ID   C5MA70_CANTT            Unreviewed;      1307 AA.
AC   C5MA70;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   RecName: Full=Rad50/SbcC-type AAA domain-containing protein {ECO:0000259|Pfam:PF13476};
GN   ORFNames=CTRG_02382 {ECO:0000313|EMBL:EER33564.1};
OS   Candida tropicalis (strain ATCC MYA-3404 / T1) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=294747 {ECO:0000313|EMBL:EER33564.1, ECO:0000313|Proteomes:UP000002037};
RN   [1] {ECO:0000313|EMBL:EER33564.1, ECO:0000313|Proteomes:UP000002037}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-3404 / T1 {ECO:0000313|Proteomes:UP000002037};
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).
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; GG692397; EER33564.1; -; Genomic_DNA.
DR   RefSeq; XP_002548085.1; XM_002548039.1.
DR   STRING; 294747.C5MA70; -.
DR   EnsemblFungi; CTRG_02382-t43_1; CTRG_02382-t43_1-p1; CTRG_02382.
DR   GeneID; 8301672; -.
DR   KEGG; ctp:CTRG_02382; -.
DR   VEuPathDB; FungiDB:CTRG_02382; -.
DR   eggNOG; KOG0962; Eukaryota.
DR   HOGENOM; CLU_006184_0_0_1; -.
DR   OrthoDB; 5477220at2759; -.
DR   Proteomes; UP000002037; Unassembled WGS sequence.
DR   GO; GO:0030870; C:Mre11 complex; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006302; P:double-strand break repair; IEA:InterPro.
DR   GO; GO:0000723; P:telomere maintenance; IEA:InterPro.
DR   Gene3D; 1.10.287.1490; -; 1.
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   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   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Meiosis {ECO:0000256|ARBA:ARBA00023254};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002037};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          6..258
FT                   /note="Rad50/SbcC-type AAA"
FT                   /evidence="ECO:0000259|Pfam:PF13476"
FT   COILED          224..296
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          584..669
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          796..948
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          988..1103
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1307 AA;  149233 MW;  60C94384E0D0568B CRC64;
     MSSIYKLSIK GIRAFEQETD ETIQFGFPLT LICGQNGCGK TTIIECLKYA TTGSLPPNSK
     GGAFVHDPTL DSRSVTNGQI KLAYKNINGK SMITTRSVQA NSKSTKSASG ATVTFKTLEG
     QLAMIEGGEK ISISSKNSEL DTQIPIYLGA SPAILENVIF CHQDDSLWPL SEPSALKKKF
     DDIFEASKFT KVLDNLKIIK KDMTTDIKLI EQSVNHLKID KDRAKKVQDR LTELTESADT
     YTEEIADLNI QIERKEKEAE DLFATNQEFQ KTLSDYENLL IKKQTLEEQI ERTKRSIEIL
     PDSDQELMNK QENFAAITEE KSRTIEDLQT KSSRMNEKLK DRTKNYNDLI RLDGSLKGKK
     VEYEQNLEEI SQIMNDYGDS LGVSLSEDTQ SNITKFKGEL EKAHKAILSE QKRLLTDNKR
     IEAEKQSELQ DVLNAISREE QHFEYATNDM ETNNQKLLVL RRKVDAGSND ETELIEKRIE
     LDSTNKQLQE KRDLNEVKEF DNKIMETNSE ISKLEFSLDE LAKKVSTSNK QSELRSKVTF
     LEDSVKSKNA EISRIISVIT DNYQEVVGSK LDIDVGDSLL NQKISHLQIK HEDQQKKVMS
     LESELEINKK TLESILKNAK DNSAKLESLK AAITTVIEED EIDEYESIVQ ELEENYRDVS
     EDVNTAEVTK DFKGSAIQMA EKSKCCLLCK RLFEEGGLDV FIKDLKQSVD ESKIQEIKSR
     AVEIKNDLDS VKSVNLKILN YRECLANVSE LESKIKDLRS NSYSIDKELT EATKDMKATK
     DLLDAALSLK KPLSDATRIN LEVQDIDIQI DELNEDLTGF GSNVASVGEL QKQQQDTNIK
     LKDMRQNLNE WTESKYKVQR EVQRLENRVK DIKLQISNLE RSLADVTNIK DNINETEKVI
     AKLEDRLKEI KDSLEKLRSD KETKERALKK AQDEIQESEE RIQKKVQDIQ DLYSSFSSLN
     ESISYYQAHI AKKLEENTSK MQQVSHECES LTLKIEEYTG SIKSLEKEVM DASRVEHNIL
     ANIDYRGQLS RLDEAELQLN SMDIENAQTR KDEYQEKSRQ LREAISSLTA DHAGKIGEVK
     QIKDQISGLK KELETEYKNV NQNYHEEWIK LQTNLLVSND LQNYSKALDN AIMKYHSIKM
     EEINRILTEL WSQTYRGSDI ATIAIKSDVN LQAKGNRSYN YRVVMIKDTS ELDMRGRCSA
     GQKVLASILI RLALAECFGA NCGMIALDEP TTNLDAENSE ALAAALTKII EYRKAQANFQ
     LIVITHDQKF LTHMQADRFT DHFYRIQRDE TSKSRIYSLP INRIQDD
//