYEDDHVLAFLDINPASKGHTLVIPKKHYENLLDLDPEELAELILAAKKVARALKKALKADGLN 80

                        90       100
                ....*....|....*....|...
gi 42573622 129 LLVNNGAAAGQVIFHTHIHIIPR 151
Cdd:cd01277  81 ILQNNGRAAGQVVFHVHVHVIPR 103
 
Name Accession Description Interval E-value
HINT_subgroup cd01277
HINT (histidine triad nucleotide-binding protein) subgroup: Members of this CD belong to the ...
 49-151 7.79e-46

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: 146.60  E-value: 7.79e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573622  49 DCVFCKIIRGESPCLKLYEDDMCLCILDTNPLSHGHSLIIPKLHYPTLEETPPSVVAAMCSKVPLISNAIVKATGSDSFN 128
Cdd:cd01277   1 DCIFCKIIAGEIPSYKVYEDDHVLAFLDINPASKGHTLVIPKKHYENLLDLDPEELAELILAAKKVARALKKALKADGLN 80

                        90       100
                ....*....|....*....|...
gi 42573622 129 LLVNNGAAAGQVIFHTHIHIIPR 151
Cdd:cd01277  81 ILQNNGRAAGQVVFHVHVHVIPR 103
HinT COG0537
Purine nucleoside phosphoramidase/Ap4A hydrolase, histidine triade (HIT) family [Nucleotide ...
 48-158 2.33e-45

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: 146.63  E-value: 2.33e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573622  48 NDCVFCKIIRGESPCLKLYEDDMCLCILDTNPLSHGHSLIIPKLHYPTLEETPPSVVAAMCSKVPLISNAIVKATGSDSF 127
Cdd:COG0537   1 MDCIFCKIIAGEIPALIVYEDEHVLAFLDINPYAPGHTLVIPKRHVASLFDLTPEELAELMRLAQKVAKALRKALGPDGF 80

                        90       100       110
                ....*....|....*....|....*....|.
gi 42573622 128 NLLVNNGAAAGQVIFHTHIHIIPRKERDCLW 158
Cdd:COG0537  81 NLGINNGEAAGQTVPHLHVHVIPRYEGDDNF 111
HIT pfam01230
HIT domain;
57-153 5.96e-28

HIT domain;


Pssm-ID: 395984 [Multi-domain]  Cd Length: 98  Bit Score: 100.85  E-value: 5.96e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573622    57 RGESPCLKLYEDDMCLCILDTNPLSHGHSLIIPKLHYPTLEETPPSVVAAMCSKVPLISNAIVKATGSDSFNLLVNNGAA 136
Cdd:pfam01230   1 RGEIPSTVVYEDDLVLAFLDIDPQAPGHILVIPKKHIRELHDLTPEELGDLMSVAQKVARALGKVFKADGYRIVINNGAH 80

                          90
                  ....*....|....*..
gi 42573622   137 AGQVIFHTHIHIIPRKE 153
Cdd:pfam01230  81 AGQSVPHLHIHVIPRRK 97
PRK10687 PRK10687
purine nucleoside phosphoramidase; Provisional
 49-149 6.33e-13

purine nucleoside phosphoramidase; Provisional


Pssm-ID: 182648 [Multi-domain]  Cd Length: 119  Bit Score: 62.60  E-value: 6.33e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573622   49 DCVFCKIIRGESPCLKLYEDDMCLCILDTNPLSHGHSLIIPKLHYPTLEETPPSVVAAMcSKVPLISNAIVKATG--SDS 126
Cdd:PRK10687   4 ETIFSKIIRREIPSDIVYQDELVTAFRDISPQAPTHILIIPNILIPTVNDVSAEHEQAL-GRMITVAAKIAEQEGiaEDG 82

                         90       100
                 ....*....|....*....|...
gi 42573622  127 FNLLVNNGAAAGQVIFHTHIHII 149
Cdd:PRK10687  83 YRLIMNTNRHGGQEVYHIHMHLL 105
 
Name Accession Description Interval E-value
HINT_subgroup cd01277
HINT (histidine triad nucleotide-binding protein) subgroup: Members of this CD belong to the ...
 49-151 7.79e-46

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: 146.60  E-value: 7.79e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573622  49 DCVFCKIIRGESPCLKLYEDDMCLCILDTNPLSHGHSLIIPKLHYPTLEETPPSVVAAMCSKVPLISNAIVKATGSDSFN 128
Cdd:cd01277   1 DCIFCKIIAGEIPSYKVYEDDHVLAFLDINPASKGHTLVIPKKHYENLLDLDPEELAELILAAKKVARALKKALKADGLN 80

                        90       100
                ....*....|....*....|...
gi 42573622 129 LLVNNGAAAGQVIFHTHIHIIPR 151
Cdd:cd01277  81 ILQNNGRAAGQVVFHVHVHVIPR 103
HinT COG0537
Purine nucleoside phosphoramidase/Ap4A hydrolase, histidine triade (HIT) family [Nucleotide ...
 48-158 2.33e-45

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: 146.63  E-value: 2.33e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573622  48 NDCVFCKIIRGESPCLKLYEDDMCLCILDTNPLSHGHSLIIPKLHYPTLEETPPSVVAAMCSKVPLISNAIVKATGSDSF 127
Cdd:COG0537   1 MDCIFCKIIAGEIPALIVYEDEHVLAFLDINPYAPGHTLVIPKRHVASLFDLTPEELAELMRLAQKVAKALRKALGPDGF 80

                        90       100       110
                ....*....|....*....|....*....|.
gi 42573622 128 NLLVNNGAAAGQVIFHTHIHIIPRKERDCLW 158
Cdd:COG0537  81 NLGINNGEAAGQTVPHLHVHVIPRYEGDDNF 111
PKCI_related cd01276
Protein Kinase C Interacting protein related (PKCI): PKCI and related proteins belong to the ...
 49-149 5.71e-30

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: 106.11  E-value: 5.71e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573622  49 DCVFCKIIRGESPCLKLYEDDMCLCILDTNPLSHGHSLIIPKLHYPTLEETPPSVVAAMcSKVPLISNAIVKATG--SDS 126
Cdd:cd01276   1 DCIFCKIIRGEIPAKKVYEDDEVLAFHDINPQAPVHILVIPKKHIASLSDATEEDEELL-GHLLSAAAKVAKDLGiaEDG 79

                        90       100
                ....*....|....*....|...
gi 42573622 127 FNLLVNNGAAAGQVIFHTHIHII 149
Cdd:cd01276  80 YRLVINCGKDGGQEVFHLHLHLL 102
HIT pfam01230
HIT domain;
57-153 5.96e-28

HIT domain;


Pssm-ID: 395984 [Multi-domain]  Cd Length: 98  Bit Score: 100.85  E-value: 5.96e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573622    57 RGESPCLKLYEDDMCLCILDTNPLSHGHSLIIPKLHYPTLEETPPSVVAAMCSKVPLISNAIVKATGSDSFNLLVNNGAA 136
Cdd:pfam01230   1 RGEIPSTVVYEDDLVLAFLDIDPQAPGHILVIPKKHIRELHDLTPEELGDLMSVAQKVARALGKVFKADGYRIVINNGAH 80

                          90
                  ....*....|....*..
gi 42573622   137 AGQVIFHTHIHIIPRKE 153
Cdd:pfam01230  81 AGQSVPHLHIHVIPRRK 97
FHIT cd01275
FHIT (fragile histidine family): FHIT proteins, related to the HIT family carry a motif HxHxH ...
 50-155 2.11e-21

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: 85.04  E-value: 2.11e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573622  50 CVFCKIIRGESPC-LKLYEDDMCLCILDTNPLSHGHSLIIPKLHYPTLEETPPSVVAAMCSKVPLISNAIVKATGSDSFN 128
Cdd:cd01275   1 CVFCDIPIKPDEDnLVFYRTKHSFAVVNLYPYNPGHVLVVPYRHVPRLEDLTPEEIADLFKLVQLAMKALKVVYKPDGFN 80

                        90       100
                ....*....|....*....|....*..
gi 42573622 129 LLVNNGAAAGQVIFHTHIHIIPRKERD 155
Cdd:cd01275  81 IGINDGKAGGGIVPHVHIHIVPRWNGD 107
PRK10687 PRK10687
purine nucleoside phosphoramidase; Provisional
 49-149 6.33e-13

purine nucleoside phosphoramidase; Provisional


Pssm-ID: 182648 [Multi-domain]  Cd Length: 119  Bit Score: 62.60  E-value: 6.33e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573622   49 DCVFCKIIRGESPCLKLYEDDMCLCILDTNPLSHGHSLIIPKLHYPTLEETPPSVVAAMcSKVPLISNAIVKATG--SDS 126
Cdd:PRK10687   4 ETIFSKIIRREIPSDIVYQDELVTAFRDISPQAPTHILIIPNILIPTVNDVSAEHEQAL-GRMITVAAKIAEQEGiaEDG 82

                         90       100
                 ....*....|....*....|...
gi 42573622  127 FNLLVNNGAAAGQVIFHTHIHII 149
Cdd:PRK10687  83 YRLIMNTNRHGGQEVYHIHMHLL 105
DcpS_C pfam11969
Scavenger mRNA decapping enzyme C-term binding; This family consists of several scavenger mRNA ...
 50-149 2.25e-11

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: 58.39  E-value: 2.25e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573622    50 CVFCKIIRGESPCLKLYEDDMCLCILDTNPLSHGHSLIIPKLHYPTLEETPPS---VVAAMCSKVplisNAIVKATGSDS 126
Cdd:pfam11969   2 WVFCIIAKGEEPERVVYEDEGFVVFKDIKPKAPLHLLVIPKRHIKSLRDLTPEhlpLLEHMREVA----KKVIEEKYIGV 77

                          90       100
                  ....*....|....*....|...
gi 42573622   127 FNLLVNNGAAAGQVIFHTHIHII 149
Cdd:pfam11969  78 DRDELRLGFHYPPSVYHLHLHVI 100
HIT_like cd00468
HIT family: HIT (Histidine triad) proteins, named for a motif related to the sequence HxHxH ...
 66-150 6.22e-11

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: 56.32  E-value: 6.22e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573622  66 YEDDMCLCILDTNPLSHGHSLIIPKLHYPTLEETPPSVVAAMCSKVPLISNAIVKATGSDSFNLLVNNGAAAGQVIFHTH 145
Cdd:cd00468   2 PDDEHSFAFVNLKPAAPGHVLVCPKRHVETLPDLDEALLADLVITAQRVAAELEKHGNVPSLTVFVNDGAAAGQSVPHVH 81


                ....*
gi 42573622 146 IHIIP 150
Cdd:cd00468  82 LHVLP 86
aprataxin_related cd01278
aprataxin related: Aprataxin, a HINT family hydrolase is mutated in ataxia oculomotor apraxia ...
 50-149 1.03e-06

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: 45.45  E-value: 1.03e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573622  50 CVFCKI--IRGESPCLKLYEDDMCLCILDTNPLSHGHSLIIPKLHYPTLEETPPSVVAAMCSKVPLISNAIVKATGSDSF 127
Cdd:cd01278   2 CHFCDIakRRDPDPEDQVYEDDRVVVFKDIYPKARHHYLVIPKEHIASLKALTKEDVPLLEHMETVGREKLLRSDNTDPS 81

                        90       100
                ....*....|....*....|..
gi 42573622 128 NLLVNNGAAAGQVIFHTHIHII 149
Cdd:cd01278  82 EFRFGFHAPPFTSVSHLHLHVI 103
 
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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