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Database: UniProt
Entry: G8B8W2_CANPC
LinkDB: G8B8W2_CANPC
Original site: G8B8W2_CANPC 
ID   G8B8W2_CANPC            Unreviewed;       634 AA.
AC   G8B8W2;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 53.
DE   RecName: Full=Double-strand break repair protein {ECO:0000256|PIRNR:PIRNR000882};
GN   OrderedLocusNames=CPAR2_300500 {ECO:0000313|CGD:CAL0000156395,
GN   ECO:0000313|EMBL:CCE41061.1};
OS   Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia
OS   parapsilosis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=578454 {ECO:0000313|EMBL:CCE41061.1, ECO:0000313|Proteomes:UP000005221};
RN   [1] {ECO:0000313|Proteomes:UP000005221}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 317 / ATCC MYA-4646 {ECO:0000313|Proteomes:UP000005221};
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA   Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA   Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA   Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA   Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA   Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA   Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
RN   [2] {ECO:0000313|Proteomes:UP000005221}
RP   GENOME REANNOTATION.
RC   STRAIN=CDC 317 / ATCC MYA-4646 {ECO:0000313|Proteomes:UP000005221};
RX   PubMed=22192698; DOI=10.1186/1471-2164-12-628;
RA   Guida A., Lindstaedt C., Maguire S.L., Ding C., Higgins D.G., Corton N.J.,
RA   Berriman M., Butler G.;
RT   "Using RNA-seq to determine the transcriptional landscape and the hypoxic
RT   response of the pathogenic yeast Candida parapsilosis.";
RL   BMC Genomics 12:628-628(2011).
CC   -!- FUNCTION: Involved in DNA double-strand break repair (DSBR). Possesses
CC       single-strand endonuclease activity and double-strand-specific 3'-5'
CC       exonuclease activity. Also involved in meiotic DSB processing.
CC       {ECO:0000256|PIRNR:PIRNR000882}.
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000882};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|PIRNR:PIRNR000882}.
CC   -!- SIMILARITY: Belongs to the MRE11/RAD32 family.
CC       {ECO:0000256|ARBA:ARBA00009028, ECO:0000256|PIRNR:PIRNR000882,
CC       ECO:0000256|RuleBase:RU003447}.
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DR   EMBL; HE605204; CCE41061.1; -; Genomic_DNA.
DR   AlphaFoldDB; G8B8W2; -.
DR   STRING; 578454.G8B8W2; -.
DR   EnsemblFungi; CPAR2_300500-T; CPAR2_300500-T-p1; CPAR2_300500.
DR   CGD; CAL0000156395; CPAR2_300500.
DR   VEuPathDB; FungiDB:CPAR2_300500; -.
DR   eggNOG; KOG2310; Eukaryota.
DR   Proteomes; UP000005221; Chromosome 3.
DR   GO; GO:0140445; C:chromosome, telomeric repeat region; IEA:EnsemblFungi.
DR   GO; GO:0030870; C:Mre11 complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0035861; C:site of double-strand break; IEA:EnsemblFungi.
DR   GO; GO:0008296; F:3'-5'-DNA exonuclease activity; IEA:EnsemblFungi.
DR   GO; GO:0004017; F:adenylate kinase activity; IEA:EnsemblFungi.
DR   GO; GO:0004520; F:DNA endonuclease activity; IEA:EnsemblFungi.
DR   GO; GO:0003691; F:double-stranded telomeric DNA binding; IEA:EnsemblFungi.
DR   GO; GO:0051880; F:G-quadruplex DNA binding; IEA:EnsemblFungi.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0060090; F:molecular adaptor activity; IEA:EnsemblFungi.
DR   GO; GO:0043047; F:single-stranded telomeric DNA binding; IEA:EnsemblFungi.
DR   GO; GO:0030437; P:ascospore formation; IEA:EnsemblFungi.
DR   GO; GO:0006284; P:base-excision repair; IEA:EnsemblFungi.
DR   GO; GO:0010791; P:DNA double-strand break processing involved in repair via synthesis-dependent strand annealing; IEA:EnsemblFungi.
DR   GO; GO:1990918; P:double-strand break repair involved in meiotic recombination; IEA:EnsemblFungi.
DR   GO; GO:0000727; P:double-strand break repair via break-induced replication; IEA:EnsemblFungi.
DR   GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IEA:EnsemblFungi.
DR   GO; GO:0035753; P:maintenance of DNA trinucleotide repeats; IEA:EnsemblFungi.
DR   GO; GO:0010780; P:meiotic DNA double-strand break formation involved in reciprocal meiotic recombination; IEA:EnsemblFungi.
DR   GO; GO:0097552; P:mitochondrial double-strand break repair via homologous recombination; IEA:EnsemblFungi.
DR   GO; GO:0031573; P:mitotic intra-S DNA damage checkpoint signaling; IEA:EnsemblFungi.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:EnsemblFungi.
DR   GO; GO:0000723; P:telomere maintenance; IEA:EnsemblFungi.
DR   CDD; cd00840; MPP_Mre11_N; 1.
DR   Gene3D; 3.60.21.10; -; 1.
DR   Gene3D; 3.30.110.110; Mre11, capping domain; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR003701; Mre11.
DR   InterPro; IPR038487; Mre11_capping_dom.
DR   InterPro; IPR007281; Mre11_DNA-bd.
DR   InterPro; IPR041796; Mre11_N.
DR   NCBIfam; TIGR00583; mre11; 1.
DR   PANTHER; PTHR10139; DOUBLE-STRAND BREAK REPAIR PROTEIN MRE11; 1.
DR   PANTHER; PTHR10139:SF1; DOUBLE-STRAND BREAK REPAIR PROTEIN MRE11; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   Pfam; PF04152; Mre11_DNA_bind; 1.
DR   PIRSF; PIRSF000882; DSB_repair_MRE11; 1.
DR   SMART; SM01347; Mre11_DNA_bind; 1.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
PE   3: Inferred from homology;
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|PIRNR:PIRNR000882};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|PIRNR:PIRNR000882};
KW   Endonuclease {ECO:0000256|ARBA:ARBA00022759,
KW   ECO:0000256|PIRNR:PIRNR000882};
KW   Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|PIRNR:PIRNR000882};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR000882};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|PIRNR:PIRNR000882};
KW   Meiosis {ECO:0000256|ARBA:ARBA00023254, ECO:0000256|PIRNR:PIRNR000882};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|PIRNR:PIRNR000882};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR000882};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005221}.
FT   DOMAIN          294..475
FT                   /note="Mre11 DNA-binding"
FT                   /evidence="ECO:0000259|SMART:SM01347"
FT   REGION          566..634
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        566..591
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        129
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000882-1"
SQ   SEQUENCE   634 AA;  70816 MW;  9E544C44992D6B79 CRC64;
     MPLVDHIENG SDTIRILLTT DNHVGCFEND PIRGDDGWKT FDEITRIAKE QDVDMLVQGG
     DLFHINKPTK KSMYHVMKSL RTNCMGDKAC QLELLSDPST TMFNGVDEVN YEDPNLNIAI
     PVFAISGNHD DATGDGLLSA LDVLAVSGLV NYFGKVKDSE SITVKPILFE KGDTKLALYG
     MSNVRDERLH RLFRDGKVKF ERPGVNTDKW FNFFAIHQNH AMHTFNSCIP ENFLPHFLDF
     VLWGHEHECV PYPVHNPETS FDVLQAGSSI ATSLSEGEVP DKKVFIINIK GNDYSLEPIE
     LKAVRPFVLK EIELSKTDLV PGAASKADVI AFLSNEVENA IEIANKSYLQ GHSELTASNP
     GKQDNITPNI PLPLIRLRVE YSGGFEIENV RRFSNQFVGR IANVNDVVQF YKKKSPQQPE
     ILRKKTKFSD DMVDESLGEK TTTELALQDI VSDFLKQTQL TLIPEAGLNE AVKKYVDNDD
     KYSLNQYINS EIKKETKMLL SVDIDDQEFH GIEDEKHSRT AFKQILLQLK EGTFAQLNLK
     AENAGKSSKT KVKGGDKPLA KSNEIVLDSS DSENEVHVAP LSGSSRGRSV SHPDTYAEDE
     NEILTSEEEY APQPVKARAT GGGGGRRRKG RDKK
//
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