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Conserved domains on  [gi|2212505746|ref|XP_047091445|]
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bifunctional bis(5'-adenosyl)-triphosphatase/adenylylsulfatase FHIT-like [Lolium rigidum]

Protein Classification

HIT family protein( domain architecture ID 10101080)

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; similar to Homo sapiens Bis(5'-adenosyl)-triphosphatase (also called fragile histidine triad protein) that cleaves P(1)-P(3)-bis(5'-adenosyl) triphosphate (Ap3A) to yield AMP and ADP

CATH:  3.30.428.10
Gene Ontology:  GO:0003824
PubMed:  1472710
SCOP:  4000950

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FHIT cd01275
FHIT (fragile histidine family): FHIT proteins, related to the HIT family carry a motif HxHxH ...
 61-181 1.36e-48

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: 155.14  E-value: 1.36e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212505746  61 YKFGPYKIDARE---VFHATALSYAMVNLRPLLPGHVLVCPKREVKRFADLSSDETSDLWVTAKEVGAKLEQYHKASSLT 137
Cdd:cd01275     1 CVFCDIPIKPDEdnlVFYRTKHSFAVVNLYPYNPGHVLVVPYRHVPRLEDLTPEEIADLFKLVQLAMKALKVVYKPDGFN 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2212505746 138 FAIQDGPQAGQTVAHVHIHVIPRKKGDFENND-EIYDAIDVKEKE 181
Cdd:cd01275    81 IGINDGKAGGGIVPHVHIHIVPRWNGDTNFMPvIIYTKVLPEDLE 125
 
Name Accession Description Interval E-value
FHIT cd01275
FHIT (fragile histidine family): FHIT proteins, related to the HIT family carry a motif HxHxH ...
 61-181 1.36e-48

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: 155.14  E-value: 1.36e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212505746  61 YKFGPYKIDARE---VFHATALSYAMVNLRPLLPGHVLVCPKREVKRFADLSSDETSDLWVTAKEVGAKLEQYHKASSLT 137
Cdd:cd01275     1 CVFCDIPIKPDEdnlVFYRTKHSFAVVNLYPYNPGHVLVVPYRHVPRLEDLTPEEIADLFKLVQLAMKALKVVYKPDGFN 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2212505746 138 FAIQDGPQAGQTVAHVHIHVIPRKKGDFENND-EIYDAIDVKEKE 181
Cdd:cd01275    81 IGINDGKAGGGIVPHVHIHIVPRWNGDTNFMPvIIYTKVLPEDLE 125
HinT COG0537
Purine nucleoside phosphoramidase/Ap4A hydrolase, histidine triade (HIT) family [Nucleotide ...
 68-186 4.15e-27

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: 100.41  E-value: 4.15e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212505746  68 IDAREVfHATALSYAMVNLRPLLPGHVLVCPKREVKRFADLSSDETSDLWVTAKEVGAKLEQYHKASSLTFAIQDGPQAG 147
Cdd:COG0537    13 IPALIV-YEDEHVLAFLDINPYAPGHTLVIPKRHVASLFDLTPEELAELMRLAQKVAKALRKALGPDGFNLGINNGEAAG 91

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2212505746 148 QTVAHVHIHVIPRKKGDFENNDEIYDAIDVKE-KEMKEKL 186
Cdd:COG0537    92 QTVPHLHVHVIPRYEGDDNFMPVIGTKVDPEElEETARKL 131
HIT pfam01230
HIT domain;
68-163 1.06e-26

HIT domain;


Pssm-ID: 395984 [Multi-domain]  Cd Length: 98  Bit Score: 98.15  E-value: 1.06e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212505746  68 IDAREVFHaTALSYAMVNLRPLLPGHVLVCPKREVKRFADLSSDETSDLWVTAKEVGAKLEQYHKASSLTFAIQDGPQAG 147
Cdd:pfam01230   4 IPSTVVYE-DDLVLAFLDIDPQAPGHILVIPKKHIRELHDLTPEELGDLMSVAQKVARALGKVFKADGYRIVINNGAHAG 82

                          90
                  ....*....|....*.
gi 2212505746 148 QTVAHVHIHVIPRKKG 163
Cdd:pfam01230  83 QSVPHLHIHVIPRRKH 98
 
Name Accession Description Interval E-value
FHIT cd01275
FHIT (fragile histidine family): FHIT proteins, related to the HIT family carry a motif HxHxH ...
 61-181 1.36e-48

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: 155.14  E-value: 1.36e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212505746  61 YKFGPYKIDARE---VFHATALSYAMVNLRPLLPGHVLVCPKREVKRFADLSSDETSDLWVTAKEVGAKLEQYHKASSLT 137
Cdd:cd01275     1 CVFCDIPIKPDEdnlVFYRTKHSFAVVNLYPYNPGHVLVVPYRHVPRLEDLTPEEIADLFKLVQLAMKALKVVYKPDGFN 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2212505746 138 FAIQDGPQAGQTVAHVHIHVIPRKKGDFENND-EIYDAIDVKEKE 181
Cdd:cd01275    81 IGINDGKAGGGIVPHVHIHIVPRWNGDTNFMPvIIYTKVLPEDLE 125
HinT COG0537
Purine nucleoside phosphoramidase/Ap4A hydrolase, histidine triade (HIT) family [Nucleotide ...
 68-186 4.15e-27

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: 100.41  E-value: 4.15e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212505746  68 IDAREVfHATALSYAMVNLRPLLPGHVLVCPKREVKRFADLSSDETSDLWVTAKEVGAKLEQYHKASSLTFAIQDGPQAG 147
Cdd:COG0537    13 IPALIV-YEDEHVLAFLDINPYAPGHTLVIPKRHVASLFDLTPEELAELMRLAQKVAKALRKALGPDGFNLGINNGEAAG 91

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2212505746 148 QTVAHVHIHVIPRKKGDFENNDEIYDAIDVKE-KEMKEKL 186
Cdd:COG0537    92 QTVPHLHVHVIPRYEGDDNFMPVIGTKVDPEElEETARKL 131
HIT pfam01230
HIT domain;
68-163 1.06e-26

HIT domain;


Pssm-ID: 395984 [Multi-domain]  Cd Length: 98  Bit Score: 98.15  E-value: 1.06e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212505746  68 IDAREVFHaTALSYAMVNLRPLLPGHVLVCPKREVKRFADLSSDETSDLWVTAKEVGAKLEQYHKASSLTFAIQDGPQAG 147
Cdd:pfam01230   4 IPSTVVYE-DDLVLAFLDIDPQAPGHILVIPKKHIRELHDLTPEELGDLMSVAQKVARALGKVFKADGYRIVINNGAHAG 82

                          90
                  ....*....|....*.
gi 2212505746 148 QTVAHVHIHVIPRKKG 163
Cdd:pfam01230  83 QSVPHLHIHVIPRRKH 98
HIT_like cd00468
HIT family: HIT (Histidine triad) proteins, named for a motif related to the sequence HxHxH ...
 74-159 2.12e-26

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: 97.15  E-value: 2.12e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212505746  74 FHATALSYAMVNLRPLLPGHVLVCPKREVKRFADLSSDETSDLWVTAKEVGAKLEQYHKASSLTFAIQDGPQAGQTVAHV 153
Cdd:cd00468     1 VPDDEHSFAFVNLKPAAPGHVLVCPKRHVETLPDLDEALLADLVITAQRVAAELEKHGNVPSLTVFVNDGAAAGQSVPHV 80


                  ....*.
gi 2212505746 154 HIHVIP 159
Cdd:cd00468    81 HLHVLP 86
HINT_subgroup cd01277
HINT (histidine triad nucleotide-binding protein) subgroup: Members of this CD belong to the ...
 77-160 6.53e-18

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: 75.34  E-value: 6.53e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212505746  77 TALSYAMVNLRPLLPGHVLVCPKREVKRFADLSSDETSDLWVTAKEVGAKLEQYHKASSLTFAIQDGPQAGQTVAHVHIH 156
Cdd:cd01277    20 DDHVLAFLDINPASKGHTLVIPKKHYENLLDLDPEELAELILAAKKVARALKKALKADGLNILQNNGRAAGQVVFHVHVH 99


                  ....
gi 2212505746 157 VIPR 160
Cdd:cd01277   100 VIPR 103
PKCI_related cd01276
Protein Kinase C Interacting protein related (PKCI): PKCI and related proteins belong to the ...
 87-158 3.15e-08

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: 49.87  E-value: 3.15e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2212505746  87 RPLLPGHVLVCPKREVKRFADL---SSDETSDLWVTAKEVGAKLEQYHKASSLTfaIQDGPQAGQTVAHVHIHVI 158
Cdd:cd01276    30 NPQAPVHILVIPKKHIASLSDAteeDEELLGHLLSAAAKVAKDLGIAEDGYRLV--INCGKDGGQEVFHLHLHLL 102
GalT COG1085
Galactose-1-phosphate uridylyltransferase [Carbohydrate transport and metabolism];
91-160 1.32e-03

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


Pssm-ID: 440702 [Multi-domain]  Cd Length: 336  Bit Score: 38.66  E-value: 1.32e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2212505746  91 PGHVLVCPKREVKRFADLSSDETSDLWVTAKEVGAKLEQYHKASSLTFAIQDGPQAGQTVA--HVHIHVIPR 160
Cdd:COG1085   226 PFETWILPKRHVSDFEELTDEERDDLARILKRVLRRLDNLLGDFPYNMGLHQAPVDGEERDhyHWHLEIYPR 297
DcpS_C pfam11969
Scavenger mRNA decapping enzyme C-term binding; This family consists of several scavenger mRNA ...
 93-158 1.66e-03

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: 36.81  E-value: 1.66e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2212505746  93 HVLVCPKREVKRFADLSSDEtSDLWVTAKEVGAKL--EQYHKASSLTFAIqdGPQAGQTVAHVHIHVI 158
Cdd:pfam11969  36 HLLVIPKRHIKSLRDLTPEH-LPLLEHMREVAKKVieEKYIGVDRDELRL--GFHYPPSVYHLHLHVI 100
 
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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