ID A0A4D9ERJ8_9SAUR Unreviewed; 284 AA.
AC A0A4D9ERJ8;
DT 03-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 03-JUL-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=TIMELESS-interacting protein {ECO:0000256|ARBA:ARBA00018750, ECO:0000256|RuleBase:RU366049};
GN ORFNames=DR999_PMT03437 {ECO:0000313|EMBL:TFK13016.1};
OS Platysternon megacephalum (big-headed turtle).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Platysternidae; Platysternon.
OX NCBI_TaxID=55544 {ECO:0000313|EMBL:TFK13016.1, ECO:0000313|Proteomes:UP000297703};
RN [1] {ECO:0000313|EMBL:TFK13016.1, ECO:0000313|Proteomes:UP000297703}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DO16091913 {ECO:0000313|EMBL:TFK13016.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:TFK13016.1};
RA Gong S.;
RT "Draft genome of the big-headed turtle Platysternon megacephalum.";
RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:TFK13016.1, ECO:0000313|Proteomes:UP000297703}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DO16091913 {ECO:0000313|EMBL:TFK13016.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:TFK13016.1};
RA Gong S.;
RT "The genome sequence of big-headed turtle.";
RL Submitted (APR-2019) 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:TFK13016.1}.
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DR EMBL; QXTE01000017; TFK13016.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4D9ERJ8; -.
DR STRING; 55544.A0A4D9ERJ8; -.
DR Proteomes; UP000297703; 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:UP000297703}.
FT DOMAIN 71..151
FT /note="Chromosome segregation in meiosis protein 3"
FT /evidence="ECO:0000259|Pfam:PF07962"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 182..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 222..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..243
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 284 AA; 32163 MW; 57BB9E23C11A4CA8 CRC64;
MIDPLANNLF ALPEYDDTED ETFPPLPPPS SPGRDDVEGA LTNEEQDGNK PSQTKDSTVS
TQKAIKRPIP KLDAQRLISE RGLPALRHVF DNAKFKGKGH ETEDLKTLLR HMEHWAHRLF
PKLQFDDFME RVESLGNKKE VQTCLKRIRL DLPILHEDFT SNEGSGGGNN GLKMSLEEEL
DPFSENVKEE FDSLSSTALT EEQQQRIERN RQLALERRQA KMQFNSPSQE NDLSATQPNE
ELKTTEAQDP DDLTEVEIQA AEAKVADMEA VDKDIPLKCA EEIK
//
