GenomeNet

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   22-NOV-2017, entry version 89.
DE   RecName: Full=Aprataxin;
DE            EC=3.1.11.7 {ECO:0000250|UniProtKB:Q7Z2E3};
DE            EC=3.1.12.2 {ECO:0000250|UniProtKB:O74859};
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   Eupercaria; 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. Also able to hydrolyze adenosine 5'-
CC       monophosphoramidate (AMP-NH(2)) and diadenosine tetraphosphate
CC       (AppppA), but with lower catalytic activity (By similarity).
CC       Likewise, catalyzes the release of 3'-linked guanosine (DNAppG)
CC       and inosine (DNAppI) from DNA, but has higher specific activity
CC       with 5'-linked adenosine (AppDNA) (By similarity).
CC       {ECO:0000250|UniProtKB:O74859, ECO:0000250|UniProtKB:Q7Z2E3}.
CC   -!- CATALYTIC ACTIVITY: Adenosine-5'-diphospho-5'-(DNA) + H(2)O = AMP
CC       + phospho-5'-(DNA). {ECO:0000250|UniProtKB:Q7Z2E3}.
CC   -!- CATALYTIC ACTIVITY: Adenosine-5'-diphospho-5'-(ribonucleotide)-
CC       (DNA) + H(2)O = AMP + 5'-phospho-(ribonucleotide)-(DNA).
CC       {ECO:0000250|UniProtKB:Q7Z2E3}.
CC   -!- CATALYTIC ACTIVITY: (DNA)-3'-diphospho-5'-guanosine + H(2)O =
CC       (DNA)-3'-phosphate + GMP. {ECO:0000250|UniProtKB:O74859}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC       {ECO:0000250|UniProtKB:Q7Z2E3}. Nucleus, nucleolus
CC       {ECO:0000250|UniProtKB:Q7Z2E3}.
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       {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.
CC       {ECO:0000250}.
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   SMR; 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; KOG0562; Eukaryota.
DR   eggNOG; KOG2134; Eukaryota.
DR   eggNOG; ENOG41102F4; LUCA.
DR   GeneTree; ENSGT00570000079163; -.
DR   InParanoid; P61800; -.
DR   KO; K10863; -.
DR   OMA; TVRDGMP; -.
DR   OrthoDB; EOG091G0KPQ; -.
DR   TreeFam; TF313308; -.
DR   Proteomes; UP000005226; 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:InterPro.
DR   GO; GO:0003677; F:DNA binding; 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   CDD; cd00060; FHA; 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; 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; PTHR12486:SF4; 1.
DR   Pfam; PF16278; zf-C2HE; 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. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00464}.
FT   ZN_FING     331    353       C2H2-type. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   REGION      207    211       Interaction with DNA substrate.
FT                                {ECO:0000250|UniProtKB:Q7Z2E3}.
FT   REGION      269    270       Interaction with DNA substrate.
FT                                {ECO:0000250|UniProtKB:Q7Z2E3}.
FT   MOTIF       272    276       Histidine triad motif.
FT   ACT_SITE    274    274       Tele-AMP-histidine intermediate.
FT                                {ECO:0000250|UniProtKB:Q7Z2E3}.
FT   SITE        188    188       Interaction with DNA substrate.
FT                                {ECO:0000250|UniProtKB:Q7Z2E3}.
FT   SITE        265    265       Interaction with DNA substrate.
FT                                {ECO:0000250|UniProtKB:Q7Z2E3}.
FT   SITE        276    276       Interaction with DNA substrate.
FT                                {ECO:0000250|UniProtKB:Q7Z2E3}.
FT   SITE        291    291       Interaction with DNA substrate.
FT                                {ECO:0000250|UniProtKB:Q7Z2E3}.
FT   VAR_SEQ     126    139       CRKSSKQGEVSVSV -> F (in isoform 2).
FT                                {ECO:0000303|Ref.1}.
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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