ID B3LQ37_YEAS1 Unreviewed; 1230 AA.
AC B3LQ37;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 24-JAN-2024, entry version 58.
DE RecName: Full=Structural maintenance of chromosomes protein {ECO:0000256|PIRNR:PIRNR005719};
GN ORFNames=SCRG_03596 {ECO:0000313|EMBL:EDV12690.1};
OS Saccharomyces cerevisiae (strain RM11-1a) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=285006 {ECO:0000313|EMBL:EDV12690.1, ECO:0000313|Proteomes:UP000008335};
RN [1] {ECO:0000313|Proteomes:UP000008335}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RM11-1a {ECO:0000313|Proteomes:UP000008335};
RG The Broad Institute Genome Sequencing Platform;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Cuomo C.,
RA Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M.,
RA Mauceli E.W., Brockman W., MacCallum I.A., Rounsley S., Young S.K.,
RA LaButti K., Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA O'Leary S., Kodira C.D., Zeng Q., Yandava C., Alvarado L., Pratt S.,
RA Kruglyak L.;
RT "Annotation of the Saccharomyces cerevisiae RM11-1a genome.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR005719}.
CC -!- SIMILARITY: Belongs to the SMC family. SMC3 subfamily.
CC {ECO:0000256|ARBA:ARBA00005917}.
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DR EMBL; CH408050; EDV12690.1; -; Genomic_DNA.
DR AlphaFoldDB; B3LQ37; -.
DR HOGENOM; CLU_001042_5_0_1; -.
DR Proteomes; UP000008335; Unassembled WGS sequence.
DR GO; GO:0005694; C:chromosome; 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:0051276; P:chromosome organization; IEA:InterPro.
DR GO; GO:0007059; P:chromosome segregation; IEA:UniProt.
DR CDD; cd03272; ABC_SMC3_euk; 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; IPR041741; SMC3_ABC_euk.
DR InterPro; IPR010935; SMC_hinge.
DR InterPro; IPR036277; SMC_hinge_sf.
DR PANTHER; PTHR43977; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN 3; 1.
DR PANTHER; PTHR43977:SF1; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN 3; 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 534..651
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 1078..1097
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 172..227
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 403..448
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 691..725
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 768..818
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 863..932
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 974..1036
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1230 AA; 141278 MW; 38D3E4C983CE26A9 CRC64;
MYIKRVIIKG FKTYRNETII DNFSPHQNVI IGSNGSGKSN FFAAIRFVLS DDYSNLKREE
RQGLIHQGSG GSVMSASVEI VFHDPDHSMI LPSGVLSRGD DEVTIRRTVG LKKDDYQLND
RNVTKGDIVR MLETAGFSMN NPYNIVPQGK IVALTNAKDK ERLQLLEDVV GAKSFEVKLK
ASLKKMEETE QKKIQINKEM GELNSKLSEM EQERKELEKY NELERNRKIY QFTLYDRELN
EVINQMERLD GDYNNTVYSS EQYIQELDKR EDMIDQVSKK LSSIEASLKI KNATDLQQAK
LRESEISQKL TNVNVKIKDV QQQIESNGEQ RNLDSATLKE IKSIIEQRKQ KLSKILPRYQ
ELTKEEAMYK LQLASLQQKQ RDLILKKGEY ARFKSKDERD TWIHSEIEEL KSSIQNLNEL
ESQLQMDRTS LRKQYSAIDE EIEELIDSIN GPDTKGQLED FDSELIHLKQ KLSESLDTRK
ELWRKEQKLQ TVLETLLSDV NQNQRNVNET MSRSLANGII NVKEITEKLK ISPESVFGTL
GELIKVNDKY KTCAEVIGGN SLFHIVVDTE ETATLIMNEL YRMKGGRVTF IPLNRLSLDS
DVKFPSNTTT QIQFTPLIKK IKYEPRFEKA VKHVFGKTIV VKDLGQGLKL AKKHKLNAIT
LDGDRADKRG VLTGGYLDQH KRTRLESLKN LNESRSQHKK ILEELDFVRN ELNDIDTKID
QVNGNIRKVS NDRESVLTNI EIYRTSLNTK KNEKLILEES LNAIILKLEK LNTNRTFAQE
KLNTFENDLL QEFDSELSKE EKERLESLTK EISAAHNKLN ITSDALEGIT TTIDSLNAEL
ESKLIPQEND LESKMSEVGD AFIFGLQDEL KELQLEKESV EKQHENAVLE LGTVQREIES
LIAEETNNKK LLEKANNQQR LLLKKLDNFQ KSVEKTMIKK TTLVTRREEL QQRIREIGLL
PEDALVNDFS DITSDQLLQR LNDMNTEISG LKNVNKRAFE NFKKFNERRK DLAERASELD
ESKDSIQDLI VKLKQQKVNA VDSTFQKVSE NFEAVFERLV PRGTAKLIIH RKNDNANDHD
ESIDVDMDAE SNESQNGKDS EIMYTGVSIS VSFNSKQNEQ LHVEQLSGGQ KTVCAIALIL
AIQMVDPASF YLFDEIDAAL DKQYRTAVAT LLKELSKNAQ FICTTFRTDM LQVADKFFRV
KYENKISTVI EVNREEAIGF IRGSNKFAEV
//