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Database: UniProt
Entry: P61800
LinkDB: P61800
Original site: P61800 
ID   APTX_TAKRU              Reviewed;         356 AA.
AC   P61800;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2004, sequence version 1.
DT   09-JUL-2014, entry version 72.
DE   RecName: Full=Aprataxin;
DE            EC=3.-.-.-;
DE   AltName: Full=Forkhead-associated domain histidine triad-like protein;
DE            Short=FHA-HIT;
GN   Name=aptx;
OS   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Percomorpharia; Tetraodontiformes; Tetradontoidea; Tetraodontidae;
OC   Takifugu.
OX   NCBI_TaxID=31033;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RA   Chen Y., Huang C.-H.;
RT   "Identification of human FHA-HIT gene homolog in pufferfish.";
RL   Submitted (DEC-2002) 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-
CC       ligatable breaks induced by reactive oxygen species. Catalyzes the
CC       release of adenylate groups covalently linked to 5'-phosphate
CC       termini, resulting in the production of 5'-phosphate termini that
CC       can be efficiently rejoined (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm (By similarity).
CC       Nucleus, nucleolus (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=Long;
CC         IsoId=P61800-1; Sequence=Displayed;
CC       Name=2; Synonyms=Short;
CC         IsoId=P61800-2; Sequence=VSP_010545;
CC   -!- DOMAIN: The histidine triad, also called HIT motif, forms part of
CC       the binding loop for the alpha-phosphate of purine mononucleotide
CC       (By similarity).
CC   -!- DOMAIN: The HIT domain is required for enzymatic activity (By
CC       similarity).
CC   -!- DOMAIN: The C2H2-type zinc finger mediates DNA-binding (By
CC       similarity).
CC   -!- SIMILARITY: Contains 1 C2H2-type zinc finger.
CC   -!- SIMILARITY: Contains 1 FHA-like domain.
CC   -!- SIMILARITY: Contains 1 HIT domain.
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DR   EMBL; AY208846; AAP86336.1; -; mRNA.
DR   EMBL; AY208847; AAP86337.1; -; mRNA.
DR   RefSeq; NP_001027825.1; NM_001032653.1. [P61800-1]
DR   UniGene; Tru.1976; -.
DR   ProteinModelPortal; P61800; -.
DR   STRING; 31033.ENSTRUP00000024613; -.
DR   Ensembl; ENSTRUT00000024713; ENSTRUP00000024613; ENSTRUG00000009794. [P61800-1]
DR   Ensembl; ENSTRUT00000024714; ENSTRUP00000024614; ENSTRUG00000009794. [P61800-2]
DR   GeneID; 445995; -.
DR   KEGG; tru:445995; -.
DR   CTD; 54840; -.
DR   eggNOG; NOG278510; -.
DR   GeneTree; ENSGT00570000079163; -.
DR   InParanoid; P61800; -.
DR   KO; K10863; -.
DR   OMA; PGQVLHM; -.
DR   OrthoDB; EOG786H3J; -.
DR   TreeFam; TF313308; -.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.200.20; -; 1.
DR   Gene3D; 3.30.428.10; -; 1.
DR   InterPro; IPR026963; Aprataxin.
DR   InterPro; IPR000253; FHA_dom.
DR   InterPro; IPR019808; Histidine_triad_CS.
DR   InterPro; IPR001310; Histidine_triad_HIT.
DR   InterPro; IPR011146; HIT-like.
DR   InterPro; IPR008984; SMAD_FHA_domain.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   PANTHER; PTHR12486; PTHR12486; 1.
DR   PANTHER; PTHR12486:SF4; PTHR12486:SF4; 1.
DR   SMART; SM00355; ZnF_C2H2; 1.
DR   SUPFAM; SSF49879; SSF49879; 1.
DR   SUPFAM; SSF54197; SSF54197; 1.
DR   PROSITE; PS00892; HIT_1; 1.
DR   PROSITE; PS51084; HIT_2; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Complete proteome; DNA damage; DNA repair;
KW   DNA-binding; Hydrolase; Metal-binding; Nucleus; Reference proteome;
KW   Zinc; Zinc-finger.
FT   CHAIN         1    356       Aprataxin.
FT                                /FTId=PRO_0000109845.
FT   DOMAIN       23     72       FHA-like.
FT   DOMAIN      182    287       HIT.
FT   ZN_FING     331    353       C2H2-type.
FT   MOTIF       272    276       Histidine triad motif.
FT   ACT_SITE    274    274       Tele-AMP-histidine intermediate (By
FT                                similarity).
FT   VAR_SEQ     126    139       CRKSSKQGEVSVSV -> F (in isoform 2).
FT                                /FTId=VSP_010545.
SQ   SEQUENCE   356 AA;  40190 MW;  6782CF8B18128325 CRC64;
     MPLCWLISVE GNHKPILLPH LQAVVLGRGP ETTIKDKKCS REQVELQAEC NKGYVKVKQL
     GLNPTSIDSL VVGKGSVSKM KPGQQLYIVN QLYPYTVQFK EDLSGSTKRS REAVSETRHN
     DKEEPCRKSS KQGEVSVSVS QKEAPKMSVR SNVHFSLLSI LLSGLLSEGV GKMLQGSVGH
     WNLGLKASMQ DPEMQVYKDD KVVVIKDKYP KARYHWLVLP WQSISSLKAL RKEHCDLVKH
     MQQVAEQMIR QCPDASTPRF RSGYHAIPSM SHVHLHVISQ DFDSPCLKNK KHWNSFTTDY
     FIESQAVIQM LETDGSISIK EGATELLKLP LRCHVCRKEF SNIPALKQHL NSHFPS
//
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