ID   A0A109FN32_9BASI        Unreviewed;      1245 AA.
AC   A0A109FN32;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=Structural maintenance of chromosomes protein {ECO:0000256|PIRNR:PIRNR005719};
GN   ORFNames=RHOSPDRAFT_28005 {ECO:0000313|EMBL:KWU47379.1};
OS   Rhodotorula sp. JG-1b.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX   NCBI_TaxID=1305733 {ECO:0000313|EMBL:KWU47379.1, ECO:0000313|Proteomes:UP000062823};
RN   [1] {ECO:0000313|EMBL:KWU47379.1, ECO:0000313|Proteomes:UP000062823}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JG-1b {ECO:0000313|EMBL:KWU47379.1,
RC   ECO:0000313|Proteomes:UP000062823};
RG   DOE Joint Genome Institute;
RA   Goordial J., Raymond-Bouchard I., Riley R., Ronholm J., Shapiro N.,
RA   Woyke T., Grigoriev I.V., Labutti K.M., Greer C., Whyte L., Bakermans C.;
RT   "Draft genome of eurypsychrophile Rhodotorula sp. JG1b isolated from
RT   permafrost in the hyper-arid Upper Elevation McMurdo Dry Valleys,
RT   Antarctica.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR005719}.
CC   -!- SIMILARITY: Belongs to the SMC family. SMC3 subfamily.
CC       {ECO:0000256|ARBA:ARBA00005917}.
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DR   EMBL; KQ954464; KWU47379.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A109FN32; -.
DR   STRING; 1305733.A0A109FN32; -.
DR   OrthoDB; 231904at2759; -.
DR   Proteomes; UP000062823; 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   CDD; cd03272; ABC_SMC3_euk; 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; IPR041741; SMC3_ABC_euk.
DR   InterPro; IPR010935; SMC_hinge.
DR   InterPro; IPR036277; SMC_hinge_sf.
DR   PANTHER; PTHR43977; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN 3; 1.
DR   PANTHER; PTHR43977:SF1; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN 3; 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|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR005719};
KW   Reference proteome {ECO:0000313|Proteomes:UP000062823}.
FT   DOMAIN          526..648
FT                   /note="SMC hinge"
FT                   /evidence="ECO:0000259|SMART:SM00968"
FT   REGION          341..366
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          418..437
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          787..810
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          877..897
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          918..956
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          189..223
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1245 AA;  142395 MW;  74108BB59B863A5C CRC64;
     MHIKILQIQG FKSYRDETVV DPFSAGLNLL VGRNGSGKSN FFSAIRFVLS DAYTSLSREE
     RQALLHDSGG AGGGATMSAF VEIEFDNADG RFPTNKPSLL LRRTIGLKKD EYQLDRKSTS
     KGEVMSLLES AGFSRSNPYY IVPQGRITHL TNQKDADRLL LLKEVAGTKV YEERRAESTK
     IMDETNAKRD KIKDLLEYIQ ARLDELEEEK EELKQYQTHD RARRSLEYCI YQRELKDVGD
     MLDQIEEGRN KDIDEANSRR EEFNQREKEL STIRRHLSTL REELAALQTE HDELSEERRE
     VTKARTQVDC LVRDAEDASR SLAARRADVV AELEKVEASI ADKETELDDS ARPDYEAKKQ
     EQEKAHAELE ELQVTLGGLY ARQGRRGQFR SKQERDQHLQ GLIVRQEEAL EARRSREEAL
     VQERDETEKE RQEVEARRVE LRKELDGQKG KLKEYLDELK RLNEENAEQS EHRKELWKKS
     SKLDAQTQHA METLKAAQRT VSTTMDRDTA NGLRAAREIA EELALDGYFG PLYELFEVDD
     RYKTAVEVTA GTSLFQIVTD TDDTATKILD RMVRDKSGRV TFMPLNRLRV YDVEYPKTNE
     AIPMRVSNGV FPGSINKLKF SEQFRPAFKQ VFGRTVVCQT LEIAGAYTRS HGLNAITLDG
     DKYDRKGALT GGYHDVRRSR LDAVKALKAA QRREGELSAE RAEVRQAIAQ TDQEVTTRVG
     QTKVIEGRLR RLQDEQQPLV DAILRAQEDE DRLKSKLARL DAQLTSHRAD VRSLEKECEM
     WRKEMESAFQ DSEGLSDEEE EEMKRLSAEA DQRKKALVEL SKAASDVSAE TEPNLQSARQ
     WLISRPVPEQ LERAKDLLEI ELNENLRRRR EELRARLDTL DTSGGQDDQN ATGGEDLEAR
     KKELKKLDKQ IQSLNRRLDE VEQETERVNK EIAESEKERE TRESQQTADQ RNIDKQGKSV
     ERYLAKRQLL LHRKDECNQK IRDLGVLPEE AFAETTAATE KLLKKLRKVN EALKAFAHVN
     KKAFEQYSSF TKQRDELIAR QEELDESQKS ILELIDVLDA RKDEAIERTF KQVAKNFAEV
     FEKLVPSGRG RLIMLKRQQE KGEDVMDVDE PEEEGSVENY NGVAIRVSFK SKSNEGLRLQ
     QLSGGQKALV ALALIFSIQK CDPAPFYLFD EIDANLDADR RTAVAAMISE LSEEAQYICT
     TFRAELIPHA DAFFGVVFNQ AKISNVKTCE SGTLGYGSAK SSAYD
//