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Conserved domains on  [gi|302883640|ref|XP_003040719|]
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uncharacterized protein NECHADRAFT_99860 [Fusarium vanettenii 77-13-4]

Protein Classification

HIT family protein( domain architecture ID 10101098)

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_subgroup cd01277
HINT (histidine triad nucleotide-binding protein) subgroup: Members of this CD belong to the ...
 7-104 2.31e-49

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: 153.15  E-value: 2.31e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302883640   7 CIFCRIIKGEIPCFKLFESDKTLAFLDIGPLSKGHALVIPKYHGEKLADIPDDHLAEVLPTLKKIVNATGATD----YNI 82
Cdd:cd01277    2 CIFCKIIAGEIPSYKVYEDDHVLAFLDINPASKGHTLVIPKKHYENLLDLDPEELAELILAAKKVARALKKALkadgLNI 81

                         90       100
                 ....*....|....*....|..
gi 302883640  83 LQNNGAIAHQEVKHVHFHMIPK 104
Cdd:cd01277   82 LQNNGRAAGQVVFHVHVHVIPR 103
 
Name Accession Description Interval E-value
HINT_subgroup cd01277
HINT (histidine triad nucleotide-binding protein) subgroup: Members of this CD belong to the ...
 7-104 2.31e-49

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: 153.15  E-value: 2.31e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302883640   7 CIFCRIIKGEIPCFKLFESDKTLAFLDIGPLSKGHALVIPKYHGEKLADIPDDHLAEVLPTLKKIVNATGATD----YNI 82
Cdd:cd01277    2 CIFCKIIAGEIPSYKVYEDDHVLAFLDINPASKGHTLVIPKKHYENLLDLDPEELAELILAAKKVARALKKALkadgLNI 81

                         90       100
                 ....*....|....*....|..
gi 302883640  83 LQNNGAIAHQEVKHVHFHMIPK 104
Cdd:cd01277   82 LQNNGRAAGQVVFHVHVHVIPR 103
HinT COG0537
Purine nucleoside phosphoramidase/Ap4A hydrolase, histidine triade (HIT) family [Nucleotide ...
 6-134 2.61e-42

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: 136.23  E-value: 2.61e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302883640   6 GCIFCRIIKGEIPCFKLFESDKTLAFLDIGPLSKGHALVIPKYHGEKLADIPDDHLAEVLPTLKKIVNA----TGATDYN 81
Cdd:COG0537    2 DCIFCKIIAGEIPALIVYEDEHVLAFLDINPYAPGHTLVIPKRHVASLFDLTPEELAELMRLAQKVAKAlrkaLGPDGFN 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 302883640  82 ILQNNGAIAHQEVKHVHFHMIPKpNEKEGLGVGWPTQSPDMDALKAYYEDIKS 134
Cdd:COG0537   82 LGINNGEAAGQTVPHLHVHVIPR-YEGDDNFMPVIGTKVDPEELEETARKLRA 133
HIT pfam01230
HIT domain;
14-104 5.84e-29

HIT domain;


Pssm-ID: 395984 [Multi-domain]  Cd Length: 98  Bit Score: 101.23  E-value: 5.84e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302883640   14 KGEIPCFKLFESDKTLAFLDIGPLSKGHALVIPKYHGEKLADIPDDHLAEVLPTLKKIVNATG----ATDYNILQNNGAI 89
Cdd:pfam01230   1 RGEIPSTVVYEDDLVLAFLDIDPQAPGHILVIPKKHIRELHDLTPEELGDLMSVAQKVARALGkvfkADGYRIVINNGAH 80

                          90
                  ....*....|....*
gi 302883640   90 AHQEVKHVHFHMIPK 104
Cdd:pfam01230  81 AGQSVPHLHIHVIPR 95
PRK10687 PRK10687
purine nucleoside phosphoramidase; Provisional
 8-102 4.16e-10

purine nucleoside phosphoramidase; Provisional


Pssm-ID: 182648 [Multi-domain]  Cd Length: 119  Bit Score: 53.74  E-value: 4.16e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302883640   8 IFCRIIKGEIPCFKLFESDKTLAFLDIGPLSKGHALVIPKYHGEKLADIPDDH---LAEVLPTLKKIVNATGATD--YNI 82
Cdd:PRK10687   6 IFSKIIRREIPSDIVYQDELVTAFRDISPQAPTHILIIPNILIPTVNDVSAEHeqaLGRMITVAAKIAEQEGIAEdgYRL 85

                         90       100
                 ....*....|....*....|
gi 302883640  83 LQNNGAIAHQEVKHVHFHMI 102
Cdd:PRK10687  86 IMNTNRHGGQEVYHIHMHLL 105
 
Name Accession Description Interval E-value
HINT_subgroup cd01277
HINT (histidine triad nucleotide-binding protein) subgroup: Members of this CD belong to the ...
 7-104 2.31e-49

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: 153.15  E-value: 2.31e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302883640   7 CIFCRIIKGEIPCFKLFESDKTLAFLDIGPLSKGHALVIPKYHGEKLADIPDDHLAEVLPTLKKIVNATGATD----YNI 82
Cdd:cd01277    2 CIFCKIIAGEIPSYKVYEDDHVLAFLDINPASKGHTLVIPKKHYENLLDLDPEELAELILAAKKVARALKKALkadgLNI 81

                         90       100
                 ....*....|....*....|..
gi 302883640  83 LQNNGAIAHQEVKHVHFHMIPK 104
Cdd:cd01277   82 LQNNGRAAGQVVFHVHVHVIPR 103
HinT COG0537
Purine nucleoside phosphoramidase/Ap4A hydrolase, histidine triade (HIT) family [Nucleotide ...
 6-134 2.61e-42

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: 136.23  E-value: 2.61e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302883640   6 GCIFCRIIKGEIPCFKLFESDKTLAFLDIGPLSKGHALVIPKYHGEKLADIPDDHLAEVLPTLKKIVNA----TGATDYN 81
Cdd:COG0537    2 DCIFCKIIAGEIPALIVYEDEHVLAFLDINPYAPGHTLVIPKRHVASLFDLTPEELAELMRLAQKVAKAlrkaLGPDGFN 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 302883640  82 ILQNNGAIAHQEVKHVHFHMIPKpNEKEGLGVGWPTQSPDMDALKAYYEDIKS 134
Cdd:COG0537   82 LGINNGEAAGQTVPHLHVHVIPR-YEGDDNFMPVIGTKVDPEELEETARKLRA 133
HIT pfam01230
HIT domain;
14-104 5.84e-29

HIT domain;


Pssm-ID: 395984 [Multi-domain]  Cd Length: 98  Bit Score: 101.23  E-value: 5.84e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302883640   14 KGEIPCFKLFESDKTLAFLDIGPLSKGHALVIPKYHGEKLADIPDDHLAEVLPTLKKIVNATG----ATDYNILQNNGAI 89
Cdd:pfam01230   1 RGEIPSTVVYEDDLVLAFLDIDPQAPGHILVIPKKHIRELHDLTPEELGDLMSVAQKVARALGkvfkADGYRIVINNGAH 80

                          90
                  ....*....|....*
gi 302883640   90 AHQEVKHVHFHMIPK 104
Cdd:pfam01230  81 AGQSVPHLHIHVIPR 95
PKCI_related cd01276
Protein Kinase C Interacting protein related (PKCI): PKCI and related proteins belong to the ...
 7-102 2.58e-28

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: 99.94  E-value: 2.58e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302883640   7 CIFCRIIKGEIPCFKLFESDKTLAFLDIGPLSKGHALVIPKYHGEKLADIPDDH---LAEVLPTLKKIVNATG--ATDYN 81
Cdd:cd01276    2 CIFCKIIRGEIPAKKVYEDDEVLAFHDINPQAPVHILVIPKKHIASLSDATEEDeelLGHLLSAAAKVAKDLGiaEDGYR 81

                         90       100
                 ....*....|....*....|.
gi 302883640  82 ILQNNGAIAHQEVKHVHFHMI 102
Cdd:cd01276   82 LVINCGKDGGQEVFHLHLHLL 102
DcpS_C pfam11969
Scavenger mRNA decapping enzyme C-term binding; This family consists of several scavenger mRNA ...
 7-113 3.00e-14

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: 64.16  E-value: 3.00e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302883640    7 CIFCRIIKGEIPCFKLFESDKTLAFLDIGPLSKGHALVIPKYHGEKLADIPDDH---LAEVLPTLKKIVNATGATDYNIL 83
Cdd:pfam11969   2 WVFCIIAKGEEPERVVYEDEGFVVFKDIKPKAPLHLLVIPKRHIKSLRDLTPEHlplLEHMREVAKKVIEEKYIGVDRDE 81

                          90       100       110
                  ....*....|....*....|....*....|
gi 302883640   84 QNNGAIAHQEVKHVHFHMIPKPNEKEGLGV 113
Cdd:pfam11969  82 LRLGFHYPPSVYHLHLHVISPDFESLGLGR 111
HIT_like cd00468
HIT family: HIT (Histidine triad) proteins, named for a motif related to the sequence HxHxH ...
 23-103 7.53e-13

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: 59.79  E-value: 7.53e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302883640  23 FESDKTLAFLDIGPLSKGHALVIPKYHGEKLADIPDDHLAEVLPTLKKIVNATGA----TDYNILQNNGAIAHQEVKHVH 98
Cdd:cd00468    2 PDDEHSFAFVNLKPAAPGHVLVCPKRHVETLPDLDEALLADLVITAQRVAAELEKhgnvPSLTVFVNDGAAAGQSVPHVH 81


                 ....*
gi 302883640  99 FHMIP 103
Cdd:cd00468   82 LHVLP 86
FHIT cd01275
FHIT (fragile histidine family): FHIT proteins, related to the HIT family carry a motif HxHxH ...
 7-103 1.64e-12

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: 60.00  E-value: 1.64e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302883640   7 CIFCRI-IKGEIPCFKLFESDKTLAFLDIGPLSKGHALVIPKYHGEKLADIPDDHLAEVLPTLKKIV----NATGATDYN 81
Cdd:cd01275    1 CVFCDIpIKPDEDNLVFYRTKHSFAVVNLYPYNPGHVLVVPYRHVPRLEDLTPEEIADLFKLVQLAMkalkVVYKPDGFN 80

                         90       100
                 ....*....|....*....|..
gi 302883640  82 ILQNNGAIAHQEVKHVHFHMIP 103
Cdd:cd01275   81 IGINDGKAGGGIVPHVHIHIVP 102
PRK10687 PRK10687
purine nucleoside phosphoramidase; Provisional
 8-102 4.16e-10

purine nucleoside phosphoramidase; Provisional


Pssm-ID: 182648 [Multi-domain]  Cd Length: 119  Bit Score: 53.74  E-value: 4.16e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302883640   8 IFCRIIKGEIPCFKLFESDKTLAFLDIGPLSKGHALVIPKYHGEKLADIPDDH---LAEVLPTLKKIVNATGATD--YNI 82
Cdd:PRK10687   6 IFSKIIRREIPSDIVYQDELVTAFRDISPQAPTHILIIPNILIPTVNDVSAEHeqaLGRMITVAAKIAEQEGIAEdgYRL 85

                         90       100
                 ....*....|....*....|
gi 302883640  83 LQNNGAIAHQEVKHVHFHMI 102
Cdd:PRK10687  86 IMNTNRHGGQEVYHIHMHLL 105
aprataxin_related cd01278
aprataxin related: Aprataxin, a HINT family hydrolase is mutated in ataxia oculomotor apraxia ...
 6-103 3.06e-09

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: 50.85  E-value: 3.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302883640   6 GCIFCRIIKGEIPCFKL--FESDKTLAFLDIGPLSKGHALVIPKYHGEKLADIPDDHlaevLPTLKKIVNatgaTDYNIL 83
Cdd:cd01278    1 LCHFCDIAKRRDPDPEDqvYEDDRVVVFKDIYPKARHHYLVIPKEHIASLKALTKED----VPLLEHMET----VGREKL 72

                         90       100
                 ....*....|....*....|
gi 302883640  84 QNNGAIAHQEVKhVHFHMIP 103
Cdd:cd01278   73 LRSDNTDPSEFR-FGFHAPP 91
CwfJ_C_1 pfam04677
Protein similar to CwfJ C-terminus 1; This region is found in the N terminus of ...
 25-107 2.10e-04

Protein similar to CwfJ C-terminus 1; This region is found in the N terminus of Schizosaccharomyces pombe protein CwfJ. CwfJ is part of the Cdc5p complex involved in mRNA splicing.


Pssm-ID: 428062  Cd Length: 122  Bit Score: 38.51  E-value: 2.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302883640   25 SDKTLAFLDIGPLSKGHALVIPKYHGEKLADIPDDHLAEVLPTLKKIVNATGAtdynilQNNGAI----AHQEVKHVHFH 100
Cdd:pfam04677  32 GNKAYLALPKGPLVSGHCLIIPIQHIPSTLSLDEEVWDEIRNFRKALTLMYKS------QGKDAVffeiASQRRPHLHIQ 105


                  ....*..
gi 302883640  101 MIPKPNE 107
Cdd:pfam04677 106 CIPVPKS 112
PLN02643 PLN02643
ADP-glucose phosphorylase
 41-130 2.29e-03

ADP-glucose phosphorylase


Pssm-ID: 215346 [Multi-domain]  Cd Length: 336  Bit Score: 36.66  E-value: 2.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302883640  41 HALVI--PKyHGEKLADIPDDHLAEVLPTLKKIVNATGATD----YNILQNNGAIAHQEVKHVHFHMIpkpnekeGLGVG 114
Cdd:PLN02643 108 HDVVIetPV-HSVQLSDLPARHIGEVLKAYKKRINQLQSDSrfkyVQVFKNHGASAGASMSHSHSQII-------ALPVV 179

                         90
                 ....*....|....*.
gi 302883640 115 WPTQSPDMDALKAYYE 130
Cdd:PLN02643 180 PPSVSARLDGSKEYFE 195
GalT COG1085
Galactose-1-phosphate uridylyltransferase [Carbohydrate transport and metabolism];
6-101 9.74e-03

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


Pssm-ID: 440702 [Multi-domain]  Cd Length: 336  Bit Score: 34.81  E-value: 9.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302883640   6 GCIFCRIIKGEIPCFK--LFESDKTLAFLDIGPLSKGHALVIPKYHGEKLADIPDDHLAEVLPTLKKIV----NATGATD 79
Cdd:COG1085  191 RCLLCDILAQELAAGErvVAENEHFVAFVPFAARWPFETWILPKRHVSDFEELTDEERDDLARILKRVLrrldNLLGDFP 270

                         90       100
                 ....*....|....*....|..
gi 302883640  80 YNILQNNGAIAHQEVKHVHFHM 101
Cdd:COG1085  271 YNMGLHQAPVDGEERDHYHWHL 292
 
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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