NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|21654864|gb|AAK94777|]
View 

histidine triad protein 4, partial [Rattus norvegicus]

Protein Classification

HIT family protein( domain architecture ID 10101103)

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
aprataxin_related cd01278
aprataxin related: Aprataxin, a HINT family hydrolase is mutated in ataxia oculomotor apraxia ...
 31-134 2.28e-50

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: 157.16  E-value: 2.28e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21654864  31 NCVFCRVAAGQEPETELLYCENKDLVCFKDIKPAALHHYLVVPKKHIGSCKDLNKDHIEMVESMVTVGKTILERNNFTDF 110
Cdd:cd01278   1 LCHFCDIAKRRDPDPEDQVYEDDRVVVFKDIYPKARHHYLVIPKEHIASLKALTKEDVPLLEHMETVGREKLLRSDNTDP 80

                        90       100
                ....*....|....*....|....
gi 21654864 111 TDVRMGFHVPPFCSVSHLHLHVIA 134
Cdd:cd01278  81 SEFRFGFHAPPFTSVSHLHLHVIA 104
 
Name Accession Description Interval E-value
aprataxin_related cd01278
aprataxin related: Aprataxin, a HINT family hydrolase is mutated in ataxia oculomotor apraxia ...
 31-134 2.28e-50

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: 157.16  E-value: 2.28e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21654864  31 NCVFCRVAAGQEPETELLYCENKDLVCFKDIKPAALHHYLVVPKKHIGSCKDLNKDHIEMVESMVTVGKTILERNNFTDF 110
Cdd:cd01278   1 LCHFCDIAKRRDPDPEDQVYEDDRVVVFKDIYPKARHHYLVIPKEHIASLKALTKEDVPLLEHMETVGREKLLRSDNTDP 80

                        90       100
                ....*....|....*....|....
gi 21654864 111 TDVRMGFHVPPFCSVSHLHLHVIA 134
Cdd:cd01278  81 SEFRFGFHAPPFTSVSHLHLHVIA 104
DcpS_C pfam11969
Scavenger mRNA decapping enzyme C-term binding; This family consists of several scavenger mRNA ...
 31-144 4.91e-41

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: 133.50  E-value: 4.91e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21654864    31 NCVFCRVAAGQEPETELLycENKDLVCFKDIKPAALHHYLVVPKKHIGSCKDLNKDHIEMVESMVTVGKTILERNNFT-D 109
Cdd:pfam11969   1 KWVFCIIAKGEEPERVVY--EDEGFVVFKDIKPKAPLHLLVIPKRHIKSLRDLTPEHLPLLEHMREVAKKVIEEKYIGvD 78

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 21654864   110 FTDVRMGFHVPPfcSVSHLHLHVIAPAKEFGFLSR 144
Cdd:pfam11969  79 RDELRLGFHYPP--SVYHLHLHVISPDFESLGLGR 111
HinT COG0537
Purine nucleoside phosphoramidase/Ap4A hydrolase, histidine triade (HIT) family [Nucleotide ...
 30-133 7.28e-15

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: 67.28  E-value: 7.28e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21654864  30 SNCVFCRVAAGQEPETELLycENKDLVCFKDIKPAALHHYLVVPKKHIGSCKDLNKDhiEMVESMVTVGKTILERNNFTD 109
Cdd:COG0537   1 MDCIFCKIIAGEIPALIVY--EDEHVLAFLDINPYAPGHTLVIPKRHVASLFDLTPE--ELAELMRLAQKVAKALRKALG 76

                        90       100
                ....*....|....*....|....*.
gi 21654864 110 FTDVRMGFHVPPFC--SVSHLHLHVI 133
Cdd:COG0537  77 PDGFNLGINNGEAAgqTVPHLHVHVI 102
PRK10687 PRK10687
purine nucleoside phosphoramidase; Provisional
 54-133 3.08e-04

purine nucleoside phosphoramidase; Provisional


Pssm-ID: 182648 [Multi-domain]  Cd Length: 119  Bit Score: 38.72  E-value: 3.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21654864   54 DLV-CFKDIKPAALHHYLVVPKKHIGSCKDLNKDHIEMVESMVTVGKTILERNNFTDftdvrMGFHVPPFCS------VS 126
Cdd:PRK10687  24 ELVtAFRDISPQAPTHILIIPNILIPTVNDVSAEHEQALGRMITVAAKIAEQEGIAE-----DGYRLIMNTNrhggqeVY 98


                 ....*..
gi 21654864  127 HLHLHVI 133
Cdd:PRK10687  99 HIHMHLL 105
 
Name Accession Description Interval E-value
aprataxin_related cd01278
aprataxin related: Aprataxin, a HINT family hydrolase is mutated in ataxia oculomotor apraxia ...
 31-134 2.28e-50

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: 157.16  E-value: 2.28e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21654864  31 NCVFCRVAAGQEPETELLYCENKDLVCFKDIKPAALHHYLVVPKKHIGSCKDLNKDHIEMVESMVTVGKTILERNNFTDF 110
Cdd:cd01278   1 LCHFCDIAKRRDPDPEDQVYEDDRVVVFKDIYPKARHHYLVIPKEHIASLKALTKEDVPLLEHMETVGREKLLRSDNTDP 80

                        90       100
                ....*....|....*....|....
gi 21654864 111 TDVRMGFHVPPFCSVSHLHLHVIA 134
Cdd:cd01278  81 SEFRFGFHAPPFTSVSHLHLHVIA 104
DcpS_C pfam11969
Scavenger mRNA decapping enzyme C-term binding; This family consists of several scavenger mRNA ...
 31-144 4.91e-41

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: 133.50  E-value: 4.91e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21654864    31 NCVFCRVAAGQEPETELLycENKDLVCFKDIKPAALHHYLVVPKKHIGSCKDLNKDHIEMVESMVTVGKTILERNNFT-D 109
Cdd:pfam11969   1 KWVFCIIAKGEEPERVVY--EDEGFVVFKDIKPKAPLHLLVIPKRHIKSLRDLTPEHLPLLEHMREVAKKVIEEKYIGvD 78

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 21654864   110 FTDVRMGFHVPPfcSVSHLHLHVIAPAKEFGFLSR 144
Cdd:pfam11969  79 RDELRLGFHYPP--SVYHLHLHVISPDFESLGLGR 111
PKCI_related cd01276
Protein Kinase C Interacting protein related (PKCI): PKCI and related proteins belong to the ...
 31-134 7.83e-18

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: 74.14  E-value: 7.83e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21654864  31 NCVFCRVAAGQEPETELLycENKDLVCFKDIKPAALHHYLVVPKKHIGSCKDLN-KDHIEMVESMVTVGKTILERNNFTD 109
Cdd:cd01276   1 DCIFCKIIRGEIPAKKVY--EDDEVLAFHDINPQAPVHILVIPKKHIASLSDATeEDEELLGHLLSAAAKVAKDLGIAED 78

                        90       100       110
                ....*....|....*....|....*....|.
gi 21654864 110 ftdvrmGFHVPPFC------SVSHLHLHVIA 134
Cdd:cd01276  79 ------GYRLVINCgkdggqEVFHLHLHLLG 103
HinT COG0537
Purine nucleoside phosphoramidase/Ap4A hydrolase, histidine triade (HIT) family [Nucleotide ...
 30-133 7.28e-15

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: 67.28  E-value: 7.28e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21654864  30 SNCVFCRVAAGQEPETELLycENKDLVCFKDIKPAALHHYLVVPKKHIGSCKDLNKDhiEMVESMVTVGKTILERNNFTD 109
Cdd:COG0537   1 MDCIFCKIIAGEIPALIVY--EDEHVLAFLDINPYAPGHTLVIPKRHVASLFDLTPE--ELAELMRLAQKVAKALRKALG 76

                        90       100
                ....*....|....*....|....*.
gi 21654864 110 FTDVRMGFHVPPFC--SVSHLHLHVI 133
Cdd:COG0537  77 PDGFNLGINNGEAAgqTVPHLHVHVI 102
HIT_like cd00468
HIT family: HIT (Histidine triad) proteins, named for a motif related to the sequence HxHxH ...
 56-134 3.43e-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: 61.72  E-value: 3.43e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21654864  56 VCFKDIKPAALHHYLVVPKKHIGSCKDLNKDhiEMVESMVTVGK--TILERNNFTDFTDVRMGFHVPPFCSVSHLHLHVI 133
Cdd:cd00468   8 FAFVNLKPAAPGHVLVCPKRHVETLPDLDEA--LLADLVITAQRvaAELEKHGNVPSLTVFVNDGAAAGQSVPHVHLHVL 85


                .
gi 21654864 134 A 134
Cdd:cd00468  86 P 86
HINT_subgroup cd01277
HINT (histidine triad nucleotide-binding protein) subgroup: Members of this CD belong to the ...
 31-133 4.00e-07

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: 46.06  E-value: 4.00e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21654864  31 NCVFCRVAAGQEPeTELLYcENKDLVCFKDIKPAALHHYLVVPKKHIGSCKDLNKDH-IEMVESMVTVGKTILERNNFtd 109
Cdd:cd01277   1 DCIFCKIIAGEIP-SYKVY-EDDHVLAFLDINPASKGHTLVIPKKHYENLLDLDPEElAELILAAKKVARALKKALKA-- 76

                        90       100       110
                ....*....|....*....|....*....|
gi 21654864 110 ftdvrMGFHV------PPFCSVSHLHLHVI 133
Cdd:cd01277  77 -----DGLNIlqnngrAAGQVVFHVHVHVI 101
FHIT cd01275
FHIT (fragile histidine family): FHIT proteins, related to the HIT family carry a motif HxHxH ...
 32-149 1.89e-06

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: 44.59  E-value: 1.89e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21654864  32 CVFCRVAAGQEPETELLYcENKDLVCFKDIKPAALHHYLVVPKKHIGSCKDLNKDHIEMVESMVTVGKTILERNNFTDFT 111
Cdd:cd01275   1 CVFCDIPIKPDEDNLVFY-RTKHSFAVVNLYPYNPGHVLVVPYRHVPRLEDLTPEEIADLFKLVQLAMKALKVVYKPDGF 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 21654864 112 DVRMGFHVPPFCSVSHLHLHVIaPAK--EFGFLSRVVYRR 149
Cdd:cd01275  80 NIGINDGKAGGGIVPHVHIHIV-PRWngDTNFMPVIIYTK 118
HIT pfam01230
HIT domain;
51-134 3.36e-06

HIT domain;


Pssm-ID: 395984 [Multi-domain]  Cd Length: 98  Bit Score: 43.45  E-value: 3.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21654864    51 ENKDLVCFKDIKPAALHHYLVVPKKHIGSCKDLN----KDHIEMVESMVTVGKTILERNNFTdfTDVRMGFHVPPfcSVS 126
Cdd:pfam01230  11 EDDLVLAFLDIDPQAPGHILVIPKKHIRELHDLTpeelGDLMSVAQKVARALGKVFKADGYR--IVINNGAHAGQ--SVP 86


                  ....*...
gi 21654864   127 HLHLHVIA 134
Cdd:pfam01230  87 HLHIHVIP 94
PRK10687 PRK10687
purine nucleoside phosphoramidase; Provisional
 54-133 3.08e-04

purine nucleoside phosphoramidase; Provisional


Pssm-ID: 182648 [Multi-domain]  Cd Length: 119  Bit Score: 38.72  E-value: 3.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21654864   54 DLV-CFKDIKPAALHHYLVVPKKHIGSCKDLNKDHIEMVESMVTVGKTILERNNFTDftdvrMGFHVPPFCS------VS 126
Cdd:PRK10687  24 ELVtAFRDISPQAPTHILIIPNILIPTVNDVSAEHEQALGRMITVAAKIAEQEGIAE-----DGYRLIMNTNrhggqeVY 98


                 ....*..
gi 21654864  127 HLHLHVI 133
Cdd:PRK10687  99 HIHMHLL 105
COG5075 COG5075
Uncharacterized conserved protein [Function unknown];
65-133 3.26e-04

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 227407 [Multi-domain]  Cd Length: 305  Bit Score: 39.86  E-value: 3.26e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21654864  65 ALHHYLVVPKKHIGSCKDLNKDHIEMVESMVTVGKTILERNNFTDFTDVRMGFHVPPfcSVSHLHLHVI 133
Cdd:COG5075 183 SLYLVAIVYRTDIKTIRDLRYYHILWLIRLNNKILTEVPYQFGVDPNELRMFVHYQP--SYYHLHVHIV 249
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH