APTX_XENLA
ID APTX_XENLA Reviewed; 347 AA.
AC Q7T287;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Aprataxin;
DE EC=3.6.1.71 {ECO:0000250|UniProtKB:Q7Z2E3};
DE EC=3.6.1.72 {ECO:0000250|UniProtKB:O74859};
DE AltName: Full=Forkhead-associated domain histidine triad-like protein;
DE Short=FHA-HIT;
GN Name=aptx;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Huang C.-H.;
RT "Identification of FHA-HIT as a novel nuclear protein involved in cell-
RT cycle regulation.";
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: DNA-binding protein involved in single-strand DNA break
CC repair, double-strand DNA break repair and base excision repair.
CC Resolves abortive DNA ligation intermediates formed either at base
CC excision sites, or when DNA ligases attempt to repair non-ligatable
CC breaks induced by reactive oxygen species. Catalyzes the release of
CC adenylate groups covalently linked to 5'-phosphate termini, resulting
CC in the production of 5'-phosphate termini that can be efficiently
CC rejoined. Also able to hydrolyze adenosine 5'-monophosphoramidate (AMP-
CC NH(2)) and diadenosine tetraphosphate (AppppA), but with lower
CC catalytic activity (By similarity). Likewise, catalyzes the release of
CC 3'-linked guanosine (DNAppG) and inosine (DNAppI) from DNA, but has
CC higher specific activity with 5'-linked adenosine (AppDNA) (By
CC similarity). {ECO:0000250|UniProtKB:O74859,
CC ECO:0000250|UniProtKB:Q7Z2E3}.
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:0000250|UniProtKB:Q7Z2E3};
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:0000250|UniProtKB:Q7Z2E3};
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:0000250|UniProtKB:O74859};
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:Q7Z2E3}. Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q7Z2E3}.
CC -!- DOMAIN: The histidine triad, also called HIT motif, forms part of the
CC binding loop for the alpha-phosphate of purine mononucleotide.
CC {ECO:0000250|UniProtKB:Q7Z2E3}.
CC -!- DOMAIN: The HIT domain is required for enzymatic activity.
CC {ECO:0000250}.
CC -!- DOMAIN: The C2H2-type zinc finger mediates DNA-binding. {ECO:0000250}.
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DR EMBL; AY040781; AAK91772.1; -; mRNA.
DR RefSeq; NP_001082689.1; NM_001089220.1.
DR AlphaFoldDB; Q7T287; -.
DR SMR; Q7T287; -.
DR DNASU; 398657; -.
DR GeneID; 398657; -.
DR KEGG; xla:398657; -.
DR CTD; 398657; -.
DR Xenbase; XB-GENE-1015074; aptx.L.
DR OrthoDB; 1290702at2759; -.
DR Proteomes; UP000186698; Chromosome 1L.
DR Bgee; 398657; Expressed in blastula and 18 other tissues.
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:InterPro.
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; cd00060; FHA; 1.
DR Gene3D; 3.30.428.10; -; 1.
DR InterPro; IPR026963; Aprataxin-like.
DR InterPro; IPR041388; FHA_2.
DR InterPro; IPR000253; FHA_dom.
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 PANTHER; PTHR12486:SF4; PTHR12486:SF4; 2.
DR Pfam; PF17913; FHA_2; 1.
DR Pfam; PF16278; zf-C2HE; 1.
DR SUPFAM; SSF49879; SSF49879; 1.
DR SUPFAM; SSF54197; SSF54197; 1.
DR PROSITE; PS00892; HIT_1; 1.
DR PROSITE; PS51084; HIT_2; 1.
PE 2: Evidence at transcript level;
KW DNA damage; DNA repair; DNA-binding; Hydrolase; Metal-binding; Nucleus;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..347
FT /note="Aprataxin"
FT /id="PRO_0000109846"
FT DOMAIN 23..72
FT /note="FHA-like"
FT DOMAIN 173..278
FT /note="HIT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00464"
FT ZN_FING 322..344
FT /note="C2H2-type"
FT REGION 110..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 198..202
FT /note="Interaction with DNA substrate"
FT /evidence="ECO:0000250|UniProtKB:Q7Z2E3"
FT REGION 260..261
FT /note="Interaction with DNA substrate"
FT /evidence="ECO:0000250|UniProtKB:Q7Z2E3"
FT MOTIF 263..267
FT /note="Histidine triad motif"
FT COMPBIAS 139..164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 265
FT /note="Tele-AMP-histidine intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q7Z2E3"
FT SITE 179
FT /note="Interaction with DNA substrate"
FT /evidence="ECO:0000250|UniProtKB:Q7Z2E3"
FT SITE 256
FT /note="Interaction with DNA substrate"
FT /evidence="ECO:0000250|UniProtKB:Q7Z2E3"
FT SITE 267
FT /note="Interaction with DNA substrate"
FT /evidence="ECO:0000250|UniProtKB:Q7Z2E3"
FT SITE 282
FT /note="Interaction with DNA substrate"
FT /evidence="ECO:0000250|UniProtKB:Q7Z2E3"
SQ SEQUENCE 347 AA; 39645 MW; 408C5CECE2700B4A CRC64;
MFECWLVSKD GKHGRIRLPH AETVVIGRGP ETQITDKKCS RHQVQLMADC NKGYVKVKQM
GTNPTSINGV DIGNEHKVEL KPGHTLYIVN NLYPYMIEFL EGSTNPRAKI ENENRSSSKR
TPENSLNVDT ETPRKLVKKE SNVSPSSSSG RISSCPTQGK SNVQEVKSQG HWSQDLKVSM
QDPTMQVFKD DKIVVIKDKY PKARYHWLVL PWQSIASLKV LRAEHLELVQ HMDAVGHNIA
REHTNSKCAP FRFGYHAIPS MSHVHLHVIS QDFDSPCLKN KKHWNSFTTD YFLESQAVIE
MLKTHGKVNV KERISDVLKT PLLCHMCKKE QATMPQLKEH LKKHWPT
