ID G0V9G8_NAUCC Unreviewed; 1409 AA.
AC G0V9G8;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Structural maintenance of chromosomes protein {ECO:0000256|PIRNR:PIRNR005719};
GN Name=NCAS0B05000 {ECO:0000313|EMBL:CCC68584.1};
GN OrderedLocusNames=NCAS_0B05000 {ECO:0000313|EMBL:CCC68584.1};
OS Naumovozyma castellii (strain ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC
OS 1992 / NRRL Y-12630) (Yeast) (Saccharomyces castellii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Naumovozyma.
OX NCBI_TaxID=1064592 {ECO:0000313|EMBL:CCC68584.1, ECO:0000313|Proteomes:UP000001640};
RN [1] {ECO:0000313|EMBL:CCC68584.1, ECO:0000313|Proteomes:UP000001640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC 1992 / NRRL Y-12630
RC {ECO:0000313|Proteomes:UP000001640};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Type strain:CBS 4309;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Genome sequence of Naumovozyma castellii.";
RL Submitted (AUG-2011) 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; HE576753; CCC68584.1; -; Genomic_DNA.
DR RefSeq; XP_003674956.1; XM_003674908.1.
DR STRING; 1064592.G0V9G8; -.
DR GeneID; 11526057; -.
DR KEGG; ncs:NCAS_0B05000; -.
DR eggNOG; KOG0996; Eukaryota.
DR HOGENOM; CLU_001042_4_1_1; -.
DR InParanoid; G0V9G8; -.
DR OMA; CPALDNM; -.
DR OrthoDB; 231904at2759; -.
DR Proteomes; UP000001640; Chromosome 2.
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; 1.10.287.1490; -; 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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000001640}.
FT DOMAIN 681..794
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 1..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 399..538
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 637..664
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 846..953
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1039..1115
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 21..110
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1409 AA; 161097 MW; DC5B22481544CEE9 CRC64;
MSLPNTKRQK VTEPESKTPE QGTEDQQANA SLRSPLQRPE HQQSISPINN SKSHTPRKLI
LGQNDNRYAF SQPSVSSSSF QVPTLQPPDS SSSRGRKDIK SYSQSPPRSP GRSPKRRLEL
IQLSPVKNNR IKLRELYDAH NSQSKKERLF INKLTLNNFK SYAGQQVVGP FHTSFSAVVG
PNGSGKSNVI DSMLFVFGFR ANKMRQDRLS DLIHKSEKFP DLTSCSVDVE FLYAIDEHDG
DTKISETKPK LVISRKAFKN NSSKYYINGK ESNYTDVTKL LKEEGIDLDH KRFLILQGEV
ENIAQMKPKA EKESDDGLLE YLEDIIGTSK YKQLIEKDLI EIESLNEICI EKENRFEIVD
REKNSLESGK NLALEFLEKE KQLTLSKSKL LQYNLWQNNS KLTNTLQKIS ALNEEYNVEK
SKNQTLQNEI NRTKQLLNES QSKIKVLEGE EKQQLKSKRI LEGEHVSLDE KLKNLTQKKA
KTEKIIATTE KTISSLTSEI QELEKSQKEY SDELETLNQQ LQSERESLEA MKLKLKEKTS
GISEEILIHE HDLEPWNIKV QEKKTEIQLV ESQISLLQEG QVKLKNDIKV LSQEVSNQTA
LKIKREEDLV NLKKQQSSIT KEISNGETEC NDGRSKLKEM KNVLNMQRQR ASEARLALAN
VQNRGKVLTA LYKLQKSGRI VGFHGRLGDL GTIDNTYDVA VSTACPRLDD IVVETVECGQ
QCIEYLRKNK LGYARFILLD KLRSFNTNTI QTPKNVPRLF DLIKPKDSKF VPAFYSVLRD
TLVAKDLKQA NRVAYGQRRY RVVTLDGKLI DVSGTMSGGG NHVSKGLMML QRKGQNYFDD
YNPEDVEQIE KDLSDKEKNF ELANNAFYEM ENELQKLNNR KPEIELEISK IIMEIDTYSA
EIKSKERQLQ EKTNIDNSEL QDNEELKVAI ENLQKLKEEH LALQDKTKAK KKKIASLKEK
IMKIGGIELQ VQNSKVTSIV QRIDILTAKQ KKDRTSKKKS DTELEKAKKT LLTSKNDITL
ITDDIKEISE RIDKISSSLN NIDKSIEEFQ AHKETLKDEC DELKDKVVDL EENINEFKSF
EIEVNNKLEK LNGLLNHIKN QIKTLEDSLS KLTLRKMHQV LMALDEESEA KAPNNGTLSD
EQIHDQTGHE LTNTAVQDDD SMDIDNGAEV ISNGLPILSD DELSALDITL VETEVSDLEK
YIESTDANIE VLEEYVKRLT EFKTRKLDLN DAVDKRETVR KQLEELKKTR YEEFMHGFGI
ISMTLKEMYQ MITMGGNAEL ELVDSLDPFS EGVTFSVMPP KKSWRNISNL SGGEKTLSSL
ALVFALHKYK PTPLYVMDEI DAALDFRNVS IVANYIKERT KNAQFIVISL RNNMFELAQQ
LVGIYKCENR THSATIKNRE ILNSDINRE
//
