ID A0A016W9X4_9BILA Unreviewed; 616 AA.
AC A0A016W9X4;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Exonuclease 1 {ECO:0000256|RuleBase:RU910737};
DE EC=3.1.-.- {ECO:0000256|RuleBase:RU910737};
GN Name=Acey_s0898.g2933 {ECO:0000313|EMBL:EYC36416.1};
GN Synonyms=Acey-exo-1 {ECO:0000313|EMBL:EYC36416.1};
GN ORFNames=Y032_0898g2933 {ECO:0000313|EMBL:EYC36416.1};
OS Ancylostoma ceylanicum.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=53326 {ECO:0000313|EMBL:EYC36416.1, ECO:0000313|Proteomes:UP000024635};
RN [1] {ECO:0000313|Proteomes:UP000024635}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX PubMed=25730766; DOI=10.1038/ng.3237;
RA Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA Aroian R.V.;
RT "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT ceylanicum identify infection-specific gene families.";
RL Nat. Genet. 47:416-422(2015).
CC -!- FUNCTION: 5'->3' double-stranded DNA exonuclease which may also possess
CC a cryptic 3'->5' double-stranded DNA exonuclease activity. Functions in
CC DNA mismatch repair. {ECO:0000256|RuleBase:RU910737}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|RuleBase:RU910737};
CC Note=Binds 2 magnesium ions per subunit. They probably participate in
CC the reaction catalyzed by the enzyme. May bind an additional third
CC magnesium ion after substrate binding. {ECO:0000256|RuleBase:RU910737};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU910737}.
CC -!- SIMILARITY: Belongs to the XPG/RAD2 endonuclease family. EXO1
CC subfamily. {ECO:0000256|RuleBase:RU910737}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EYC36416.1}.
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DR EMBL; JARK01000498; EYC36416.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A016W9X4; -.
DR STRING; 53326.A0A016W9X4; -.
DR Proteomes; UP000024635; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0035312; F:5'-3' DNA exonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR CDD; cd09857; PIN_EXO1; 1.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR Gene3D; 3.40.50.1010; 5'-nuclease; 1.
DR InterPro; IPR036279; 5-3_exonuclease_C_sf.
DR InterPro; IPR008918; HhH2.
DR InterPro; IPR029060; PIN-like_dom_sf.
DR InterPro; IPR044752; PIN-like_EXO1.
DR InterPro; IPR006086; XPG-I_dom.
DR InterPro; IPR006084; XPG/Rad2.
DR InterPro; IPR006085; XPG_DNA_repair_N.
DR PANTHER; PTHR11081:SF8; EXONUCLEASE 1; 1.
DR PANTHER; PTHR11081; FLAP ENDONUCLEASE FAMILY MEMBER; 1.
DR Pfam; PF00867; XPG_I; 1.
DR Pfam; PF00752; XPG_N; 1.
DR PRINTS; PR00853; XPGRADSUPER.
DR SMART; SM00279; HhH2; 1.
DR SMART; SM00484; XPGI; 1.
DR SMART; SM00485; XPGN; 1.
DR SUPFAM; SSF47807; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR SUPFAM; SSF88723; PIN domain-like; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU910737};
KW DNA excision {ECO:0000256|RuleBase:RU910737};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|RuleBase:RU910737};
KW DNA-binding {ECO:0000256|RuleBase:RU910737};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW Excision nuclease {ECO:0000256|RuleBase:RU910737};
KW Exonuclease {ECO:0000256|RuleBase:RU910737};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU910737};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU910737};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU910737};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|RuleBase:RU910737};
KW Nucleus {ECO:0000256|RuleBase:RU910737};
KW Reference proteome {ECO:0000313|Proteomes:UP000024635}.
FT DOMAIN 1..99
FT /note="XPG N-terminal"
FT /evidence="ECO:0000259|SMART:SM00485"
FT DOMAIN 139..208
FT /note="XPG-I"
FT /evidence="ECO:0000259|SMART:SM00484"
FT REGION 305..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 446..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 563..616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..331
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 456..486
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 569..589
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 616 AA; 68725 MW; 52F57C4AD6BD4620 CRC64;
MGIQNLLPFV KKACRQGNVS EFAGCSVAVD VSCLLHRGLF GCMESVAQGK KTTFYIHYVS
KHIKALLDLG CHVVMVFDGR PLPAKKNTND ERRQRRAENV KAAELLLSEG KINEAVDKFK
RATSITPEVV ESTIEHFRTY KNVDVLVSPY ESDAQLAFLV NEGLADVVVT EDSDLIAFGC
EKIAFKWNSE TGECTIYEKK ELPRCFSGVM SSQFDFTKFR RICILSGCDY LQAGLPGIGL
NKALSFFSKT SRTDLKTLLP RIPNYLNMSK LTVSKEFIEE FIRAENTFIH QVIFDPRQRC
QRPLTPYPCP RKEDQKGSDE NDDDFVTSDE KKQTSEFSYA GEVLSSNLAV RLALGNQIEK
SVITDKFFLP SPVPEWSVWS DRFESCGKRK RRLEEERKRE EKKCGSAFRF DSPSKKRMKL
DTSAAIEFID LEPEIVLDVA APKAKEKEQK QSLEKQTSQS EDAPNKRAQE NGITPPTRPK
SLKNQADCSW SVDEVMKMYG SQESTYTTRT SITETTAAAN SQPAVLTAAT ITTVTASTGL
GRSAYFVRRS ASCANPFRKP VLKPTSIAPK SDAKEEVQES TKAATTVEEE KPEPSAATII
KPVGCRPPGL RASFSS
//
