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Database: UniProt
Entry: G0W5B0_NAUDC
LinkDB: G0W5B0_NAUDC
Original site: G0W5B0_NAUDC 
ID   G0W5B0_NAUDC            Unreviewed;      1119 AA.
AC   G0W5B0;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   RecName: Full=Structural maintenance of chromosomes protein 5 {ECO:0000256|ARBA:ARBA00018687};
GN   Name=NDAI0A08450 {ECO:0000313|EMBL:CCD22998.1};
GN   OrderedLocusNames=NDAI_0A08450 {ECO:0000313|EMBL:CCD22998.1};
OS   Naumovozyma dairenensis (strain ATCC 10597 / BCRC 20456 / CBS 421 / NBRC
OS   0211 / NRRL Y-12639) (Saccharomyces dairenensis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Naumovozyma.
OX   NCBI_TaxID=1071378 {ECO:0000313|EMBL:CCD22998.1, ECO:0000313|Proteomes:UP000000689};
RN   [1] {ECO:0000313|EMBL:CCD22998.1, ECO:0000313|Proteomes:UP000000689}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10597 / BCRC 20456 / CBS 421 / NBRC 0211 / NRRL Y-12639
RC   {ECO:0000313|Proteomes:UP000000689};
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).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the SMC family. SMC5 subfamily.
CC       {ECO:0000256|ARBA:ARBA00010171}.
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DR   EMBL; HE580267; CCD22998.1; -; Genomic_DNA.
DR   RefSeq; XP_003668241.1; XM_003668193.1.
DR   AlphaFoldDB; G0W5B0; -.
DR   STRING; 1071378.G0W5B0; -.
DR   GeneID; 11493636; -.
DR   KEGG; ndi:NDAI_0A08450; -.
DR   eggNOG; KOG0979; Eukaryota.
DR   HOGENOM; CLU_004969_2_0_1; -.
DR   OMA; RFWTSQP; -.
DR   OrthoDB; 232016at2759; -.
DR   Proteomes; UP000000689; Chromosome 1.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0030915; C:Smc5-Smc6 complex; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0007059; P:chromosome segregation; IEA:UniProt.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:InterPro.
DR   Gene3D; 1.20.5.110; -; 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; IPR027131; SMC5.
DR   PANTHER; PTHR45916; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN 5; 1.
DR   PANTHER; PTHR45916:SF1; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN 5; 1.
DR   Pfam; PF02463; SMC_N; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   DNA recombination {ECO:0000256|ARBA:ARBA00023172};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000689}.
FT   DOMAIN          52..1075
FT                   /note="RecF/RecN/SMC N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02463"
FT   COILED          235..262
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          302..329
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          697..769
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1119 AA;  130227 MW;  CE3BCDC787CE403E CRC64;
     MATTIMNLDR YVRPRNDNDN DDDDGIDYNT SRKSKKLKLS TVNYDKFQPA SIVKIKLENF
     VTYKLTEFNL SPSLNMIIGP NGSGKSTFVC AACLGLAGKP EYIGRSKRVD DYIKNGEDRS
     KIEIFLKNVE SMDKLKNFNN NNNKNNNNGA QVDLKCGQLD LIKFTRIIHR DKKKSDYYIN
     DKPVSELTVK NLVKALSIQL DNLCQFLSQE RVEEFARLKS DKLLVETVRS IDPNLLDILE
     ELKVLQNEEQ TVEDELEIKQ KRYTELCNER TKLEASVQSL KEFENKKLEI EYHNKLLPYV
     MIKDHREKLQ KFKGDYEIAK RNLRDLMKDK KPFVKTKLEI EENLNEIAED KRTNETALES
     SKDALSKTVE NLNAIRESIV KKQSQISYYQ SRTKKLQQQI LSTKSELERQ QSLFDSMTPP
     EISLFDEFDK KREELINEDL KINDQLIAIK NKGSQNNHEI GMLTKKIENK KKSFTGTDKI
     GVLMRNSRPT DIYNAVLYIR EIPEMKGKVL EPPLISVSAK NPQFASYLDQ CIDRNTSQAL
     TLIDSDSYER FSDDILKRFR VNLRELEDID LTPPVPRNQL QEFGFEGYLS DFLTGDKNVI
     KMLCQINKLH TIPVSRRELT PSQLERLLLP DQNGRIMFSK IIHGRRQLTI RQSNYTKQTS
     SIDSNIYSNT RNYQSSVMSD EQKDRINKEI DEFKTLIKER QSKFETLSNE RSELEHQLRQ
     IQNETAKVTQ KGQELNQQRE RYTMTQTTIQ TLETKLDELK RDARKDVSQH IHVVEKKIAQ
     ELEQQTKLLA DMVSMLKKVD IDQKELIRLD IAYFEAKNKD ITMKDVVGFF DDKERELKDE
     YESKRRSFTE LKETSEYHTW LRQIKSYDEP TRDKLNEYAE KYQNQDTFNV EYITDIIERL
     ESEISMINHD ASSITILKKV ETEINELEQT LPTMTSGLAT TKEKIKQNRL ELEPGLDSMI
     SKISKQFALL FNNVGSAGAV NLEKPHRFAD WKVEIMVKFR DNATLKKLDS HTQSGGERAV
     STVLYMIALQ EFTAAPFRVV DEINQGMDSR NERIVHKAMV ENACAENTSQ YFLITPKLLT
     DLHYHEKMRI HCVMAGSWIP NPSDDPEMVH FGETSNYIL
//
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