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Conserved domains on  [gi|1658472267|ref|NP_001357602|]
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aprataxin isoform j [Homo sapiens]

Protein Classification

aprataxin_related and zf-C2HE domain-containing protein( domain architecture ID 10841342)

aprataxin_related and zf-C2HE domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
aprataxin_related cd01278
aprataxin related: Aprataxin, a HINT family hydrolase is mutated in ataxia oculomotor apraxia ...
 76-177 1.27e-49

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: 158.32  E-value: 1.27e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658472267  76 LGHWSQGLKISMQDPKMQVYKDEQVVVIKDKYPKARYHWLVLPWTSISSLKAVAREHLELLKHMHTVGEKVIVDFAGSSK 155
Cdd:cd01278     1 LCHFCDIAKRRDPDPEDQVYEDDRVVVFKDIYPKARHHYLVIPKEHIASLKALTKEDVPLLEHMETVGREKLLRSDNTDP 80

                          90       100
                  ....*....|....*....|....
gi 1658472267 156 LRFRLGYHAIP--SMSHVHLHVIS 177
Cdd:cd01278    81 SEFRFGFHAPPftSVSHLHLHVIA 104
zf-C2HE pfam16278
C2HE / C2H2 / C2HC zinc-binding finger; zf-C2HE is an unusual zinc-binding domain found in ...
 195-254 8.35e-19

C2HE / C2H2 / C2HC zinc-binding finger; zf-C2HE is an unusual zinc-binding domain found in fungi, plants and metazoa. It is often found at the C-terminus of HIT-domain-containing proteins, pfam01230. In fungi the fourth ligand is a Glu, in plants it is Cys and in metazoans it is usually a His. The fourth ligand is often mutated in neurogenerative disease-states.


:

Pssm-ID: 465082  Cd Length: 60  Bit Score: 77.71  E-value: 8.35e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658472267 195 NTEYFLESQAVIEMVQEAGRVTVRDGMPELLKLPLRCHECQQLLPSIPQLKEHLRKHWTQ 254
Cdd:pfam16278   1 NTPFFVPLDDVPEWLEEDGKIELLPSEVLLLKTPLKCHRCGNFGNNFPKLKAHLEEHFEK 60
 
Name Accession Description Interval E-value
aprataxin_related cd01278
aprataxin related: Aprataxin, a HINT family hydrolase is mutated in ataxia oculomotor apraxia ...
 76-177 1.27e-49

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: 158.32  E-value: 1.27e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658472267  76 LGHWSQGLKISMQDPKMQVYKDEQVVVIKDKYPKARYHWLVLPWTSISSLKAVAREHLELLKHMHTVGEKVIVDFAGSSK 155
Cdd:cd01278     1 LCHFCDIAKRRDPDPEDQVYEDDRVVVFKDIYPKARHHYLVIPKEHIASLKALTKEDVPLLEHMETVGREKLLRSDNTDP 80

                          90       100
                  ....*....|....*....|....
gi 1658472267 156 LRFRLGYHAIP--SMSHVHLHVIS 177
Cdd:cd01278    81 SEFRFGFHAPPftSVSHLHLHVIA 104
DcpS_C pfam11969
Scavenger mRNA decapping enzyme C-term binding; This family consists of several scavenger mRNA ...
 85-190 5.77e-40

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: 133.88  E-value: 5.77e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658472267  85 ISMQDPKMQVYKDEQVVVIKDKYPKARYHWLVLPWTSISSLKAVAREHLELLKHMHTVGEKVIVD-FAGSSKLRFRLGYH 163
Cdd:pfam11969   8 AKGEEPERVVYEDEGFVVFKDIKPKAPLHLLVIPKRHIKSLRDLTPEHLPLLEHMREVAKKVIEEkYIGVDRDELRLGFH 87

                          90       100
                  ....*....|....*....|....*..
gi 1658472267 164 AIPSMSHVHLHVISQDFDSPCLKNKKH 190
Cdd:pfam11969  88 YPPSVYHLHLHVISPDFESLGLGRKKG 114
zf-C2HE pfam16278
C2HE / C2H2 / C2HC zinc-binding finger; zf-C2HE is an unusual zinc-binding domain found in ...
 195-254 8.35e-19

C2HE / C2H2 / C2HC zinc-binding finger; zf-C2HE is an unusual zinc-binding domain found in fungi, plants and metazoa. It is often found at the C-terminus of HIT-domain-containing proteins, pfam01230. In fungi the fourth ligand is a Glu, in plants it is Cys and in metazoans it is usually a His. The fourth ligand is often mutated in neurogenerative disease-states.


Pssm-ID: 465082  Cd Length: 60  Bit Score: 77.71  E-value: 8.35e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658472267 195 NTEYFLESQAVIEMVQEAGRVTVRDGMPELLKLPLRCHECQQLLPSIPQLKEHLRKHWTQ 254
Cdd:pfam16278   1 NTPFFVPLDDVPEWLEEDGKIELLPSEVLLLKTPLKCHRCGNFGNNFPKLKAHLEEHFEK 60
HinT COG0537
Purine nucleoside phosphoramidase/Ap4A hydrolase, histidine triade (HIT) family [Nucleotide ...
 85-176 1.40e-06

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: 46.48  E-value: 1.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658472267  85 ISMQDPKMQVYKDEQVVVIKDKYPKARYHWLVLP---WTSISSLKAvarehlELLKHMHTVGEKVIVDF-AGSSKLRFRL 160
Cdd:COG0537     9 IAGEIPALIVYEDEHVLAFLDINPYAPGHTLVIPkrhVASLFDLTP------EELAELMRLAQKVAKALrKALGPDGFNL 82

                          90       100
                  ....*....|....*....|
gi 1658472267 161 GYHAIP----SMSHVHLHVI 176
Cdd:COG0537    83 GINNGEaagqTVPHLHVHVI 102
 
Name Accession Description Interval E-value
aprataxin_related cd01278
aprataxin related: Aprataxin, a HINT family hydrolase is mutated in ataxia oculomotor apraxia ...
 76-177 1.27e-49

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: 158.32  E-value: 1.27e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658472267  76 LGHWSQGLKISMQDPKMQVYKDEQVVVIKDKYPKARYHWLVLPWTSISSLKAVAREHLELLKHMHTVGEKVIVDFAGSSK 155
Cdd:cd01278     1 LCHFCDIAKRRDPDPEDQVYEDDRVVVFKDIYPKARHHYLVIPKEHIASLKALTKEDVPLLEHMETVGREKLLRSDNTDP 80

                          90       100
                  ....*....|....*....|....
gi 1658472267 156 LRFRLGYHAIP--SMSHVHLHVIS 177
Cdd:cd01278    81 SEFRFGFHAPPftSVSHLHLHVIA 104
DcpS_C pfam11969
Scavenger mRNA decapping enzyme C-term binding; This family consists of several scavenger mRNA ...
 85-190 5.77e-40

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: 133.88  E-value: 5.77e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658472267  85 ISMQDPKMQVYKDEQVVVIKDKYPKARYHWLVLPWTSISSLKAVAREHLELLKHMHTVGEKVIVD-FAGSSKLRFRLGYH 163
Cdd:pfam11969   8 AKGEEPERVVYEDEGFVVFKDIKPKAPLHLLVIPKRHIKSLRDLTPEHLPLLEHMREVAKKVIEEkYIGVDRDELRLGFH 87

                          90       100
                  ....*....|....*....|....*..
gi 1658472267 164 AIPSMSHVHLHVISQDFDSPCLKNKKH 190
Cdd:pfam11969  88 YPPSVYHLHLHVISPDFESLGLGRKKG 114
zf-C2HE pfam16278
C2HE / C2H2 / C2HC zinc-binding finger; zf-C2HE is an unusual zinc-binding domain found in ...
 195-254 8.35e-19

C2HE / C2H2 / C2HC zinc-binding finger; zf-C2HE is an unusual zinc-binding domain found in fungi, plants and metazoa. It is often found at the C-terminus of HIT-domain-containing proteins, pfam01230. In fungi the fourth ligand is a Glu, in plants it is Cys and in metazoans it is usually a His. The fourth ligand is often mutated in neurogenerative disease-states.


Pssm-ID: 465082  Cd Length: 60  Bit Score: 77.71  E-value: 8.35e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658472267 195 NTEYFLESQAVIEMVQEAGRVTVRDGMPELLKLPLRCHECQQLLPSIPQLKEHLRKHWTQ 254
Cdd:pfam16278   1 NTPFFVPLDDVPEWLEEDGKIELLPSEVLLLKTPLKCHRCGNFGNNFPKLKAHLEEHFEK 60
HIT pfam01230
HIT domain;
94-181 1.15e-07

HIT domain;


Pssm-ID: 395984 [Multi-domain]  Cd Length: 98  Bit Score: 48.46  E-value: 1.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658472267  94 VYKDEQVVVIKDKYPKARYHWLVLPWTSISSLKAVAREhlELLKHMHT---VGEKVIVDFAGSSklrFRL----GYHAIP 166
Cdd:pfam01230   9 VYEDDLVLAFLDIDPQAPGHILVIPKKHIRELHDLTPE--ELGDLMSVaqkVARALGKVFKADG---YRIvinnGAHAGQ 83

                          90
                  ....*....|....*
gi 1658472267 167 SMSHVHLHVISQDFD 181
Cdd:pfam01230  84 SVPHLHIHVIPRRKH 98
HinT COG0537
Purine nucleoside phosphoramidase/Ap4A hydrolase, histidine triade (HIT) family [Nucleotide ...
 85-176 1.40e-06

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: 46.48  E-value: 1.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658472267  85 ISMQDPKMQVYKDEQVVVIKDKYPKARYHWLVLP---WTSISSLKAvarehlELLKHMHTVGEKVIVDF-AGSSKLRFRL 160
Cdd:COG0537     9 IAGEIPALIVYEDEHVLAFLDINPYAPGHTLVIPkrhVASLFDLTP------EELAELMRLAQKVAKALrKALGPDGFNL 82

                          90       100
                  ....*....|....*....|
gi 1658472267 161 GYHAIP----SMSHVHLHVI 176
Cdd:COG0537    83 GINNGEaagqTVPHLHVHVI 102
HIT_like cd00468
HIT family: HIT (Histidine triad) proteins, named for a motif related to the sequence HxHxH ...
 94-176 3.57e-06

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: 44.00  E-value: 3.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1658472267  94 VYKDEQVVVIKDKYPKARYHWLVLPWTSISSL----KAVAREHLELLKHMHTVGEKvivDFAGSSkLRFRLGYHAIP--S 167
Cdd:cd00468     1 VPDDEHSFAFVNLKPAAPGHVLVCPKRHVETLpdldEALLADLVITAQRVAAELEK---HGNVPS-LTVFVNDGAAAgqS 76


                  ....*....
gi 1658472267 168 MSHVHLHVI 176
Cdd:cd00468    77 VPHVHLHVL 85
 
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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