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Conserved domains on  [gi|2502938378|ref|WP_282003756|]
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HIT family protein [Geotalea uraniireducens]

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
PubMed:  1472710|9323207|12504684|12119013
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 ...
 2-128 6.86e-46

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: 145.09  E-value: 6.86e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502938378   2 NSCPFCTPNQ----SAILLANDRALAIPDAYPVTPGHTLIVPKRHITSLFEASKEEQAALFDLVAKMRQLILQDRQPDGF 77
Cdd:COG0537     1 MDCIFCKIIAgeipALIVYEDEHVLAFLDINPYAPGHTLVIPKRHVASLFDLTPEELAELMRLAQKVAKALRKALGPDGF 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2502938378  78 NIGINDGIAAGQTVMHLHIHLIPRYAGDTEDPRGGVRWIMPKNAP-YWKQIR 128
Cdd:COG0537    81 NLGINNGEAAGQTVPHLHVHVIPRYEGDDNFMPVIGTKVDPEELEeTARKLR 132
 
Name Accession Description Interval E-value
HinT COG0537
Purine nucleoside phosphoramidase/Ap4A hydrolase, histidine triade (HIT) family [Nucleotide ...
 2-128 6.86e-46

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: 145.09  E-value: 6.86e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502938378   2 NSCPFCTPNQ----SAILLANDRALAIPDAYPVTPGHTLIVPKRHITSLFEASKEEQAALFDLVAKMRQLILQDRQPDGF 77
Cdd:COG0537     1 MDCIFCKIIAgeipALIVYEDEHVLAFLDINPYAPGHTLVIPKRHVASLFDLTPEELAELMRLAQKVAKALRKALGPDGF 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2502938378  78 NIGINDGIAAGQTVMHLHIHLIPRYAGDTEDPRGGVRWIMPKNAP-YWKQIR 128
Cdd:COG0537    81 NLGINNGEAAGQTVPHLHVHVIPRYEGDDNFMPVIGTKVDPEELEeTARKLR 132
FHIT cd01275
FHIT (fragile histidine family): FHIT proteins, related to the HIT family carry a motif HxHxH ...
 4-108 1.03e-33

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: 113.93  E-value: 1.03e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502938378   4 CPFCT-----PNQSAILLANDRALAIPDAYPVTPGHTLIVPKRHITSLFEASKEEQAALFDLVAKMRQLILQDRQPDGFN 78
Cdd:cd01275     1 CVFCDipikpDEDNLVFYRTKHSFAVVNLYPYNPGHVLVVPYRHVPRLEDLTPEEIADLFKLVQLAMKALKVVYKPDGFN 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 2502938378  79 IGINDGIAAGQTVMHLHIHLIPRYAGDTED 108
Cdd:cd01275    81 IGINDGKAGGGIVPHVHIHIVPRWNGDTNF 110
HIT pfam01230
HIT domain;
12-104 1.40e-28

HIT domain;


Pssm-ID: 395984 [Multi-domain]  Cd Length: 98  Bit Score: 100.08  E-value: 1.40e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502938378  12 SAILLANDRALAIPDAYPVTPGHTLIVPKRHITSLFEASKEEQAALFDLVAKMRQLILQDRQPDGFNIGINDGIAAGQTV 91
Cdd:pfam01230   6 STVVYEDDLVLAFLDIDPQAPGHILVIPKKHIRELHDLTPEELGDLMSVAQKVARALGKVFKADGYRIVINNGAHAGQSV 85

                          90
                  ....*....|...
gi 2502938378  92 MHLHIHLIPRYAG 104
Cdd:pfam01230  86 PHLHIHVIPRRKH 98
PRK10687 PRK10687
purine nucleoside phosphoramidase; Provisional
 12-99 3.09e-08

purine nucleoside phosphoramidase; Provisional


Pssm-ID: 182648 [Multi-domain]  Cd Length: 119  Bit Score: 48.35  E-value: 3.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502938378  12 SAILLANDRALAIPDAYPVTPGHTLIVPKRHITSLFEASKEEQAALFDLVAKMRQLILQDR-QPDGFNIGINDGIAAGQT 90
Cdd:PRK10687   17 SDIVYQDELVTAFRDISPQAPTHILIIPNILIPTVNDVSAEHEQALGRMITVAAKIAEQEGiAEDGYRLIMNTNRHGGQE 96


                  ....*....
gi 2502938378  91 VMHLHIHLI 99
Cdd:PRK10687   97 VYHIHMHLL 105
 
Name Accession Description Interval E-value
HinT COG0537
Purine nucleoside phosphoramidase/Ap4A hydrolase, histidine triade (HIT) family [Nucleotide ...
 2-128 6.86e-46

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: 145.09  E-value: 6.86e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502938378   2 NSCPFCTPNQ----SAILLANDRALAIPDAYPVTPGHTLIVPKRHITSLFEASKEEQAALFDLVAKMRQLILQDRQPDGF 77
Cdd:COG0537     1 MDCIFCKIIAgeipALIVYEDEHVLAFLDINPYAPGHTLVIPKRHVASLFDLTPEELAELMRLAQKVAKALRKALGPDGF 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2502938378  78 NIGINDGIAAGQTVMHLHIHLIPRYAGDTEDPRGGVRWIMPKNAP-YWKQIR 128
Cdd:COG0537    81 NLGINNGEAAGQTVPHLHVHVIPRYEGDDNFMPVIGTKVDPEELEeTARKLR 132
FHIT cd01275
FHIT (fragile histidine family): FHIT proteins, related to the HIT family carry a motif HxHxH ...
 4-108 1.03e-33

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: 113.93  E-value: 1.03e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502938378   4 CPFCT-----PNQSAILLANDRALAIPDAYPVTPGHTLIVPKRHITSLFEASKEEQAALFDLVAKMRQLILQDRQPDGFN 78
Cdd:cd01275     1 CVFCDipikpDEDNLVFYRTKHSFAVVNLYPYNPGHVLVVPYRHVPRLEDLTPEEIADLFKLVQLAMKALKVVYKPDGFN 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 2502938378  79 IGINDGIAAGQTVMHLHIHLIPRYAGDTED 108
Cdd:cd01275    81 IGINDGKAGGGIVPHVHIHIVPRWNGDTNF 110
HINT_subgroup cd01277
HINT (histidine triad nucleotide-binding protein) subgroup: Members of this CD belong to the ...
 3-101 3.24e-33

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: 111.93  E-value: 3.24e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502938378   3 SCPFCT------PnqSAILLANDRALAIPDAYPVTPGHTLIVPKRHITSLFEASKEEQAALFDLVAKMRQLILQDRQPDG 76
Cdd:cd01277     1 DCIFCKiiageiP--SYKVYEDDHVLAFLDINPASKGHTLVIPKKHYENLLDLDPEELAELILAAKKVARALKKALKADG 78

                          90       100
                  ....*....|....*....|....*
gi 2502938378  77 FNIGINDGIAAGQTVMHLHIHLIPR 101
Cdd:cd01277    79 LNILQNNGRAAGQVVFHVHVHVIPR 103
HIT pfam01230
HIT domain;
12-104 1.40e-28

HIT domain;


Pssm-ID: 395984 [Multi-domain]  Cd Length: 98  Bit Score: 100.08  E-value: 1.40e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502938378  12 SAILLANDRALAIPDAYPVTPGHTLIVPKRHITSLFEASKEEQAALFDLVAKMRQLILQDRQPDGFNIGINDGIAAGQTV 91
Cdd:pfam01230   6 STVVYEDDLVLAFLDIDPQAPGHILVIPKKHIRELHDLTPEELGDLMSVAQKVARALGKVFKADGYRIVINNGAHAGQSV 85

                          90
                  ....*....|...
gi 2502938378  92 MHLHIHLIPRYAG 104
Cdd:pfam01230  86 PHLHIHVIPRRKH 98
HIT_like cd00468
HIT family: HIT (Histidine triad) proteins, named for a motif related to the sequence HxHxH ...
 19-100 6.88e-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: 77.51  E-value: 6.88e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502938378  19 DRALAIPDAYPVTPGHTLIVPKRHITSLFEASKEEQAALFDLVAKMRQLILQDRQPDGFNIGINDGIAAGQTVMHLHIHL 98
Cdd:cd00468     5 EHSFAFVNLKPAAPGHVLVCPKRHVETLPDLDEALLADLVITAQRVAAELEKHGNVPSLTVFVNDGAAAGQSVPHVHLHV 84


                  ..
gi 2502938378  99 IP 100
Cdd:cd00468    85 LP 86
PKCI_related cd01276
Protein Kinase C Interacting protein related (PKCI): PKCI and related proteins belong to the ...
 12-99 1.17e-17

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: 72.21  E-value: 1.17e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502938378  12 SAILLANDRALAIPDAYPVTPGHTLIVPKRHITSLFEASKEEQAALFDLVAKMRQLI-LQDRQPDGFNIGINDGIAAGQT 90
Cdd:cd01276    14 AKKVYEDDEVLAFHDINPQAPVHILVIPKKHIASLSDATEEDEELLGHLLSAAAKVAkDLGIAEDGYRLVINCGKDGGQE 93


                  ....*....
gi 2502938378  91 VMHLHIHLI 99
Cdd:cd01276    94 VFHLHLHLL 102
DcpS_C pfam11969
Scavenger mRNA decapping enzyme C-term binding; This family consists of several scavenger mRNA ...
 3-99 5.24e-15

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: 65.70  E-value: 5.24e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502938378   3 SCPFC----TPNQSAILLANDRALAIPDAYPVTPGHTLIVPKRHITSLFEASKEEQAALFDLVAKMRQlILQDRQPDGFN 78
Cdd:pfam11969   1 KWVFCiiakGEEPERVVYEDEGFVVFKDIKPKAPLHLLVIPKRHIKSLRDLTPEHLPLLEHMREVAKK-VIEEKYIGVDR 79

                          90       100
                  ....*....|....*....|.
gi 2502938378  79 IGINDGIAAGQTVMHLHIHLI 99
Cdd:pfam11969  80 DELRLGFHYPPSVYHLHLHVI 100
PRK10687 PRK10687
purine nucleoside phosphoramidase; Provisional
 12-99 3.09e-08

purine nucleoside phosphoramidase; Provisional


Pssm-ID: 182648 [Multi-domain]  Cd Length: 119  Bit Score: 48.35  E-value: 3.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502938378  12 SAILLANDRALAIPDAYPVTPGHTLIVPKRHITSLFEASKEEQAALFDLVAKMRQLILQDR-QPDGFNIGINDGIAAGQT 90
Cdd:PRK10687   17 SDIVYQDELVTAFRDISPQAPTHILIIPNILIPTVNDVSAEHEQALGRMITVAAKIAEQEGiAEDGYRLIMNTNRHGGQE 96


                  ....*....
gi 2502938378  91 VMHLHIHLI 99
Cdd:PRK10687   97 VYHIHMHLL 105
aprataxin_related cd01278
aprataxin related: Aprataxin, a HINT family hydrolase is mutated in ataxia oculomotor apraxia ...
 3-99 3.86e-07

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: 45.07  E-value: 3.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502938378   3 SCPFCT------PNQSAILLANDRALAIPDAYPVTPGHTLIVPKRHITSLFEASKEEQAALFDLVAKMRQLILQDRQPDG 76
Cdd:cd01278     1 LCHFCDiakrrdPDPEDQVYEDDRVVVFKDIYPKARHHYLVIPKEHIASLKALTKEDVPLLEHMETVGREKLLRSDNTDP 80

                          90       100
                  ....*....|....*....|...
gi 2502938378  77 FNIGINDGIAAGQTVMHLHIHLI 99
Cdd:cd01278    81 SEFRFGFHAPPFTSVSHLHLHVI 103
GalT COG1085
Galactose-1-phosphate uridylyltransferase [Carbohydrate transport and metabolism];
14-102 8.49e-07

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


Pssm-ID: 440702 [Multi-domain]  Cd Length: 336  Bit Score: 46.36  E-value: 8.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502938378  14 ILLANDRALAI-PDAyPVTPGHTLIVPKRHITSLFEASKEEQA----ALFDLVAKMRQLIlqDRQPdgFNIGI-----ND 83
Cdd:COG1085   208 VVAENEHFVAFvPFA-ARWPFETWILPKRHVSDFEELTDEERDdlarILKRVLRRLDNLL--GDFP--YNMGLhqapvDG 282

                          90
                  ....*....|....*....
gi 2502938378  84 GIAAGqtvMHLHIHLIPRY 102
Cdd:COG1085   283 EERDH---YHWHLEIYPRL 298
CwfJ_C_1 pfam04677
Protein similar to CwfJ C-terminus 1; This region is found in the N terminus of ...
 3-100 2.50e-05

Protein similar to CwfJ C-terminus 1; This region is found in the N terminus of Schizosaccharomyces pombe protein CwfJ. CwfJ is part of the Cdc5p complex involved in mRNA splicing.


Pssm-ID: 428062  Cd Length: 122  Bit Score: 40.82  E-value: 2.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502938378   3 SCPFCTPNQSA-----ILLANDRALAIPDAyPVTPGHTLIVPKRHITSLFEASKEE-------QAALFDLVAKMRQ-LIL 69
Cdd:pfam04677  13 SCWFCLSNPNLekhliVSIGNKAYLALPKG-PLVSGHCLIIPIQHIPSTLSLDEEVwdeirnfRKALTLMYKSQGKdAVF 91

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2502938378  70 QDRQPdgfnigindgiaagQTVMHLHIHLIP 100
Cdd:pfam04677  92 FEIAS--------------QRRPHLHIQCIP 108
 
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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