ID A0A0W8E0W4_PHYNI Unreviewed; 165 AA.
AC A0A0W8E0W4;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE SubName: Full=Phospholipase D {ECO:0000313|EMBL:KUF98127.1};
DE SubName: Full=TIMELESS-interacting protein {ECO:0000313|EMBL:KUG02121.1};
GN ORFNames=AM587_10006228 {ECO:0000313|EMBL:KUF89660.1}, AM587_10011928
GN {ECO:0000313|EMBL:KUG02121.1}, AM588_10007474
GN {ECO:0000313|EMBL:KUF98127.1};
OS Phytophthora nicotianae (Buckeye rot agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=4790 {ECO:0000313|EMBL:KUG02121.1, ECO:0000313|Proteomes:UP000052943};
RN [1] {ECO:0000313|Proteomes:UP000052943, ECO:0000313|Proteomes:UP000054636}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Race 0 {ECO:0000313|EMBL:KUG02121.1}, race 0
RC {ECO:0000313|Proteomes:UP000052943}, race 1
RC {ECO:0000313|Proteomes:UP000054636}, and Race 1
RC {ECO:0000313|EMBL:KUF98127.1};
RA Liu H., Ma X., Yu H., Fang D., Li Y., Wang X., Wang W., Dong Y., Xiao B.;
RT "Genomes and virulence difference between two physiological races of
RT Phytophthora nicotianae.";
RL Submitted (NOV-2015) 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 -!- 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KUG02121.1}.
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DR EMBL; LNFO01001644; KUF89660.1; -; Genomic_DNA.
DR EMBL; LNFP01000080; KUF98127.1; -; Genomic_DNA.
DR EMBL; LNFO01000070; KUG02121.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0W8E0W4; -.
DR STRING; 4790.A0A0W8E0W4; -.
DR EnsemblProtists; KUF89660; KUF89660; AM587_10006228.
DR EnsemblProtists; KUF98127; KUF98127; AM588_10007474.
DR EnsemblProtists; KUG02121; KUG02121; AM587_10011928.
DR OMA; WAYDLYP; -.
DR OrthoDB; 76475at2759; -.
DR Proteomes; UP000052943; Unassembled WGS sequence.
DR Proteomes; UP000054636; 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: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 Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU366049};
KW Reference proteome {ECO:0000313|Proteomes:UP000052943}.
FT DOMAIN 53..134
FT /note="Chromosome segregation in meiosis protein 3"
FT /evidence="ECO:0000259|Pfam:PF07962"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 137..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 165 AA; 18450 MW; 588FD0B891872373 CRC64;
MASRGWERDE DLARHDDASS ATADAAPATQ DGGGDAGNAD APVVTQKRRR NLLRESHLAS
AEGFKKVHRT FPYQVSADVS GREAQALASL VKMYKQWAFD LYPGLNFEDF VDRTEALGKG
HQVQGLMVEL REKERIKAVK KREEQEEKER EEKGESDSEG EEAML
//
