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Database: UniProt
Entry: B2G497_ZYGRO
LinkDB: B2G497_ZYGRO
Original site: B2G497_ZYGRO 
ID   B2G497_ZYGRO            Unreviewed;      1304 AA.
AC   B2G497;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   24-JAN-2024, entry version 61.
DE   SubName: Full=DNA repair protein RAD50 {ECO:0000313|EMBL:CAQ43406.1};
GN   Name=Zr_RAD50 {ECO:0000313|EMBL:CAQ43406.1};
GN   ORFNames=Zrou_4p7 {ECO:0000313|EMBL:CAQ43406.1};
OS   Zygosaccharomyces rouxii (Candida mogii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Zygosaccharomyces.
OX   NCBI_TaxID=4956 {ECO:0000313|EMBL:CAQ43406.1};
RN   [1] {ECO:0000313|EMBL:CAQ43406.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CBS 732 {ECO:0000313|EMBL:CAQ43406.1};
RA   Gordon J.L., Wolfe K.H.;
RT   "Zygosaccharomyces rouxii homologs of Saccharomyces cerevisiae chromosome
RT   III.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the SMC family. RAD50 subfamily.
CC       {ECO:0000256|ARBA:ARBA00009439}.
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DR   EMBL; AM989983; CAQ43406.1; -; Genomic_DNA.
DR   RefSeq; XP_002497898.1; XM_002497853.1.
DR   GeneID; 8205670; -.
DR   KEGG; zro:ZYRO0F16038g; -.
DR   OMA; FSDYYYR; -.
DR   OrthoDB; 5477220at2759; -.
DR   GO; GO:0030870; C:Mre11 complex; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006302; P:double-strand break repair; IEA:InterPro.
DR   GO; GO:0000723; P:telomere maintenance; IEA:InterPro.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038729; Rad50/SbcC_AAA.
DR   InterPro; IPR004584; Rad50_eukaryotes.
DR   InterPro; IPR013134; Zn_hook_RAD50.
DR   NCBIfam; TIGR00606; rad50; 1.
DR   PANTHER; PTHR18867:SF12; DNA REPAIR PROTEIN RAD50; 1.
DR   PANTHER; PTHR18867; RAD50; 1.
DR   Pfam; PF13476; AAA_23; 1.
DR   Pfam; PF04423; Rad50_zn_hook; 1.
DR   Pfam; PF13558; SbcC_Walker_B; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51131; ZN_HOOK; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Meiosis {ECO:0000256|ARBA:ARBA00023254};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU00471}; Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00471}.
FT   DOMAIN          632..733
FT                   /note="Zinc-hook"
FT                   /evidence="ECO:0000259|PROSITE:PS51131"
FT   COILED          226..371
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          466..523
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          711..918
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1000..1097
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         679
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00471"
FT   BINDING         682
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00471"
SQ   SEQUENCE   1304 AA;  150640 MW;  F6F303D6865C24D0 CRC64;
     MSAIYKLSIQ GIRSFDSNDR ETIQFGKPLT LIVGSNGSGK TTIIECLKYA TTGDLPPNSK
     GGAFVHDPKI TGEKDVRAQV KLAFTSANAL NMIVTRNIQL LTKKTTATFK TLEGQLVIVN
     GNGDRNTLGT RSLELDAQVP LYLGVPKAIL EYVIFCHQED SLWPLSEPSN LKKKFDEIFQ
     AMKFTRALDN LKGIKKDMTV DIKLLKQAVE HLKVDKDRSR VMTMNITRLQ AKSEEYQAQV
     KEVEKQLKDI TEQSDKLFKS NQDFQKVLSK LESLKNSQQS KLEQIDRLSN SIDPIDLGKE
     ELENLLSNFS SSLTEKEEEL RSMEKSLRES KAKAAGIQNK CNSLMQRQGE LSASKENHER
     NKSVLRELQR ELQTSYALSG FTENLDDFAH SLKELVHKTE NNLLNFTHSN KSELNSSNNE
     LSELNNSLIV QTQRLDYSKM DKQKLASEIQ NLELQVDISD FTDEDLEGAR QDLNKFSEKL
     KDWEKQGLVS SISQQIKEKN EQMLILEYEI EELQVKISRT NQQADLFAKL GLLKKSLQDR
     QLELGKFTQS FKMDSKSKEW GLQCGHDVDM DFKKFYINMQ KNLSTKSRQQ NELDKKFMEG
     SLQLTNTEMD LRKNEEFIIN ATKHLQESLP EDCTIDDYTE VVAEAEASYR TALENLKIHQ
     TTLEFNKKAL EVAKTESCCY LCTRKFDDEG FKSSILLRLQ EKTDGKFNTI LKESLESEKE
     YLNSLRNLEK DVISLNDSRS RITGLSDKVT DMRNRNVKMR EELDTVNKEL ESMKEDKDHA
     EKEVRPLVEN IVRLRKASNE LESDIKSITD ELAIYRSSEG KVETVEELQN EQRNKNESLR
     RLRKEVGQLQ DERETKSKEH SNLLNLIREK DLKISEIEKS ISMRKNLESD LDNKKNQLKV
     LEETVKKLEG DVKEGSRKVN SLKVDLERKT HDFEKSLDEN NKEFKAMVLN NERFISINQQ
     VKGFTASVPL EYEKCVAELE SAKKQLVDLD HINENMNSGI TELAKKLNDS NREKRNLKEN
     LDLMELRADL SSIERQIDEL DIQNAEAERD RYQQESMRLR SQFERLSSEN AGKLGERKQL
     QNQIDSMQQQ LRTDYKDVDV KYQKQWVELQ AKTFVTDDID TYSNALDSAI MRYHKLKMED
     INRIIDELWK RTYSGTDVDT IQLRSEEVGS GVKMKSYNYR VVMFKQDAEL DMRGRCSAGQ
     KVLASIIIRL ALSETFGVNC GVIALDEPTT NLDEENIESL ARSLHNIIEL RRHQKNFQLI
     VITHDEKFLN HMDASQFTDH FFKVKRDDRQ KSQIEWVDIN KVTD
//
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