TOF1_CANGA
ID TOF1_CANGA Reviewed; 1176 AA.
AC Q6FNX7;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=Topoisomerase 1-associated factor 1;
GN Name=TOF1; OrderedLocusNames=CAGL0J08250g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; CR380956; CAG61018.1; -; Genomic_DNA.
DR RefSeq; XP_448067.1; XM_448067.1.
DR AlphaFoldDB; Q6FNX7; -.
DR SMR; Q6FNX7; -.
DR STRING; 5478.XP_448067.1; -.
DR PRIDE; Q6FNX7; -.
DR EnsemblFungi; CAG61018; CAG61018; CAGL0J08250g.
DR GeneID; 2889924; -.
DR KEGG; cgr:CAGL0J08250g; -.
DR CGD; CAL0129427; CAGL0J08250g.
DR VEuPathDB; FungiDB:CAGL0J08250g; -.
DR eggNOG; KOG1974; Eukaryota.
DR HOGENOM; CLU_008440_0_0_1; -.
DR InParanoid; Q6FNX7; -.
DR OMA; WLKLYDE; -.
DR Proteomes; UP000002428; Chromosome J.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR GO; GO:0031298; C:replication fork protection complex; IEA:EnsemblFungi.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0000076; P:DNA replication checkpoint signaling; IEA:EnsemblFungi.
DR GO; GO:0043570; P:maintenance of DNA repeat elements; IEA:EnsemblFungi.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0007064; P:mitotic sister chromatid cohesion; IEA:EnsemblFungi.
DR GO; GO:0043111; P:replication fork arrest; IEA:EnsemblFungi.
DR GO; GO:0048478; P:replication fork protection; IEA:EnsemblFungi.
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..1176
FT /note="Topoisomerase 1-associated factor 1"
FT /id="PRO_0000301734"
FT REGION 375..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 915..949
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 974..998
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1148..1176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..390
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 915..931
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1155..1176
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1176 AA; 135249 MW; 27C925FDEBE21EC6 CRC64;
MSDTESPLTV LKARIALLAT AIGGPDYTSQ IDPPPYQIGD DCLACLKDLK RWFRLVDDNQ
RRWDVAMAVA EYKILTDDLL PILIDWENKC YLATKLSKGN SDISAHFKNK QYYDKIALNC
LQLMVLMTWP LILTEQSSTN QINLYSELKK HQLTYKKAIL SVENGKVLKA AIRIAIDVIK
LDRLARTPRD NMVLKMVLNF IRNILAIEPG ELTITARKNI ASKGINSVDT LPPNVTQDDI
SQSTVISCFK KNKVFPFLLT LGSSMTKEFD QDFINIPLME VMFFLTKDIS QDSLLFKSGE
LDTAQSENHL SKAGQELNDL LQKESQLKKK VIMNTSTRHS RFGAMLSIQT LDQKRLTVSG
SQNLLDNSKA LQKIDDSKKS KGRRPMIRNE TDNESLPTNL LNVHKKSGTY LPLTISKYLN
DFINDFIDSS FNYLLKSVTN YFVTEEDKII SLEKIEYLLF FAWFNKYQIL RCQVDKDADI
MMISESIKET TFILVSSLLR SSYDSKAWAV VHSSMLAFNE LLKLVNSLKK FEDNEDIEYV
LSRLFSDERI QLLSNLPRIA STHSLSFMKT SIELTHTVLK ILEMYSGDNS LVVESKRRAK
KMKSISKEDY ERLVNEEGYD PDEAIEILNP GHKTIVINFK RVQSSFFHRN TIDLYINTLK
RFNELEYSHI KMIISFLYRL FVENNEETLF YRLDFIILLK DMLKQDGLPR TSKARTHIND
FAKYYLSRLK RKLKSSPAWH VGILFPPLND GVVGYFQKYG EHKMTKESEI YAVQPSQFIP
FEQQEMMSEN MILDMQIGVL VSTLIDEGSQ NLVELVRENV QHLIAVFTSH LEVAGENEKT
PNNEAFILKE EYDVNPLHYN RHIRALLQLV GFEIPILKSD PCFYRGTTEF SRLVKCEESI
TKYLNIPFET PNGLPSSSYL KQQSEKNNSL ESDGWKGNED YDYTDPNIVP DNEVDDNDYF
KDLDKSTNIR KEKRTVGIAS KKTQSKNKTS RNRKKASFRL PNAIEGKDKQ PQENLEVFSK
EYISDSDEDD EEILNPVFFE NEMYMRWLLD KYNGQLPNDK FLSFGRFVNE RLSNNGKVVS
DFTSLFDGPV PPIDALPLEG ITRKGPDKTL LTLSRVEINE SNQDNENTQV NEQVDETSEN
LTINKNARNI GISHGHVESE ADDDEPITKK RRTSAN
