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Conserved domains on  [gi|17506713|ref|NP_492056|]
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Histidine triad nucleotide-binding protein 1 [Caenorhabditis elegans]

Protein Classification

histidine triad nucleotide-binding protein( domain architecture ID 10101095)

histidine triad nucleotide-binding protein of the histidine triad family 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
PKCI_related cd01276
Protein Kinase C Interacting protein related (PKCI): PKCI and related proteins belong to the ...
 20-122 3.51e-57

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: 172.75  E-value: 3.51e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506713  20 DTLFGKIIRKEIPAKIIFEDDEALAFHDVSPQAPIHFLVIPKRRIDMLENAVDSDAALIGKLMVTASKVAKQLGMA-NGY 98
Cdd:cd01276   1 DCIFCKIIRGEIPAKKVYEDDEVLAFHDINPQAPVHILVIPKKHIASLSDATEEDEELLGHLLSAAAKVAKDLGIAeDGY 80

                        90       100
                ....*....|....*....|....
gi 17506713  99 RVVVNNGKDGAQSVFHLHLHVLGG 122
Cdd:cd01276  81 RLVINCGKDGGQEVFHLHLHLLGG 104
 
Name Accession Description Interval E-value
PKCI_related cd01276
Protein Kinase C Interacting protein related (PKCI): PKCI and related proteins belong to the ...
 20-122 3.51e-57

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: 172.75  E-value: 3.51e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506713  20 DTLFGKIIRKEIPAKIIFEDDEALAFHDVSPQAPIHFLVIPKRRIDMLENAVDSDAALIGKLMVTASKVAKQLGMA-NGY 98
Cdd:cd01276   1 DCIFCKIIRGEIPAKKVYEDDEVLAFHDINPQAPVHILVIPKKHIASLSDATEEDEELLGHLLSAAAKVAKDLGIAeDGY 80

                        90       100
                ....*....|....*....|....
gi 17506713  99 RVVVNNGKDGAQSVFHLHLHVLGG 122
Cdd:cd01276  81 RLVINCGKDGGQEVFHLHLHLLGG 104
HinT COG0537
Purine nucleoside phosphoramidase/Ap4A hydrolase, histidine triade (HIT) family [Nucleotide ...
 19-123 5.82e-37

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: 122.36  E-value: 5.82e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506713  19 NDTLFGKIIRKEIPAKIIFEDDEALAFHDVSPQAPIHFLVIPKRRIDmleNAVDSDAALIGKLMVTASKVAKQLGMA--- 95
Cdd:COG0537   1 MDCIFCKIIAGEIPALIVYEDEHVLAFLDINPYAPGHTLVIPKRHVA---SLFDLTPEELAELMRLAQKVAKALRKAlgp 77

                        90       100
                ....*....|....*....|....*...
gi 17506713  96 NGYRVVVNNGKDGAQSVFHLHLHVLGGR 123
Cdd:COG0537  78 DGFNLGINNGEAAGQTVPHLHVHVIPRY 105
HIT pfam01230
HIT domain;
28-125 7.83e-36

HIT domain;


Pssm-ID: 395984 [Multi-domain]  Cd Length: 98  Bit Score: 118.57  E-value: 7.83e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506713    28 RKEIPAKIIFEDDEALAFHDVSPQAPIHFLVIPKRRIDMLENAvdsDAALIGKLMVTASKVAKQLGM---ANGYRVVVNN 104
Cdd:pfam01230   1 RGEIPSTVVYEDDLVLAFLDIDPQAPGHILVIPKKHIRELHDL---TPEELGDLMSVAQKVARALGKvfkADGYRIVINN 77

                          90       100
                  ....*....|....*....|.
gi 17506713   105 GKDGAQSVFHLHLHVLGGRQL 125
Cdd:pfam01230  78 GAHAGQSVPHLHIHVIPRRKH 98
PRK10687 PRK10687
purine nucleoside phosphoramidase; Provisional
 18-125 4.93e-34

purine nucleoside phosphoramidase; Provisional


Pssm-ID: 182648 [Multi-domain]  Cd Length: 119  Bit Score: 114.60  E-value: 4.93e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506713   18 ANDTLFGKIIRKEIPAKIIFEDDEALAFHDVSPQAPIHFLVIPKRRIDMLENAVDSDAALIGKLMVTASKVAKQLGMA-N 96
Cdd:PRK10687   2 AEETIFSKIIRREIPSDIVYQDELVTAFRDISPQAPTHILIIPNILIPTVNDVSAEHEQALGRMITVAAKIAEQEGIAeD 81

                         90       100
                 ....*....|....*....|....*....
gi 17506713   97 GYRVVVNNGKDGAQSVFHLHLHVLGGRQL 125
Cdd:PRK10687  82 GYRLIMNTNRHGGQEVYHIHMHLLGGRPL 110
 
Name Accession Description Interval E-value
PKCI_related cd01276
Protein Kinase C Interacting protein related (PKCI): PKCI and related proteins belong to the ...
 20-122 3.51e-57

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: 172.75  E-value: 3.51e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506713  20 DTLFGKIIRKEIPAKIIFEDDEALAFHDVSPQAPIHFLVIPKRRIDMLENAVDSDAALIGKLMVTASKVAKQLGMA-NGY 98
Cdd:cd01276   1 DCIFCKIIRGEIPAKKVYEDDEVLAFHDINPQAPVHILVIPKKHIASLSDATEEDEELLGHLLSAAAKVAKDLGIAeDGY 80

                        90       100
                ....*....|....*....|....
gi 17506713  99 RVVVNNGKDGAQSVFHLHLHVLGG 122
Cdd:cd01276  81 RLVINCGKDGGQEVFHLHLHLLGG 104
HinT COG0537
Purine nucleoside phosphoramidase/Ap4A hydrolase, histidine triade (HIT) family [Nucleotide ...
 19-123 5.82e-37

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: 122.36  E-value: 5.82e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506713  19 NDTLFGKIIRKEIPAKIIFEDDEALAFHDVSPQAPIHFLVIPKRRIDmleNAVDSDAALIGKLMVTASKVAKQLGMA--- 95
Cdd:COG0537   1 MDCIFCKIIAGEIPALIVYEDEHVLAFLDINPYAPGHTLVIPKRHVA---SLFDLTPEELAELMRLAQKVAKALRKAlgp 77

                        90       100
                ....*....|....*....|....*...
gi 17506713  96 NGYRVVVNNGKDGAQSVFHLHLHVLGGR 123
Cdd:COG0537  78 DGFNLGINNGEAAGQTVPHLHVHVIPRY 105
HIT pfam01230
HIT domain;
28-125 7.83e-36

HIT domain;


Pssm-ID: 395984 [Multi-domain]  Cd Length: 98  Bit Score: 118.57  E-value: 7.83e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506713    28 RKEIPAKIIFEDDEALAFHDVSPQAPIHFLVIPKRRIDMLENAvdsDAALIGKLMVTASKVAKQLGM---ANGYRVVVNN 104
Cdd:pfam01230   1 RGEIPSTVVYEDDLVLAFLDIDPQAPGHILVIPKKHIRELHDL---TPEELGDLMSVAQKVARALGKvfkADGYRIVINN 77

                          90       100
                  ....*....|....*....|.
gi 17506713   105 GKDGAQSVFHLHLHVLGGRQL 125
Cdd:pfam01230  78 GAHAGQSVPHLHIHVIPRRKH 98
PRK10687 PRK10687
purine nucleoside phosphoramidase; Provisional
 18-125 4.93e-34

purine nucleoside phosphoramidase; Provisional


Pssm-ID: 182648 [Multi-domain]  Cd Length: 119  Bit Score: 114.60  E-value: 4.93e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506713   18 ANDTLFGKIIRKEIPAKIIFEDDEALAFHDVSPQAPIHFLVIPKRRIDMLENAVDSDAALIGKLMVTASKVAKQLGMA-N 96
Cdd:PRK10687   2 AEETIFSKIIRREIPSDIVYQDELVTAFRDISPQAPTHILIIPNILIPTVNDVSAEHEQALGRMITVAAKIAEQEGIAeD 81

                         90       100
                 ....*....|....*....|....*....
gi 17506713   97 GYRVVVNNGKDGAQSVFHLHLHVLGGRQL 125
Cdd:PRK10687  82 GYRLIMNTNRHGGQEVYHIHMHLLGGRPL 110
HINT_subgroup cd01277
HINT (histidine triad nucleotide-binding protein) subgroup: Members of this CD belong to the ...
 20-119 3.14e-28

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: 99.22  E-value: 3.14e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506713  20 DTLFGKIIRKEIPAKIIFEDDEALAFHDVSPQAPIHFLVIPKRRidmLENAVDSDAALIGKLMVTASKVAKQLGMA---N 96
Cdd:cd01277   1 DCIFCKIIAGEIPSYKVYEDDHVLAFLDINPASKGHTLVIPKKH---YENLLDLDPEELAELILAAKKVARALKKAlkaD 77

                        90       100
                ....*....|....*....|...
gi 17506713  97 GYRVVVNNGKDGAQSVFHLHLHV 119
Cdd:cd01277  78 GLNILQNNGRAAGQVVFHVHVHV 100
DcpS_C pfam11969
Scavenger mRNA decapping enzyme C-term binding; This family consists of several scavenger mRNA ...
 23-121 1.02e-23

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: 88.05  E-value: 1.02e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506713    23 FGKIIRKEIPAKIIFEDDEALAFHDVSPQAPIHFLVIPKRRIDMLENAVDSDAALIGKLMVTASKVAKQLGMAnGYRVVV 102
Cdd:pfam11969   4 FCIIAKGEEPERVVYEDEGFVVFKDIKPKAPLHLLVIPKRHIKSLRDLTPEHLPLLEHMREVAKKVIEEKYIG-VDRDEL 82

                          90
                  ....*....|....*....
gi 17506713   103 NNGKDGAQSVFHLHLHVLG 121
Cdd:pfam11969  83 RLGFHYPPSVYHLHLHVIS 101
HIT_like cd00468
HIT family: HIT (Histidine triad) proteins, named for a motif related to the sequence HxHxH ...
 36-121 1.12e-20

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: 79.82  E-value: 1.12e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506713  36 IFEDDEALAFHDVSPQAPIHFLVIPKRRIDMLEnavDSDAALIGKLMVTASKVAKQL---GMANGYRVVVNNGKDGAQSV 112
Cdd:cd00468   1 VPDDEHSFAFVNLKPAAPGHVLVCPKRHVETLP---DLDEALLADLVITAQRVAAELekhGNVPSLTVFVNDGAAAGQSV 77


                ....*....
gi 17506713 113 FHLHLHVLG 121
Cdd:cd00468  78 PHVHLHVLP 86
FHIT cd01275
FHIT (fragile histidine family): FHIT proteins, related to the HIT family carry a motif HxHxH ...
 23-120 2.66e-14

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: 64.23  E-value: 2.66e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506713  23 FGKIIRKEIPAKIIF-EDDEALAFHDVSPQAPIHFLVIPKRRIDMLENAVDSDAALIGKLMVTASKVAKQLGMANGYRVV 101
Cdd:cd01275   3 FCDIPIKPDEDNLVFyRTKHSFAVVNLYPYNPGHVLVVPYRHVPRLEDLTPEEIADLFKLVQLAMKALKVVYKPDGFNIG 82

                        90
                ....*....|....*....
gi 17506713 102 VNNGKDGAQSVFHLHLHVL 120
Cdd:cd01275  83 INDGKAGGGIVPHVHIHIV 101
aprataxin_related cd01278
aprataxin related: Aprataxin, a HINT family hydrolase is mutated in ataxia oculomotor apraxia ...
 27-120 5.09e-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: 42.37  E-value: 5.09e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506713  27 IRKEIPAKIIFEDDEALAFHDVSPQAPIHFLVIPKRRIDMLENAVDSDAALIGKLMVTASKVAKQLGMANGYRVVVNNGK 106
Cdd:cd01278  10 RRDPDPEDQVYEDDRVVVFKDIYPKARHHYLVIPKEHIASLKALTKEDVPLLEHMETVGREKLLRSDNTDPSEFRFGFHA 89

                        90
                ....*....|....
gi 17506713 107 DGAQSVFHLHLHVL 120
Cdd:cd01278  90 PPFTSVSHLHLHVI 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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