TOF1_LODEL
ID TOF1_LODEL Reviewed; 1175 AA.
AC A5E2H7;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 25-MAY-2022, entry version 44.
DE RecName: Full=Topoisomerase 1-associated factor 1;
GN Name=TOF1; ORFNames=LELG_03814;
OS Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC Lodderomyces.
OX NCBI_TaxID=379508;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL
RC YB-4239;
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EDK45635.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CH981528; EDK45635.1; ALT_FRAME; Genomic_DNA.
DR RefSeq; XP_001524782.1; XM_001524732.1.
DR AlphaFoldDB; A5E2H7; -.
DR SMR; A5E2H7; -.
DR STRING; 379508.A5E2H7; -.
DR EnsemblFungi; EDK45635; EDK45635; LELG_03814.
DR GeneID; 5232181; -.
DR KEGG; lel:LELG_03814; -.
DR eggNOG; KOG1974; Eukaryota.
DR HOGENOM; CLU_008440_0_0_1; -.
DR InParanoid; A5E2H7; -.
DR OrthoDB; 839367at2759; -.
DR Proteomes; UP000001996; 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..1175
FT /note="Topoisomerase 1-associated factor 1"
FT /id="PRO_0000301741"
FT REGION 894..982
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1043..1175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 941..972
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1054..1073
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1077..1113
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1114..1129
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1130..1155
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1156..1175
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1175 AA; 134406 MW; A8944BAD44198CBE CRC64;
MEEDKIRALT TTLKPNETQA QKLLKAHIAV LVSALGGIDK TSEIVPPPYK LGHDALACLK
DIKRWIRAVD ERQHNYEVAL ACAESGLVQN DLIIILCQWD SQMQNKKQKT DTMVRNKTAM
EKIMLSCLEI LVLLTWPMEF GTNLSENQKL LFAQVRKIQV LHKKHILTYN DGQVLKAVIR
LALPVIAKTR IDREPRDNQI LRLVLYFTRN LLAIEPENDS ISTKTNNKRA TPSSNLPNGV
SPDDISINNL LRVFKKNKVL MLLLTITGSI NSEFEKDLFN EICLESVYLL IKGLEAKDVL
VNKPTSTTKM NTKTAAAAAT TATTATTTTT NTTSSVDISA TTPLQPLSST VGLQLQDLLN
TEAKKRQSQK QHIATRHGKF GTLLSIRSAD ANSYVVSGEE ALINSNGTMD KLDKSKTWKM
KNHFTYDSDE FVKTNSPIYL NAQGRQILSY FIEEFLSGGC FNNLIESMTS KLTSQLEYSL
IDELTQASYF YTIAWFLNYQ REQITLSGLQ TFDFGVVRAA LSEVNFILIV AYFRDSHQKR
LWNSLHVAMI CFKELLHISN SIFGKKRART TNDDTIGDDE QYEIDRELAE GIIRKLFSFN
EFLNTLVQVP QIAYKHSPRF LAESIRVITI ILKSFESFAK EDLQLYVQTK RRRNKKKQQR
INELDRDTES KLSTAIYESD EELAQENLRE VTRERKLNFQ ATEVRFFHQN VVTTYIEYMS
RFEDLTHEDI KMCLTYFHKL FVVRKDYNGL FRLDFMQLIY KLRNHLPKGS PIRLKVDEFI
YYFMKKFKLA ITRFPNPLEI LFPRFEETRF KHYLSTGELY QLDTAVDPRA IRNLNKEVID
NDYNDAVDND NNNDNYNEDD EDGIAFEIEA NPEAADNHAY DLDRLDELES QLTNYQSRNK
NRSSLEKGIA KKRNSRKKST KTSKVNSDGG DSDDDDDDAD AAAAAKAHRK RRVPRDLLFE
EPKPLRSAEF INDSDDESDD EKNAEFFARE ERLRQLLNQT GNITDAQKLE EFKKVWQQYS
KTGGSIMQDA VANAVKEVSL FISDGDDDDD DGNGNENQKG KRKRTRDEAD DFDGVSTILD
SVQSQVLDNG SSQGNFASDA EVYHASSNTS DTELETNKRA KIDDAEEKED EGKGEKEEDD
NADEDEDEDE DVDGEESFPV VHHKKKRAII SDDEE