ID G0VJP4_NAUCC Unreviewed; 1095 AA.
AC G0VJP4;
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=NCAS0I00570 {ECO:0000313|EMBL:CCC71725.1};
GN OrderedLocusNames=NCAS_0I00570 {ECO:0000313|EMBL:CCC71725.1};
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:CCC71725.1, ECO:0000313|Proteomes:UP000001640};
RN [1] {ECO:0000313|EMBL:CCC71725.1, 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 -!- SIMILARITY: Belongs to the SMC family. SMC5 subfamily.
CC {ECO:0000256|ARBA:ARBA00010171}.
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DR EMBL; HE576760; CCC71725.1; -; Genomic_DNA.
DR RefSeq; XP_003678070.1; XM_003678022.1.
DR AlphaFoldDB; G0VJP4; -.
DR STRING; 1064592.G0VJP4; -.
DR GeneID; 11525456; -.
DR KEGG; ncs:NCAS_0I00570; -.
DR eggNOG; KOG0979; Eukaryota.
DR HOGENOM; CLU_004969_2_0_1; -.
DR InParanoid; G0VJP4; -.
DR OMA; RFWTSQP; -.
DR OrthoDB; 232016at2759; -.
DR Proteomes; UP000001640; Chromosome 9.
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; 1.20.5.170; -; 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:UP000001640}.
FT DOMAIN 38..1051
FT /note="RecF/RecN/SMC N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02463"
FT COILED 226..341
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 659..745
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 893..920
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1095 AA; 126610 MW; A5ED2A62468A5041 CRC64;
MATASIMDLS RFASSSGPQT KKLKLAPRTY DQFQPGSIVK IKLQNFVTYR LTEFNLSPSL
NMIIGPNGSG KSTFVCAVCL GLAGKPEFIG RAKRVDDFIK NGEDTSRIEI FLKNYEDPTE
LQSSLNLKFN LAGKDLLKVT RLIQRDGNKC KSDYFINDKP VTENVIKNLV KFLNIQLDNL
CQFLSQERVE EFARLKSDKL LVETVRSIDA QLLQILDDLK SSQNDETTLE NEVDIKQKRF
NELETDRNKL EASVRSLKEF ETMKEDIEIH KKLLPYVKVK DHKENLQRLK GDYELAKQNL
RALLKDKKPF VDTKLDMETK VDEFAENKRS KEEELKLTRN KLMNVFNDLK VVRENIIKKQ
TQTAYYKTRT KKLHEEMAKT KETLEANQTK LTQIALPDAT LLEEIEKKRS ALLDEDSNVR
NKMGDIDNKA NSINHEIRQL TRQAENKVKS LTGTDKIGIL DLDRSFIEIK RAVQYIRTIP
AMKGKVLEPP LMTVSAKHPQ FAKYLANSVD FNTSIALTMI DSNAYEQFND QILKQFRINL
REISNRESQQ PMPREQLAQY GFEGYLSDFV TGDTNVINML RQINNIHTIP VSRKELTPRQ
LERLLQPGPN GKVLFRRALH GDRVFDIRQS SYTGQIYSVD SSLKPTRYYQ SSIISDEQKN
RIEEDVRKLK SQVEERKAKL ENLSNERGEF KHQLSSIARE NERISQKGHE LNEVRKQYSM
VKSTIESLES KFQELNNDAR KDVSQKIKAV EASISKELKI QTDLLKQMVG LMGNVNSCQK
ELFKADLEYL EAKNNDVSMN DVIGFFNDRE DELKKEFETK RETVRRLRDT EEYQQWIRQI
RSYDDSTREK LNDYAEGYEK DGTFNVTHIT EIIDKLESEI SMINHDASSI TILKQVEKEI
SQLEETLPKQ QVELKSIKEK IKQGRSTLEP KLDEIIEKIS TRFSRLFKNV GSAGAVNLVK
PHQFSEWKIE IMVKFRDNAT LKRLDSHTQS GGERAVSTVL YMIALQEFTS APFRVVDEIN
QGMDARNERI VHKAMVENAC AENTSQYFLI TPKLLTDLHY HEKMRIHCVM AGSWIPNPSE
EPEMVHFGET SNYVF
//
