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Conserved domains on  [gi|685329142|ref|XP_009102671|]
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14 kDa zinc-binding protein [Brassica rapa]

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 ...
 71-175 1.11e-52

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: 163.50  E-value: 1.11e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685329142  71 PTIFDKIIAKEIPSDIVYEDENVLAFRDINPQAPVHVLVIPKLRDGltTLGKAEPRHIEVLGQLLHASKIVAEKEGIV-D 149
Cdd:cd01276    1 DCIFCKIIRGEIPAKKVYEDDEVLAFHDINPQAPVHILVIPKKHIA--SLSDATEEDEELLGHLLSAAAKVAKDLGIAeD 78

                         90       100
                 ....*....|....*....|....*.
gi 685329142 150 GFRVVINNGAEGCQSVYHLHLHVLGG 175
Cdd:cd01276   79 GYRLVINCGKDGGQEVFHLHLHLLGG 104
 
Name Accession Description Interval E-value
PKCI_related cd01276
Protein Kinase C Interacting protein related (PKCI): PKCI and related proteins belong to the ...
 71-175 1.11e-52

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: 163.50  E-value: 1.11e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685329142  71 PTIFDKIIAKEIPSDIVYEDENVLAFRDINPQAPVHVLVIPKLRDGltTLGKAEPRHIEVLGQLLHASKIVAEKEGIV-D 149
Cdd:cd01276    1 DCIFCKIIRGEIPAKKVYEDDEVLAFHDINPQAPVHILVIPKKHIA--SLSDATEEDEELLGHLLSAAAKVAKDLGIAeD 78

                         90       100
                 ....*....|....*....|....*.
gi 685329142 150 GFRVVINNGAEGCQSVYHLHLHVLGG 175
Cdd:cd01276   79 GYRLVINCGKDGGQEVFHLHLHLLGG 104
HinT COG0537
Purine nucleoside phosphoramidase/Ap4A hydrolase, histidine triade (HIT) family [Nucleotide ...
 71-178 5.27e-36

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: 121.98  E-value: 5.27e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685329142  71 PTIFDKIIAKEIPSDIVYEDENVLAFRDINPQAPVHVLVIPKlrdglttlgkaepRHI--------EVLGQLLHASKIVA 142
Cdd:COG0537    2 DCIFCKIIAGEIPALIVYEDEHVLAFLDINPYAPGHTLVIPK-------------RHVaslfdltpEELAELMRLAQKVA 68

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 685329142 143 E--KEGI-VDGFRVVINNGAEGCQSVYHLHLHVLGGRQM 178
Cdd:COG0537   69 KalRKALgPDGFNLGINNGEAAGQTVPHLHVHVIPRYEG 107
PRK10687 PRK10687
purine nucleoside phosphoramidase; Provisional
 72-178 7.65e-35

purine nucleoside phosphoramidase; Provisional


Pssm-ID: 182648 [Multi-domain]  Cd Length: 119  Bit Score: 118.84  E-value: 7.65e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685329142  72 TIFDKIIAKEIPSDIVYEDENVLAFRDINPQAPVHVLVIPKLRdgLTTLGKAEPRHIEVLGQLLHASKIVAEKEGIV-DG 150
Cdd:PRK10687   5 TIFSKIIRREIPSDIVYQDELVTAFRDISPQAPTHILIIPNIL--IPTVNDVSAEHEQALGRMITVAAKIAEQEGIAeDG 82

                         90       100
                 ....*....|....*....|....*...
gi 685329142 151 FRVVINNGAEGCQSVYHLHLHVLGGRQM 178
Cdd:PRK10687  83 YRLIMNTNRHGGQEVYHIHMHLLGGRPL 110
HIT pfam01230
HIT domain;
80-178 3.21e-33

HIT domain;


Pssm-ID: 395984 [Multi-domain]  Cd Length: 98  Bit Score: 113.94  E-value: 3.21e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685329142   80 KEIPSDIVYEDENVLAFRDINPQAPVHVLVIPKlrDGLTTLGKAEPrhiEVLGQLLHASKIVAEKEGIV---DGFRVVIN 156
Cdd:pfam01230   2 GEIPSTVVYEDDLVLAFLDIDPQAPGHILVIPK--KHIRELHDLTP---EELGDLMSVAQKVARALGKVfkaDGYRIVIN 76

                          90       100
                  ....*....|....*....|..
gi 685329142  157 NGAEGCQSVYHLHLHVLGGRQM 178
Cdd:pfam01230  77 NGAHAGQSVPHLHIHVIPRRKH 98
 
Name Accession Description Interval E-value
PKCI_related cd01276
Protein Kinase C Interacting protein related (PKCI): PKCI and related proteins belong to the ...
 71-175 1.11e-52

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: 163.50  E-value: 1.11e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685329142  71 PTIFDKIIAKEIPSDIVYEDENVLAFRDINPQAPVHVLVIPKLRDGltTLGKAEPRHIEVLGQLLHASKIVAEKEGIV-D 149
Cdd:cd01276    1 DCIFCKIIRGEIPAKKVYEDDEVLAFHDINPQAPVHILVIPKKHIA--SLSDATEEDEELLGHLLSAAAKVAKDLGIAeD 78

                         90       100
                 ....*....|....*....|....*.
gi 685329142 150 GFRVVINNGAEGCQSVYHLHLHVLGG 175
Cdd:cd01276   79 GYRLVINCGKDGGQEVFHLHLHLLGG 104
HinT COG0537
Purine nucleoside phosphoramidase/Ap4A hydrolase, histidine triade (HIT) family [Nucleotide ...
 71-178 5.27e-36

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: 121.98  E-value: 5.27e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685329142  71 PTIFDKIIAKEIPSDIVYEDENVLAFRDINPQAPVHVLVIPKlrdglttlgkaepRHI--------EVLGQLLHASKIVA 142
Cdd:COG0537    2 DCIFCKIIAGEIPALIVYEDEHVLAFLDINPYAPGHTLVIPK-------------RHVaslfdltpEELAELMRLAQKVA 68

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 685329142 143 E--KEGI-VDGFRVVINNGAEGCQSVYHLHLHVLGGRQM 178
Cdd:COG0537   69 KalRKALgPDGFNLGINNGEAAGQTVPHLHVHVIPRYEG 107
PRK10687 PRK10687
purine nucleoside phosphoramidase; Provisional
 72-178 7.65e-35

purine nucleoside phosphoramidase; Provisional


Pssm-ID: 182648 [Multi-domain]  Cd Length: 119  Bit Score: 118.84  E-value: 7.65e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685329142  72 TIFDKIIAKEIPSDIVYEDENVLAFRDINPQAPVHVLVIPKLRdgLTTLGKAEPRHIEVLGQLLHASKIVAEKEGIV-DG 150
Cdd:PRK10687   5 TIFSKIIRREIPSDIVYQDELVTAFRDISPQAPTHILIIPNIL--IPTVNDVSAEHEQALGRMITVAAKIAEQEGIAeDG 82

                         90       100
                 ....*....|....*....|....*...
gi 685329142 151 FRVVINNGAEGCQSVYHLHLHVLGGRQM 178
Cdd:PRK10687  83 YRLIMNTNRHGGQEVYHIHMHLLGGRPL 110
HIT pfam01230
HIT domain;
80-178 3.21e-33

HIT domain;


Pssm-ID: 395984 [Multi-domain]  Cd Length: 98  Bit Score: 113.94  E-value: 3.21e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685329142   80 KEIPSDIVYEDENVLAFRDINPQAPVHVLVIPKlrDGLTTLGKAEPrhiEVLGQLLHASKIVAEKEGIV---DGFRVVIN 156
Cdd:pfam01230   2 GEIPSTVVYEDDLVLAFLDIDPQAPGHILVIPK--KHIRELHDLTP---EELGDLMSVAQKVARALGKVfkaDGYRIVIN 76

                          90       100
                  ....*....|....*....|..
gi 685329142  157 NGAEGCQSVYHLHLHVLGGRQM 178
Cdd:pfam01230  77 NGAHAGQSVPHLHIHVIPRRKH 98
DcpS_C pfam11969
Scavenger mRNA decapping enzyme C-term binding; This family consists of several scavenger mRNA ...
 72-174 6.95e-30

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: 105.77  E-value: 6.95e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685329142   72 TIFDKIIAKEIPSDIVYEDENVLAFRDINPQAPVHVLVIPKlrDGLTTLGKAEPRHIEVLGQLLHASKIVAEKEGIvDGF 151
Cdd:pfam11969   2 WVFCIIAKGEEPERVVYEDEGFVVFKDIKPKAPLHLLVIPK--RHIKSLRDLTPEHLPLLEHMREVAKKVIEEKYI-GVD 78

                          90       100
                  ....*....|....*....|...
gi 685329142  152 RVVINNGAEGCQSVYHLHLHVLG 174
Cdd:pfam11969  79 RDELRLGFHYPPSVYHLHLHVIS 101
HINT_subgroup cd01277
HINT (histidine triad nucleotide-binding protein) subgroup: Members of this CD belong to the ...
 73-172 5.26e-27

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: 98.06  E-value: 5.26e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685329142  73 IFDKIIAKEIPSDIVYEDENVLAFRDINPQAPVHVLVIPKlrdglttlgkaepRHI--------EVLGQLLHASKIVA-- 142
Cdd:cd01277    3 IFCKIIAGEIPSYKVYEDDHVLAFLDINPASKGHTLVIPK-------------KHYenlldldpEELAELILAAKKVAra 69

                         90       100       110
                 ....*....|....*....|....*....|.
gi 685329142 143 -EKEGIVDGFRVVINNGAEGCQSVYHLHLHV 172
Cdd:cd01277   70 lKKALKADGLNILQNNGRAAGQVVFHVHVHV 100
HIT_like cd00468
HIT family: HIT (Histidine triad) proteins, named for a motif related to the sequence HxHxH ...
 87-174 2.74e-17

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: 72.50  E-value: 2.74e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685329142  87 VYEDENVLAFRDINPQAPVHVLVIPKLR-DGLTTLGKAEPRHIEVLGQLLHAskiVAEKEGIVDGFRVVINNGAEGCQSV 165
Cdd:cd00468    1 VPDDEHSFAFVNLKPAAPGHVLVCPKRHvETLPDLDEALLADLVITAQRVAA---ELEKHGNVPSLTVFVNDGAAAGQSV 77


                 ....*....
gi 685329142 166 YHLHLHVLG 174
Cdd:cd00468   78 PHVHLHVLP 86
aprataxin_related cd01278
aprataxin related: Aprataxin, a HINT family hydrolase is mutated in ataxia oculomotor apraxia ...
 83-173 6.42e-10

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: 53.93  E-value: 6.42e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685329142  83 PSDIVYEDENVLAFRDINPQAPVHVLVIPKLR-DGLTTLGKAeprHIEVLGQLLHASKIVAEKEGIVDGFRVVINNGAEG 161
Cdd:cd01278   15 PEDQVYEDDRVVVFKDIYPKARHHYLVIPKEHiASLKALTKE---DVPLLEHMETVGREKLLRSDNTDPSEFRFGFHAPP 91

                         90
                 ....*....|..
gi 685329142 162 CQSVYHLHLHVL 173
Cdd:cd01278   92 FTSVSHLHLHVI 103
FHIT cd01275
FHIT (fragile histidine family): FHIT proteins, related to the HIT family carry a motif HxHxH ...
 86-173 2.55e-08

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: 49.98  E-value: 2.55e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685329142  86 IVYEDENVLAFRDINPQAPVHVLVIPKL-RDGLTTLGKAEprhIEVLGQLLHASKIVAEKEGIVDGFRVVINNGAEGCQS 164
Cdd:cd01275   16 VFYRTKHSFAVVNLYPYNPGHVLVVPYRhVPRLEDLTPEE---IADLFKLVQLAMKALKVVYKPDGFNIGINDGKAGGGI 92


                 ....*....
gi 685329142 165 VYHLHLHVL 173
Cdd:cd01275   93 VPHVHIHIV 101
 
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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