SGO1_CANGA
ID SGO1_CANGA Reviewed; 603 AA.
AC Q6FMT2;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=Shugoshin;
GN Name=SGO1; OrderedLocusNames=CAGL0K05445g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=15229592; DOI=10.1038/nature02579;
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.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Plays a central role in chromosome cohesion during cell
CC division by preventing premature dissociation of cohesin complex from
CC centromeres after prophase, when most of cohesin complex dissociates
CC from chromosomes arms. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome, centromere
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the shugoshin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR380957; CAG61423.1; -; Genomic_DNA.
DR RefSeq; XP_448462.1; XM_448462.1.
DR AlphaFoldDB; Q6FMT2; -.
DR SMR; Q6FMT2; -.
DR STRING; 5478.XP_448462.1; -.
DR EnsemblFungi; CAG61423; CAG61423; CAGL0K05445g.
DR GeneID; 2890486; -.
DR KEGG; cgr:CAGL0K05445g; -.
DR CGD; CAL0134399; CAGL0K05445g.
DR VEuPathDB; FungiDB:CAGL0K05445g; -.
DR eggNOG; ENOG502QSMK; Eukaryota.
DR HOGENOM; CLU_019322_0_0_1; -.
DR InParanoid; Q6FMT2; -.
DR OMA; SKIKHSM; -.
DR Proteomes; UP000002428; Chromosome K.
DR GO; GO:0000776; C:kinetochore; IEA:EnsemblFungi.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0034508; P:centromere complex assembly; IEA:EnsemblFungi.
DR GO; GO:0070199; P:establishment of protein localization to chromosome; IEA:EnsemblFungi.
DR GO; GO:0051383; P:kinetochore organization; IEA:EnsemblFungi.
DR GO; GO:0034090; P:maintenance of meiotic sister chromatid cohesion; IEA:EnsemblFungi.
DR GO; GO:0051757; P:meiotic sister chromatid separation; IEA:EnsemblFungi.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IEA:EnsemblFungi.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IEA:EnsemblFungi.
DR GO; GO:0034096; P:positive regulation of maintenance of meiotic sister chromatid cohesion; IEA:EnsemblFungi.
DR GO; GO:0031134; P:sister chromatid biorientation; IEA:EnsemblFungi.
DR InterPro; IPR011515; Shugoshin_C.
DR InterPro; IPR011516; Shugoshin_N.
DR Pfam; PF07557; Shugoshin_C; 1.
DR Pfam; PF07558; Shugoshin_N; 1.
PE 3: Inferred from homology;
KW Cell cycle; Cell division; Centromere; Chromosome; Chromosome partition;
KW Coiled coil; Nucleus; Reference proteome.
FT CHAIN 1..603
FT /note="Shugoshin"
FT /id="PRO_0000055446"
FT REGION 112..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 331..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 455..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 583..603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 11..74
FT /evidence="ECO:0000255"
FT COILED 304..325
FT /evidence="ECO:0000255"
FT COILED 431..451
FT /evidence="ECO:0000255"
FT COMPBIAS 123..144
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..163
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..363
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..482
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..519
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 603 AA; 68724 MW; DD5BC8C6A9417AAB CRC64;
MSNLYSAGTP HIQELQNILD SQQEEWAAIK ENYTTQNSLI AKENCTLKMK LSELENKVSQ
LIRENVQLRS QVSLNKLEFQ NKLASQINVL ENGVIQRLEE VLYMFDSIRK KESLPSRPTS
TNETVDRIKK RRQSNEEARN RRRSRSVSTG SAHSTSSMKR RSSTFGEDLI DASIKRALDN
AQSNSLQTSD TLRLSELPGL NEIDTNNVNN DNLLSPIPHK KRKSNRRKSI YVPELPKPNN
EPLMENTIEQ QENICSESLI QEGEQSEKLG ENLDADQSHV EDQSFSFTNS VLEYSIPEEN
TLPKQDILDE TEKRDTAVNQ KKKLEIFHDP PVEELSSSKN EKPPENSITN DPAFITVTGN
NKVKHSMKSR KPKKNKGSVD ESMPCTQSTE SVDFDRPRRT RGKTVDYRLP SLRAKMRRPT
EKLVDATTTV NIQDLQVKYK KSKKVLEKEL KTDMKAMKSP KKNEKTFESG TIFKKISRDN
ESRPSSTHST SSVDAECSHN NSHSENINSS INDTTHSSFN NSTKSVLSDI TNISKNKQQQ
KTKKLLKTAI INDIYDDKTK NAQKTVSFRV NEDDLSVFDL IQHNDTNKSS PKTYRSRSRK
NKA