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Conserved domains on  [gi|759489647|ref|WP_043210538|]
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histidine triad nucleotide-binding protein [Bordetella pseudohinzii]

Protein Classification

histidine triad nucleotide-binding protein( domain architecture ID 10101095)

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
PKCI_related cd01276
Protein Kinase C Interacting protein related (PKCI): PKCI and related proteins belong to the ...
 4-110 2.29e-57

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: 172.75  E-value: 2.29e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759489647   4 NCIFCKIAQGDIPAKKVYEDDEFVVFHDINPAAPVHLLLIPRRHIASMQDITAEDAGWLGRMMTLVPRLAQENGCNpgpE 83
Cdd:cd01276    1 DCIFCKIIRGEIPAKKVYEDDEVLAFHDINPQAPVHILVIPKKHIASLSDATEEDEELLGHLLSAAAKVAKDLGIA---E 77

                         90       100
                 ....*....|....*....|....*..
gi 759489647  84 GGFRLLANSGAEGGQEVPHLHFHIIGG 110
Cdd:cd01276   78 DGYRLVINCGKDGGQEVFHLHLHLLGG 104
 
Name Accession Description Interval E-value
PKCI_related cd01276
Protein Kinase C Interacting protein related (PKCI): PKCI and related proteins belong to the ...
 4-110 2.29e-57

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: 172.75  E-value: 2.29e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759489647   4 NCIFCKIAQGDIPAKKVYEDDEFVVFHDINPAAPVHLLLIPRRHIASMQDITAEDAGWLGRMMTLVPRLAQENGCNpgpE 83
Cdd:cd01276    1 DCIFCKIIRGEIPAKKVYEDDEVLAFHDINPQAPVHILVIPKKHIASLSDATEEDEELLGHLLSAAAKVAKDLGIA---E 77

                         90       100
                 ....*....|....*....|....*..
gi 759489647  84 GGFRLLANSGAEGGQEVPHLHFHIIGG 110
Cdd:cd01276   78 DGYRLVINCGKDGGQEVFHLHLHLLGG 104
HinT COG0537
Purine nucleoside phosphoramidase/Ap4A hydrolase, histidine triade (HIT) family [Nucleotide ...
 3-110 1.91e-47

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: 148.56  E-value: 1.91e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759489647   3 ENCIFCKIAQGDIPAKKVYEDDEFVVFHDINPAAPVHLLLIPRRHIASMQDITAEDagwLGRMMTLVPRL--AQENGCNP 80
Cdd:COG0537    1 MDCIFCKIIAGEIPALIVYEDEHVLAFLDINPYAPGHTLVIPKRHVASLFDLTPEE---LAELMRLAQKVakALRKALGP 77

                         90       100       110
                 ....*....|....*....|....*....|
gi 759489647  81 gpeGGFRLLANSGAEGGQEVPHLHFHIIGG 110
Cdd:COG0537   78 ---DGFNLGINNGEAAGQTVPHLHVHVIPR 104
DcpS_C pfam11969
Scavenger mRNA decapping enzyme C-term binding; This family consists of several scavenger mRNA ...
 4-109 5.44e-32

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: 108.85  E-value: 5.44e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759489647    4 NCIFCKIAQGDIPAKKVYEDDEFVVFHDINPAAPVHLLLIPRRHIASMQDITAEDAGWLGRMMTLVPRLAQENGcnpgpE 83
Cdd:pfam11969   1 KWVFCIIAKGEEPERVVYEDEGFVVFKDIKPKAPLHLLVIPKRHIKSLRDLTPEHLPLLEHMREVAKKVIEEKY-----I 75

                          90       100
                  ....*....|....*....|....*.
gi 759489647   84 GGFRLLANSGAEGGQEVPHLHFHIIG 109
Cdd:pfam11969  76 GVDRDELRLGFHYPPSVYHLHLHVIS 101
PRK10687 PRK10687
purine nucleoside phosphoramidase; Provisional
 1-110 3.48e-30

purine nucleoside phosphoramidase; Provisional


Pssm-ID: 182648 [Multi-domain]  Cd Length: 119  Bit Score: 104.59  E-value: 3.48e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759489647   1 MSENCIFCKIAQGDIPAKKVYEDDEFVVFHDINPAAPVHLLLIPRRHIASMQDITAEDAGWLGRMMTLVPRLAQENGCnp 80
Cdd:PRK10687   1 MAEETIFSKIIRREIPSDIVYQDELVTAFRDISPQAPTHILIIPNILIPTVNDVSAEHEQALGRMITVAAKIAEQEGI-- 78

                         90       100       110
                 ....*....|....*....|....*....|
gi 759489647  81 gPEGGFRLLANSGAEGGQEVPHLHFHIIGG 110
Cdd:PRK10687  79 -AEDGYRLIMNTNRHGGQEVYHIHMHLLGG 107
 
Name Accession Description Interval E-value
PKCI_related cd01276
Protein Kinase C Interacting protein related (PKCI): PKCI and related proteins belong to the ...
 4-110 2.29e-57

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: 172.75  E-value: 2.29e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759489647   4 NCIFCKIAQGDIPAKKVYEDDEFVVFHDINPAAPVHLLLIPRRHIASMQDITAEDAGWLGRMMTLVPRLAQENGCNpgpE 83
Cdd:cd01276    1 DCIFCKIIRGEIPAKKVYEDDEVLAFHDINPQAPVHILVIPKKHIASLSDATEEDEELLGHLLSAAAKVAKDLGIA---E 77

                         90       100
                 ....*....|....*....|....*..
gi 759489647  84 GGFRLLANSGAEGGQEVPHLHFHIIGG 110
Cdd:cd01276   78 DGYRLVINCGKDGGQEVFHLHLHLLGG 104
HinT COG0537
Purine nucleoside phosphoramidase/Ap4A hydrolase, histidine triade (HIT) family [Nucleotide ...
 3-110 1.91e-47

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: 148.56  E-value: 1.91e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759489647   3 ENCIFCKIAQGDIPAKKVYEDDEFVVFHDINPAAPVHLLLIPRRHIASMQDITAEDagwLGRMMTLVPRL--AQENGCNP 80
Cdd:COG0537    1 MDCIFCKIIAGEIPALIVYEDEHVLAFLDINPYAPGHTLVIPKRHVASLFDLTPEE---LAELMRLAQKVakALRKALGP 77

                         90       100       110
                 ....*....|....*....|....*....|
gi 759489647  81 gpeGGFRLLANSGAEGGQEVPHLHFHIIGG 110
Cdd:COG0537   78 ---DGFNLGINNGEAAGQTVPHLHVHVIPR 104
HINT_subgroup cd01277
HINT (histidine triad nucleotide-binding protein) subgroup: Members of this CD belong to the ...
 4-108 3.96e-36

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: 118.86  E-value: 3.96e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759489647   4 NCIFCKIAQGDIPAKKVYEDDEFVVFHDINPAAPVHLLLIPRRHIASMQDITAEDagwLGRMMTLVPRLAQENGCNPGPE 83
Cdd:cd01277    1 DCIFCKIIAGEIPSYKVYEDDHVLAFLDINPASKGHTLVIPKKHYENLLDLDPEE---LAELILAAKKVARALKKALKAD 77

                         90       100
                 ....*....|....*....|....*
gi 759489647  84 gGFRLLANSGAEGGQEVPHLHFHII 108
Cdd:cd01277   78 -GLNILQNNGRAAGQVVFHVHVHVI 101
DcpS_C pfam11969
Scavenger mRNA decapping enzyme C-term binding; This family consists of several scavenger mRNA ...
 4-109 5.44e-32

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: 108.85  E-value: 5.44e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759489647    4 NCIFCKIAQGDIPAKKVYEDDEFVVFHDINPAAPVHLLLIPRRHIASMQDITAEDAGWLGRMMTLVPRLAQENGcnpgpE 83
Cdd:pfam11969   1 KWVFCIIAKGEEPERVVYEDEGFVVFKDIKPKAPLHLLVIPKRHIKSLRDLTPEHLPLLEHMREVAKKVIEEKY-----I 75

                          90       100
                  ....*....|....*....|....*.
gi 759489647   84 GGFRLLANSGAEGGQEVPHLHFHIIG 109
Cdd:pfam11969  76 GVDRDELRLGFHYPPSVYHLHLHVIS 101
HIT pfam01230
HIT domain;
12-110 1.12e-31

HIT domain;


Pssm-ID: 395984 [Multi-domain]  Cd Length: 98  Bit Score: 107.78  E-value: 1.12e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759489647   12 QGDIPAKKVYEDDEFVVFHDINPAAPVHLLLIPRRHIASMQDITAEDagwLGRMMTLVPRLAQENGCNPGPEgGFRLLAN 91
Cdd:pfam01230   1 RGEIPSTVVYEDDLVLAFLDIDPQAPGHILVIPKKHIRELHDLTPEE---LGDLMSVAQKVARALGKVFKAD-GYRIVIN 76

                          90
                  ....*....|....*....
gi 759489647   92 SGAEGGQEVPHLHFHIIGG 110
Cdd:pfam01230  77 NGAHAGQSVPHLHIHVIPR 95
PRK10687 PRK10687
purine nucleoside phosphoramidase; Provisional
 1-110 3.48e-30

purine nucleoside phosphoramidase; Provisional


Pssm-ID: 182648 [Multi-domain]  Cd Length: 119  Bit Score: 104.59  E-value: 3.48e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759489647   1 MSENCIFCKIAQGDIPAKKVYEDDEFVVFHDINPAAPVHLLLIPRRHIASMQDITAEDAGWLGRMMTLVPRLAQENGCnp 80
Cdd:PRK10687   1 MAEETIFSKIIRREIPSDIVYQDELVTAFRDISPQAPTHILIIPNILIPTVNDVSAEHEQALGRMITVAAKIAEQEGI-- 78

                         90       100       110
                 ....*....|....*....|....*....|
gi 759489647  81 gPEGGFRLLANSGAEGGQEVPHLHFHIIGG 110
Cdd:PRK10687  79 -AEDGYRLIMNTNRHGGQEVYHIHMHLLGG 107
HIT_like cd00468
HIT family: HIT (Histidine triad) proteins, named for a motif related to the sequence HxHxH ...
 20-109 6.60e-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: 69.80  E-value: 6.60e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759489647  20 VYEDDEFVVFHDINPAAPVHLLLIPRRHIASMQDITaEDAgwLGRMMTLVPRLAQENGCNPGPEgGFRLLANSGAEGGQE 99
Cdd:cd00468    1 VPDDEHSFAFVNLKPAAPGHVLVCPKRHVETLPDLD-EAL--LADLVITAQRVAAELEKHGNVP-SLTVFVNDGAAAGQS 76

                         90
                 ....*....|
gi 759489647 100 VPHLHFHIIG 109
Cdd:cd00468   77 VPHVHLHVLP 86
aprataxin_related cd01278
aprataxin related: Aprataxin, a HINT family hydrolase is mutated in ataxia oculomotor apraxia ...
 4-108 1.00e-16

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: 69.72  E-value: 1.00e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759489647   4 NCIFCKIAQGDIPAKK--VYEDDEFVVFHDINPAAPVHLLLIPRRHIASMQDITAEDAGWLGRMMT-LVPRLAQENGCNP 80
Cdd:cd01278    1 LCHFCDIAKRRDPDPEdqVYEDDRVVVFKDIYPKARHHYLVIPKEHIASLKALTKEDVPLLEHMETvGREKLLRSDNTDP 80

                         90       100       110
                 ....*....|....*....|....*....|
gi 759489647  81 GPEG-GFRLL-ANSgaeggqeVPHLHFHII 108
Cdd:cd01278   81 SEFRfGFHAPpFTS-------VSHLHLHVI 103
FHIT cd01275
FHIT (fragile histidine family): FHIT proteins, related to the HIT family carry a motif HxHxH ...
 5-108 1.11e-13

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: 62.69  E-value: 1.11e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759489647   5 CIFCKIAQGDIPAKKV-YEDDEFVVFHDINPAAPVHLLLIPRRHIASMQDITAEDAGWLGRMMTLVPRlAQENGCNPGpe 83
Cdd:cd01275    1 CVFCDIPIKPDEDNLVfYRTKHSFAVVNLYPYNPGHVLVVPYRHVPRLEDLTPEEIADLFKLVQLAMK-ALKVVYKPD-- 77

                         90       100
                 ....*....|....*....|....*
gi 759489647  84 gGFRLLANSGAEGGQEVPHLHFHII 108
Cdd:cd01275   78 -GFNIGINDGKAGGGIVPHVHIHIV 101
GalT COG1085
Galactose-1-phosphate uridylyltransferase [Carbohydrate transport and metabolism];
5-107 2.89e-07

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


Pssm-ID: 440702 [Multi-domain]  Cd Length: 336  Bit Score: 47.52  E-value: 2.89e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759489647   5 CIFCKIAQGDIPAKK--VYEDDEFVVFhdiNPAA---PVHLLLIPRRHIASMQDITAEDAGWLGRMM-TLVPRLAQENGC 78
Cdd:COG1085  192 CLLCDILAQELAAGErvVAENEHFVAF---VPFAarwPFETWILPKRHVSDFEELTDEERDDLARILkRVLRRLDNLLGD 268

                         90       100
                 ....*....|....*....|....*....
gi 759489647  79 NPgpeggFRLLANSGAEGGQEVPHLHFHI 107
Cdd:COG1085  269 FP-----YNMGLHQAPVDGEERDHYHWHL 292
GalT cd00608
Galactose-1-phosphate uridyl transferase (GalT): This enzyme plays a key role in galactose ...
 5-108 3.36e-04

Galactose-1-phosphate uridyl transferase (GalT): This enzyme plays a key role in galactose metabolism by catalysing the transfer of a uridine 5'-phosphoryl group from UDP-galactose 1-phosphate. The structure of E.coli GalT reveals that the enzyme contains two identical subunits. It also demonstrates that the active site is formed by amino acid residues from both subunits of the dimer.


Pssm-ID: 238341 [Multi-domain]  Cd Length: 329  Bit Score: 38.44  E-value: 3.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759489647   5 CIFCKIAQGDIPAKK--VYEDDEFVVFhdiNPAA---PVHLLLIPRRHIASMQDITAEDAGWLGRMMTLV-PRLAQENGC 78
Cdd:cd00608  186 CLLCDYLKLELESKEriVVENEHFVAV---VPFWarwPFEVHILPKRHVSRFTDLTDEEREDLAEILKRLlARYDNLFNC 262

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 759489647  79 NP--------GPEGGFRlLANSGAeggqevpHLHFHII 108
Cdd:cd00608  263 SFpysmgwhqAPTGGKE-LENWYY-------HWHFEIP 292
PLN02643 PLN02643
ADP-glucose phosphorylase
 4-107 1.71e-03

ADP-glucose phosphorylase


Pssm-ID: 215346 [Multi-domain]  Cd Length: 336  Bit Score: 36.66  E-value: 1.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759489647   4 NCIFCKIAQGDIpakKVYEDDEFVVFHDINPAAPVHLLLIPRRHIASMQDITAEDAGWLGRMMTLVPR-LAQENGCnpgP 82
Cdd:PLN02643 199 KCSLCEVVKKDL---LIDESSHFVSIAPFAATFPFEIWIIPRDHSSNFHEIDDDKAVDLGGLLKLMLQkISKQLND---P 272

                         90       100
                 ....*....|....*....|....*
gi 759489647  83 EGGFRLLANSGAEGGQEVPHLHFHI 107
Cdd:PLN02643 273 PYNYMIQTSPLGVEESNLPYTHWFL 297
 
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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