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TOF1_ASPCL
ID   TOF1_ASPCL              Reviewed;        1178 AA.
AC   A1C928;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 60.
DE   RecName: Full=Topoisomerase 1-associated factor 1;
GN   Name=tof1; ORFNames=ACLA_053980;
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS   NRRL 1 / QM 1276 / 107).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=344612;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027048; EAW13352.1; -; Genomic_DNA.
DR   RefSeq; XP_001274778.1; XM_001274777.1.
DR   AlphaFoldDB; A1C928; -.
DR   SMR; A1C928; -.
DR   STRING; 5057.CADACLAP00005220; -.
DR   PRIDE; A1C928; -.
DR   EnsemblFungi; EAW13352; EAW13352; ACLA_053980.
DR   GeneID; 4707118; -.
DR   KEGG; act:ACLA_053980; -.
DR   VEuPathDB; FungiDB:ACLA_053980; -.
DR   eggNOG; KOG1974; Eukaryota.
DR   HOGENOM; CLU_004390_0_0_1; -.
DR   OMA; WLKLYDE; -.
DR   OrthoDB; 839367at2759; -.
DR   Proteomes; UP000006701; 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..1178
FT                   /note="Topoisomerase 1-associated factor 1"
FT                   /id="PRO_0000301728"
FT   REGION          576..596
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          792..811
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          896..965
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          980..1178
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        936..965
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1003..1055
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1083..1099
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1115..1132
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1178 AA;  135716 MW;  2E86E4A0AF1323D0 CRC64;
     MDDEGAPLSE SAQVVDPDVR AHVYSLVTAL GGFNGENADR YVLGDDALAC LRDIKRWLKL
     HDEKNNRMDV ARCLGEANLV NGDLLPILTL WSTSGQNSKF MSRIALACLE LLVPLTWPLE
     LHSEMTVNHH RHTPYLQQAQ VLYKRGILGP GGSSLLRTII RIGLPSMAVP RSDRTTRDEG
     ILKLMLYLLR NIAVISPHSR LSAEGDEEET SRSATINAFQ DQDAFALLLT MCSNVADDFN
     LQDVVLLEIL FHIVKGVNVE KLFMNDTQRK AKRTEELGDL LQKESSLRRE YAKNAPTRHG
     RFGTMIWVKR DDAKVSTVSG QDVLKDSQTT LYKMDQSKKW NKPQVRRRQT EVTVNNDFNT
     PVNLNSTATK NLRIFIEEFL DSGFNPLFTH VRKAIEREAD RIMDINSRHY FYTVAWFLEA
     ERVRRKYQRE RHSQEDKSLK KMEPDSFALV ASVLNQETFV FLNRSMQKSF DNKEVEDLTA
     EMRCFTQILL TVQEMAQSPL DDDQEVADNI QNRIFYEETT HDRIISIIRG YKDQGFGYLD
     ACTQLAHVFL RMLEHYSKEN VDMQIRSRRR IKRKAKQDDQ AIDVEDEEHA SEDEELMEAE
     RVSKERKFDF KRFAAKFCNQ KCVDTFVAFI KYYKELNTDQ LKRAHRYFYR IAFKQEMSVL
     LFRLDIINLF YRMIKGPGAL DSSKPIFKEW EELVRQILRR MIKKIDQRPA LITELLFSKI
     NSTVFYLEFG FEKQTISVSK RPPAELEVDP REAKTTDEKL SIVVRVMIKD EHINLVKWIS
     EVLRLAADER ESWESREQQP GEPTAPNPMI PVKPDDEACQ KAMFSNAKLR LLMTLIGFER
     LGMEDVPGAS WVVPSSFTSD DLRHTKRVID QCLIEPATED PDQDLSRLIR RKYANDARGG
     GRDEQNLDID FGSDSEGEDN VPDGPLFPPN HRSKANALDQ LKKQRQKRRK EDGDRETPDD
     EVLEERRRAR LENALARQAK IKSDLYIHAS DEESDEEADE EFFRLEEQRR KEQAARIKHA
     LLHGVVEEIS DKSSKKTGRK RQSDQHTTLN IDAHTKRQRR KNRTDKLDEG DDLVMAGTEA
     QSPDSPGLGS SSHDAKGIEN TPLTSDEDEL EFDDDLAFSR DRNRRKDFTP NVDKMVIEPA
     QQDADPAAPD EDDDEDAPVV GSSRRRVRGG FVIESDSE
 
 
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