ID W6MTU3_9ASCO Unreviewed; 266 AA.
AC W6MTU3;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Chromosome segregation in meiosis protein {ECO:0000256|RuleBase:RU366049};
GN ORFNames=KUCA_T00005912001 {ECO:0000313|EMBL:CDK29918.1};
OS Kuraishia capsulata CBS 1993.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetales incertae sedis; Kuraishia.
OX NCBI_TaxID=1382522 {ECO:0000313|EMBL:CDK29918.1};
RN [1] {ECO:0000313|EMBL:CDK29918.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS 1993 {ECO:0000313|EMBL:CDK29918.1};
RA Genoscope - CEA;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDK29918.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS 1993 {ECO:0000313|EMBL:CDK29918.1};
RA Morales L., Noel B., Porcel B., Marcet-Houben M., Hullo M-F., Sacerdot C.,
RA Tekaia F., Leh-Louis V., Despons L., Khanna V., Aury J-M., Barbe V.,
RA Couloux A., Labadie K., Pelletier E., Souciet J-L., Boekhout T.,
RA Gabaldon T., Wincker P., Dujon B.;
RT "Complete DNA sequence of /Kuraishia capsulata/ illustrates novel genomic
RT features among budding yeasts (/Saccharomycotina/).";
RL Submitted (FEB-2014) 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 -!- SUBUNIT: Component of the fork protection complex (FPC) consisting of
CC TOF1 and CSM3. {ECO:0000256|ARBA:ARBA00011217}.
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; HG793131; CDK29918.1; -; Genomic_DNA.
DR AlphaFoldDB; W6MTU3; -.
DR STRING; 1382522.W6MTU3; -.
DR HOGENOM; CLU_1142925_0_0_1; -.
DR OrthoDB; 1388129at2759; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0000076; P:DNA replication checkpoint signaling; IEA:UniProtKB-UniRule.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
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 repair {ECO:0000256|ARBA:ARBA00023204};
KW DNA replication inhibitor {ECO:0000256|ARBA:ARBA00022880};
KW Meiosis {ECO:0000256|ARBA:ARBA00023254};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU366049}.
FT DOMAIN 46..142
FT /note="Chromosome segregation in meiosis protein 3"
FT /evidence="ECO:0000259|Pfam:PF07962"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 157..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..181
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..228
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 266 AA; 30467 MW; 55D7D32A6E8C7C4C CRC64;
MDFENLGLSP VSGSPLPGDQ SIEENLGLTD GVPMLKNKTK RLNYNLNTEL LLSKRGLPEL
RRYASNFKFK RHQPSRLRRD PRRDKFVNSV AFQNLTRILQ MYQVWGHNIF PKARLADFID
LVKKTGNKKE IKAYRIECIE EEVARIRGLE HGFGIDIGED AGNGDNLKNT NSTNDNLPNR
QSQSVDEDED DEEIRRPTRT NNLFVGDDYD DSEPAPTSTS QPPDELESLL TRNNDDNLDD
FDLADFAENE ADQYEDEMDV MRELGI
//