ID A0A0J0XFQ7_9TREE Unreviewed; 1211 AA.
AC A0A0J0XFQ7;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=Structural maintenance of chromosomes protein {ECO:0000256|PIRNR:PIRNR005719};
GN ORFNames=CC85DRAFT_264703 {ECO:0000313|EMBL:KLT39903.1};
OS Cutaneotrichosporon oleaginosum.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Trichosporonales; Trichosporonaceae; Cutaneotrichosporon.
OX NCBI_TaxID=879819 {ECO:0000313|EMBL:KLT39903.1, ECO:0000313|Proteomes:UP000053611};
RN [1] {ECO:0000313|EMBL:KLT39903.1, ECO:0000313|Proteomes:UP000053611}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBC0246 {ECO:0000313|EMBL:KLT39903.1,
RC ECO:0000313|Proteomes:UP000053611};
RG DOE Joint Genome Institute;
RA Kourist R., Kracht O., Bracharz F., Lipzen A., Nolan M., Ohm R.,
RA Grigoriev I., Sun S., Heitman J., Bruck T., Nowrousian M.;
RT "Genomics and transcriptomics of the oil-accumulating basidiomycete yeast
RT T. oleaginosus allow insights into substrate utilization and the diverse
RT evolutionary trajectories of mating systems in fungi.";
RL Submitted (MAR-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; KQ087246; KLT39903.1; -; Genomic_DNA.
DR RefSeq; XP_018276394.1; XM_018420966.1.
DR AlphaFoldDB; A0A0J0XFQ7; -.
DR STRING; 879819.A0A0J0XFQ7; -.
DR GeneID; 28981569; -.
DR OrthoDB; 231904at2759; -.
DR Proteomes; UP000053611; 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:UP000053611}.
FT DOMAIN 523..635
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 411..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 187..281
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 324..369
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 449..504
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 695..917
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 992..1033
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1211 AA; 138383 MW; EE6A3033E4CC99F2 CRC64;
MHIKTITIQG FKSYRDQVAI DPFSPRHNVV VGRNGSGKSN FFAAIRFVLS DAYTTLSRDE
RQRLLHEGTS TTTTLSAYVE IVFDNADGRF PTGQPELHLR RTIGLKKDEY SLDRKSVTKA
EVMNLLESAG FSRSNPYYIV PQGRITHLTN ISEKDRLNLL KEVAGTKVYE QKRAESTRIM
EDTDSKRDKI NDLLANIETR LAELETEKNE LKEFQSLDRD RRCLEYSLQQ RELDDITAAL
DQLEEDRSNG HHEINEQEKA LYELEARIKK MEDELTRSKH SHSTLSIALQ QYEFEMEDLV
RTKTEVECIV ADFAQASESN ETRRLETIEQ LESLERRVKR TTDRLAELNA ALEERIAEER
AAKDLLDTTQ SRLQVLYAKQ GRTRQFRSKA ERDAYLTNEI KSLDSYEKQQ QKIISDRERD
VQGAKEHLED VSARSAEQQD YEEGQRETLK RMSEQQSKLK IDLDGMKEKR KELWREDGKL
SQSATNAKNE LDNAQRLLQG MMDKDTSNGL RSVRSVARRL GLEGVYGPLY ELFEVSDKYK
TAVETVAGTS LFHVVVDNDD TASRLIDAMN KERSGRVTFM PLNRLKSVNV QYPKANDAVP
LISKLTYDRA YQMAFEQVFG RTVVCSDLAT AAQYTRSHGL NGVTDSGDRV DRKGALTGGY
HDNRRSRLDI VKQVKRWSEE YERDATRHTE VKDGLAKLEQ QISQAMGEIQ RIDAKRKAMV
EDRGHQARQV NWMLREVEQA RQRLARLEGS LADDEANLKA ASAKKAALEE ELKTPLQQQL
SPAEVQELET LSKAAEQQKQ ALLEASQKRQ QMASERSELE IELTENLRRR RNQLRAKLDD
LDGASGSGVI NAGEVEQRKA ELGSVSRSIE TLSAQIQSTE EELEALATTI SEQQAKLEEL
HNEANDVTRA MLRIQKSQER YLSKKQTLDN RKEECEVAIR DLGVLPDEAF TKYTGDKYMS
ASGMEKLVKL LHKVNDGLKK FAHVNKKAFE QYSNFTKQRD ELIARREELD QSADSIQDLI
DTLDQRKDEA IERTFKQVSK YFEEVFELLV PAGRGRLIMQ KRTDTYVDEE SERQAEKNGK
SEIDSYTGVS IKVSFNSKED EGQRISQLSG GQKSLVALAT VFAIQKCDPA PFYLFDEIDA
NLDTQYRTAV ANMIHTLSDS AQFITTTFRS EMLVNADKFY GVYFDKQKVS TIQTITQEEA
QKFIDTAAGM T
//
