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 03-APR-2013, entry version 65.
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; Euteleostei; Neoteleostei;
OC Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes;
OC Tetradontoidea; Tetraodontidae; 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.
DR UniGene; Tru.1976; -.
DR ProteinModelPortal; P61800; -.
DR STRING; 31033.ENSTRUP00000024613; -.
DR Ensembl; ENSTRUT00000024713; ENSTRUP00000024613; ENSTRUG00000009794.
DR Ensembl; ENSTRUT00000024714; ENSTRUP00000024614; ENSTRUG00000009794.
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; EOG4FTW17; -.
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:0008270; F:zinc ion binding; IEA:InterPro.
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; 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 SMART; SM00355; ZnF_C2H2; 1.
DR SUPFAM; SSF54197; His_triad-like_motif; 1.
DR SUPFAM; SSF49879; SMAD_FHA; 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
//
