ID A0A0K3CJY7_RHOTO Unreviewed; 1205 AA.
AC A0A0K3CJY7;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Structural maintenance of chromosomes protein {ECO:0000256|PIRNR:PIRNR005719};
GN Name=FGENESH: predicted gene_9.460 {ECO:0000313|EMBL:CTR09253.1};
GN ORFNames=AAT19DRAFT_16793 {ECO:0000313|EMBL:PRQ72869.1},
GN BN2166_0051140 {ECO:0000313|EMBL:CTR09253.1};
OS Rhodotorula toruloides (Yeast) (Rhodosporidium toruloides).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=5286 {ECO:0000313|EMBL:CTR09253.1, ECO:0000313|Proteomes:UP000199069};
RN [1] {ECO:0000313|EMBL:CTR09253.1, ECO:0000313|Proteomes:UP000199069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Single colony {ECO:0000313|EMBL:CTR09253.1};
RA Cajimat M.N.B., Milazzo M.L., Fulhorst C.F.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PRQ72869.1, ECO:0000313|Proteomes:UP000239560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 0880 {ECO:0000313|EMBL:PRQ72869.1,
RC ECO:0000313|Proteomes:UP000239560};
RX PubMed=29521624;
RA Coradetti S.T., Pinel D., Geiselman G., Ito M., Mondo S., Reilly M.C.,
RA Cheng Y.F., Bauer S., Grigoriev I., Gladden J.M., Simmons B.A., Brem R.,
RA Arkin A.P., Skerker J.M.;
RT "Functional genomics of lipid metabolism in the oleaginous yeast
RT Rhodosporidium toruloides.";
RL Elife 7:0-0(2018).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|PIRNR:PIRNR005719}.
CC -!- SIMILARITY: Belongs to the SMC family. SMC2 subfamily.
CC {ECO:0000256|ARBA:ARBA00005231}.
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DR EMBL; CWKI01000009; CTR09253.1; -; Genomic_DNA.
DR EMBL; LCTV02000009; PRQ72869.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K3CJY7; -.
DR STRING; 5286.A0A0K3CJY7; -.
DR OMA; HNKIAME; -.
DR OrthoDB; 231904at2759; -.
DR Proteomes; UP000199069; Unassembled WGS sequence.
DR Proteomes; UP000239560; 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:0030261; P:chromosome condensation; IEA:UniProtKB-KW.
DR CDD; cd03273; ABC_SMC2_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; IPR027120; Smc2_ABC.
DR InterPro; IPR010935; SMC_hinge.
DR InterPro; IPR036277; SMC_hinge_sf.
DR PANTHER; PTHR43977:SF2; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN; 1.
DR PANTHER; PTHR43977; 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 DNA condensation {ECO:0000256|ARBA:ARBA00023067};
KW Mitosis {ECO:0000256|ARBA:ARBA00022776};
KW Nucleus {ECO:0000256|PIRNR:PIRNR005719};
KW Reference proteome {ECO:0000313|Proteomes:UP000199069}.
FT DOMAIN 522..640
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 342..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1167..1205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 404..473
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 677..707
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 740..932
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 342..357
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1205 AA; 134905 MW; 0C92459E43E91C3A CRC64;
MRVTELILDG FKSYPVRTSI AGWDPSFNAI TGLNGSGKSN ILDAICFVLG ITNLTTVRAA
NLLDLIYKRG QAGVTRASVT IVFDNSDKTQ SPVGFENMPE ISVTRQISVN GQSKYLICGH
RSTQQAVQNL FQSVQLNINN PNFLIMQGKI TKVLNMRPLE ILSMIEEAAG TSMFEEKKDK
AIKTMSKKEK KLDEIQSLLK EEIVPKLDRL REEKRTFLEF QKTASELERL SKLVIAWDWT
QDHLRVEKAK DAIKEGETKK KDAVESKKRM EGEIKKMEQS MKEIEKARDK ELAKGGKVQG
LEKQLNALDM EIAKLKTQAE GKEREIKEEE ARIKELEKAQ KDLTAQRKAR ESSSKENAEA
FAARQAELEA ASKSLTQSED LLQTIEYGKG LSKDAKSSGY DGQLAAAKEL AGRLETEAQL
AKHRIDSLQK ELKEKEPKAK KAAAESKGLV ANVENARKEK EALEQRLKAS GYDEAEEVRL
EGERDQRAQT VEQLRQRREL KRREIVRTDF RADDPYPGFD RASVYGTIAS LVELPEANAA
AATALEYAAG GALYNVAVRD DATVAAFVKA RTIKTRTNLL PVNSLQVYVA DKSRVAAARK
HGAELALNLI NFDERARRAM ESVFGNVLIA PNKTIAKRCT DDPAVRMRCV TYEGDIYDTT
PELRGGNSTS ERVLIKVQEL RKIEQELEMH RKALEELEVK LQHSKGAVDL KKALDQKAHA
LSLLEKSMQN SNATRVIGEV DTLRATIADL QEKIEESKSK QKDAQADVKR IEREMSELSK
DKGSKVKQIK ADIAKQKTQV AKLEEAVESL RSEVLTDELE LDQMKKEIAS AGVELAEARS
QINKIRQSLS KGQGVMEEKL AELQEVQCVI AEETKKLKGY NDELDSLKEA IKGRKGDIVE
LELQVTQVEK EVEKAKKDAK DAADKVAKRE KEFDWIADEC QTFGKPNSPY NFNGTDMRNV
KEKCRQLEET HRTMKRKVNP KVLSMIDSVE KKEKDLLDMY KQVMKDKTKI EETVAKLDEH
KRDTLEKTWT KVDSEFGNIF AELLPGNFCK LQALEGKEIT QGLEVKVRLG SVWKASLTEL
SGGQRSLIAL SLIMSLLRFK PAPMYILDEV DAALDMSHTE NIGRLFRTRF KGSQFIVVSL
KDGLFSNANV LFRARFRDGT SVVERTSQRT ASGLYDKENA GPRAGGAGKA GKSRTGGAGR
VEVAA
//
