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Database: UniProt
Entry: Q6FUN1_CANGA
LinkDB: Q6FUN1_CANGA
Original site: Q6FUN1_CANGA 
ID   Q6FUN1_CANGA            Unreviewed;      1223 AA.
AC   Q6FUN1;
DT   19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 132.
DE   RecName: Full=Structural maintenance of chromosomes protein {ECO:0000256|PIRNR:PIRNR005719};
GN   OrderedLocusNames=CAGL0F02079g {ECO:0000313|CGD:CAL0131032,
GN   ECO:0000313|EMBL:CAG58987.1};
OS   Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 /
OS   NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces.
OX   NCBI_TaxID=284593 {ECO:0000313|EMBL:CAG58987.1, ECO:0000313|Proteomes:UP000002428};
RN   [1] {ECO:0000313|EMBL:CAG58987.1, ECO:0000313|Proteomes:UP000002428}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65
RC   {ECO:0000313|Proteomes:UP000002428};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L.,
RA   Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA   Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|PIRNR:PIRNR005719}.
CC   -!- SIMILARITY: Belongs to the SMC family. SMC1 subfamily.
CC       {ECO:0000256|ARBA:ARBA00005597}.
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DR   EMBL; CR380952; CAG58987.1; -; Genomic_DNA.
DR   RefSeq; XP_446063.1; XM_446063.1.
DR   AlphaFoldDB; Q6FUN1; -.
DR   STRING; 284593.Q6FUN1; -.
DR   EnsemblFungi; CAGL0F02079g-T; CAGL0F02079g-T-p1; CAGL0F02079g.
DR   GeneID; 2887737; -.
DR   KEGG; cgr:CAGL0F02079g; -.
DR   CGD; CAL0131032; CAGL0F02079g.
DR   VEuPathDB; FungiDB:CAGL0F02079g; -.
DR   eggNOG; KOG0018; Eukaryota.
DR   HOGENOM; CLU_001042_0_1_1; -.
DR   InParanoid; Q6FUN1; -.
DR   OMA; SYIRDHT; -.
DR   Proteomes; UP000002428; Chromosome F.
DR   GO; GO:0030892; C:mitotic cohesin complex; IEA:EnsemblFungi.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0003690; F:double-stranded DNA binding; IEA:EnsemblFungi.
DR   GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR   GO; GO:0003680; F:minor groove of adenine-thymine-rich DNA binding; IEA:EnsemblFungi.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0006302; P:double-strand break repair; IEA:EnsemblFungi.
DR   GO; GO:0007064; P:mitotic sister chromatid cohesion; IEA:EnsemblFungi.
DR   GO; GO:0000070; P:mitotic sister chromatid segregation; IEA:EnsemblFungi.
DR   CDD; cd03275; ABC_SMC1_euk; 2.
DR   Gene3D; 1.10.287.1490; -; 1.
DR   Gene3D; 1.20.1060.20; -; 1.
DR   Gene3D; 3.30.70.1620; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR003395; RecF/RecN/SMC_N.
DR   InterPro; IPR024704; SMC.
DR   InterPro; IPR028468; Smc1_ABC.
DR   InterPro; IPR010935; SMC_hinge.
DR   InterPro; IPR036277; SMC_hinge_sf.
DR   PANTHER; PTHR18937:SF12; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN; 1.
DR   PANTHER; PTHR18937; STRUCTURAL MAINTENANCE OF CHROMOSOMES SMC FAMILY MEMBER; 1.
DR   Pfam; PF06470; SMC_hinge; 1.
DR   Pfam; PF02463; SMC_N; 1.
DR   PIRSF; PIRSF005719; SMC; 1.
DR   SMART; SM00968; SMC_hinge; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF75553; Smc hinge domain; 1.
PE   3: Inferred from homology;
KW   Cell cycle {ECO:0000256|ARBA:ARBA00022776};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Mitosis {ECO:0000256|ARBA:ARBA00022776};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR005719};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002428}.
FT   DOMAIN          525..640
FT                   /note="SMC hinge"
FT                   /evidence="ECO:0000259|SMART:SM00968"
FT   COILED          251..365
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          405..443
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          729..785
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          809..934
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1223 AA;  140433 MW;  F40BDB3F398BDC8E CRC64;
     MGRLVGLELY NFKSYKGTVN VDFGDSNFTS IIGPNGSGKS NLMDAISFVL GIRSSSLRSS
     ALKDLIYRDI ISRENTPTGA DNDENGNRTA YVKAFYEYDG KVVELMRLIS RLGDTSYKLD
     GNTVTYKEYS QFLESQNILI KAKNFLVFQG DVEQIASQSP LGLTKLIEEV SGSMQYKKEY
     EELKDQYDKI CQASTESIKK RRRIHAELKT YKEGMSRDEE YRKYVQKKKR VQTNLSLWQL
     YHMEDERYQC LQKLEESQND VDVIREKLEA EEKNLEVFKK ALSKEAVLLT KKKNHIRSIS
     KEKEKAESDL KVVKIPQNAS INRLKNLDKR VDSLQKDLER EEANLEKYKH QLKVVTDSKN
     AFEQEILSKS KNNNKFTLSE DDLKLYDELK GEYLNNGGIE IEDTLNLLDN KKEEITADLK
     IINDKVEISK QRIEDELVTK KEEQDAKIRD STLLLNEKND LHSHKLDELR KTQKDIEYWN
     NKEFDLNHKL RDTLVKLDDL NATQRESNKE RKLRENVAML KRFFPGVRGL VHELCKPKRD
     KYKLAVSTVL GKNFDSVIVD SLSVAQECIS FLKKQRAGVI SFIPLDTIDA ATPRMPVPES
     ETYTLAINTV EYKDDLVRAM YYVCSDTIIC DNLDIARDLK WNKNANVKIV TLDGALINKT
     GLMTGGITSD SANRWDKDEY QSLLDLKDKL IVDVEEAANK SRQSTLIARE LEISLSSLTS
     EISYIRTQIT QTKRAVEETE TEINHHNNLI DREFIPQVKD LENKISGLED EIRDWNTKRE
     ALQEKCFARL TEKVGFTMKD YESHTGEMIR KQTKELQILQ KQILNLENKV EFETGRCNAT
     KDRLQNVQET KNSVQHELNE LVDQEKSIKL SIETLEGELD GKNEELKSIK AAFDSKQKDA
     SATEDIISEY NNRLASIESD RNEIKDDITR LDLEKMSILK NCQVSGIIVP VVSEVGLEEL
     PASKVDDEAI EIAKKIEIDF SKLPRKYKEA TSAAVKQDLN NQIRDIDDVL EELQPNARAV
     ERFDDAKSRF DEVDKETEGL KTEERKVFDE FLKVKQKRKE LFENAFEKIN EHLDAIYSEL
     TRNVNSTSIL GGGSASMTIE DEDEPFNAGI RYHATPPMKR FKDMEYLSGG EKTVAALALL
     FAINSYNPSP FFILDEVDAA LDISNVQRIA AYIRRHGNPD LQFIVISLKN TMFEKSDALV
     GVFRQQQENS SKIVTLDLNQ YAT
//
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