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Database: UniProt
Entry: A0A1E3QEQ9_LIPST
LinkDB: A0A1E3QEQ9_LIPST
Original site: A0A1E3QEQ9_LIPST 
ID   A0A1E3QEQ9_LIPST        Unreviewed;       318 AA.
AC   A0A1E3QEQ9;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Chromosome segregation in meiosis protein {ECO:0000256|RuleBase:RU366049};
GN   ORFNames=LIPSTDRAFT_67064 {ECO:0000313|EMBL:ODQ76191.1};
OS   Lipomyces starkeyi NRRL Y-11557.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Lipomycetaceae; Lipomyces.
OX   NCBI_TaxID=675824 {ECO:0000313|EMBL:ODQ76191.1, ECO:0000313|Proteomes:UP000094385};
RN   [1] {ECO:0000313|EMBL:ODQ76191.1, ECO:0000313|Proteomes:UP000094385}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL Y-11557 {ECO:0000313|EMBL:ODQ76191.1,
RC   ECO:0000313|Proteomes:UP000094385};
RX   PubMed=27535936; DOI=10.1073/pnas.1603941113;
RA   Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goeker M.,
RA   Salamov A.A., Wisecaver J.H., Long T.M., Calvey C.H., Aerts A.L.,
RA   Barry K.W., Choi C., Clum A., Coughlan A.Y., Deshpande S., Douglass A.P.,
RA   Hanson S.J., Klenk H.-P., LaButti K.M., Lapidus A., Lindquist E.A.,
RA   Lipzen A.M., Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J.L.,
RA   Peng Y., Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C.,
RA   Stielow J.B., Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V.,
RA   Jeffries T.W.;
RT   "Comparative genomics of biotechnologically important yeasts.";
RL   Proc. Natl. Acad. Sci. U.S.A. 113:9882-9887(2016).
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; KV454289; ODQ76191.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1E3QEQ9; -.
DR   STRING; 675824.A0A1E3QEQ9; -.
DR   OrthoDB; 1388129at2759; -.
DR   Proteomes; UP000094385; Unassembled WGS sequence.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000094385}.
FT   DOMAIN          95..175
FT                   /note="Chromosome segregation in meiosis protein 3"
FT                   /evidence="ECO:0000259|Pfam:PF07962"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          178..230
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          246..318
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        178..192
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        248..271
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   318 AA;  35554 MW;  735DD85968CBC471 CRC64;
     MENLFGPDDD DDYPDVDDEI NMGYGASTVE IDIESDLATG VARLPTPPYD INLDAELYPR
     TGDEPSLVPA AKPPDVVDLG IDKEVVIKQK STRAKLDNQR LLSADGLITI KRRAPKVRFK
     GKGHEYRYLG RLLECYQIWG HQLFPKANFE DFLAMTERLG RSKQMKIVRR QWIDEWKPAR
     PPEEESDLDQ RQTYDDGTGF VVGAGFSDDG DNENREFGSQ EHQKTNAGDN SMRFSEAGVA
     HLNDDLVAPG QNNMNRSPSR IDSVTPEQNP TPPRSDAVPS DIPPSADSQE FAPSRGESPS
     SHHGALFLFD DDEDDLYD
//
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