ID A0A182FSS4_ANOAL Unreviewed; 839 AA.
AC A0A182FSS4;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=Exonuclease 1 {ECO:0000256|ARBA:ARBA00020324, ECO:0000256|RuleBase:RU910737};
DE EC=3.1.-.- {ECO:0000256|RuleBase:RU910737};
OS Anopheles albimanus (New world malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=7167 {ECO:0000313|EnsemblMetazoa:AALB009604-PA, ECO:0000313|Proteomes:UP000069272};
RN [1] {ECO:0000313|EnsemblMetazoa:AALB009604-PA}
RP IDENTIFICATION.
RC STRAIN=STECLA/ALBI9_A {ECO:0000313|EnsemblMetazoa:AALB009604-PA};
RG EnsemblMetazoa;
RL Submitted (AUG-2022) to UniProtKB.
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}.
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DR AlphaFoldDB; A0A182FSS4; -.
DR STRING; 7167.A0A182FSS4; -.
DR EnsemblMetazoa; AALB009604-RA; AALB009604-PA; AALB009604.
DR VEuPathDB; VectorBase:AALB009604; -.
DR VEuPathDB; VectorBase:AALB20_028558; -.
DR OrthoDB; 126305at2759; -.
DR Proteomes; UP000069272; Chromosome 2R.
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; 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; 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; PS00841; XPG_1; 1.
DR PROSITE; PS00842; XPG_2; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU910737};
KW DNA excision {ECO:0000256|ARBA:ARBA00022769,
KW 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 Endonuclease {ECO:0000256|ARBA:ARBA00022759};
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|RuleBase:RU910737}.
FT DOMAIN 1..99
FT /note="XPG N-terminal"
FT /evidence="ECO:0000259|SMART:SM00485"
FT DOMAIN 138..211
FT /note="XPG-I"
FT /evidence="ECO:0000259|SMART:SM00484"
SQ SEQUENCE 839 AA; 93366 MW; ABF51CF43F331A81 CRC64;
MGITGLLPFL EKASSACHLK ELRGKCVAID SYCWLHRGAF GCAERLARGE QTDAHIRYCL
KYVQLLLSYN IKPILVFDGR HLPAKAATEA KRRESRENAR KRGAELLRLG RIDEARSFLR
RCVDITHEMA LQLIQECRKR NVDCVVAPYE ADAQLAFLNR ADIAQYVITE DSDLVLFGCS
RILFKLDLAG NGRLVESTKL HLAMGCREER YQFDKFRQMC ILSGCDYLES LPGIGLAKAC
RFILKTEDPD IKRALAKIPA YLNMRQLSVS EEYKSEFLKA EATFKHMVVY DPVERRQKRL
TEPLDEGTPE EYCCNAGEFL DEDTAFNLAL GNLDPFSLRL LDNWHPDKTP EGHGAGDIKR
SRHLSIWQQN RSSAGEETCE KQSLPTASIT NAQKQQPFVK RSLMNAAFEE QGTKDTIADV
LQAYGIEAPP EPPMKRLCPA EFPQPSSIRS IAFEYEDVNV LEAMALLERQ ESPKRYRNPF
VVATNTAVSC REASNALLSP TKITPSNRSL LQNLSPVKRI DYSVSHSSGQ DIKMASQVDN
TATAVTTSRL SRFKRTNTTA SCSASAGQKV ISRFFCSQTS TVNSCTVNND LSPKQDQPEA
TGESPTAIVR KFKSKQETQK LAAAALYLRS PEAQLKLRGD RTPEKRRTGC DYETSTIEKA
FPSVEEGLVV KVDSGIVVND EEPNASDGDG LSLSQKENDD SAMNTVVFES NETKGRKAAR
LSLFEHKHVT RIESEDDKGS DDLAIVLDDA DDGSSEAKAD NHTDNEGTKT DLKLEHGKPP
FTITASSHAS RKTNSKPTCR RPGLSAIRGK PSKDAAGLTQ SRLSMFGFQK KSSMQLDKR
//
