ID A0A3Q4HN17_NEOBR Unreviewed; 658 AA.
AC A0A3Q4HN17;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Exonuclease 1 {ECO:0000256|ARBA:ARBA00020324, ECO:0000256|RuleBase:RU910737};
DE EC=3.1.-.- {ECO:0000256|RuleBase:RU910737};
OS Neolamprologus brichardi (Fairy cichlid) (Lamprologus brichardi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Lamprologini; Neolamprologus.
OX NCBI_TaxID=32507 {ECO:0000313|Ensembl:ENSNBRP00000024950.1, ECO:0000313|Proteomes:UP000261580};
RN [1] {ECO:0000313|Ensembl:ENSNBRP00000024950.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) 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; A0A3Q4HN17; -.
DR Ensembl; ENSNBRT00000025603.1; ENSNBRP00000024950.1; ENSNBRG00000019048.1.
DR GeneTree; ENSGT00510000047676; -.
DR OMA; AFCMKLV; -.
DR Proteomes; UP000261580; Unplaced.
DR Bgee; ENSNBRG00000019048; Expressed in testis.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000261580}.
FT DOMAIN 1..99
FT /note="XPG N-terminal"
FT /evidence="ECO:0000259|SMART:SM00485"
FT DOMAIN 138..208
FT /note="XPG-I"
FT /evidence="ECO:0000259|SMART:SM00484"
FT REGION 337..543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 555..605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..371
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 389..420
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..464
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 474..543
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 591..605
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 658 AA; 72984 MW; 81748A81D0E11773 CRC64;
MGISGLLQFI KAAAEPINVK KYKGQTVAVD TYCWLHKGAF SCAEKLAKGE PTDQYVWYCM
KLVDMLLTFS VKPILVFDGR NLPSKQEVEK ARRERRETNL HKGRQLLREG KLSEARECFN
RCVNISPAMA HNLIKAARAR GVDCVVAPYE ADAQLAYLSK SGLAQAVITE DSDLLAFGCK
KVILKMDKQG NGLEIDQSNL GRCRSLGNVF TEEKFRYMCI LSGCDYLSSL HGIGLGKACK
LLQLAKDPDI LRVIRKMGQY LKMSLVVPEQ YIEGFVRANN TFLYQLVFDP VRRKVVPLNP
YPEHVDPATL SYAGLHLGDD KGLQMALGNL DINSMERIDD FSPDKPLPQQ SKGRSHSWNY
SPASTGPSIW SRGFTPAPAQ PPTSPDRPPS TRGKKRVINL DGLRMPCREL QVKRPGEDSS
ISDQDVLQEY SSSSPKRSRS DQPADKPTVT SLPRSRNIFA TVLQRRNQEA EEDGQVTRSS
PAQKSSPSIQ NCDTESSDGP SLETTKPSPS PSTTSSASRG LSLFRWSDGP STEQSTTPLS
TSSLSALQQF QYKKESCSSP PKVTRPSGDS VLPEPFSQDR TSEKDELSDS PPSQDSAYFS
QSQPYLTSYH NEEAPTYSFS SSYQEDAASV SWCKSPRFTN AVCPLWLGQR HHSFISVE
//
