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Conserved domains on  [gi|1582669069|gb|TBE49419|]
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HIT family protein [Rhizobium ruizarguesonis]

Protein Classification

HIT family protein( domain architecture ID 10001677)

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

CATH:  3.30.428.10
Gene Ontology:  GO:1904047
SCOP:  3000223

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HinT COG0537
Purine nucleoside phosphoramidase/Ap4A hydrolase, histidine triade (HIT) family [Nucleotide ...
9-140 8.95e-55

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: 168.20  E-value: 8.95e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582669069   9 DNNIFAKILRGEIPSHRVYEDEYTIAFMDVMPQAPGHVLVLPKAPSRNLLDADPATLTHAISVVQKIANAVKDVFDADGV 88
Cdd:COG0537     1 MDCIFCKIIAGEIPALIVYEDEHVLAFLDINPYAPGHTLVIPKRHVASLFDLTPEELAELMRLAQKVAKALRKALGPDGF 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1582669069  89 FIAQFNEPAAGQTVFHLHFHVIPRHEGAALKPHS-GKMEDGAVLAANAEKIRA 140
Cdd:COG0537    81 NLGINNGEAAGQTVPHLHVHVIPRYEGDDNFMPViGTKVDPEELEETARKLRA 133
 
Name Accession Description Interval E-value
HinT COG0537
Purine nucleoside phosphoramidase/Ap4A hydrolase, histidine triade (HIT) family [Nucleotide ...
9-140 8.95e-55

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: 168.20  E-value: 8.95e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582669069   9 DNNIFAKILRGEIPSHRVYEDEYTIAFMDVMPQAPGHVLVLPKAPSRNLLDADPATLTHAISVVQKIANAVKDVFDADGV 88
Cdd:COG0537     1 MDCIFCKIIAGEIPALIVYEDEHVLAFLDINPYAPGHTLVIPKRHVASLFDLTPEELAELMRLAQKVAKALRKALGPDGF 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1582669069  89 FIAQFNEPAAGQTVFHLHFHVIPRHEGAALKPHS-GKMEDGAVLAANAEKIRA 140
Cdd:COG0537    81 NLGINNGEAAGQTVPHLHVHVIPRYEGDDNFMPViGTKVDPEELEETARKLRA 133
HINT_subgroup cd01277
HINT (histidine triad nucleotide-binding protein) subgroup: Members of this CD belong to the ...
10-112 1.13e-49

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: 154.30  E-value: 1.13e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582669069  10 NNIFAKILRGEIPSHRVYEDEYTIAFMDVMPQAPGHVLVLPKAPSRNLLDADPATLTHAISVVQKIANAVKDVFDADGVF 89
Cdd:cd01277     1 DCIFCKIIAGEIPSYKVYEDDHVLAFLDINPASKGHTLVIPKKHYENLLDLDPEELAELILAAKKVARALKKALKADGLN 80
                          90       100
                  ....*....|....*....|...
gi 1582669069  90 IAQFNEPAAGQTVFHLHFHVIPR 112
Cdd:cd01277    81 ILQNNGRAAGQVVFHVHVHVIPR 103
HIT pfam01230
HIT domain;
18-115 1.71e-35

HIT domain;


Pssm-ID: 395984 [Multi-domain]  Cd Length: 98  Bit Score: 118.18  E-value: 1.71e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582669069  18 RGEIPSHRVYEDEYTIAFMDVMPQAPGHVLVLPKAPSRNLLDADPATLTHAISVVQKIANAVKDVFDADGVFIAQFNEPA 97
Cdd:pfam01230   1 RGEIPSTVVYEDDLVLAFLDIDPQAPGHILVIPKKHIRELHDLTPEELGDLMSVAQKVARALGKVFKADGYRIVINNGAH 80
                          90
                  ....*....|....*...
gi 1582669069  98 AGQTVFHLHFHVIPRHEG 115
Cdd:pfam01230  81 AGQSVPHLHIHVIPRRKH 98
PRK10687 PRK10687
purine nucleoside phosphoramidase; Provisional
9-123 1.42e-16

purine nucleoside phosphoramidase; Provisional


Pssm-ID: 182648 [Multi-domain]  Cd Length: 119  Bit Score: 70.69  E-value: 1.42e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582669069   9 DNNIFAKILRGEIPSHRVYEDEYTIAFMDVMPQAPGHVLVLPKAPSRNLLDADP---ATLTHAISVVQKIANavKDVFDA 85
Cdd:PRK10687    3 EETIFSKIIRREIPSDIVYQDELVTAFRDISPQAPTHILIIPNILIPTVNDVSAeheQALGRMITVAAKIAE--QEGIAE 80
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1582669069  86 DGVFIAQFNEPAAGQTVFHLHFHVIPRHEGAALKPHSG 123
Cdd:PRK10687   81 DGYRLIMNTNRHGGQEVYHIHMHLLGGRPLGPMLAHKG 118
 
Name Accession Description Interval E-value
HinT COG0537
Purine nucleoside phosphoramidase/Ap4A hydrolase, histidine triade (HIT) family [Nucleotide ...
9-140 8.95e-55

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: 168.20  E-value: 8.95e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582669069   9 DNNIFAKILRGEIPSHRVYEDEYTIAFMDVMPQAPGHVLVLPKAPSRNLLDADPATLTHAISVVQKIANAVKDVFDADGV 88
Cdd:COG0537     1 MDCIFCKIIAGEIPALIVYEDEHVLAFLDINPYAPGHTLVIPKRHVASLFDLTPEELAELMRLAQKVAKALRKALGPDGF 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1582669069  89 FIAQFNEPAAGQTVFHLHFHVIPRHEGAALKPHS-GKMEDGAVLAANAEKIRA 140
Cdd:COG0537    81 NLGINNGEAAGQTVPHLHVHVIPRYEGDDNFMPViGTKVDPEELEETARKLRA 133
HINT_subgroup cd01277
HINT (histidine triad nucleotide-binding protein) subgroup: Members of this CD belong to the ...
10-112 1.13e-49

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: 154.30  E-value: 1.13e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582669069  10 NNIFAKILRGEIPSHRVYEDEYTIAFMDVMPQAPGHVLVLPKAPSRNLLDADPATLTHAISVVQKIANAVKDVFDADGVF 89
Cdd:cd01277     1 DCIFCKIIAGEIPSYKVYEDDHVLAFLDINPASKGHTLVIPKKHYENLLDLDPEELAELILAAKKVARALKKALKADGLN 80
                          90       100
                  ....*....|....*....|...
gi 1582669069  90 IAQFNEPAAGQTVFHLHFHVIPR 112
Cdd:cd01277    81 ILQNNGRAAGQVVFHVHVHVIPR 103
HIT pfam01230
HIT domain;
18-115 1.71e-35

HIT domain;


Pssm-ID: 395984 [Multi-domain]  Cd Length: 98  Bit Score: 118.18  E-value: 1.71e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582669069  18 RGEIPSHRVYEDEYTIAFMDVMPQAPGHVLVLPKAPSRNLLDADPATLTHAISVVQKIANAVKDVFDADGVFIAQFNEPA 97
Cdd:pfam01230   1 RGEIPSTVVYEDDLVLAFLDIDPQAPGHILVIPKKHIRELHDLTPEELGDLMSVAQKVARALGKVFKADGYRIVINNGAH 80
                          90
                  ....*....|....*...
gi 1582669069  98 AGQTVFHLHFHVIPRHEG 115
Cdd:pfam01230  81 AGQSVPHLHIHVIPRRKH 98
PKCI_related cd01276
Protein Kinase C Interacting protein related (PKCI): PKCI and related proteins belong to the ...
10-110 1.20e-29

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: 103.41  E-value: 1.20e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582669069  10 NNIFAKILRGEIPSHRVYEDEYTIAFMDVMPQAPGHVLVLPKAPSRNLLDA---DPATLTHAISVVQKIANAVKdvFDAD 86
Cdd:cd01276     1 DCIFCKIIRGEIPAKKVYEDDEVLAFHDINPQAPVHILVIPKKHIASLSDAteeDEELLGHLLSAAAKVAKDLG--IAED 78
                          90       100
                  ....*....|....*....|....
gi 1582669069  87 GVFIAQFNEPAAGQTVFHLHFHVI 110
Cdd:cd01276    79 GYRLVINCGKDGGQEVFHLHLHLL 102
HIT_like cd00468
HIT family: HIT (Histidine triad) proteins, named for a motif related to the sequence HxHxH ...
26-111 2.41e-18

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: 74.04  E-value: 2.41e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582669069  26 VYEDEYTIAFMDVMPQAPGHVLVLPKAPSRNLLDADPATLTHAISVVQKIANAVKDVFDADGVFIAQFNEPAAGQTVFHL 105
Cdd:cd00468     1 VPDDEHSFAFVNLKPAAPGHVLVCPKRHVETLPDLDEALLADLVITAQRVAAELEKHGNVPSLTVFVNDGAAAGQSVPHV 80

                  ....*.
gi 1582669069 106 HFHVIP 111
Cdd:cd00468    81 HLHVLP 86
FHIT cd01275
FHIT (fragile histidine family): FHIT proteins, related to the HIT family carry a motif HxHxH ...
12-115 3.51e-18

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: 75.02  E-value: 3.51e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582669069  12 IFAKILRGE-IPSHRVYEDEYTIAFMDVMPQAPGHVLVLPKAPSRNLLDADPATLTHAISVVQKIANAVKDVFDADGVFI 90
Cdd:cd01275     2 VFCDIPIKPdEDNLVFYRTKHSFAVVNLYPYNPGHVLVVPYRHVPRLEDLTPEEIADLFKLVQLAMKALKVVYKPDGFNI 81
                          90       100
                  ....*....|....*....|....*
gi 1582669069  91 AQFNEPAAGQTVFHLHFHVIPRHEG 115
Cdd:cd01275    82 GINDGKAGGGIVPHVHIHIVPRWNG 106
PRK10687 PRK10687
purine nucleoside phosphoramidase; Provisional
9-123 1.42e-16

purine nucleoside phosphoramidase; Provisional


Pssm-ID: 182648 [Multi-domain]  Cd Length: 119  Bit Score: 70.69  E-value: 1.42e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582669069   9 DNNIFAKILRGEIPSHRVYEDEYTIAFMDVMPQAPGHVLVLPKAPSRNLLDADP---ATLTHAISVVQKIANavKDVFDA 85
Cdd:PRK10687    3 EETIFSKIIRREIPSDIVYQDELVTAFRDISPQAPTHILIIPNILIPTVNDVSAeheQALGRMITVAAKIAE--QEGIAE 80
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1582669069  86 DGVFIAQFNEPAAGQTVFHLHFHVIPRHEGAALKPHSG 123
Cdd:PRK10687   81 DGYRLIMNTNRHGGQEVYHIHMHLLGGRPLGPMLAHKG 118
DcpS_C pfam11969
Scavenger mRNA decapping enzyme C-term binding; This family consists of several scavenger mRNA ...
12-119 4.03e-13

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: 61.47  E-value: 4.03e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582669069  12 IFAKILRGEIPSHRVYEDEYTIAFMDVMPQAPGHVLVLPKAPSRNLLDADPATLTHAISVVQKIANAVKDVFDADGVFIA 91
Cdd:pfam11969   3 VFCIIAKGEEPERVVYEDEGFVVFKDIKPKAPLHLLVIPKRHIKSLRDLTPEHLPLLEHMREVAKKVIEEKYIGVDRDEL 82
                          90       100
                  ....*....|....*....|....*....
gi 1582669069  92 QFNEPaAGQTVFHLHFHVI-PRHEGAALK 119
Cdd:pfam11969  83 RLGFH-YPPSVYHLHLHVIsPDFESLGLG 110
GalT cd00608
Galactose-1-phosphate uridyl transferase (GalT): This enzyme plays a key role in galactose ...
11-141 1.45e-04

Galactose-1-phosphate uridyl transferase (GalT): This enzyme plays a key role in galactose metabolism by catalysing the transfer of a uridine 5'-phosphoryl group from UDP-galactose 1-phosphate. The structure of E.coli GalT reveals that the enzyme contains two identical subunits. It also demonstrates that the active site is formed by amino acid residues from both subunits of the dimer.


Pssm-ID: 238341 [Multi-domain]  Cd Length: 329  Bit Score: 40.36  E-value: 1.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582669069  11 NIFAKILRGEIPS-HR-VYEDEYTIAFMDVMPQAPGHVLVLPKAPSRNLLDADPA---TLTHAIS-VVQKIANavkdVFD 84
Cdd:cd00608   186 CLLCDYLKLELESkERiVVENEHFVAVVPFWARWPFEVHILPKRHVSRFTDLTDEereDLAEILKrLLARYDN----LFN 261
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1582669069  85 AD-----GVFIAQFNEPAAGQTVFHLHFHVIPRHEGAALKPHSGkMEDGAVLAAN-------AEKIRAA 141
Cdd:cd00608   262 CSfpysmGWHQAPTGGKELENWYYHWHFEIPPRRSATVLKFMAG-FELGAGEFINdvtpeqaAARLREV 329
aprataxin_related cd01278
aprataxin related: Aprataxin, a HINT family hydrolase is mutated in ataxia oculomotor apraxia ...
26-110 2.08e-03

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: 35.44  E-value: 2.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582669069  26 VYEDEYTIAFMDVMPQAPGHVLVLPKAPSRNLLD---ADPATLTHAISVVQKIANAVKDVFDADgvFIAQFNEPAAgQTV 102
Cdd:cd01278    19 VYEDDRVVVFKDIYPKARHHYLVIPKEHIASLKAltkEDVPLLEHMETVGREKLLRSDNTDPSE--FRFGFHAPPF-TSV 95

                  ....*...
gi 1582669069 103 FHLHFHVI 110
Cdd:cd01278    96 SHLHLHVI 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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