ID B3LT54_YEAS1 Unreviewed; 1418 AA.
AC B3LT54;
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_05070 {ECO:0000313|EMBL:EDV09389.1};
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:EDV09389.1, 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|ARBA:ARBA00004123,
CC ECO:0000256|PIRNR:PIRNR005719}.
CC -!- SIMILARITY: Belongs to the SMC family. SMC4 subfamily.
CC {ECO:0000256|ARBA:ARBA00006005}.
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DR EMBL; CH408054; EDV09389.1; -; Genomic_DNA.
DR HOGENOM; CLU_001042_4_1_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 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; IPR010935; SMC_hinge.
DR InterPro; IPR036277; SMC_hinge_sf.
DR PANTHER; PTHR18937:SF172; 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|PIRNR:PIRNR005719}.
FT DOMAIN 686..799
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 1..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1156..1188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 404..525
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 565..669
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 865..965
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1016..1095
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1225..1262
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..19
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..96
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1166..1188
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1418 AA; 162177 MW; D452DB31C8DD7264 CRC64;
MSDSPLSKRQ KRKAAQEPEL SLDQGDAEEE SQVENRVNLS ENTPEPDLPA LEASYSKSYT
PRKLVLSSGE NRYAFSQPTN STTTSLHVPN LQPPKTSSRG RDHKSYSQSP PRSPGRSPTR
RLELLQLSPV KNSRVELQKI YDSHQSSSKQ QSRLFINELV LENFKSYAGK QVVGPFHTSF
SAVVGPNGSG KSNVIDSMLF VFGFRANKMR QDRLSDLIHK SEAFPSLQSC SVAVHFQYVI
DESSGTSRID EEKPGLIITR KAFKNNSSKY YINEKESSYT EVTKLLKNEG IDLDHKRFLI
LQGEVENIAQ MKPKAEKESD DGLLEYLEDI IGTANYKPLI EERMGQIENL NEVCLEKENR
FEIVDREKNS LESGKETALE FLEKEKQLTL LRSKLFQFKL LQSNSKLAST LEKISSSNKD
LEDERMKFQE SLKKVDEIKA QRKEIKDRIS SCSSKEKTLV LERRELEGTR VSLEERTKNL
VSKMEKAEKT LKSTKHSISE AENMLEELRG QQTEHETEIK DLTQLLEKER SILDDIKLSL
KDKTKDISAE IIRHEKELEP WDLQLQEKES QIQLAESELS LLEETQAKLK KNVETLEEKI
LAKKTHKQEL QDLILDLKKK LNSLKDERSQ GEKNFTSAHL KLKEMQKVLN AHRQRAMEAR
SSLSKAQNKS KVLTALSRLQ KSGRINGFHG RLGDLGVIDD SFDIAISTAC PRLDDVVVDT
VECAQHCIDY LRKNKLGYAR FILLDRLRQF NLQPISTPEN VPRLFDLVKP KNPKFSNAFY
SVLRDTLVAQ NLKQANNVAY GKKRFRVVTV DGKLIDISGT MSGGGNHVAK GLMKLGTNQS
DKVDDYTPEE VDKIERELSE RENNFRVASD TVHEMEEELK KLRDHEPDLE SQISKAEMEA
DSLASELTLA EQQVKEAEMA YVKAVSDKAQ LNVVMKNLER LRGEYNDLQS ETKTKKEKIK
GLQDEIMKIG GIKLQMQNSK VESVCQKLDI LVAKLKKVKS ASKKSGGDVV KFQKLLQNSE
RDVELSSNEL KVIEEQLKHT KLALAENDTN MTETLNLKVE LKEQSEQLKE QMEDMEESIN
EFKSIEIEMK NKLEKLNSLL TYIKSEITQQ EKGLNELSIR DVTHTLGMLD DNKMDSVKED
VKNNQELDQE YRSCETQDES EIKDDETSCD NYHPMNVDET SDEVSRGIPR LSEDELRELD
VELIESKINE LSYYVEETNV DIGVLEEYAR RLAEFKRRKL DLNNAVQKRD EVKEQLGILK
KKRFDEFMAG FNIISMTLKE MYQMITMGGN AELELVDSLD PFSEGVTFSV MPPKKSWRNI
TNLSGGEKTL SSLALVFALH KYKPTPLYVM DEIDAALDFR NVSIVANYIK ERTKNAQFIV
ISLRNNMFEL AQQLVGVYKR DNRTKSTTIK NIDILNRT
//
