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Conserved domains on  [gi|49176077|ref|NP_415621|]
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purine nucleoside phosphoramidase [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

histidine triad nucleotide-binding protein( domain architecture ID 10013601)

histidine triad nucleotide-binding protein of the histidine triad family of nucleotide hydrolases and transferases, which act on the alpha-phosphate of ribonucleotides

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10687 PRK10687
purine nucleoside phosphoramidase; Provisional
 1-119 5.54e-83

purine nucleoside phosphoramidase; Provisional


:

Pssm-ID: 182648 [Multi-domain]  Cd Length: 119  Bit Score: 237.87  E-value: 5.54e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176077    1 MAEETIFSKIIRREIPSDIVYQDDLVTAFRDISPQAPTHILIIPNILIPTVNDVSAEHEQALGRMITVAAKIAEQEGIAE 80
Cdd:PRK10687   1 MAEETIFSKIIRREIPSDIVYQDELVTAFRDISPQAPTHILIIPNILIPTVNDVSAEHEQALGRMITVAAKIAEQEGIAE 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 49176077   81 DGYRLIMNTNRHGGQEVYHIHMHLLGGRPLGPMLAHKGL 119
Cdd:PRK10687  81 DGYRLIMNTNRHGGQEVYHIHMHLLGGRPLGPMLAHKGL 119
 
Name Accession Description Interval E-value
PRK10687 PRK10687
purine nucleoside phosphoramidase; Provisional
 1-119 5.54e-83

purine nucleoside phosphoramidase; Provisional


Pssm-ID: 182648 [Multi-domain]  Cd Length: 119  Bit Score: 237.87  E-value: 5.54e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176077    1 MAEETIFSKIIRREIPSDIVYQDDLVTAFRDISPQAPTHILIIPNILIPTVNDVSAEHEQALGRMITVAAKIAEQEGIAE 80
Cdd:PRK10687   1 MAEETIFSKIIRREIPSDIVYQDELVTAFRDISPQAPTHILIIPNILIPTVNDVSAEHEQALGRMITVAAKIAEQEGIAE 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 49176077   81 DGYRLIMNTNRHGGQEVYHIHMHLLGGRPLGPMLAHKGL 119
Cdd:PRK10687  81 DGYRLIMNTNRHGGQEVYHIHMHLLGGRPLGPMLAHKGL 119
PKCI_related cd01276
Protein Kinase C Interacting protein related (PKCI): PKCI and related proteins belong to the ...
 4-107 2.12e-50

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: 155.03  E-value: 2.12e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176077   4 ETIFSKIIRREIPSDIVYQDDLVTAFRDISPQAPTHILIIPNILIPTVNDVSAEHEQALGRMITVAAKIAEQEGIAEDGY 83
Cdd:cd01276   1 DCIFCKIIRGEIPAKKVYEDDEVLAFHDINPQAPVHILVIPKKHIASLSDATEEDEELLGHLLSAAAKVAKDLGIAEDGY 80

                        90       100
                ....*....|....*....|....
gi 49176077  84 RLIMNTNRHGGQEVYHIHMHLLGG 107
Cdd:cd01276  81 RLVINCGKDGGQEVFHLHLHLLGG 104
HinT COG0537
Purine nucleoside phosphoramidase/Ap4A hydrolase, histidine triade (HIT) family [Nucleotide ...
 3-108 1.70e-30

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: 105.42  E-value: 1.70e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176077   3 EETIFSKIIRREIPSDIVYQDDLVTAFRDISPQAPTHILIIPNILIPTVNDVSAEheqALGRMITVAAKIAE--QEGIAE 80
Cdd:COG0537   1 MDCIFCKIIAGEIPALIVYEDEHVLAFLDINPYAPGHTLVIPKRHVASLFDLTPE---ELAELMRLAQKVAKalRKALGP 77

                        90       100
                ....*....|....*....|....*...
gi 49176077  81 DGYRLIMNTNRHGGQEVYHIHMHLLGGR 108
Cdd:COG0537  78 DGFNLGINNGEAAGQTVPHLHVHVIPRY 105
HIT pfam01230
HIT domain;
12-110 1.74e-29

HIT domain;


Pssm-ID: 395984 [Multi-domain]  Cd Length: 98  Bit Score: 102.00  E-value: 1.74e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176077    12 RREIPSDIVYQDDLVTAFRDISPQAPTHILIIPNILIPTVNDVSAEheqALGRMITVAAKIAEQEGI--AEDGYRLIMNT 89
Cdd:pfam01230   1 RGEIPSTVVYEDDLVLAFLDIDPQAPGHILVIPKKHIRELHDLTPE---ELGDLMSVAQKVARALGKvfKADGYRIVINN 77

                          90       100
                  ....*....|....*....|.
gi 49176077    90 NRHGGQEVYHIHMHLLGGRPL 110
Cdd:pfam01230  78 GAHAGQSVPHLHIHVIPRRKH 98
 
Name Accession Description Interval E-value
PRK10687 PRK10687
purine nucleoside phosphoramidase; Provisional
 1-119 5.54e-83

purine nucleoside phosphoramidase; Provisional


Pssm-ID: 182648 [Multi-domain]  Cd Length: 119  Bit Score: 237.87  E-value: 5.54e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176077    1 MAEETIFSKIIRREIPSDIVYQDDLVTAFRDISPQAPTHILIIPNILIPTVNDVSAEHEQALGRMITVAAKIAEQEGIAE 80
Cdd:PRK10687   1 MAEETIFSKIIRREIPSDIVYQDELVTAFRDISPQAPTHILIIPNILIPTVNDVSAEHEQALGRMITVAAKIAEQEGIAE 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 49176077   81 DGYRLIMNTNRHGGQEVYHIHMHLLGGRPLGPMLAHKGL 119
Cdd:PRK10687  81 DGYRLIMNTNRHGGQEVYHIHMHLLGGRPLGPMLAHKGL 119
PKCI_related cd01276
Protein Kinase C Interacting protein related (PKCI): PKCI and related proteins belong to the ...
 4-107 2.12e-50

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: 155.03  E-value: 2.12e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176077   4 ETIFSKIIRREIPSDIVYQDDLVTAFRDISPQAPTHILIIPNILIPTVNDVSAEHEQALGRMITVAAKIAEQEGIAEDGY 83
Cdd:cd01276   1 DCIFCKIIRGEIPAKKVYEDDEVLAFHDINPQAPVHILVIPKKHIASLSDATEEDEELLGHLLSAAAKVAKDLGIAEDGY 80

                        90       100
                ....*....|....*....|....
gi 49176077  84 RLIMNTNRHGGQEVYHIHMHLLGG 107
Cdd:cd01276  81 RLVINCGKDGGQEVFHLHLHLLGG 104
HinT COG0537
Purine nucleoside phosphoramidase/Ap4A hydrolase, histidine triade (HIT) family [Nucleotide ...
 3-108 1.70e-30

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: 105.42  E-value: 1.70e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176077   3 EETIFSKIIRREIPSDIVYQDDLVTAFRDISPQAPTHILIIPNILIPTVNDVSAEheqALGRMITVAAKIAE--QEGIAE 80
Cdd:COG0537   1 MDCIFCKIIAGEIPALIVYEDEHVLAFLDINPYAPGHTLVIPKRHVASLFDLTPE---ELAELMRLAQKVAKalRKALGP 77

                        90       100
                ....*....|....*....|....*...
gi 49176077  81 DGYRLIMNTNRHGGQEVYHIHMHLLGGR 108
Cdd:COG0537  78 DGFNLGINNGEAAGQTVPHLHVHVIPRY 105
HIT pfam01230
HIT domain;
12-110 1.74e-29

HIT domain;


Pssm-ID: 395984 [Multi-domain]  Cd Length: 98  Bit Score: 102.00  E-value: 1.74e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176077    12 RREIPSDIVYQDDLVTAFRDISPQAPTHILIIPNILIPTVNDVSAEheqALGRMITVAAKIAEQEGI--AEDGYRLIMNT 89
Cdd:pfam01230   1 RGEIPSTVVYEDDLVLAFLDIDPQAPGHILVIPKKHIRELHDLTPE---ELGDLMSVAQKVARALGKvfKADGYRIVINN 77

                          90       100
                  ....*....|....*....|.
gi 49176077    90 NRHGGQEVYHIHMHLLGGRPL 110
Cdd:pfam01230  78 GAHAGQSVPHLHIHVIPRRKH 98
DcpS_C pfam11969
Scavenger mRNA decapping enzyme C-term binding; This family consists of several scavenger mRNA ...
 5-106 1.20e-19

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: 77.26  E-value: 1.20e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176077     5 TIFSKIIRREIPSDIVYQDDLVTAFRDISPQAPTHILIIPNILIPTVNDVSAEHEQALGRMITVAAKIAEQEGIAedGYR 84
Cdd:pfam11969   2 WVFCIIAKGEEPERVVYEDEGFVVFKDIKPKAPLHLLVIPKRHIKSLRDLTPEHLPLLEHMREVAKKVIEEKYIG--VDR 79

                          90       100
                  ....*....|....*....|..
gi 49176077    85 LIMNTNRHGGQEVYHIHMHLLG 106
Cdd:pfam11969  80 DELRLGFHYPPSVYHLHLHVIS 101
HINT_subgroup cd01277
HINT (histidine triad nucleotide-binding protein) subgroup: Members of this CD belong to the ...
 6-104 3.03e-19

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: 76.11  E-value: 3.03e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176077   6 IFSKIIRREIPSDIVYQDDLVTAFRDISPQAPTHILIIPNILIPTVNDVSAEheqALGRMITVAAKIAE--QEGIAEDGY 83
Cdd:cd01277   3 IFCKIIAGEIPSYKVYEDDHVLAFLDINPASKGHTLVIPKKHYENLLDLDPE---ELAELILAAKKVARalKKALKADGL 79

                        90       100
                ....*....|....*....|.
gi 49176077  84 RLIMNTNRHGGQEVYHIHMHL 104
Cdd:cd01277  80 NILQNNGRAAGQVVFHVHVHV 100
HIT_like cd00468
HIT family: HIT (Histidine triad) proteins, named for a motif related to the sequence HxHxH ...
 20-106 6.43e-09

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: 49.00  E-value: 6.43e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176077  20 VYQDDLVTAFRDISPQAPTHILIIPNILIPTVNDVSaehEQALGRMITVAAKIAE--QEGIAEDGYRLIMNTNRHGGQEV 97
Cdd:cd00468   1 VPDDEHSFAFVNLKPAAPGHVLVCPKRHVETLPDLD---EALLADLVITAQRVAAelEKHGNVPSLTVFVNDGAAAGQSV 77


                ....*....
gi 49176077  98 YHIHMHLLG 106
Cdd:cd00468  78 PHVHLHVLP 86
aprataxin_related cd01278
aprataxin related: Aprataxin, a HINT family hydrolase is mutated in ataxia oculomotor apraxia ...
 5-105 6.82e-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: 44.30  E-value: 6.82e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49176077   5 TIFSKI--IRREIPSDIVYQDDLVTAFRDISPQAPTHILIIPNILIPTVNDVSAEHEQALGRMITVAAKIAEQE-GIAED 81
Cdd:cd01278   2 CHFCDIakRRDPDPEDQVYEDDRVVVFKDIYPKARHHYLVIPKEHIASLKALTKEDVPLLEHMETVGREKLLRSdNTDPS 81

                        90       100
                ....*....|....*....|....*...
gi 49176077  82 ----GYRLIMNTNrhggqeVYHIHMHLL 105
Cdd:cd01278  82 efrfGFHAPPFTS------VSHLHLHVI 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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