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Database: UniProt
Entry: A0A0D2CEF4_9EURO
LinkDB: A0A0D2CEF4_9EURO
Original site: A0A0D2CEF4_9EURO 
ID   A0A0D2CEF4_9EURO        Unreviewed;       484 AA.
AC   A0A0D2CEF4;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=Chromosome segregation in meiosis protein {ECO:0000256|RuleBase:RU366049};
GN   ORFNames=PV06_00882 {ECO:0000313|EMBL:KIW48277.1};
OS   Exophiala oligosperma.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=215243 {ECO:0000313|EMBL:KIW48277.1, ECO:0000313|Proteomes:UP000053342};
RN   [1] {ECO:0000313|EMBL:KIW48277.1, ECO:0000313|Proteomes:UP000053342}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 72588 {ECO:0000313|EMBL:KIW48277.1,
RC   ECO:0000313|Proteomes:UP000053342};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Exophiala oligosperma CBS72588.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Forms a fork protection complex (FPC) with TOF1 and which is
CC       required for chromosome segregation during meiosis and DNA damage
CC       repair. FPC coordinates leading and lagging strand synthesis and moves
CC       with the replication fork. FPC stabilizes replication forks in a
CC       configuration that is recognized by replication checkpoint sensors.
CC       {ECO:0000256|ARBA:ARBA00025496}.
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; KN847332; KIW48277.1; -; Genomic_DNA.
DR   RefSeq; XP_016268493.1; XM_016401440.1.
DR   AlphaFoldDB; A0A0D2CEF4; -.
DR   STRING; 215243.A0A0D2CEF4; -.
DR   GeneID; 27352956; -.
DR   VEuPathDB; FungiDB:PV06_00882; -.
DR   HOGENOM; CLU_036204_2_0_1; -.
DR   OrthoDB; 1388129at2759; -.
DR   Proteomes; UP000053342; 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: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:UP000053342}.
FT   DOMAIN          83..170
FT                   /note="Chromosome segregation in meiosis protein 3"
FT                   /evidence="ECO:0000259|Pfam:PF07962"
FT   REGION          1..71
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          173..255
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          268..484
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        31..45
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        46..71
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        173..187
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        205..225
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        232..246
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        326..341
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        347..363
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        388..415
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        433..458
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   484 AA;  52395 MW;  ABDDAD556D38E28E CRC64;
     MATDTTTEAA IDDIFNFDST DDEDPFKDTN TNNKSSRSNG DDNNKPGSSP DRKRKAEDGE
     GSDSDLGINK EVKITKKRKP IAKLDEARLL SAPGIPKLRA LARSGKFSKK LRLKGKGHEF
     SDVARLLNYY QLWLDNLYPR AKFADGLQMV EKVGHSKRMQ IMRKEWIDEG KPGYARKWGR
     KDDELDDQDG QAVADDWFGG SGKPVENSSK PTPSANATTA VDAGTGGGDS SLFIPDSRSG
     NNDPPQGEDT LPDDDELEAL LAEQDAITTA VGQQKVASTK PTADVDSEGE DDLDALLAEQ
     ESRRTVVKSS NPPAAKIHQS PFDDGDDEEG MIDDDDDLDA LLAEQEVRHQ PSSSKAANQT
     PPQTSSKPPE PAEVDDEEDD LEALLAEQEA RQSTSRAHAS VENSMDNLET LPGTTHDNDV
     NEEDGGGEAM FLSSPVRTTQ RSRAGGDSTS NSDRAATLPE QARAQEDTED LEAGDMFSSS
     PVKG
//
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