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Conserved domains on  [gi|451172109|ref|NP_001094295|]
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adenosine 5'-monophosphoramidase HINT3 isoform 1 [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

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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 ...
 40-143 2.15e-51

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: 159.86  E-value: 2.15e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451172109  40 NCVFCRVAAGQEPETELLYCENKDLVCFKDIKPAALHHYLVVPKKHIGSCKDLNKDHIEMVESMVTVGKTILERNNFTDF 119
Cdd:cd01278    1 LCHFCDIAKRRDPDPEDQVYEDDRVVVFKDIYPKARHHYLVIPKEHIASLKALTKEDVPLLEHMETVGREKLLRSDNTDP 80

                         90       100
                 ....*....|....*....|....
gi 451172109 120 TDVRMGFHVPPFCSVSHLHLHVIA 143
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 ...
 40-143 2.15e-51

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: 159.86  E-value: 2.15e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451172109  40 NCVFCRVAAGQEPETELLYCENKDLVCFKDIKPAALHHYLVVPKKHIGSCKDLNKDHIEMVESMVTVGKTILERNNFTDF 119
Cdd:cd01278    1 LCHFCDIAKRRDPDPEDQVYEDDRVVVFKDIYPKARHHYLVIPKEHIASLKALTKEDVPLLEHMETVGREKLLRSDNTDP 80

                         90       100
                 ....*....|....*....|....
gi 451172109 120 TDVRMGFHVPPFCSVSHLHLHVIA 143
Cdd:cd01278   81 SEFRFGFHAPPFTSVSHLHLHVIA 104
DcpS_C pfam11969
Scavenger mRNA decapping enzyme C-term binding; This family consists of several scavenger mRNA ...
 40-153 3.32e-42

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: 136.97  E-value: 3.32e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451172109   40 NCVFCRVAAGQEPETELLycENKDLVCFKDIKPAALHHYLVVPKKHIGSCKDLNKDHIEMVESMVTVGKTILERNNFT-D 118
Cdd:pfam11969   1 KWVFCIIAKGEEPERVVY--EDEGFVVFKDIKPKAPLHLLVIPKRHIKSLRDLTPEHLPLLEHMREVAKKVIEEKYIGvD 78

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 451172109  119 FTDVRMGFHVPPfcSVSHLHLHVIAPAKEFGFLSR 153
Cdd:pfam11969  79 RDELRLGFHYPP--SVYHLHLHVISPDFESLGLGR 111
HinT COG0537
Purine nucleoside phosphoramidase/Ap4A hydrolase, histidine triade (HIT) family [Nucleotide ...
 39-142 4.00e-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: 68.05  E-value: 4.00e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451172109  39 SNCVFCRVAAGQEPETELLycENKDLVCFKDIKPAALHHYLVVPKKHIGSCKDLNKDhiEMVESMVTVGKTILERNNFTD 118
Cdd:COG0537    1 MDCIFCKIIAGEIPALIVY--EDEHVLAFLDINPYAPGHTLVIPKRHVASLFDLTPE--ELAELMRLAQKVAKALRKALG 76

                         90       100
                 ....*....|....*....|....*.
gi 451172109 119 FTDVRMGFHVPPFC--SVSHLHLHVI 142
Cdd:COG0537   77 PDGFNLGINNGEAAgqTVPHLHVHVI 102
PRK10687 PRK10687
purine nucleoside phosphoramidase; Provisional
 63-142 3.46e-04

purine nucleoside phosphoramidase; Provisional


Pssm-ID: 182648 [Multi-domain]  Cd Length: 119  Bit Score: 38.72  E-value: 3.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451172109  63 DLV-CFKDIKPAALHHYLVVPKKHIGSCKDLNKDHIEMVESMVTVGKTILERNNFTDftdvrMGFHVPPFCS------VS 135
Cdd:PRK10687  24 ELVtAFRDISPQAPTHILIIPNILIPTVNDVSAEHEQALGRMITVAAKIAEQEGIAE-----DGYRLIMNTNrhggqeVY 98


                 ....*..
gi 451172109 136 HLHLHVI 142
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 ...
 40-143 2.15e-51

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: 159.86  E-value: 2.15e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451172109  40 NCVFCRVAAGQEPETELLYCENKDLVCFKDIKPAALHHYLVVPKKHIGSCKDLNKDHIEMVESMVTVGKTILERNNFTDF 119
Cdd:cd01278    1 LCHFCDIAKRRDPDPEDQVYEDDRVVVFKDIYPKARHHYLVIPKEHIASLKALTKEDVPLLEHMETVGREKLLRSDNTDP 80

                         90       100
                 ....*....|....*....|....
gi 451172109 120 TDVRMGFHVPPFCSVSHLHLHVIA 143
Cdd:cd01278   81 SEFRFGFHAPPFTSVSHLHLHVIA 104
DcpS_C pfam11969
Scavenger mRNA decapping enzyme C-term binding; This family consists of several scavenger mRNA ...
 40-153 3.32e-42

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: 136.97  E-value: 3.32e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451172109   40 NCVFCRVAAGQEPETELLycENKDLVCFKDIKPAALHHYLVVPKKHIGSCKDLNKDHIEMVESMVTVGKTILERNNFT-D 118
Cdd:pfam11969   1 KWVFCIIAKGEEPERVVY--EDEGFVVFKDIKPKAPLHLLVIPKRHIKSLRDLTPEHLPLLEHMREVAKKVIEEKYIGvD 78

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 451172109  119 FTDVRMGFHVPPfcSVSHLHLHVIAPAKEFGFLSR 153
Cdd:pfam11969  79 RDELRLGFHYPP--SVYHLHLHVISPDFESLGLGR 111
PKCI_related cd01276
Protein Kinase C Interacting protein related (PKCI): PKCI and related proteins belong to the ...
 40-143 4.61e-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: 74.91  E-value: 4.61e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451172109  40 NCVFCRVAAGQEPETELLycENKDLVCFKDIKPAALHHYLVVPKKHIGSCKDLN-KDHIEMVESMVTVGKTILERNNFTD 118
Cdd:cd01276    1 DCIFCKIIRGEIPAKKVY--EDDEVLAFHDINPQAPVHILVIPKKHIASLSDATeEDEELLGHLLSAAAKVAKDLGIAED 78

                         90       100       110
                 ....*....|....*....|....*....|.
gi 451172109 119 ftdvrmGFHVPPFC------SVSHLHLHVIA 143
Cdd:cd01276   79 ------GYRLVINCgkdggqEVFHLHLHLLG 103
HinT COG0537
Purine nucleoside phosphoramidase/Ap4A hydrolase, histidine triade (HIT) family [Nucleotide ...
 39-142 4.00e-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: 68.05  E-value: 4.00e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451172109  39 SNCVFCRVAAGQEPETELLycENKDLVCFKDIKPAALHHYLVVPKKHIGSCKDLNKDhiEMVESMVTVGKTILERNNFTD 118
Cdd:COG0537    1 MDCIFCKIIAGEIPALIVY--EDEHVLAFLDINPYAPGHTLVIPKRHVASLFDLTPE--ELAELMRLAQKVAKALRKALG 76

                         90       100
                 ....*....|....*....|....*.
gi 451172109 119 FTDVRMGFHVPPFC--SVSHLHLHVI 142
Cdd:COG0537   77 PDGFNLGINNGEAAgqTVPHLHVHVI 102
HIT_like cd00468
HIT family: HIT (Histidine triad) proteins, named for a motif related to the sequence HxHxH ...
 65-143 1.66e-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: 62.49  E-value: 1.66e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451172109  65 VCFKDIKPAALHHYLVVPKKHIGSCKDLNKDhiEMVESMVTVGK--TILERNNFTDFTDVRMGFHVPPFCSVSHLHLHVI 142
Cdd:cd00468    8 FAFVNLKPAAPGHVLVCPKRHVETLPDLDEA--LLADLVITAQRvaAELEKHGNVPSLTVFVNDGAAAGQSVPHVHLHVL 85


                 .
gi 451172109 143 A 143
Cdd:cd00468   86 P 86
HINT_subgroup cd01277
HINT (histidine triad nucleotide-binding protein) subgroup: Members of this CD belong to the ...
 40-142 2.17e-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: 46.83  E-value: 2.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451172109  40 NCVFCRVAAGQEPeTELLYcENKDLVCFKDIKPAALHHYLVVPKKHIGSCKDLNKDH-IEMVESMVTVGKTILERNNFtd 118
Cdd:cd01277    1 DCIFCKIIAGEIP-SYKVY-EDDHVLAFLDINPASKGHTLVIPKKHYENLLDLDPEElAELILAAKKVARALKKALKA-- 76

                         90       100       110
                 ....*....|....*....|....*....|
gi 451172109 119 ftdvrMGFHV------PPFCSVSHLHLHVI 142
Cdd:cd01277   77 -----DGLNIlqnngrAAGQVVFHVHVHVI 101
FHIT cd01275
FHIT (fragile histidine family): FHIT proteins, related to the HIT family carry a motif HxHxH ...
 41-158 1.24e-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: 45.36  E-value: 1.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451172109  41 CVFCRVAAGQEPETELLYcENKDLVCFKDIKPAALHHYLVVPKKHIGSCKDLNKDHIEMVESMVTVGKTILERNNFTDFT 120
Cdd:cd01275    1 CVFCDIPIKPDEDNLVFY-RTKHSFAVVNLYPYNPGHVLVVPYRHVPRLEDLTPEEIADLFKLVQLAMKALKVVYKPDGF 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 451172109 121 DVRMGFHVPPFCSVSHLHLHVIaPAK--EFGFLSRVVYRR 158
Cdd:cd01275   80 NIGINDGKAGGGIVPHVHIHIV-PRWngDTNFMPVIIYTK 118
HIT pfam01230
HIT domain;
51-143 1.79e-06

HIT domain;


Pssm-ID: 395984 [Multi-domain]  Cd Length: 98  Bit Score: 44.22  E-value: 1.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451172109   51 EPETELLYcENKDLVCFKDIKPAALHHYLVVPKKHIGSCKDLN----KDHIEMVESMVTVGKTILERNNFTdfTDVRMGF 126
Cdd:pfam01230   3 EIPSTVVY-EDDLVLAFLDIDPQAPGHILVIPKKHIRELHDLTpeelGDLMSVAQKVARALGKVFKADGYR--IVINNGA 79

                          90
                  ....*....|....*..
gi 451172109  127 HVPPfcSVSHLHLHVIA 143
Cdd:pfam01230  80 HAGQ--SVPHLHIHVIP 94
COG5075 COG5075
Uncharacterized conserved protein [Function unknown];
74-142 2.76e-04

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 227407 [Multi-domain]  Cd Length: 305  Bit Score: 40.24  E-value: 2.76e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 451172109  74 ALHHYLVVPKKHIGSCKDLNKDHIEMVESMVTVGKTILERNNFTDFTDVRMGFHVPPfcSVSHLHLHVI 142
Cdd:COG5075  183 SLYLVAIVYRTDIKTIRDLRYYHILWLIRLNNKILTEVPYQFGVDPNELRMFVHYQP--SYYHLHVHIV 249
PRK10687 PRK10687
purine nucleoside phosphoramidase; Provisional
 63-142 3.46e-04

purine nucleoside phosphoramidase; Provisional


Pssm-ID: 182648 [Multi-domain]  Cd Length: 119  Bit Score: 38.72  E-value: 3.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 451172109  63 DLV-CFKDIKPAALHHYLVVPKKHIGSCKDLNKDHIEMVESMVTVGKTILERNNFTDftdvrMGFHVPPFCS------VS 135
Cdd:PRK10687  24 ELVtAFRDISPQAPTHILIIPNILIPTVNDVSAEHEQALGRMITVAAKIAEQEGIAE-----DGYRLIMNTNrhggqeVY 98


                 ....*..
gi 451172109 136 HLHLHVI 142
Cdd:PRK10687  99 HIHMHLL 105
 
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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