ID A0A0J0XS79_9TREE Unreviewed; 369 AA.
AC A0A0J0XS79;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Chromosome segregation in meiosis protein {ECO:0000256|RuleBase:RU366049};
GN ORFNames=CC85DRAFT_283965 {ECO:0000313|EMBL:KLT43921.1};
OS Cutaneotrichosporon oleaginosum.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Trichosporonales; Trichosporonaceae; Cutaneotrichosporon.
OX NCBI_TaxID=879819 {ECO:0000313|EMBL:KLT43921.1, ECO:0000313|Proteomes:UP000053611};
RN [1] {ECO:0000313|EMBL:KLT43921.1, ECO:0000313|Proteomes:UP000053611}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBC0246 {ECO:0000313|EMBL:KLT43921.1,
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 -!- FUNCTION: Plays an important role in the control of DNA replication and
CC the maintenance of replication fork stability.
CC {ECO:0000256|RuleBase:RU366049}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU366049}.
CC -!- SIMILARITY: Belongs to the CSM3 family. {ECO:0000256|ARBA:ARBA00006075,
CC ECO:0000256|RuleBase:RU366049}.
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DR EMBL; KQ087190; KLT43921.1; -; Genomic_DNA.
DR RefSeq; XP_018280412.1; XM_018422560.1.
DR AlphaFoldDB; A0A0J0XS79; -.
DR STRING; 879819.A0A0J0XS79; -.
DR GeneID; 28983163; -.
DR OrthoDB; 1388129at2759; -.
DR Proteomes; UP000053611; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:DNA damage response; IEA:UniProtKB-KW.
DR GO; GO:0000076; P:DNA replication checkpoint signaling; IEA:UniProtKB-UniRule.
DR GO; GO:0008156; P:negative regulation of DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0031297; P:replication fork processing; IEA:UniProtKB-UniRule.
DR InterPro; IPR012923; Csm3.
DR InterPro; IPR040038; TIPIN/Csm3/Swi3.
DR PANTHER; PTHR13220; TIMELESS INTERACTING-RELATED; 1.
DR PANTHER; PTHR13220:SF11; TIMELESS-INTERACTING PROTEIN; 1.
DR Pfam; PF07962; Swi3; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|RuleBase:RU366049};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU366049};
KW DNA replication inhibitor {ECO:0000256|ARBA:ARBA00022880};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU366049};
KW Reference proteome {ECO:0000313|Proteomes:UP000053611}.
FT DOMAIN 171..251
FT /note="Chromosome segregation in meiosis protein 3"
FT /evidence="ECO:0000259|Pfam:PF07962"
FT REGION 1..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 248..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..61
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..293
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..359
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 369 AA; 40673 MW; 03DC5677D846FCD2 CRC64;
MSLTDLFNDD SPPPSPWRKE ALFLDGESAS GEDESMSGDG ESAISDDEST SSERPMKRQR
RLYDSSPSPP PFSLAELLRS PGFQRDLQEI TRAAERGRLD ILDESGPPAP APRRRLDNAD
GSGVPDPTPE LQGIAPRVLA ELFDDPLAAQ DPLAAGGASE EEPKRRRVIA KVDPDRLLGP
KGFPALVAAA RKFKVKGKGH ETSDLERLMD TYQVWAHGMF PKGEFGYTIG RIEAVCRKNQ
MVNAIRGLRD EFHPPPRTPS PDPEEQGSAA GSPRREEESL DAFIERGEES MGDETFRYAP
GAETLAADRR PLFAPGPDVD DDEDEDELAA LAEMERETGV EESTALETRR ETRVDFGDEP
PAFDEEEEW
//
