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Conserved domains on  [gi|489196181|ref|WP_003105490|]
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MULTISPECIES: HIT family protein [Pseudomonas]

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 ...
 9-141 4.84e-52

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: 161.27  E-value: 4.84e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196181   9 SQNIFAKIIRGEAPCYKVYEDEDVLAFLDLFPQSYGHTLVIPKhAEARNLLEIDAQNLAKVMAVVQRLTRALVEEVQPDG 88
Cdd:COG0537    1 MDCIFCKIIAGEIPALIVYEDEHVLAFLDINPYAPGHTLVIPK-RHVASLFDLTPEELAELMRLAQKVAKALRKALGPDG 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 489196181  89 VQVAQFNGAPAGQTVFHIHFHVIPRFSGE-NLGIHAAKQGDPEVLAQLQERLAQ 141
Cdd:COG0537   80 FNLGINNGEAAGQTVPHLHVHVIPRYEGDdNFMPVIGTKVDPEELEETARKLRA 133
 
Name Accession Description Interval E-value
HinT COG0537
Purine nucleoside phosphoramidase/Ap4A hydrolase, histidine triade (HIT) family [Nucleotide ...
 9-141 4.84e-52

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: 161.27  E-value: 4.84e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196181   9 SQNIFAKIIRGEAPCYKVYEDEDVLAFLDLFPQSYGHTLVIPKhAEARNLLEIDAQNLAKVMAVVQRLTRALVEEVQPDG 88
Cdd:COG0537    1 MDCIFCKIIAGEIPALIVYEDEHVLAFLDINPYAPGHTLVIPK-RHVASLFDLTPEELAELMRLAQKVAKALRKALGPDG 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 489196181  89 VQVAQFNGAPAGQTVFHIHFHVIPRFSGE-NLGIHAAKQGDPEVLAQLQERLAQ 141
Cdd:COG0537   80 FNLGINNGEAAGQTVPHLHVHVIPRYEGDdNFMPVIGTKVDPEELEETARKLRA 133
HINT_subgroup cd01277
HINT (histidine triad nucleotide-binding protein) subgroup: Members of this CD belong to the ...
 11-113 2.90e-51

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: 158.15  E-value: 2.90e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196181  11 NIFAKIIRGEAPCYKVYEDEDVLAFLDLFPQSYGHTLVIPKHaEARNLLEIDAQNLAKVMAVVQRLTRALVEEVQPDGVQ 90
Cdd:cd01277    2 CIFCKIIAGEIPSYKVYEDDHVLAFLDINPASKGHTLVIPKK-HYENLLDLDPEELAELILAAKKVARALKKALKADGLN 80

                         90       100
                 ....*....|....*....|...
gi 489196181  91 VAQFNGAPAGQTVFHIHFHVIPR 113
Cdd:cd01277   81 ILQNNGRAAGQVVFHVHVHVIPR 103
HIT pfam01230
HIT domain;
18-116 8.64e-30

HIT domain;


Pssm-ID: 395984 [Multi-domain]  Cd Length: 98  Bit Score: 103.54  E-value: 8.64e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196181   18 RGEAPCYKVYEDEDVLAFLDLFPQSYGHTLVIPKhAEARNLLEIDAQNLAKVMAVVQRLTRALVEEVQPDGVQVAQFNGA 97
Cdd:pfam01230   1 RGEIPSTVVYEDDLVLAFLDIDPQAPGHILVIPK-KHIRELHDLTPEELGDLMSVAQKVARALGKVFKADGYRIVINNGA 79

                          90
                  ....*....|....*....
gi 489196181   98 PAGQTVFHIHFHVIPRFSG 116
Cdd:pfam01230  80 HAGQSVPHLHIHVIPRRKH 98
PRK10687 PRK10687
purine nucleoside phosphoramidase; Provisional
 10-127 2.27e-12

purine nucleoside phosphoramidase; Provisional


Pssm-ID: 182648 [Multi-domain]  Cd Length: 119  Bit Score: 59.90  E-value: 2.27e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196181  10 QNIFAKIIRGEAPCYKVYEDEDVLAFLDLFPQSYGHTLVIPkhaearNLL-----EIDAQN---LAKVMAVVQRLTRAlv 81
Cdd:PRK10687   4 ETIFSKIIRREIPSDIVYQDELVTAFRDISPQAPTHILIIP------NILiptvnDVSAEHeqaLGRMITVAAKIAEQ-- 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 489196181  82 EEVQPDGVQVAQFNGAPAGQTVFHIHFHVIprfSGENLGIHAAKQG 127
Cdd:PRK10687  76 EGIAEDGYRLIMNTNRHGGQEVYHIHMHLL---GGRPLGPMLAHKG 118
 
Name Accession Description Interval E-value
HinT COG0537
Purine nucleoside phosphoramidase/Ap4A hydrolase, histidine triade (HIT) family [Nucleotide ...
 9-141 4.84e-52

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: 161.27  E-value: 4.84e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196181   9 SQNIFAKIIRGEAPCYKVYEDEDVLAFLDLFPQSYGHTLVIPKhAEARNLLEIDAQNLAKVMAVVQRLTRALVEEVQPDG 88
Cdd:COG0537    1 MDCIFCKIIAGEIPALIVYEDEHVLAFLDINPYAPGHTLVIPK-RHVASLFDLTPEELAELMRLAQKVAKALRKALGPDG 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 489196181  89 VQVAQFNGAPAGQTVFHIHFHVIPRFSGE-NLGIHAAKQGDPEVLAQLQERLAQ 141
Cdd:COG0537   80 FNLGINNGEAAGQTVPHLHVHVIPRYEGDdNFMPVIGTKVDPEELEETARKLRA 133
HINT_subgroup cd01277
HINT (histidine triad nucleotide-binding protein) subgroup: Members of this CD belong to the ...
 11-113 2.90e-51

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: 158.15  E-value: 2.90e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196181  11 NIFAKIIRGEAPCYKVYEDEDVLAFLDLFPQSYGHTLVIPKHaEARNLLEIDAQNLAKVMAVVQRLTRALVEEVQPDGVQ 90
Cdd:cd01277    2 CIFCKIIAGEIPSYKVYEDDHVLAFLDINPASKGHTLVIPKK-HYENLLDLDPEELAELILAAKKVARALKKALKADGLN 80

                         90       100
                 ....*....|....*....|...
gi 489196181  91 VAQFNGAPAGQTVFHIHFHVIPR 113
Cdd:cd01277   81 ILQNNGRAAGQVVFHVHVHVIPR 103
HIT pfam01230
HIT domain;
18-116 8.64e-30

HIT domain;


Pssm-ID: 395984 [Multi-domain]  Cd Length: 98  Bit Score: 103.54  E-value: 8.64e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196181   18 RGEAPCYKVYEDEDVLAFLDLFPQSYGHTLVIPKhAEARNLLEIDAQNLAKVMAVVQRLTRALVEEVQPDGVQVAQFNGA 97
Cdd:pfam01230   1 RGEIPSTVVYEDDLVLAFLDIDPQAPGHILVIPK-KHIRELHDLTPEELGDLMSVAQKVARALGKVFKADGYRIVINNGA 79

                          90
                  ....*....|....*....
gi 489196181   98 PAGQTVFHIHFHVIPRFSG 116
Cdd:pfam01230  80 HAGQSVPHLHIHVIPRRKH 98
PKCI_related cd01276
Protein Kinase C Interacting protein related (PKCI): PKCI and related proteins belong to the ...
 10-111 1.65e-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: 103.03  E-value: 1.65e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196181  10 QNIFAKIIRGEAPCYKVYEDEDVLAFLDLFPQSYGHTLVIPKHAEAR--NLLEIDAQNLAKVMAVVQRLTRALveEVQPD 87
Cdd:cd01276    1 DCIFCKIIRGEIPAKKVYEDDEVLAFHDINPQAPVHILVIPKKHIASlsDATEEDEELLGHLLSAAAKVAKDL--GIAED 78

                         90       100
                 ....*....|....*....|....
gi 489196181  88 GVQVAQFNGAPAGQTVFHIHFHVI 111
Cdd:cd01276   79 GYRLVINCGKDGGQEVFHLHLHLL 102
FHIT cd01275
FHIT (fragile histidine family): FHIT proteins, related to the HIT family carry a motif HxHxH ...
 26-117 4.84e-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: 74.64  E-value: 4.84e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196181  26 VYEDEDVLAFLDLFPQSYGHTLVIPKHAEARnLLEIDAQNLAKVMAVVQRLTRALVEEVQPDGVQVAQFNGAPAGQTVFH 105
Cdd:cd01275   17 FYRTKHSFAVVNLYPYNPGHVLVVPYRHVPR-LEDLTPEEIADLFKLVQLAMKALKVVYKPDGFNIGINDGKAGGGIVPH 95

                         90
                 ....*....|..
gi 489196181 106 IHFHVIPRFSGE 117
Cdd:cd01275   96 VHIHIVPRWNGD 107
HIT_like cd00468
HIT family: HIT (Histidine triad) proteins, named for a motif related to the sequence HxHxH ...
 26-112 2.98e-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: 71.35  E-value: 2.98e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196181  26 VYEDEDVLAFLDLFPQSYGHTLVIPK-HAEarNLLEIDAQNLAKVMAVVQRLTRALVEEVQPDGVQVAQFNGAPAGQTVF 104
Cdd:cd00468    1 VPDDEHSFAFVNLKPAAPGHVLVCPKrHVE--TLPDLDEALLADLVITAQRVAAELEKHGNVPSLTVFVNDGAAAGQSVP 78


                 ....*...
gi 489196181 105 HIHFHVIP 112
Cdd:cd00468   79 HVHLHVLP 86
DcpS_C pfam11969
Scavenger mRNA decapping enzyme C-term binding; This family consists of several scavenger mRNA ...
 12-111 1.01e-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: 63.01  E-value: 1.01e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196181   12 IFAKIIRGEAPCYKVYEDEDVLAFLDLFPQSYGHTLVIPKH--AEARNLLEIDAQNLAKVMAVVqrltRALVEEVQPDGV 89
Cdd:pfam11969   3 VFCIIAKGEEPERVVYEDEGFVVFKDIKPKAPLHLLVIPKRhiKSLRDLTPEHLPLLEHMREVA----KKVIEEKYIGVD 78

                          90       100
                  ....*....|....*....|..
gi 489196181   90 QVAQFNGAPAGQTVFHIHFHVI 111
Cdd:pfam11969  79 RDELRLGFHYPPSVYHLHLHVI 100
PRK10687 PRK10687
purine nucleoside phosphoramidase; Provisional
 10-127 2.27e-12

purine nucleoside phosphoramidase; Provisional


Pssm-ID: 182648 [Multi-domain]  Cd Length: 119  Bit Score: 59.90  E-value: 2.27e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196181  10 QNIFAKIIRGEAPCYKVYEDEDVLAFLDLFPQSYGHTLVIPkhaearNLL-----EIDAQN---LAKVMAVVQRLTRAlv 81
Cdd:PRK10687   4 ETIFSKIIRREIPSDIVYQDELVTAFRDISPQAPTHILIIP------NILiptvnDVSAEHeqaLGRMITVAAKIAEQ-- 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 489196181  82 EEVQPDGVQVAQFNGAPAGQTVFHIHFHVIprfSGENLGIHAAKQG 127
Cdd:PRK10687  76 EGIAEDGYRLIMNTNRHGGQEVYHIHMHLL---GGRPLGPMLAHKG 118
aprataxin_related cd01278
aprataxin related: Aprataxin, a HINT family hydrolase is mutated in ataxia oculomotor apraxia ...
 26-123 3.32e-05

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: 40.45  E-value: 3.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196181  26 VYEDEDVLAFLDLFPQSYGHTLVIPKHaearnllEIDAqnlakvmavVQRLTRA---LVEEVQPDGVQVAQFNGAPAgQT 102
Cdd:cd01278   19 VYEDDRVVVFKDIYPKARHHYLVIPKE-------HIAS---------LKALTKEdvpLLEHMETVGREKLLRSDNTD-PS 81

                         90       100
                 ....*....|....*....|.
gi 489196181 103 VFHIHFHVIPRFSGENLGIHA 123
Cdd:cd01278   82 EFRFGFHAPPFTSVSHLHLHV 102
 
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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