ID   TOF1_CHAGB              Reviewed;        1251 AA.
AC   Q2HBI0;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   25-MAY-2022, entry version 44.
DE   RecName: Full=Topoisomerase 1-associated factor 1;
GN   Name=TOF1; ORFNames=CHGG_02424;
OS   Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS   NRRL 1970) (Soil fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX   NCBI_TaxID=306901;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970;
RX   PubMed=25720678; DOI=10.1128/genomea.00021-15;
RA   Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT   "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL   Genome Announc. 3:E0002115-E0002115(2015).
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; CH408030; EAQ90489.1; -; Genomic_DNA.
DR   RefSeq; XP_001228940.1; XM_001228939.1.
DR   AlphaFoldDB; Q2HBI0; -.
DR   SMR; Q2HBI0; -.
DR   STRING; 38033.XP_001228940.1; -.
DR   PRIDE; Q2HBI0; -.
DR   EnsemblFungi; EAQ90489; EAQ90489; CHGG_02424.
DR   GeneID; 4389167; -.
DR   eggNOG; KOG1974; Eukaryota.
DR   HOGENOM; CLU_004390_0_0_1; -.
DR   InParanoid; Q2HBI0; -.
DR   OMA; WLKLYDE; -.
DR   OrthoDB; 839367at2759; -.
DR   Proteomes; UP000001056; 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..1251
FT                   /note="Topoisomerase 1-associated factor 1"
FT                   /id="PRO_0000301735"
FT   REGION          328..354
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          564..601
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          901..1021
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1041..1251
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        901..916
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        917..934
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        967..1021
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1077..1099
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1102..1120
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1159..1177
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1185..1206
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1251 AA;  140834 MW;  B8AC10E031B533F3 CRC64;
     MEDVGVNNDT VHPEARAYIT SLVSALGGYG VDDDGGYTLG DDALEVLRDL KRWVRFYDER
     TNRMDVARCL AESNLVTSDL LQIMAKWVSN ESSSKYMERI AFACLEIMVP LTWPIERDSE
     TMTVNHHRHL PVLQLAQLGY KRAIINFDVA PILSTAVRIA LPCMAIPNGD RSSRDQATIK
     LILYFLRNIA MIAPPPGLKY EGDETQVSRS TLIDAFTFQD IFLTILTIAS NMGEDFRTED
     VIILDIIFHI VKRVDSSKLF VSEKRLHKIK EDELTAAMRK EAAMLKSYNK NAPTRHSRFG
     TMIWVKRESG KLATVSGQDA LLDAATRERK MDSNKSFKPP RRARKEDMEP KDLGPRVSLD
     ERARRQLQSF VSEFLDSGFN PLFSHVRRSL DREAPHVLQS HHSQFFYLVA WFLEAERMRK
     KAAKDSKNQT STGEDVGSFN LVAEVLNQEM FITMSRTLDR AYGDKDWRLL TTVMRCFTQI
     LLTIQEMASS GNEENEEIAD NILSRLFYEE TTHDLIANIV RTYKDQGFEY LDACTELTHT
     FVRILEAYSK ENVDLQVRSR KRTRRKKKAA KAAGDQGDDE GQGDAEDDSA DDERQAEKTS
     QERKFDFKRF ALRFAPQGVV DTFVTFTKYY RDLDDSQLKR AHRYFFKLAF KQDMSVMLFR
     LDIIHLFYNM IKGPEPLDKS SSMYKEWEDL AMQTIRKCVK KLEERPALFT ELLFSKITST
     AHYLEYGHEK QTISNPRPAA ELEFKREVER EQQIAILVGV LIDRSQTDHL GWIKKQLSDA
     ESERRAWENA ERALAAERPD DEVMAGSAEA IAAKTPDHVT MRPDTDARRT AMFKNPHLRL
     LMKLVGLERL APTLDETPDA IWIIPGTLTA DALKETISLI NKAEFTPPIF DDGELAEDQL
     RRKTAPRKRA AYDDDDNLDG INDLINDGSD DDGDDGTGIL FPAGGPTARK RTAQDEPPKK
     RLQRRRRRGG SDDPDADTAE TDAQAEARAR ARRKKELEKA RKIKSEMYVD PREDDSDYEG
     NKERDRLFFA REEERQAVKD ATFGLSSRPE GVGEGAWEAL VGAVMGGGDG DDGEGEDAVV
     GERPPKVGGR KRKSGVADLA ESGGEDSEEG DEDDESRSEE DGSAVSEAEA PAAAGRRPNK
     RRKPAQKKKK RVVDISSGED DDVGMDMDVD VDADADADAM DFTQSSKDGA VTNDTPLSSD
     PSRTTKPGGA EGSGDKGGGE DEDEDMPVAK PVARARPRAR AGFIVESSDE E