TOF1_CANAL
ID TOF1_CANAL Reviewed; 1263 AA.
AC Q59NW5; A0A1D8PN65; Q59NR6;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 2.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Topoisomerase 1-associated factor 1;
GN Name=YBL053; Synonyms=TOF1; OrderedLocusNames=CAALFM_C501460WA;
GN ORFNames=CaO19.11613, CaO19.4136;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
CC -!- FUNCTION: Forms a fork protection complex (FPC) with CSM3 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 TOF1 and CSM3. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the timeless family. {ECO:0000305}.
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DR EMBL; CP017627; AOW29579.1; -; Genomic_DNA.
DR RefSeq; XP_711340.2; XM_706248.2.
DR AlphaFoldDB; Q59NW5; -.
DR SMR; Q59NW5; -.
DR BioGRID; 1230086; 1.
DR STRING; 237561.Q59NW5; -.
DR PRIDE; Q59NW5; -.
DR GeneID; 3647045; -.
DR KEGG; cal:CAALFM_C501460WA; -.
DR CGD; CAL0000201417; YBL053.
DR VEuPathDB; FungiDB:C5_01460W_A; -.
DR eggNOG; KOG1974; Eukaryota.
DR HOGENOM; CLU_008440_0_0_1; -.
DR InParanoid; Q59NW5; -.
DR OrthoDB; 839367at2759; -.
DR PRO; PR:Q59NW5; -.
DR Proteomes; UP000000559; Chromosome 5.
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; IBA:GO_Central.
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; IPR044998; Timeless.
DR InterPro; IPR006906; Timeless_N.
DR PANTHER; PTHR22940; PTHR22940; 1.
DR Pfam; PF04821; TIMELESS; 1.
PE 3: Inferred from homology;
KW Cell cycle; DNA damage; DNA repair; DNA replication inhibitor; Meiosis;
KW Nucleus; Reference proteome.
FT CHAIN 1..1263
FT /note="Topoisomerase 1-associated factor 1"
FT /id="PRO_0000301733"
FT REGION 1042..1098
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1178..1263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1060..1085
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1190..1209
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1210..1228
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1229..1263
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1263 AA; 144952 MW; CF2D415776F3A4AE CRC64;
MSDYESGSDI DNYYEADEFD DFIEYSDNEV EQEKSKPTPG QIEVEEIEEP EEDRIRTLTT
TLKPNETQAQ KLLKAHISVL VSALGGPDHT SDIQPPPYKL GHDALACLKD IKRWIRAVDE
KKNNYEVALA CAESGLVTND LIVIMCQWED KMQKKEIIKN KTTTEKTMLA CLELLVLLTW
PVEFGKDLSE SQKLLYSEIK KVHVSYKKQI LMFNNGQLLK AAIRLVLPTI AKSRIDREPR
DNQILKLVLY LIRNLLAIEP ANLSISNKSR KGASVTASDL PLGVTQDDIS INNVLSVFKK
NKVLMLLLTI SGSLGTEFDR DMFGEICLES IYLIIKGLSA SEVLVKKNLG STPVAAPSQN
TVPDAINASQ PLQPVTTTVG MQLQDLLATE SKKKKIQTQN IASRHGRFGS LLSIRSADSN
SFVVSGQEAL INTDSSLAKL DKSKKWKDRT YFKYDSDEYV NTSTPVYLNL TGQDILYNFV
EQFLSGGCFN NLIECMGSRL TSQTDLNMVD ELTLASYFFT ISWFLSYQRE RIGLDSENKE
LNYGSVGAAL SEVNFILIIG YFRDSFSVKK WNSLHVAMIC FKELLQISNS VFGKEITNQT
GEGDEISQHE IDRELAEGII RKLFSFNDFL SIIVQIPQTA AKHSPDYLRV SVSVVHILLK
AFETFANEDV HLYIQSKRKQ SKRNRKRVNN LDKSTEDRLR DVIYASDEEL DQSSAKEITQ
ERKLDFKKTE ARFFHQAIVS TYINYLSRYE DLSNQEIKTC LSYFHRLFVV RKDFTGLYRL
DFMQLLQKLR NYLQRGSSLR LQVEEFIYYF MKKFKTAFER FPMPIEVLFP RFEDNECKVY
LATGEVYEKE ETTSTSRSPR LAKDLEFVRD FGLDDQIKIL VSQLHVQEKQ SLLKWLIQEL
ERIINDRILN SDSIAELNAS NQQRRLFINN GYLRFLLRII GFDLPYTMEE VPELATTVDM
EHLTKVTELI KKWDSSQPVI FEDDKVPSYF VRTREAGYDE DQYNENDQEY DFNDDSIAFE
TEANPNSNRN HVSELDHLEE LERQLSSNGS RVNSKERNGT KGKARKKSKE KKRPEPKKVR
GLKRRRIPKD LLDDDDSQHV VKSAEFVHDS DDESDDEKDK AFFEREEKMR NLLNDMGGIA
TSEQLKEIQK VWKNLETGGN NKVASTVAKA VKEVGLFVEE SDNDDEVEEE SRNSAPVNEE
ADRTIFESGE VDTQQDLSDN TSNTSDMESE TETTKRSFVE DPEEISHVQP KRKRLVISDD
EEE
