ID H2PRY2_PONAB Unreviewed; 292 AA.
AC H2PRY2; A0A2J8XIN0;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 2.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=Aprataxin {ECO:0000256|ARBA:ARBA00018614};
DE EC=3.6.1.71 {ECO:0000256|ARBA:ARBA00012496};
DE EC=3.6.1.72 {ECO:0000256|ARBA:ARBA00012495};
DE AltName: Full=Forkhead-associated domain histidine triad-like protein {ECO:0000256|ARBA:ARBA00032750};
GN Name=APTX {ECO:0000313|Ensembl:ENSPPYP00000021447.2};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601 {ECO:0000313|Ensembl:ENSPPYP00000021447.2, ECO:0000313|Proteomes:UP000001595};
RN [1] {ECO:0000313|Ensembl:ENSPPYP00000021447.2, ECO:0000313|Proteomes:UP000001595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wilson R.K., Mardis E.;
RT "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPPYP00000021447.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 3'-end 2'-deoxyribonucleotide-3'-diphospho-5'-guanosine-DNA
CC + H2O = a 3'-end 2'-deoxyribonucleotide 3'-phosphate-DNA + GMP + 2
CC H(+); Xref=Rhea:RHEA:52140, Rhea:RHEA-COMP:13186, Rhea:RHEA-
CC COMP:13187, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58115,
CC ChEBI:CHEBI:136419, ChEBI:CHEBI:136420; EC=3.6.1.72;
CC Evidence={ECO:0000256|ARBA:ARBA00024601};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end adenosine-5'-diphospho-5'-(2'-deoxyribonucleoside)-
CC DNA + H2O = a 5'-end 5'-monophospho-2'-deoxyribonucleoside-DNA + AMP
CC + 2 H(+); Xref=Rhea:RHEA:52128, Rhea:RHEA-COMP:13180, Rhea:RHEA-
CC COMP:13181, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:136412,
CC ChEBI:CHEBI:136413, ChEBI:CHEBI:456215; EC=3.6.1.71;
CC Evidence={ECO:0000256|ARBA:ARBA00024545};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end adenosine-5'-diphospho-5'-ribonucleoside-2'-
CC deoxyribonucleotide-DNA + H2O = a 5'-end 5'-monophospho-
CC ribonucleoside-2'-deoxyribonucleotide-DNA + AMP + 2 H(+);
CC Xref=Rhea:RHEA:52132, Rhea:RHEA-COMP:13182, Rhea:RHEA-COMP:13183,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:136414,
CC ChEBI:CHEBI:136415, ChEBI:CHEBI:456215; EC=3.6.1.71;
CC Evidence={ECO:0000256|ARBA:ARBA00024480};
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000256|ARBA:ARBA00004604}. Nucleus, nucleoplasm
CC {ECO:0000256|ARBA:ARBA00004642}.
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DR AlphaFoldDB; H2PRY2; -.
DR STRING; 9601.ENSPPYP00000021447; -.
DR Ensembl; ENSPPYT00000022315.2; ENSPPYP00000021447.2; ENSPPYG00000019142.3.
DR eggNOG; KOG0562; Eukaryota.
DR eggNOG; KOG2134; Eukaryota.
DR GeneTree; ENSGT00940000156806; -.
DR HOGENOM; CLU_066882_2_0_1; -.
DR InParanoid; H2PRY2; -.
DR OrthoDB; 12181at2759; -.
DR TreeFam; TF313308; -.
DR Proteomes; UP000001595; Chromosome 9.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0033699; F:DNA 5'-adenosine monophosphate hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0120108; F:DNA-3'-diphospho-5'-guanosine diphosphatase; IEA:UniProtKB-EC.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR CDD; cd01278; aprataxin_related; 1.
DR CDD; cd22735; FHA_APTX; 1.
DR Gene3D; 2.60.200.20; -; 1.
DR Gene3D; 3.30.428.10; HIT-like; 1.
DR InterPro; IPR041388; FHA_2.
DR InterPro; IPR047289; FHA_APTX.
DR InterPro; IPR019808; Histidine_triad_CS.
DR InterPro; IPR011146; HIT-like.
DR InterPro; IPR036265; HIT-like_sf.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR PANTHER; PTHR12486:SF4; APRATAXIN; 1.
DR PANTHER; PTHR12486; APRATAXIN-RELATED; 1.
DR Pfam; PF11969; DcpS_C; 1.
DR Pfam; PF17913; FHA_2; 1.
DR SUPFAM; SSF54197; HIT-like; 1.
DR SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR PROSITE; PS00892; HIT_1; 1.
DR PROSITE; PS51084; HIT_2; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000001595}.
FT DOMAIN 168..273
FT /note="HIT"
FT /evidence="ECO:0000259|PROSITE:PS51084"
FT REGION 108..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 258..262
FT /note="Histidine triad motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00464"
FT COMPBIAS 108..129
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 292 AA; 33390 MW; 74481D549478A707 CRC64;
MMRVCWLVRQ DSRHQRIRLP HLEAVVIGRG PETKITDKKC SRQQVQLKAE CNKGYVKVKQ
VGVNPTSIDS VVIGKDQEVK LQPGQVLHMV NELYPYIVEF EEEAKNPGLE THRKRKRSGN
SDSIERDAAQ EAEPGTGLEP GSNPSQCSVP LKKGKDAPIK KESLGHWSQG LKISMQDPKM
QVYKDEQVVV IKDKYPKARY HWLVLPWTSI SSLKAVTREH LELLKHMHTV GEKVIVDFAG
SSKLRFRLGY HAIPSMSHVH LHVISQDFDS PCLKNKKHWN SFNTEYFLES QE
//
