ID B9WLG8_CANDC Unreviewed; 1240 AA.
AC B9WLG8;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=Structural maintenance of chromosomes protein {ECO:0000256|PIRNR:PIRNR005719};
GN OrderedLocusNames=Cd36_28880 {ECO:0000313|CGD:CAL0000159559};
GN ORFNames=CD36_28880 {ECO:0000313|EMBL:CAX39930.1};
OS Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 /
OS NRRL Y-17841) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=573826 {ECO:0000313|EMBL:CAX39930.1, ECO:0000313|Proteomes:UP000002605};
RN [1] {ECO:0000313|EMBL:CAX39930.1, ECO:0000313|Proteomes:UP000002605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841
RC {ECO:0000313|Proteomes:UP000002605};
RX PubMed=19745113; DOI=10.1101/gr.097501.109;
RA Jackson A.P., Gamble J.A., Yeomans T., Moran G.P., Saunders D., Harris D.,
RA Aslett M., Barrell J.F., Butler G., Citiulo F., Coleman D.C.,
RA de Groot P.W.J., Goodwin T.J., Quail M.A., McQuillan J., Munro C.A.,
RA Pain A., Poulter R.T., Rajandream M.A., Renauld H., Spiering M.J.,
RA Tivey A., Gow N.A.R., Barrell B., Sullivan D.J., Berriman M.;
RT "Comparative genomics of the fungal pathogens Candida dubliniensis and
RT Candida albicans.";
RL Genome Res. 19:2231-2244(2009).
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; FM992695; CAX39930.1; -; Genomic_DNA.
DR RefSeq; XP_002421929.1; XM_002421884.1.
DR AlphaFoldDB; B9WLG8; -.
DR GeneID; 8049565; -.
DR KEGG; cdu:CD36_28880; -.
DR CGD; CAL0000159559; Cd36_28880.
DR VEuPathDB; FungiDB:CD36_28880; -.
DR eggNOG; KOG0018; Eukaryota.
DR HOGENOM; CLU_001042_0_1_1; -.
DR OrthoDB; 231904at2759; -.
DR Proteomes; UP000002605; Chromosome R.
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:0007059; P:chromosome segregation; IEA:UniProt.
DR GO; GO:0007062; P:sister chromatid cohesion; IEA:InterPro.
DR CDD; cd03275; ABC_SMC1_euk; 2.
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}.
FT DOMAIN 526..644
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT COILED 174..366
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 404..460
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 765..792
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 832..936
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1024..1058
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1240 AA; 141605 MW; CE77576DE7F16DDF CRC64;
MGRLIGLELF NFKSYKGKSI IGFGSSYFTS IIGPNGAGKS NMMDAISFVL GVNSYHLRSQ
NLKDLIYRGR RNVDTDNTTL DAIEQDPTSA YVMATYEKDN GEILKLKRTI TASGNSDYQI
NGQSVTMLNY SMVLKQENIL IKARNFLVFQ GDVETIASQN PKDLTKLIET ISGSNEYISE
YEKLKEEQEK AHELTTSVFS RKRTLNSESK QYKEQMAEQR QFEEKIITKN DTIKKINLYK
LFHNEKKHNQ LKDEIKSKNE ELKLAKKELS NKEKTYKSIM ADYSSSVLNA KKQKQQTETA
QQKIDSTKRE LIPVEANQRS LSNKINFHKV KVDDLKKDIA RQKTLVSSVE RQLRDAQRMF
DDFQTKIAAA VASSTNISPE GQKEYEELRS KFLADNGSEL EEQISLLLNS KDSLNSAKSN
LENQKANAQN RIAELESIVA TDLKSKLHDV SNEINEVLDK KSSKVEARNA LIKQKDEFNH
EELKLNTRLR DVLVQLDELA SQQRESNKQK KLRENVATLK RLFPQGAIKG LVYELVRPTQ
QKYESALATL LGANFDSIIV ESSAVAYKCI DILKERRAGV ATFIPLDSIE TDIINLSHLR
SIHPSALPGV DIIEYQDKSL EPAVNYIIGN TVVVDSIDTA RNLKWQSNTR FENRIVTLQG
SVIHKSGLMT GGQQQQKSSA SLSWSKQEWT KLNELKEELN QKIFKLQEKR PKDLAINLLA
EEIGSLDDKL PVLRNQKTSI ERIIKDRESE IEFQTGLFKG FDKSIQEKMN EITKLNEKIE
KINEEMKSSK ESIFAEFCEK YGFTNGIEDY ENMHGSTLRV RAKERAQFSK TISVLQSKLD
FEKERLKETK DRRKNIESLV VDLENDLANV LTEKKKLEEI LDKAEAEYEV LQVEISKFDD
SIQSQLRTSK SIESDLDDSR QLVSALVKEI TQIEENLLKT DSERANVLRN CKIQNINLPL
IDGDLDSISI GENLESSIKE VYKIDLDYDM LEEKFKEVFT NKLESELEVT LQNTISDLEK
LTPNAKAVER LQEVETKLQD YDKEYNVARQ KERQVSERFK RVQEKRYDKF MDAFNHISGS
IDSIYKELTK SAMSPLGGSA YLTLEDEDSP FLSGIKYHAM PPMKRFRDME LLSGGEKTMA
ALALLFAIHS YQPSPFFVLD EIDAALDNAN VARIGNYIKK YAGPNFQFIV ISLKNSLFEK
SDALVGIYRE QRENSSKTVT LDLREYPDED IALSTVTATT
//