ID   CSM3_YARLI              Reviewed;         368 AA.
AC   Q6C656;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=Chromosome segregation in meiosis protein 3;
GN   Name=CSM3; OrderedLocusNames=YALI0E12287g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of the fork protection complex (FPC) consisting of
CC       TOF1 and CSM3. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CSM3 family. {ECO:0000305}.
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DR   EMBL; CR382131; CAG79449.1; -; Genomic_DNA.
DR   RefSeq; XP_503856.1; XM_503856.1.
DR   AlphaFoldDB; Q6C656; -.
DR   SMR; Q6C656; -.
DR   STRING; 4952.CAG79449; -.
DR   EnsemblFungi; CAG79449; CAG79449; YALI0_E12287g.
DR   GeneID; 2912821; -.
DR   KEGG; yli:YALI0E12287g; -.
DR   VEuPathDB; FungiDB:YALI0_E12287g; -.
DR   HOGENOM; CLU_752747_0_0_1; -.
DR   InParanoid; Q6C656; -.
DR   OMA; MEAHRND; -.
DR   Proteomes; UP000001300; Chromosome E.
DR   GO; GO:0031298; C:replication fork protection complex; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0000076; P:DNA replication checkpoint signaling; IBA:GO_Central.
DR   GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0043111; P:replication fork arrest; IBA:GO_Central.
DR   GO; GO:0048478; P:replication fork protection; IBA:GO_Central.
DR   InterPro; IPR012923; Csm3.
DR   InterPro; IPR040038; TIPIN/Csm3/Swi3.
DR   PANTHER; PTHR13220; PTHR13220; 1.
DR   Pfam; PF07962; Swi3; 1.
PE   3: Inferred from homology;
KW   Cell cycle; DNA damage; DNA repair; DNA replication inhibitor; Meiosis;
KW   Nucleus; Reference proteome.
FT   CHAIN           1..368
FT                   /note="Chromosome segregation in meiosis protein 3"
FT                   /id="PRO_0000301726"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          153..358
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..33
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        153..167
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        187..240
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        277..291
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        292..315
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        330..358
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   368 AA;  40939 MW;  D67DBFF864F638FC CRC64;
     MDNDYESPWG LSQLEAPADS QNIDSQPLND DELGINTEVQ VKRTRHVAKL DDTRMMDDKG
     LPALKHLCTK VNLKGNGHEV GDLGRLLDMY QMWSHDLFPK GQFKSLYPLT SKAGRTATVR
     GLRLAWIDEE QRKKQTADVA TAVDELEDIT DFRDRGRHFE TEPRYSRQSE PPVETSVNVD
     NPDDLFVGMD SVDHRLVSDE DVDIQAEVSR REDDEDREQD VSELLEGARA QRDKDNSRSS
     GRLSLFDLGG SGSPSESDRG GSTLEGDIFG TGSLDPTPPP ASETSTQAPA AQPPATQPPQ
     APAPTQPPSN QAPVKAPPQP MRQMDDLELD MLADFEPDFE DQEQHEPEPD PEDYEDDEAM
     AVMREMGL