ID S7RXF1_GLOTA Unreviewed; 451 AA.
AC S7RXF1;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Chromosome segregation in meiosis protein {ECO:0000256|RuleBase:RU366049};
GN ORFNames=GLOTRDRAFT_114564 {ECO:0000313|EMBL:EPQ58019.1};
OS Gloeophyllum trabeum (strain ATCC 11539 / FP-39264 / Madison 617) (Brown
OS rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Gloeophyllales; Gloeophyllaceae; Gloeophyllum.
OX NCBI_TaxID=670483 {ECO:0000313|EMBL:EPQ58019.1, ECO:0000313|Proteomes:UP000030669};
RN [1] {ECO:0000313|EMBL:EPQ58019.1, ECO:0000313|Proteomes:UP000030669}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11539 {ECO:0000313|EMBL:EPQ58019.1,
RC ECO:0000313|Proteomes:UP000030669};
RX PubMed=22745431; DOI=10.1126/science.1221748;
RA Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT 31 fungal genomes.";
RL Science 336:1715-1719(2012).
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; KB469298; EPQ58019.1; -; Genomic_DNA.
DR RefSeq; XP_007863314.1; XM_007865123.1.
DR AlphaFoldDB; S7RXF1; -.
DR STRING; 670483.S7RXF1; -.
DR GeneID; 19299905; -.
DR KEGG; gtr:GLOTRDRAFT_114564; -.
DR eggNOG; KOG3004; Eukaryota.
DR HOGENOM; CLU_050882_0_0_1; -.
DR OMA; DEGWDEM; -.
DR OrthoDB; 1388129at2759; -.
DR Proteomes; UP000030669; 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: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 replication inhibitor {ECO:0000256|ARBA:ARBA00022880};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU366049};
KW Reference proteome {ECO:0000313|Proteomes:UP000030669}.
FT DOMAIN 150..231
FT /note="Chromosome segregation in meiosis protein 3"
FT /evidence="ECO:0000259|Pfam:PF07962"
FT REGION 1..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 313..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 355..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..70
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..152
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..334
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..380
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 419..437
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 451 AA; 49693 MW; 6380AFD641912B10 CRC64;
MSATLDDIWD APVEPSSPRR PSASDAPQSN TPERSERPLF LASDSEDDEP KTRKRTPQTK
KSARPDIDAM FDNLDDDENA FQPLAPALDM NALQREAEQR HARSSQGGDL HAILPSSSPG
REQSRDMADS NNENKKSNKD GPKERKVLPK LDEARLLGPN GFPALIAEAK KFKPRGKGQE
ATDLNRVIQL YQFWAHKMYP KMQFRDTVNR VEKLCHSKRM HVALSVWRDE AKGLVNGMKP
DDPIDLVSDS DEDDADDGER TKPDGRQSLG RDVGGASDAR SRAPSRPPSS PSIGQVTDVD
DFDIDAMIRE EQEMEADRVP APQDTHRPTE GATAGDDMDI DDEAMWAEMM MEDAGVPSIP
PVPTSIKNTD DNTTAAAAQT GGASVMDDED MWDVVREMEL ESQKPGSSVA AGPETLPSED
HTTGPSSEGL TSSPQRKRRM SNADDWDDMY V
//
