ID W6KZ57_9TRYP Unreviewed; 749 AA.
AC W6KZ57;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Exonuclease 1 {ECO:0000256|RuleBase:RU910737};
DE EC=3.1.-.- {ECO:0000256|RuleBase:RU910737};
GN ORFNames=GSHART1_T00003600001 {ECO:0000313|EMBL:CCW67500.1};
OS Phytomonas sp. Hart1.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Phytomonas.
OX NCBI_TaxID=223615 {ECO:0000313|EMBL:CCW67500.1, ECO:0000313|Proteomes:UP000053358};
RN [1] {ECO:0000313|EMBL:CCW67500.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Hart1 {ECO:0000313|EMBL:CCW67500.1};
RA Genoscope - CEA;
RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CCW67500.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hart1 {ECO:0000313|EMBL:CCW67500.1};
RX PubMed=24516393; DOI=10.1371/journal.pgen.1004007;
RA Porcel B.M., Denoeud F., Opperdoes F., Noel B., Madoui M.A.,
RA Hammarton T.C., Field M.C., Da Silva C., Couloux A., Poulain J.,
RA Katinka M., Jabbari K., Aury J.M., Campbell D.A., Cintron R., Dickens N.J.,
RA Docampo R., Sturm N.R., Koumandou V.L., Fabre S., Flegontov P., Lukes J.,
RA Michaeli S., Mottram J.C., Szoor B., Zilberstein D., Bringaud F.,
RA Wincker P., Dollet M.;
RT "The Streamlined Genome of Phytomonas spp. Relative to Human Pathogenic
RT Kinetoplastids Reveals a Parasite Tailored for Plants.";
RL PLoS Genet. 10:e1004007-e1004007(2014).
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}.
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DR EMBL; HF955200; CCW67500.1; -; Genomic_DNA.
DR AlphaFoldDB; W6KZ57; -.
DR EnsemblProtists; CCW67500; CCW67500; GSHART1_T00003600001.
DR OrthoDB; 126305at2759; -.
DR Proteomes; UP000053358; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004518; F:nuclease activity; IEA:UniProtKB-KW.
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; 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; 2.
DR PRINTS; PR00853; XPGRADSUPER.
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|RuleBase:RU910737};
KW DNA excision {ECO:0000256|RuleBase:RU910737};
KW DNA repair {ECO:0000256|RuleBase:RU910737};
KW DNA-binding {ECO:0000256|RuleBase:RU910737};
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|RuleBase:RU910737};
KW Metal-binding {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:UP000053358}.
FT DOMAIN 1..140
FT /note="XPG N-terminal"
FT /evidence="ECO:0000259|SMART:SM00485"
FT DOMAIN 197..267
FT /note="XPG-I"
FT /evidence="ECO:0000259|SMART:SM00484"
FT REGION 529..673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 685..732
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..574
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 592..611
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..651
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 714..728
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 749 AA; 81549 MW; 3FD3141D6CC6A1BB CRC64;
MGIKGLWQAM QSYIQDGHLS QFKGKRVSVD MYVWLHQGIR HGMELNEERV WRHFEALDAR
VSGDQTEGEA ASGDGLEGPS EAALKMEDAY LMNDRYVDYI VQKVDALLRY GAVPVCVFDG
AEMPMKRRTN VERQERREAN FQQALRLLEG NYRRSRAGQR RGFQTHARSY SEALECLWKA
VDVSTELAHI LIQVLREERR VECLVAPYEA EAQMAYLCRQ GYVEAALSED SDLIAYYCPC
IIAKVETASG RCVVVHPKVS VPAFFSSIAA MNLPQRARAR GDGILAEARP LNSSTSSTNP
APAPIPFSYE SFLLGCIMSG CDYLANLRNI GVKTAFKLVS HARSLVEVLQ LLKTQFGFPA
DELQSYRRRL LDAFYCFAHH IVYDPSLRKL MTFFPLPNSS PSLSSSALAL REDLVGSMWS
VEETHRVCEE CLFDPNTHRL YVGSFNSCLS AYLRRARRGQ VRLTTFSGFT AKQAPKVVLD
PQQKRAEAEF GPGPLQKVRE AAGVWAQGAP KVMVRSRYFL RSGRLHAQED WSASSGTSGG
EGLAGGGGSQ DSASHTAPSS DSATLASQEF GEKAPTSPSF RAREAAGPTA RTPLADSTSG
ARGSGLLGSP STAATPPPAR AEKGLWVGEG AEEAWRPSHP GPKRERPPSQ DDASTSARAA
SEGVEQPSQG IGGASYFAKA FKAPRRVETA TASSPGDTPD CAGPVDPSDP AHATATPAES
SKPTEPTENG VNLGVFEQLL FTGRYSTTT
//
