ID   G0WH32_NAUDC            Unreviewed;      1108 AA.
AC   G0WH32;
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=RecF/RecN/SMC N-terminal domain-containing protein {ECO:0000259|Pfam:PF02463};
GN   Name=NDAI0J02180 {ECO:0000313|EMBL:CCD27110.1};
GN   OrderedLocusNames=NDAI_0J02180 {ECO:0000313|EMBL:CCD27110.1};
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:CCD27110.1, ECO:0000313|Proteomes:UP000000689};
RN   [1] {ECO:0000313|EMBL:CCD27110.1, 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: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the SMC family. SMC6 subfamily.
CC       {ECO:0000256|ARBA:ARBA00006793}.
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DR   EMBL; HE580276; CCD27110.1; -; Genomic_DNA.
DR   RefSeq; XP_003672353.1; XM_003672305.1.
DR   AlphaFoldDB; G0WH32; -.
DR   STRING; 1071378.G0WH32; -.
DR   GeneID; 11494448; -.
DR   KEGG; ndi:NDAI_0J02180; -.
DR   eggNOG; KOG0250; Eukaryota.
DR   HOGENOM; CLU_009063_0_0_1; -.
DR   OMA; FMCHRSL; -.
DR   OrthoDB; 78166at2759; -.
DR   Proteomes; UP000000689; Chromosome 10.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; 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; 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; IPR036277; SMC_hinge_sf.
DR   PANTHER; PTHR19306; STRUCTURAL MAINTENANCE OF CHROMOSOMES 5,6 SMC5, SMC6; 1.
DR   PANTHER; PTHR19306:SF6; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN 6; 1.
DR   Pfam; PF02463; SMC_N; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   SUPFAM; SSF75553; Smc hinge domain; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000689}.
FT   DOMAIN          75..1076
FT                   /note="RecF/RecN/SMC N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02463"
FT   REGION          23..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          47..68
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          271..337
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          373..489
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          696..730
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          768..858
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1108 AA;  126587 MW;  4FDA1D96097F826A CRC64;
     MTDMVSPSKR SVEEVDNDLL ALAAEQNHVH NEQQKKKRRR QYAPMTQYNT NSAATQSASV
     NSDSNSRKDD LPCGYIKKVI LRNFMCHEHF ELDLGPRLNF IVGNNGSGKS AVLTAITIGL
     GAKASDTNRG NAMKDLIREG CYSAKVTLVL DNSHAGPYNH GTFGDEIIIE RTLRMESAPT
     YSLRTENGKE VSNKKKDVQT VVDFFCVPVS NPMCFLSQDA ARSFLTASTS HDKYNHFMKG
     TLLQEIRDSL NNAQDIQADV VQNMAFHYDN IAILKNEYEE SKKLLRELNQ TSNLAQRKRL
     LQGKSLWIDV DKNHEIYSKL ENEVTLNEKK ITETMEKIKM RKAKIDRYTA DQKSVEEETA
     SKVVLVGEKD EAHQAVRDQL RAVRSEFDKE KENQKEAENG ISECKRRIET LNRTIEHLEQ
     ELEKQMGGDR GKMKEELAQL QAENEQLRDK VENISNELLE MQDKERTIAA ERQQDLRTIE
     HNIQSKRNEL QKIAQGNNSF LTNFDQNMDR LLLQIKQRSG EFSSIPLGPL GSFVSVKAGF
     EKWSRSIQSA ISGTLGSFVV SNQKDASILR NMIKNCGIKA NIPIITYKLK HFDYSQGKAQ
     TNYPTISDAL EYSNPSVEFV FVDHNRIEKV ILIEDKDEAR SILKSKPHNV SMALSFRDQS
     SGFQLIGGSR LDTVYYQPKM KLKVGSSSDD GASYIKDLIT QETEELQNTR DRYERQINQI
     RSEYSGMEKI SREQKAQMQR NRSRINKLKI NVGKAVDTGI LTTKINERKS QEQAIIGYEA
     AINELEIKIR EIAATAEPLK EHYDKTKNEF NELQATLGQL RDDYNTYSAK IEACKDDIKH
     YEDKKLSYEK TIEHLNSNII ATRDGIQKIT DSANELCTRE QLEGMDLPED QQAIKNELGR
     ISQQIQRAEK NIGFSHDKVV DLFEKSRDKY KDAEKKFGSV DRALRQLQHS IEVRSQNYTN
     IQNNTCLEAD LDFRASLKVR KFTGNLTFQI AERKLDMLIL TANDEKARNV DTLSGGEKSF
     SQLALLLATW KPMRSRIIAL DEFDVFMDQV NRRIGTTLVV KKLKDLLRTQ TIIITPQDIG
     KIANVDSEGV NIHRMRDPQR QNNSNFYV
//