ID   A0A0P1BRY4_9BASI        Unreviewed;      1237 AA.
AC   A0A0P1BRY4;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=Structural maintenance of chromosomes protein {ECO:0000256|PIRNR:PIRNR005719};
OS   Ceraceosorus bombacis.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Exobasidiomycetes; Ceraceosorales; Ceraceosoraceae; Ceraceosorus.
OX   NCBI_TaxID=401625 {ECO:0000313|EMBL:CEH19151.1, ECO:0000313|Proteomes:UP000054845};
RN   [1] {ECO:0000313|EMBL:CEH19151.1, ECO:0000313|Proteomes:UP000054845}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Magalhaes I.L.F., Oliveira U., Santos F.R., Vidigal T.H.D.A.,
RA   Brescovit A.D., Santos A.J.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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; CCYA01000277; CEH19151.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0P1BRY4; -.
DR   STRING; 401625.A0A0P1BRY4; -.
DR   OrthoDB; 231904at2759; -.
DR   Proteomes; UP000054845; Unassembled WGS sequence.
DR   GO; GO:0008278; C:cohesin complex; IEA:InterPro.
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:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007062; P:sister chromatid cohesion; IEA:InterPro.
DR   CDD; cd03275; ABC_SMC1_euk; 1.
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:UP000054845}.
FT   DOMAIN          530..646
FT                   /note="SMC hinge"
FT                   /evidence="ECO:0000259|SMART:SM00968"
FT   REGION          74..98
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          358..384
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          440..464
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          721..755
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          815..916
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1034..1075
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        358..379
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1237 AA;  140603 MW;  DCC5B4E04D513F39 CRC64;
     MPLVQLEVEN FKSYRGKQII GPFNSFTAII GPNGSGKSNL MDAVSFVLGV KSAQLRSSQL
     KDLIYRGRKM AREEGDEEAE ALRSDEEDEG EGTAGKASVS AVYRDKQGAE WRFTRNITSS
     GASEYRVNNK VHSWNSYNDR LRSFNILVKA KNFLVFQGDV EAVAQQGPKE LSRLIDQISG
     SLEYKEAYEA AKAAQDRAIE QSTYSFNKRR GINGELKTYR EQKSEAEKWE RLQSERDAHI
     LQHILWRLYH IEEELEQTSS TIDSESSKLP QLRKQVRDEE SHVEQARKEV AQLDKDIAKQ
     ESSLRKRERE LEALQPSIGA IDEKIAHSNR RRTNAEELCV SVERDVERLT ARIAKLRRDH
     DSAKDAADEA AEEQRRAAQE RGQALSGQEL AEYHELKAQA NLRATAERQQ LETLSRDIRA
     NKATADELDE KLKALQRAKE KQEAISESQK ERKQALEGRA RQVEKSLKDA RNELTRVQKQ
     RADIVKREDE LNKTLEDCVN KLLQAGSDAR ETEREMRMKE TYAALARMFP GVHGRLADLC
     KPVQRKYDTA ISTVLGRNND ALIVDNEKTA IDCIEYLRSQ RAGQATFIPL DTIQVKPIND
     RLRNIASGAR LAVDVLQFDA AVERAMHFAC GNAVVCDSMP IARFVCYEKK VEVKAVTLDG
     TLIHKSGNIT GGVTAGERTH RWEEREVDGL GRQRDQCLAE LKELGKQRYE LSQDDDLRSS
     LQRSEADLST LRDELTEVNS RLDGARDELK IINSQIKDTT GRFNKARTAQ QDAENRATGL
     MDTVEGADDA VFGAFCQRIG VPNIRAYEAR QLRVLEQQSQ ARLKYEEQMK RLDHQIRFEE
     RQLADAEERL ELNRRVITKE AERVQARRAE KEELEAQIQE LQERIEQVNE RLAELREQQQ
     QRLKALSEAK KNEILANKTL GAKVTEISRC NDVIEKLSAE RSSIYRRCRL EEIDLPLKQG
     SLSSIPLEDN PDLAPMDIDE DVTQRAIEAA DYGIEVDFTD LDDEEKADGG EDMAKELQGR
     IDDVIAQIEQ MQPNMKAIER LDDAELKLKE TEKEFARSRN DAQKARDEFN RIKKKRCDLF
     NAAFSHISER IDSTYKELTK GKASPMGGVA YLSLEDSDEP YLSGVRYHIM PPMKRFRDMS
     DLSGGEKTIG ALALLFAIST FRAPPLWILD EVDAALDSTN VSRVANYLRS HASDQTQFIV
     ISLKASMYER ASSLCGIYRQ QDINSSRSLT LDLDAYA
//