ID A0A091HBB7_BUCRH Unreviewed; 778 AA.
AC A0A091HBB7;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 03-MAY-2023, entry version 30.
DE RecName: Full=Exonuclease 1 {ECO:0000256|ARBA:ARBA00020324, ECO:0000256|RuleBase:RU910737};
DE EC=3.1.-.- {ECO:0000256|RuleBase:RU910737};
DE Flags: Fragment;
GN ORFNames=N320_07520 {ECO:0000313|EMBL:KFO92092.1};
OS Buceros rhinoceros silvestris.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Bucerotiformes; Bucerotidae; Buceros.
OX NCBI_TaxID=175836 {ECO:0000313|EMBL:KFO92092.1, ECO:0000313|Proteomes:UP000054064};
RN [1] {ECO:0000313|EMBL:KFO92092.1, ECO:0000313|Proteomes:UP000054064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N320 {ECO:0000313|EMBL:KFO92092.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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 EMBL; KL528800; KFO92092.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091HBB7; -.
DR Proteomes; UP000054064; 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; 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, ECO:0000313|EMBL:KFO92092.1};
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:UP000054064}.
FT DOMAIN 1..73
FT /note="XPG N-terminal"
FT /evidence="ECO:0000259|SMART:SM00485"
FT DOMAIN 112..182
FT /note="XPG-I"
FT /evidence="ECO:0000259|SMART:SM00484"
FT REGION 415..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 556..642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..450
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..591
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 604..642
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFO92092.1"
FT NON_TER 778
FT /evidence="ECO:0000313|EMBL:KFO92092.1"
SQ SEQUENCE 778 AA; 87399 MW; C6ECD3E76270D4FA CRC64;
VAVDTYCWLH KGAYACAEKL ARGEPTDLYV AFCMKLVDML LSFGIKPILV FDGCTLPSKK
EVEKARREKR QASLLKGKQL LQEGRLSEAR ECFGRSVNVT HAMAHEVIKA ARARGVDCIV
APYEADAQLA YLNKNGMVQA IITEDSDLLA FGCKKVFLKI DKFGNGLEID QSRLGNCKQL
GNVFTEEKFR YMCILSGCDY LSSIHGIGLA KACKLLKLAN NPDIIKVIRK MGQYLKMNIT
VPEEYIQGFT RANNTFLYQL VFDPVNRKLV PLNAYEDDID PETLIYAGRH FGDGTAFQIA
IGNVDIDTME QIDNYNPDTA QPVQQRSCGW NDKRANHVNS IWSRDYKLDP NVHTVPHKTN
LLEKPTTKGI EKIISVKGLK LPSKDLLAKR PRSGLEEISD GDLLNQYTFS KAKKFKKESD
RDGQAQKSIT AVQSLDSSEN SDTQESSNSL TRVRNKFASF LQRKNKEKDA VIVPGTRSRF
FCNDAIMFDG RAKKDDSDLT QNAEQDCQKQ EIKHVADDVS HFSESEKSRR TIFTPPGETQ
RNCFRWFSSL INNSGNSGPS HTVLSQKSHQ QRSNCVVSQE DEINGTQTGS EEACGELEEE
SSPLTEQEQS TQSQRSCEPS ECSLETSEIP QMSDNNSNSK LADDHCTLSP VFSAVQSDRK
NTIVKTKVPG LHKPSCRGSL IVTKLKPLIP AKVSGLSRKL SPVQKRNHCD AENKLGMQAT
ISELRKNFQF KREYEKLPSY KKSDPLSPIK DNIQLTPETE EEIFNHLEHS HLQRAIFQ
//
