ID   CSM3_NEUCR              Reviewed;         409 AA.
AC   Q7SHE8;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Chromosome segregation in meiosis protein 3;
GN   Name=csm-3; ORFNames=NCU01858;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
CC   -!- FUNCTION: Forms a fork protection complex (FPC) with tof-1 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       tof-1 and csm-3. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CSM3 family. {ECO:0000305}.
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DR   EMBL; CM002236; EAA36253.1; -; Genomic_DNA.
DR   RefSeq; XP_965489.1; XM_960396.2.
DR   AlphaFoldDB; Q7SHE8; -.
DR   SMR; Q7SHE8; -.
DR   STRING; 5141.EFNCRP00000001202; -.
DR   EnsemblFungi; EAA36253; EAA36253; NCU01858.
DR   GeneID; 3881667; -.
DR   KEGG; ncr:NCU01858; -.
DR   VEuPathDB; FungiDB:NCU01858; -.
DR   HOGENOM; CLU_036204_1_0_1; -.
DR   InParanoid; Q7SHE8; -.
DR   Proteomes; UP000001805; Chromosome 1, Linkage Group I.
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..409
FT                   /note="Chromosome segregation in meiosis protein 3"
FT                   /id="PRO_0000301722"
FT   REGION          20..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          150..367
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          388..409
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        152..170
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        286..300
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        344..366
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   409 AA;  44291 MW;  7E5EBE8CCAFF43CB CRC64;
     MPAQDNDNNT SAFVNEFLAG WDDDDPFRSP SPETAGTNKT NNKKRKEPDT LGIDKEIDVT
     KKARVPRVKL DDARLLSDKG IPKLRKTASK LKLKGKGHEF SDAARLLSFY QEWLDDLFPK
     ATFVDALAMC EKAGHKTTLR NARLKWIAEG KPRSTTAEEE EDRDREGQPS ASAEPTRMAP
     IFEKATGAKS KTPTLDNNLF GDDDIYNATP RRNQPTAAPG DIPDDDELDA LMAEAESGAA
     PGASKATNNG AASDSIFGGG AINRRPRPSE VPDDDDLDAL MAEAESYRPS TTNHGSIFGN
     GSASGGGKDK PAMAAPPQED DDDLDALMAE AEMHASLATK TTGKESTSRE RTSEQDGGKD
     AQNYDEDDLD AWMAEAEAYT KTTSIQVAQP KDTDDDWEAE AAMAEMHGF