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
//