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Conserved domains on  [gi|1816539582|ref|WP_163532366|]
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histidine triad nucleotide-binding protein [Helicobacter suis]

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 ...
 3-102 6.72e-49

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: 150.79  E-value: 6.72e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816539582   3 NVFEKIIDGEIPCKKVLENEAFLAFEDINPKAPIHVLVIPKVGVKDFNAIT---PELIANMSAFILEVVEVLGIKQSGYR 79
Cdd:cd01276     2 CIFCKIIRGEIPAKKVYEDDEVLAFHDINPQAPVHILVIPKKHIASLSDATeedEELLGHLLSAAAKVAKDLGIAEDGYR 81

                          90       100
                  ....*....|....*....|...
gi 1816539582  80 LITNTGTDGGQEIPHLHFHILGG 102
Cdd:cd01276    82 LVINCGKDGGQEVFHLHLHLLGG 104
 
Name Accession Description Interval E-value
PKCI_related cd01276
Protein Kinase C Interacting protein related (PKCI): PKCI and related proteins belong to the ...
 3-102 6.72e-49

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: 150.79  E-value: 6.72e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816539582   3 NVFEKIIDGEIPCKKVLENEAFLAFEDINPKAPIHVLVIPKVGVKDFNAIT---PELIANMSAFILEVVEVLGIKQSGYR 79
Cdd:cd01276     2 CIFCKIIRGEIPAKKVYEDDEVLAFHDINPQAPVHILVIPKKHIASLSDATeedEELLGHLLSAAAKVAKDLGIAEDGYR 81

                          90       100
                  ....*....|....*....|...
gi 1816539582  80 LITNTGTDGGQEIPHLHFHILGG 102
Cdd:cd01276    82 LVINCGKDGGQEVFHLHLHLLGG 104
HinT COG0537
Purine nucleoside phosphoramidase/Ap4A hydrolase, histidine triade (HIT) family [Nucleotide ...
 1-104 2.69e-38

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: 125.06  E-value: 2.69e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816539582   1 MKNVFEKIIDGEIPCKKVLENEAFLAFEDINPKAPIHVLVIPKVGVKDFNAITPELIANMSAFILEVVEVL--GIKQSGY 78
Cdd:COG0537     1 MDCIFCKIIAGEIPALIVYEDEHVLAFLDINPYAPGHTLVIPKRHVASLFDLTPEELAELMRLAQKVAKALrkALGPDGF 80

                          90       100
                  ....*....|....*....|....*.
gi 1816539582  79 RLITNTGTDGGQEIPHLHFHILGGTK 104
Cdd:COG0537    81 NLGINNGEAAGQTVPHLHVHVIPRYE 106
HIT pfam01230
HIT domain;
11-105 1.59e-29

HIT domain;


Pssm-ID: 395984 [Multi-domain]  Cd Length: 98  Bit Score: 101.62  E-value: 1.59e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816539582  11 GEIPCKKVLENEAFLAFEDINPKAPIHVLVIPKVGVKDFNAITPELIANMSAFILEVVEVLGIKQS--GYRLITNTGTDG 88
Cdd:pfam01230   2 GEIPSTVVYEDDLVLAFLDIDPQAPGHILVIPKKHIRELHDLTPEELGDLMSVAQKVARALGKVFKadGYRIVINNGAHA 81

                          90
                  ....*....|....*..
gi 1816539582  89 GQEIPHLHFHILGGTKL 105
Cdd:pfam01230  82 GQSVPHLHIHVIPRRKH 98
PRK10687 PRK10687
purine nucleoside phosphoramidase; Provisional
 2-105 6.93e-25

purine nucleoside phosphoramidase; Provisional


Pssm-ID: 182648 [Multi-domain]  Cd Length: 119  Bit Score: 90.72  E-value: 6.93e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816539582   2 KNVFEKIIDGEIPCKKVLENEAFLAFEDINPKAPIHVLVIPKVGVKDFNAITPE---LIANMSAFILEVVEVLGIKQSGY 78
Cdd:PRK10687    4 ETIFSKIIRREIPSDIVYQDELVTAFRDISPQAPTHILIIPNILIPTVNDVSAEheqALGRMITVAAKIAEQEGIAEDGY 83

                          90       100
                  ....*....|....*....|....*..
gi 1816539582  79 RLITNTGTDGGQEIPHLHFHILGGTKL 105
Cdd:PRK10687   84 RLIMNTNRHGGQEVYHIHMHLLGGRPL 110
 
Name Accession Description Interval E-value
PKCI_related cd01276
Protein Kinase C Interacting protein related (PKCI): PKCI and related proteins belong to the ...
 3-102 6.72e-49

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: 150.79  E-value: 6.72e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816539582   3 NVFEKIIDGEIPCKKVLENEAFLAFEDINPKAPIHVLVIPKVGVKDFNAIT---PELIANMSAFILEVVEVLGIKQSGYR 79
Cdd:cd01276     2 CIFCKIIRGEIPAKKVYEDDEVLAFHDINPQAPVHILVIPKKHIASLSDATeedEELLGHLLSAAAKVAKDLGIAEDGYR 81

                          90       100
                  ....*....|....*....|...
gi 1816539582  80 LITNTGTDGGQEIPHLHFHILGG 102
Cdd:cd01276    82 LVINCGKDGGQEVFHLHLHLLGG 104
HinT COG0537
Purine nucleoside phosphoramidase/Ap4A hydrolase, histidine triade (HIT) family [Nucleotide ...
 1-104 2.69e-38

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: 125.06  E-value: 2.69e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816539582   1 MKNVFEKIIDGEIPCKKVLENEAFLAFEDINPKAPIHVLVIPKVGVKDFNAITPELIANMSAFILEVVEVL--GIKQSGY 78
Cdd:COG0537     1 MDCIFCKIIAGEIPALIVYEDEHVLAFLDINPYAPGHTLVIPKRHVASLFDLTPEELAELMRLAQKVAKALrkALGPDGF 80

                          90       100
                  ....*....|....*....|....*.
gi 1816539582  79 RLITNTGTDGGQEIPHLHFHILGGTK 104
Cdd:COG0537    81 NLGINNGEAAGQTVPHLHVHVIPRYE 106
HIT pfam01230
HIT domain;
11-105 1.59e-29

HIT domain;


Pssm-ID: 395984 [Multi-domain]  Cd Length: 98  Bit Score: 101.62  E-value: 1.59e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816539582  11 GEIPCKKVLENEAFLAFEDINPKAPIHVLVIPKVGVKDFNAITPELIANMSAFILEVVEVLGIKQS--GYRLITNTGTDG 88
Cdd:pfam01230   2 GEIPSTVVYEDDLVLAFLDIDPQAPGHILVIPKKHIRELHDLTPEELGDLMSVAQKVARALGKVFKadGYRIVINNGAHA 81

                          90
                  ....*....|....*..
gi 1816539582  89 GQEIPHLHFHILGGTKL 105
Cdd:pfam01230  82 GQSVPHLHIHVIPRRKH 98
HINT_subgroup cd01277
HINT (histidine triad nucleotide-binding protein) subgroup: Members of this CD belong to the ...
 3-99 2.08e-26

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: 93.83  E-value: 2.08e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816539582   3 NVFEKIIDGEIPCKKVLENEAFLAFEDINPKAPIHVLVIPKVGVKDFNAITPELIANMSAFILEVVEVLG--IKQSGYRL 80
Cdd:cd01277     2 CIFCKIIAGEIPSYKVYEDDHVLAFLDINPASKGHTLVIPKKHYENLLDLDPEELAELILAAKKVARALKkaLKADGLNI 81

                          90
                  ....*....|....*....
gi 1816539582  81 ITNTGTDGGQEIPHLHFHI 99
Cdd:cd01277    82 LQNNGRAAGQVVFHVHVHV 100
PRK10687 PRK10687
purine nucleoside phosphoramidase; Provisional
 2-105 6.93e-25

purine nucleoside phosphoramidase; Provisional


Pssm-ID: 182648 [Multi-domain]  Cd Length: 119  Bit Score: 90.72  E-value: 6.93e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816539582   2 KNVFEKIIDGEIPCKKVLENEAFLAFEDINPKAPIHVLVIPKVGVKDFNAITPE---LIANMSAFILEVVEVLGIKQSGY 78
Cdd:PRK10687    4 ETIFSKIIRREIPSDIVYQDELVTAFRDISPQAPTHILIIPNILIPTVNDVSAEheqALGRMITVAAKIAEQEGIAEDGY 83

                          90       100
                  ....*....|....*....|....*..
gi 1816539582  79 RLITNTGTDGGQEIPHLHFHILGGTKL 105
Cdd:PRK10687   84 RLIMNTNRHGGQEVYHIHMHLLGGRPL 110
DcpS_C pfam11969
Scavenger mRNA decapping enzyme C-term binding; This family consists of several scavenger mRNA ...
 4-101 6.47e-21

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: 80.34  E-value: 6.47e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816539582   4 VFEKIIDGEIPCKKVLENEAFLAFEDINPKAPIHVLVIPKVGVKDFNAITPE---LIANMSAFILEVVEvlGIKQSGYRL 80
Cdd:pfam11969   3 VFCIIAKGEEPERVVYEDEGFVVFKDIKPKAPLHLLVIPKRHIKSLRDLTPEhlpLLEHMREVAKKVIE--EKYIGVDRD 80

                          90       100
                  ....*....|....*....|.
gi 1816539582  81 ITNTGTDGGQEIPHLHFHILG 101
Cdd:pfam11969  81 ELRLGFHYPPSVYHLHLHVIS 101
HIT_like cd00468
HIT family: HIT (Histidine triad) proteins, named for a motif related to the sequence HxHxH ...
 18-101 1.78e-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: 1.78e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816539582  18 VLENEAFLAFEDINPKAPIHVLVIPKVGVKDFNAITPELIANMSAFILEVVEVLGIKQS--GYRLITNTGTDGGQEIPHL 95
Cdd:cd00468     1 VPDDEHSFAFVNLKPAAPGHVLVCPKRHVETLPDLDEALLADLVITAQRVAAELEKHGNvpSLTVFVNDGAAAGQSVPHV 80


                  ....*.
gi 1816539582  96 HFHILG 101
Cdd:cd00468    81 HLHVLP 86
FHIT cd01275
FHIT (fragile histidine family): FHIT proteins, related to the HIT family carry a motif HxHxH ...
 26-100 1.56e-09

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: 51.52  E-value: 1.56e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1816539582  26 AFEDINPKAPIHVLVIPKVGVKDFNAITPELIANMSAFILEVVEVLG--IKQSGYRLITNTGTDGGQEIPHLHFHIL 100
Cdd:cd01275    25 AVVNLYPYNPGHVLVVPYRHVPRLEDLTPEEIADLFKLVQLAMKALKvvYKPDGFNIGINDGKAGGGIVPHVHIHIV 101
GalT COG1085
Galactose-1-phosphate uridylyltransferase [Carbohydrate transport and metabolism];
2-99 1.92e-06

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


Pssm-ID: 440702 [Multi-domain]  Cd Length: 336  Bit Score: 44.44  E-value: 1.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816539582   2 KNVFEKIIDGEIPCKK--VLENEAFLAFEdinPKA---PIHVLVIPKVGVKDFNAITPELIANMSAFILEVVE----VLG 72
Cdd:COG1085   191 RCLLCDILAQELAAGErvVAENEHFVAFV---PFAarwPFETWILPKRHVSDFEELTDEERDDLARILKRVLRrldnLLG 267

                          90       100
                  ....*....|....*....|....*..
gi 1816539582  73 IkqSGYRLITNTGTDGGQEIPHLHFHI 99
Cdd:COG1085   268 D--FPYNMGLHQAPVDGEERDHYHWHL 292
aprataxin_related cd01278
aprataxin related: Aprataxin, a HINT family hydrolase is mutated in ataxia oculomotor apraxia ...
 18-100 2.89e-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: 2.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816539582  18 VLENEAFLAFEDINPKAPIHVLVIPKVGVKDFNAITPE---LIANMSAFILEV-VEVLGIKQSGYRLitntgtdGGQEIP 93
Cdd:cd01278    19 VYEDDRVVVFKDIYPKARHHYLVIPKEHIASLKALTKEdvpLLEHMETVGREKlLRSDNTDPSEFRF-------GFHAPP 91

                          90
                  ....*....|..
gi 1816539582  94 -----HLHFHIL 100
Cdd:cd01278    92 ftsvsHLHLHVI 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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