TOF1_PICGU
ID TOF1_PICGU Reviewed; 1216 AA.
AC A5DJ85;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 2.
DT 03-AUG-2022, entry version 52.
DE RecName: Full=Topoisomerase 1-associated factor 1;
GN Name=TOF1; ORFNames=PGUG_03336;
OS Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX NCBI_TaxID=294746;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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; CH408158; EDK39238.2; -; Genomic_DNA.
DR RefSeq; XP_001483955.1; XM_001483905.1.
DR AlphaFoldDB; A5DJ85; -.
DR SMR; A5DJ85; -.
DR STRING; 4929.XP_001483955.1; -.
DR PRIDE; A5DJ85; -.
DR EnsemblFungi; EDK39238; EDK39238; PGUG_03336.
DR GeneID; 5126086; -.
DR KEGG; pgu:PGUG_03336; -.
DR VEuPathDB; FungiDB:PGUG_03336; -.
DR eggNOG; KOG1974; Eukaryota.
DR HOGENOM; CLU_008440_0_0_1; -.
DR InParanoid; A5DJ85; -.
DR OMA; WLKLYDE; -.
DR OrthoDB; 839367at2759; -.
DR Proteomes; UP000001997; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0008156; P:negative regulation of DNA replication; IEA:UniProtKB-KW.
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..1216
FT /note="Topoisomerase 1-associated factor 1"
FT /id="PRO_0000301746"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1018..1082
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1139..1216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1023..1050
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1052..1082
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1139..1192
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1197..1216
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1216 AA; 139181 MW; A5F0E25019A0306C CRC64;
MSDFDSYAAD SELEDFVVDD EPPVDNSNNP QNPQDESNEA SETRDRIRDL TTALQPNETP
TQKLLKAHIS VLVTALGGPD HVGSLKDSSS EYKLGHDALA CLKDIKRWIK SVDEIGHKYD
VALACADCGL VENDLTVMLC QWDSQQKHSN TSKRTTEKIM LSALEILVLL TWPVEMSSEM
SENQQLNFVA VRKSQLVYKK HILSYNNGQT FKAVLRLALP TISKDTSDRE PRDNAILGLV
LFFIRNMLYI EPPSLSTSSK LRKTMMEIDN LPANMRYDDV SINTVLSCFK RNKVLLFLLT
MCGSLGSDFD RETFAPCCLE CIFLIVRGVE ARDLVDNVRP VPETNDANGN NLPTLSSTSD
MALQDLLKEE KRRKKVQSQN ISTRHGRFGT LLSLQGENSS YVVSGQEALS SANQTFAQLD
KSKKWNDRKH FKYDSDAFVN TTPNFITSTT ISLLKEFINE FLVGGCFNSL MSSVGWIFSG
ASDLSYINEY EKASYFLTTA WFFAYKRARI EILKNRILNE NEDTLDYGSV AAGLSEVNFV
LIIGYVRESF ERHYWDSLHV AMICFREMLL ISNSVFESKH KDTNSEQDEE DRDMAEGIIR
KLFSLEQFVN LITHIPQSAS KHSPEYLSVC VSVVYILLKS FENFSKEDIK LYVQSKRKQR
RNAKNFKNVD SLELKDIIEG SDEEIDEETV KQVSRERKFD FNKTEMKFFQ SSIVTAHIDF
LSRYEDLTHE QIKQCLVYFH RLFIVRKDYS GLFRLDFLHV LNSLRDFLPR KSNIRNHVEE
FTFHFMKRFK NLFRRFPNPV ELLFPRMEDE SLRTYLSLGE VVEKPIKKAK EREIRYAKEL
EFTRSNFSED EKYKILVSAI YFEDNEKFLS WLIEELSRIV EIAEKDSEAS TIKLQVQGEY
EPLVLENATV RFLLENVGFV VPESSSDECT CTVGTSELTQ SLEYIKKWLS VQPVAFDEDK
DASHYLRVRD DANDGEFNIG YDENEDEIAF ETAPTNRYRE DLEALDNLEE LEARISSSNG
VKGVARKKRR PKGKISDTKH RSKPSSTHRK PRNLGVHSDD EEDKPLKSGE YVHDSDDESD
NEDARAFFER EEKLRRMLTE SGGIVNPQQL EEFKRAWGKI VGGEAVDNVL STLGLQTGAS
QSSLPLASQS QVDSQPQIDS QPQIDSELQS QSLSQVVEDG PSVESTQESS SEEFLSADEE
LPARKKRRVI DDSDEE
