ID A0A0D2FKU1_9EURO Unreviewed; 495 AA.
AC A0A0D2FKU1;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Chromosome segregation in meiosis protein {ECO:0000256|RuleBase:RU366049};
GN ORFNames=Z518_08473 {ECO:0000313|EMBL:KIX02532.1};
OS Rhinocladiella mackenziei CBS 650.93.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Rhinocladiella.
OX NCBI_TaxID=1442369 {ECO:0000313|EMBL:KIX02532.1, ECO:0000313|Proteomes:UP000053617};
RN [1] {ECO:0000313|EMBL:KIX02532.1, ECO:0000313|Proteomes:UP000053617}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 650.93 {ECO:0000313|EMBL:KIX02532.1,
RC ECO:0000313|Proteomes:UP000053617};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Rhinocladiella mackenzie CBS 650.93.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Forms a fork protection complex (FPC) with TOF1 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.
CC {ECO:0000256|ARBA:ARBA00025496}.
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; KN847480; KIX02532.1; -; Genomic_DNA.
DR RefSeq; XP_013269668.1; XM_013414214.1.
DR AlphaFoldDB; A0A0D2FKU1; -.
DR STRING; 1442369.A0A0D2FKU1; -.
DR GeneID; 25296544; -.
DR VEuPathDB; FungiDB:Z518_08473; -.
DR HOGENOM; CLU_036204_2_0_1; -.
DR OrthoDB; 1388129at2759; -.
DR Proteomes; UP000053617; 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:UP000053617}.
FT DOMAIN 75..162
FT /note="Chromosome segregation in meiosis protein 3"
FT /evidence="ECO:0000259|Pfam:PF07962"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 169..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..48
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..188
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..340
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..359
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..401
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..453
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..469
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 495 AA; 54427 MW; F10888F592EFBA42 CRC64;
MAADPLTAAT VNDLFNFDST DDEDPFHDKS WPNGRDDKTT LSPGKRKADD DDNLGVDLGL
DEEVKLIKKR KPIAKLDEAR LLSAAGIPKL RALARSGKIS KKLHFKGKGH EFSDVARLLN
YYQLWLDNLY PRAKFADGLQ LVEKAGHSKR MQVMRKEWID EGKPGYIKEK TKKADEEREK
EGDTDDLSAG DSKTSGNNWE NNASVSPRVD AEGGSLFIPD SRPTRDDENN LPEDDELDAL
LAQQDNARAP HAPKSTSRQA MDLDSEGEDD LDALLAEQET RRGPPTASAP SDTSKSKPSP
FDEDDEDPDD LDALIAEQEA TSEPSTEQPR SDTQLPTVRN KVLTILDDND RHKDVMNEDN
GLDALIVEQE ARQQEKIKQR SSSTRATTSP GTSTHSNTDA DVQVDPDADA DADADGEDMF
SSSPIRTNEA RSRSSNIVPG LSAPVPTRST TDMETERGSN RKGKMADEED SIEAEADNND
MGADDMFSSS PVQND
//
