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Conserved domains on  [gi|261278358|ref|NP_001159715|]
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bis(5'-adenosyl)-triphosphatase isoform 1 [Homo sapiens]

Protein Classification

HIT domain-containing protein( domain architecture ID 10101080)

HIT (histidine triad) domain-containing protein such as 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

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 ...
 5-124 1.20e-49

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: 1.20e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261278358   5 FGQHLIKPS---VVFLKTELSFALVNRKPVVPGHVLVCPLRPVERFHDLRPDEVADLFQTTQRVGTVVEKHFHGTSLTFS 81
Cdd:cd01275    3 FCDIPIKPDednLVFYRTKHSFAVVNLYPYNPGHVLVVPYRHVPRLEDLTPEEIADLFKLVQLAMKALKVVYKPDGFNIG 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 261278358  82 MQDGPEAGQTVKHVHVHVLPRKAGDFHRNDSI-YEELQKHDKED 124
Cdd:cd01275   83 INDGKAGGGIVPHVHIHIVPRWNGDTNFMPVIiYTKVLPEDLED 126
 
Name Accession Description Interval E-value
FHIT cd01275
FHIT (fragile histidine family): FHIT proteins, related to the HIT family carry a motif HxHxH ...
 5-124 1.20e-49

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: 1.20e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261278358   5 FGQHLIKPS---VVFLKTELSFALVNRKPVVPGHVLVCPLRPVERFHDLRPDEVADLFQTTQRVGTVVEKHFHGTSLTFS 81
Cdd:cd01275    3 FCDIPIKPDednLVFYRTKHSFAVVNLYPYNPGHVLVVPYRHVPRLEDLTPEEIADLFKLVQLAMKALKVVYKPDGFNIG 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 261278358  82 MQDGPEAGQTVKHVHVHVLPRKAGDFHRNDSI-YEELQKHDKED 124
Cdd:cd01275   83 INDGKAGGGIVPHVHIHIVPRWNGDTNFMPVIiYTKVLPEDLED 126
HIT pfam01230
HIT domain;
12-105 4.43e-32

HIT domain;


Pssm-ID: 395984 [Multi-domain]  Cd Length: 98  Bit Score: 109.71  E-value: 4.43e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261278358   12 PSVVFLKTELSFALVNRKPVVPGHVLVCPLRPVERFHDLRPDEVADLFQTTQRVGTVVEKHFHGTSLTFSMQDGPEAGQT 91
Cdd:pfam01230   5 PSTVVYEDDLVLAFLDIDPQAPGHILVIPKKHIRELHDLTPEELGDLMSVAQKVARALGKVFKADGYRIVINNGAHAGQS 84

                          90
                  ....*....|....
gi 261278358   92 VKHVHVHVLPRKAG 105
Cdd:pfam01230  85 VPHLHIHVIPRRKH 98
HinT COG0537
Purine nucleoside phosphoramidase/Ap4A hydrolase, histidine triade (HIT) family [Nucleotide ...
 12-113 2.11e-26

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: 96.17  E-value: 2.11e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261278358  12 PSVVFLKTELSFALVNRKPVVPGHVLVCPLRPVERFHDLRPDEVADLFQTTQRVGTVVEKHFHGTSLTFSMQDGPEAGQT 91
Cdd:COG0537   14 PALIVYEDEHVLAFLDINPYAPGHTLVIPKRHVASLFDLTPEELAELMRLAQKVAKALRKALGPDGFNLGINNGEAAGQT 93

                         90       100
                 ....*....|....*....|..
gi 261278358  92 VKHVHVHVLPRKAGDFHRNDSI 113
Cdd:COG0537   94 VPHLHVHVIPRYEGDDNFMPVI 115
 
Name Accession Description Interval E-value
FHIT cd01275
FHIT (fragile histidine family): FHIT proteins, related to the HIT family carry a motif HxHxH ...
 5-124 1.20e-49

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: 1.20e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261278358   5 FGQHLIKPS---VVFLKTELSFALVNRKPVVPGHVLVCPLRPVERFHDLRPDEVADLFQTTQRVGTVVEKHFHGTSLTFS 81
Cdd:cd01275    3 FCDIPIKPDednLVFYRTKHSFAVVNLYPYNPGHVLVVPYRHVPRLEDLTPEEIADLFKLVQLAMKALKVVYKPDGFNIG 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 261278358  82 MQDGPEAGQTVKHVHVHVLPRKAGDFHRNDSI-YEELQKHDKED 124
Cdd:cd01275   83 INDGKAGGGIVPHVHIHIVPRWNGDTNFMPVIiYTKVLPEDLED 126
HIT_like cd00468
HIT family: HIT (Histidine triad) proteins, named for a motif related to the sequence HxHxH ...
 16-101 1.83e-34

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: 115.26  E-value: 1.83e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261278358  16 FLKTELSFALVNRKPVVPGHVLVCPLRPVERFHDLRPDEVADLFQTTQRVGTVVEKHFHGTSLTFSMQDGPEAGQTVKHV 95
Cdd:cd00468    1 VPDDEHSFAFVNLKPAAPGHVLVCPKRHVETLPDLDEALLADLVITAQRVAAELEKHGNVPSLTVFVNDGAAAGQSVPHV 80


                 ....*.
gi 261278358  96 HVHVLP 101
Cdd:cd00468   81 HLHVLP 86
HIT pfam01230
HIT domain;
12-105 4.43e-32

HIT domain;


Pssm-ID: 395984 [Multi-domain]  Cd Length: 98  Bit Score: 109.71  E-value: 4.43e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261278358   12 PSVVFLKTELSFALVNRKPVVPGHVLVCPLRPVERFHDLRPDEVADLFQTTQRVGTVVEKHFHGTSLTFSMQDGPEAGQT 91
Cdd:pfam01230   5 PSTVVYEDDLVLAFLDIDPQAPGHILVIPKKHIRELHDLTPEELGDLMSVAQKVARALGKVFKADGYRIVINNGAHAGQS 84

                          90
                  ....*....|....
gi 261278358   92 VKHVHVHVLPRKAG 105
Cdd:pfam01230  85 VPHLHIHVIPRRKH 98
HinT COG0537
Purine nucleoside phosphoramidase/Ap4A hydrolase, histidine triade (HIT) family [Nucleotide ...
 12-113 2.11e-26

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: 96.17  E-value: 2.11e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261278358  12 PSVVFLKTELSFALVNRKPVVPGHVLVCPLRPVERFHDLRPDEVADLFQTTQRVGTVVEKHFHGTSLTFSMQDGPEAGQT 91
Cdd:COG0537   14 PALIVYEDEHVLAFLDINPYAPGHTLVIPKRHVASLFDLTPEELAELMRLAQKVAKALRKALGPDGFNLGINNGEAAGQT 93

                         90       100
                 ....*....|....*....|..
gi 261278358  92 VKHVHVHVLPRKAGDFHRNDSI 113
Cdd:COG0537   94 VPHLHVHVIPRYEGDDNFMPVI 115
HINT_subgroup cd01277
HINT (histidine triad nucleotide-binding protein) subgroup: Members of this CD belong to the ...
 12-102 1.25e-20

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: 80.73  E-value: 1.25e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261278358  12 PSVVFLKTELSFALVNRKPVVPGHVLVCPLRPVERFHDLRPDEVADLFQTTQRVGTVVEKHFHGTSLTFSMQDGPEAGQT 91
Cdd:cd01277   13 PSYKVYEDDHVLAFLDINPASKGHTLVIPKKHYENLLDLDPEELAELILAAKKVARALKKALKADGLNILQNNGRAAGQV 92

                         90
                 ....*....|.
gi 261278358  92 VKHVHVHVLPR 102
Cdd:cd01277   93 VFHVHVHVIPR 103
PKCI_related cd01276
Protein Kinase C Interacting protein related (PKCI): PKCI and related proteins belong to the ...
 12-100 2.54e-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: 48.71  E-value: 2.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261278358  12 PSVVFLKTELSFALVNRKPVVPGHVLVCPLRPVERFHDLRPD---EVADLFQTTQRVgtVVEKHFHGTSLTFSMQDGPEA 88
Cdd:cd01276   13 PAKKVYEDDEVLAFHDINPQAPVHILVIPKKHIASLSDATEEdeeLLGHLLSAAAKV--AKDLGIAEDGYRLVINCGKDG 90

                         90
                 ....*....|..
gi 261278358  89 GQTVKHVHVHVL 100
Cdd:cd01276   91 GQEVFHLHLHLL 102
DcpS_C pfam11969
Scavenger mRNA decapping enzyme C-term binding; This family consists of several scavenger mRNA ...
 29-100 5.49e-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: 34.50  E-value: 5.49e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 261278358   29 KPVVPGHVLVCPLRPVERFHDLRPDEVaDLFQTTQRVG--TVVEKHFHGTSLTFSMqdGPEAGQTVKHVHVHVL 100
Cdd:pfam11969  30 KPKAPLHLLVIPKRHIKSLRDLTPEHL-PLLEHMREVAkkVIEEKYIGVDRDELRL--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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