APTX_CIOIN
ID APTX_CIOIN Reviewed; 380 AA.
AC P61802;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2004, sequence version 1.
DT 25-MAY-2022, entry version 96.
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 Ciona intestinalis (Transparent sea squirt) (Ascidia intestinalis).
OC Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Phlebobranchia;
OC Cionidae; Ciona.
OX NCBI_TaxID=7719;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Chen Y., Huang C.-H.;
RT "Identification of human FHA-HIT gene homolog in sea squirt.";
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-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; AY208848; AAP86338.1; -; mRNA.
DR RefSeq; NP_001027704.1; NM_001032532.1.
DR AlphaFoldDB; P61802; -.
DR SMR; P61802; -.
DR STRING; 7719.NP_001027704.1; -.
DR GeneID; 445730; -.
DR KEGG; cin:445730; -.
DR CTD; 54840; -.
DR eggNOG; KOG0562; Eukaryota.
DR eggNOG; KOG2134; Eukaryota.
DR InParanoid; P61802; -.
DR OrthoDB; 1290702at2759; -.
DR Proteomes; UP000008144; Unassembled WGS sequence.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0033699; F:DNA 5'-adenosine monophosphate hydrolase activity; IBA:GO_Central.
DR GO; GO:0120108; F:DNA-3'-diphospho-5'-guanosine diphosphatase; IEA:UniProtKB-EC.
DR GO; GO:0003725; F:double-stranded RNA binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030983; F:mismatched DNA binding; IBA:GO_Central.
DR GO; GO:1990165; F:single-strand break-containing DNA binding; IBA:GO_Central.
DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0006302; P:double-strand break repair; IBA:GO_Central.
DR GO; GO:0000012; P:single strand break repair; IBA:GO_Central.
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; 1.
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..380
FT /note="Aprataxin"
FT /id="PRO_0000109848"
FT DOMAIN 36..85
FT /note="FHA-like"
FT DOMAIN 206..312
FT /note="HIT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00464"
FT ZN_FING 356..378
FT /note="C2H2-type; atypical"
FT REGION 176..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 231..235
FT /note="Interaction with DNA substrate"
FT /evidence="ECO:0000250|UniProtKB:Q7Z2E3"
FT REGION 294..295
FT /note="Interaction with DNA substrate"
FT /evidence="ECO:0000250|UniProtKB:Q7Z2E3"
FT MOTIF 297..301
FT /note="Histidine triad motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00464"
FT ACT_SITE 299
FT /note="Tele-AMP-histidine intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q7Z2E3"
FT SITE 212
FT /note="Interaction with DNA substrate"
FT /evidence="ECO:0000250|UniProtKB:Q7Z2E3"
FT SITE 290
FT /note="Interaction with DNA substrate"
FT /evidence="ECO:0000250|UniProtKB:Q7Z2E3"
FT SITE 301
FT /note="Interaction with DNA substrate"
FT /evidence="ECO:0000250|UniProtKB:Q7Z2E3"
FT SITE 316
FT /note="Interaction with DNA substrate"
FT /evidence="ECO:0000250|UniProtKB:Q7Z2E3"
SQ SEQUENCE 380 AA; 43441 MW; DFE5DE05FBE0D427 CRC64;
MRILYRLLKM ADDTVKCYLE CCKSSHPKLP LPHNVPVIIG RTPELGITDK LCSRSQLELT
SNCYKRYVLV KRLGANTSQI NGIDIEKNKS SRLEEGQDLH VVNGKFPHRV YFTGCQNDTK
TEKAVVPKLP TKSTDLTKSD LSIKQPERKK LKVSENKSKV LNSKIKPQEK FSSESVYAFD
SPSPMSSRCE KKAESNKRAP THKHWSQGLK ASMEDPELVV KEDEQIVVIK DKYPKAKYHW
LILPKDSISS TKNLSTDNIE LLKHILKVGQ ELAAEVKDKQ PDVEFRFGYH AVASMSQMHM
HVISQDFQSS SFKTKKHWNS FTTDYFVDAT DIINELETGG KVKDRRTMTS LLNEPLKCHR
CKKPQKNIPT LKKHIDSCQK
