TOF1_DEBHA
ID TOF1_DEBHA Reviewed; 1299 AA.
AC Q6BPI8; B5RU06;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 25-MAY-2022, entry version 70.
DE RecName: Full=Topoisomerase 1-associated factor 1;
GN Name=TOF1; OrderedLocusNames=DEHA2E13288g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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: Involved in chromosome segregation during meiosis and DNA
CC damage repair. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the timeless family. {ECO:0000305}.
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DR EMBL; CR382137; CAR65818.1; -; Genomic_DNA.
DR RefSeq; XP_002770475.1; XM_002770429.1.
DR AlphaFoldDB; Q6BPI8; -.
DR SMR; Q6BPI8; -.
DR STRING; 4959.XP_002770475.1; -.
DR EnsemblFungi; CAR65818; CAR65818; DEHA2E13288g.
DR GeneID; 8998743; -.
DR KEGG; dha:DEHA2E13288g; -.
DR VEuPathDB; FungiDB:DEHA2E13288g; -.
DR eggNOG; KOG1974; Eukaryota.
DR HOGENOM; CLU_008440_0_0_1; -.
DR InParanoid; Q6BPI8; -.
DR OMA; WLKLYDE; -.
DR OrthoDB; 839367at2759; -.
DR Proteomes; UP000000599; Chromosome E.
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..1299
FT /note="Topoisomerase 1-associated factor 1"
FT /id="PRO_0000301738"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 338..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1052..1134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1209..1299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..41
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1052..1069
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1070..1097
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1098..1134
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1209..1252
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1253..1299
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1299 AA; 149139 MW; 77B5A6AEA311F663 CRC64;
MSRSGSEEER FSSDEGMEEL GDFIVSDEEP NHESARDDDA EVHNDRLLQM TSTLKPNESQ
TQKLLRAHIS VLVSALGGPD HTSPISPPPY KLGQDALACL KDIKRWIKSV DEKKGNFDVA
LACADSGLVV NDLLVILCQW DSQQNSKKPL KNARTMEKIM LSCLELLVLL TWPTDLNSES
SENQKLHFAS VRKSQIVYKK HILAYNKGQT LKAVIRLVLP TIAKHRIDRE PRDNAILRLV
LFFIRNVLNI EPANSSISTK SRKHVTNLDN LPTNVNYDDI SMNAVLSCFK NNKVLMFLLT
LSGSLGTDFD KETFGQPCLE CIYLIIKGVK TQDILNPQQN SKQQQRYQQQ QREQSQQDQN
PIQSVTTTSG LELQDLLSEE SKRKKFQTQN ISTRHGRFGS LLSIQGNNTS YVISGQEALL
DTNSSLAKLD ESKKWNNRSH FKYDSDDYVK ATSEFLNGSS VIILKEFIEQ FLSGGCFNTL
IECIGWLLSG TNDLNYVDDY EKACYFLTVA WFLNYKRERN VLFDILGTAN LDEDDDGLDY
GSVSAGLSEV NFILIISYFR ESFEAKNWNS LHVAMICFKE LLLISYSIFS RFSDRGLQGE
EEADDDQEEI DKELAEGIIR KLFSFNDFLN IVIQIPQTAS KHSPEYLSVC ISVVHIILKS
FESFANENIK LYIQTKRKRT KQNKKSINTL DKATEESLRD VIEGSDDELE NERVKEVSRE
RRLDFKVTEV RFFQTSIVST YVEYLSRYEE LTHEEIKRCL SYFHRLFVIR KDFTGLYRMD
FMYILQKLRS YLPKGSSTRD HVDEFIYYFM KKFKNAFERF PNPVEILFPR FEDMEYKIFL
ATGDLYLKPE KNNKRSSVKI AKNIEFIRDN FSLDEKLKIL VTVLYIQEKE SLVTWVIQEL
TKITTNRLMN LSSEQIESNT NEAVQLYPLE QHRRLLINNP YIRLLLTLVG FKVPFILEEP
CELPDNVETS NLTECLDSIK MWSNKQPVTF DDGKDAMFFL RTKEGYNYEQ DDDYDGHYDE
NDESIAFETG ANPDGERHNL NELDELDKLE AALEGKSNKD TDLPRGVARI KNKKPKKDLP
KKSKANSRKK HLSRRPPKSF KVVSDGEEEK QEKTKSAEFV HGSDDESDYE KENEFFDREE
RLRRLLEESG GIVNPKQLAE FKVSWSKLES SNGTDTAISV SKAIENTSFV EDTMPHTQNI
PEELTLGAIN ESNSDIDTSS DSEPELNGSG AESVSAIEND KTSVSSFTPD IHNETSSKKR
HIILQDRDSE DEVDITTGNH EIKASNPRKR RVVISDDEE