ID A0A3Q0D4Q0_MESAU Unreviewed; 370 AA.
AC A0A3Q0D4Q0;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
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|RefSeq:XP_021087913.1};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036 {ECO:0000313|Proteomes:UP000189706, ECO:0000313|RefSeq:XP_021087913.1};
RN [1] {ECO:0000313|RefSeq:XP_021087913.1}
RP IDENTIFICATION.
RG RefSeq;
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 RefSeq; XP_021087913.1; XM_021232254.1.
DR AlphaFoldDB; A0A3Q0D4Q0; -.
DR STRING; 10036.ENSMAUP00000004598; -.
DR OrthoDB; 12181at2759; -.
DR Proteomes; UP000189706; Unplaced.
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:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0120108; F:DNA-3'-diphospho-5'-guanosine diphosphatase; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 InterPro; IPR032566; Znf-C2HE.
DR InterPro; IPR013087; Znf_C2H2_type.
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 Pfam; PF16278; zf-C2HE; 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.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 4: Predicted;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000189706};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 196..301
FT /note="HIT"
FT /evidence="ECO:0000259|PROSITE:PS51084"
FT REGION 138..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 286..290
FT /note="Histidine triad motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00464"
FT COMPBIAS 138..153
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..177
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 370 AA; 41731 MW; FF1C6A77720288E3 CRC64;
MSIPEYLFRI TYSGAMLQPV IPEGCVFGAM KRVCWLVRQD CRHQRIKLPH LEAVVIGRSP
VTKITDKKCS RQQVQLKAEC NKGYVKVKQV GVNPTSIDSV IIGKDQEMKL QPGQVLYMVN
ELYPYIVEFE EVAKSPDLET QRKRKRSDYD GEDMDTAQAA ESGTGTAPGS SPSQCAVPSK
KGKDGVTKEE SLGHWSQGLK TSMKDPKMQV YKDDLVVVIK DKYPKARHHW LVLPWASIPS
LKAVTSEHLE LLKHMHTVGE KVIADFAGSS KLSFRLGYHA IPSMSHVHLH VISQDFDSPC
LKNKKHWNSF NTEYFLESQA VIKMVQEAGR VTVQDGTSEL LKLPLHCHKC QQLLPSIPQL
KEHLRKHWGG
//
