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EXO1_DANRE
ID   EXO1_DANRE              Reviewed;         806 AA.
AC   Q803U7;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Exonuclease 1;
DE            EC=3.1.-.-;
DE   AltName: Full=Exonuclease I;
GN   Name=exo1; ORFNames=zgc:55521;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=AB;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: 5'->3' double-stranded DNA exonuclease which may also contain
CC       a cryptic 3'->5' double-stranded DNA exonuclease activity. Also
CC       exhibits endonuclease activity against 5'-overhanging flap structures
CC       similar to those generated by displacement synthesis when DNA
CC       polymerase encounters the 5'-end of a downstream Okazaki fragment.
CC       Required for DNA mismatch repair (MMR) (By similarity). {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
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:0000250};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the XPG/RAD2 endonuclease family. EXO1
CC       subfamily. {ECO:0000305}.
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DR   EMBL; BC044187; AAH44187.1; -; mRNA.
DR   RefSeq; NP_998634.1; NM_213469.1.
DR   AlphaFoldDB; Q803U7; -.
DR   SMR; Q803U7; -.
DR   STRING; 7955.ENSDARP00000073846; -.
DR   PaxDb; Q803U7; -.
DR   GeneID; 406778; -.
DR   KEGG; dre:406778; -.
DR   CTD; 9156; -.
DR   ZFIN; ZDB-GENE-040426-2828; exo1.
DR   eggNOG; KOG2518; Eukaryota.
DR   InParanoid; Q803U7; -.
DR   OrthoDB; 796591at2759; -.
DR   PhylomeDB; Q803U7; -.
DR   Reactome; R-DRE-5358565; Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha).
DR   Reactome; R-DRE-5685938; HDR through Single Strand Annealing (SSA).
DR   Reactome; R-DRE-5685942; HDR through Homologous Recombination (HRR).
DR   Reactome; R-DRE-5693568; Resolution of D-loop Structures through Holliday Junction Intermediates.
DR   Reactome; R-DRE-5693579; Homologous DNA Pairing and Strand Exchange.
DR   Reactome; R-DRE-5693607; Processing of DNA double-strand break ends.
DR   Reactome; R-DRE-5693616; Presynaptic phase of homologous DNA pairing and strand exchange.
DR   Reactome; R-DRE-6804756; Regulation of TP53 Activity through Phosphorylation.
DR   Reactome; R-DRE-69473; G2/M DNA damage checkpoint.
DR   PRO; PR:Q803U7; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0035312; F:5'-3' exodeoxyribonuclease activity; IBA:GO_Central.
DR   GO; GO:0017108; F:5'-flap endonuclease activity; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0048256; F:flap endonuclease activity; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0045145; F:single-stranded DNA 5'-3' exodeoxyribonuclease activity; ISS:UniProtKB.
DR   GO; GO:0006310; P:DNA recombination; ISS:UniProtKB.
DR   GO; GO:0006298; P:mismatch repair; ISS:UniProtKB.
DR   CDD; cd09908; H3TH_EXO1; 1.
DR   CDD; cd09857; PIN_EXO1; 1.
DR   InterPro; IPR036279; 5-3_exonuclease_C_sf.
DR   InterPro; IPR032641; Exo1.
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; PTHR11081; 1.
DR   PANTHER; PTHR11081:SF8; PTHR11081:SF8; 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; SSF47807; 1.
DR   SUPFAM; SSF88723; SSF88723; 1.
DR   PROSITE; PS00841; XPG_1; 1.
DR   PROSITE; PS00842; XPG_2; 1.
PE   2: Evidence at transcript level;
KW   DNA damage; DNA excision; DNA repair; DNA-binding; Endonuclease;
KW   Excision nuclease; Exonuclease; Hydrolase; Magnesium; Metal-binding;
KW   Nuclease; Nucleus; Reference proteome.
FT   CHAIN           1..806
FT                   /note="Exonuclease 1"
FT                   /id="PRO_0000154041"
FT   REGION          1..99
FT                   /note="N-domain"
FT   REGION          138..229
FT                   /note="I-domain"
FT   REGION          337..426
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          443..475
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          512..754
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        351..388
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        448..475
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        515..541
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        556..587
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        599..618
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        627..672
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         30
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         78
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         150
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         152
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         171
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         173
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         225
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   806 AA;  88594 MW;  B7822D194A0C6AE6 CRC64;
     MGIQGLLQFI KDASEPMHVK KYRGQTVAVD TYCWLHKGAF SCAEKLAKGE PTDQYVSYCM
     KFVDMLLSFG VKPILVFDGR NLPSKQEVEK SRRERRQANL QKGKQLLREG KITEARECFT
     RSVNITPSMA HDVIRAARTR GVDCVVAPYE ADAQLAFLNK SDIAQAVITE DSDLLAFGCK
     KVILKMDKQG NGLEIEQCHL GRCKSLGNIF TEEKFRYMCI LSGCDYLQSL YGIGLGKACK
     LLRMANNPDI LKVIKKMGQY LKMDISVPEE YIEGFTKANN TFLYQLVFDP LRRKVVPLNP
     YPDHINPAAL SYAGTNVGDE KGLQMALGNL DINTMQRIDD FNPDAPQTQP PKAPRSSSWN
     DRCDKTATTQ ASIWSQNYEP GCTKSQSPTS PKRPPPTRGK ERIVSVQSLK LPQRESQVKR
     PREDTSLSVD DLLEQYTAGV KRHCPETQPT TKPLTNDNKV SKENHCGSTS GPFRPRNRFA
     TLLQWRNRSE EGTEEQGTCS RFFCHDESNI AETQEDSKQD SSQSVESQEK HVSQSGGDTS
     SLCEEPEREQ DKDEPSSPPA SPSCSSRPAS VGLGVFSWSG TTKELNKSVS HPARDSTERQ
     RSSSTPSGLS TLQQFHRNKA RISWAGPGLS LSSSPVEGSE DAGNSPGSPP SQDSAYFSQS
     SSISASVENS LVTEDNSDKE KERDSVVSNS PSSSPLDRLK PAVNRTKVSG LSRKGACGQG
     KGGKIETSAP ARASGLRRKP SGKKNVNNEN SPGLQATISG LWGAFSFKKD SPKLSATKKG
     EPMSPVGENV VMETTQADKE IFIIAE
 
 
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