ID A0A1E5R2M4_9ASCO Unreviewed; 858 AA.
AC A0A1E5R2M4;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Exonuclease 1 {ECO:0000256|RuleBase:RU910737};
DE EC=3.1.-.- {ECO:0000256|RuleBase:RU910737};
GN ORFNames=AWRI3579_g4118 {ECO:0000313|EMBL:OEJ81134.1};
OS Hanseniaspora osmophila.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycodaceae; Hanseniaspora.
OX NCBI_TaxID=56408 {ECO:0000313|EMBL:OEJ81134.1, ECO:0000313|Proteomes:UP000095728};
RN [1] {ECO:0000313|Proteomes:UP000095728}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AWRI3579 {ECO:0000313|Proteomes:UP000095728};
RX PubMed=27856586; DOI=10.1128/genomea.01287-16;
RA Sternes P.R., Lee D., Kutyna D.R., Borneman A.R.;
RT "Genome sequences of three species of Hanseniaspora isolated from
RT spontaneous wine fermentations.";
RL Genome Announc. 4:E01287-E01287(2016).
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|ARBA:ARBA00010563,
CC 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:OEJ81134.1}.
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DR EMBL; LPNM01000011; OEJ81134.1; -; Genomic_DNA.
DR STRING; 56408.A0A1E5R2M4; -.
DR InParanoid; A0A1E5R2M4; -.
DR OrthoDB; 126305at2759; -.
DR Proteomes; UP000095728; 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:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR CDD; cd09908; H3TH_EXO1; 1.
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; IPR037315; EXO1_H3TH.
DR InterPro; IPR008918; HhH2.
DR InterPro; IPR029060; PIN-like_dom_sf.
DR InterPro; IPR044752; PIN-like_EXO1.
DR InterPro; IPR019734; TPR_repeat.
DR InterPro; IPR006086; XPG-I_dom.
DR InterPro; IPR006084; XPG/Rad2.
DR InterPro; IPR019974; XPG_CS.
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.
DR PROSITE; PS50005; TPR; 1.
DR PROSITE; PS00841; XPG_1; 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|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU910737};
KW Excision nuclease {ECO:0000256|ARBA:ARBA00022881,
KW 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|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU910737};
KW Reference proteome {ECO:0000313|Proteomes:UP000095728};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339}.
FT DOMAIN 1..100
FT /note="XPG N-terminal"
FT /evidence="ECO:0000259|SMART:SM00485"
FT REPEAT 97..130
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 139..210
FT /note="XPG-I"
FT /evidence="ECO:0000259|SMART:SM00484"
FT REGION 379..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 528..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 805..828
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 805..820
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 858 AA; 97187 MW; 8382BDE64C4B67CA CRC64;
MGVTGLLPQL KPIQNPVSLH RYEGCTLAVD GYAWLHRAAH GCCEQLCLGE PTTRYLSFLI
KKIDLLKRQH KITPFLVFDG DRLDAKAGTE LKRRVKREEN RKLGCELHKR GEKKKAWEYF
QKSVDVTPEM AKCWIDYLQT HRLPYVVAPF EADAQMVYLE QQGFVDGIIS EDSDLLIFGC
TRLITKLKDN GECIEICRND FEKLPRKFPL YELNMEQLRI LVCLSGCDYT DGINRVGLNK
AMDFVKKHNT MEKILLAIQR DGKYEVPKNF MDEYKRATIC FQYQRVFCPK LQKLVTLNEL
PENPLDVNSK FFEYIGYGIS VETGLKEYLC DLEMIDHNAH YLISIGEKTP GNHKRDLINR
EINVTQSFSN AISMSTSTST TTIGAGPVGG NGDTFSQPTS NPAKRSITID SFFLRSRDSL
TCNASFESKQ VANAAEVERE MDKNKPVASA RKIGHKNLQH MLEKRNSLLE TRSKLGISSL
SIKQQLNNVI IDKRKLVPKT GISSSSKFFC TKAEKCKSTE LKSEXIAMDN EEQKKTESLD
IAGDQNSEAP KTASGLQIEE VMCPEPLAFE EKTDKKFDQH CQEEDFLDGS EDISFDVSRD
LDEIEAENSN HLLSGMSSSK NASTDTVXDL KQNVEKTFVF NDDXEKDFVN KTGSQQLLNS
RTSKRSANVM GFPVFGGNDN INEEYCEENA VNHENNSISI KNKPVKRSLV FSKFAYTNSL
RNTKGDDNKG ISDIDHDRIG DIKRVLRPKN PNVNISNNLV RKDVNFATIH VDTEEYNDTD
QSKKLKVDKI SIHSLQKRLT SSQTGLSSNA TTSHHNALHC NNGHGLNKRQ LFRSNTTSPI
KSTVNKRIPS LSRFIYRE
//
