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TOF1_COCIM
ID   TOF1_COCIM              Reviewed;        1171 AA.
AC   Q1DM35; A0A0D6K9N4; J3K6H1;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   25-MAY-2022, entry version 65.
DE   RecName: Full=Topoisomerase 1-associated factor 1;
GN   Name=TOF1; ORFNames=CIMG_08628;
OS   Coccidioides immitis (strain RS) (Valley fever fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX   NCBI_TaxID=246410;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RS;
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=RS;
RX   PubMed=20516208; DOI=10.1101/gr.103911.109;
RA   Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA   Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA   Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA   FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA   Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA   Taylor J.W., Rounsley S.D.;
RT   "Population genomic sequencing of Coccidioides fungi reveals recent
RT   hybridization and transposon control.";
RL   Genome Res. 20:938-946(2010).
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=EAS29882.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; GG704913; EAS29882.2; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_001241465.2; XM_001241464.2.
DR   AlphaFoldDB; Q1DM35; -.
DR   SMR; Q1DM35; -.
DR   STRING; 246410.Q1DM35; -.
DR   PRIDE; Q1DM35; -.
DR   EnsemblFungi; EAS29882; EAS29882; CIMG_08628.
DR   GeneID; 4560065; -.
DR   KEGG; cim:CIMG_08628; -.
DR   InParanoid; Q1DM35; -.
DR   OrthoDB; 839367at2759; -.
DR   Proteomes; UP000001261; 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..1171
FT                   /note="Topoisomerase 1-associated factor 1"
FT                   /id="PRO_0000301736"
FT   REGION          568..592
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          880..1171
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        880..908
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        949..991
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1004..1018
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1045..1074
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1086..1105
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1171 AA;  133840 MW;  3E6A7E20D7BAA9B0 CRC64;
     MEIEPPQAVE VVDPEVRSYV YSLVTALGGT AGNETGRYVL GDDALGCLRD LKKWLRFYDE
     KLNRMDVARC LAECKLLNGD LVPIISLYGD AEQSDKHKAR IMLACLELLV PLTWPVEVHG
     QMTFNHHRHT PYLQYSQVEY KRGILGFAPS PILRALIRVG LPSMAIPRSE RSTRDEGIIR
     LMLYFFRNIA VISSPPNLPI DSDDDKATRS ATINAFQQQD VFALLLTMCS NMGNDFTFQD
     VIILEILFNL VKGVDVDQLF KLNERAGTIK TDDLQDILQK EDELNREHSK NAPTRHGRFG
     TMIWVKRDDE KLSTVSGQDV LKGDRATFLK MDKTKKWNKP KFKREVVDPS SNNFNLKVRL
     TSSATKHLRT FVEEFLDSGF NPLFTHLRKA IEREADRVTE STSRQFWYAV SWFLHAERAR
     REHQKETRQR SKGTSREIEP DSFSLVASVL NQETFVGLNR FMQHSIDFKD WQDLTAGMKC
     LTQILLTVQE MAISPLEEDQ EIAENIQSRI FYEETTHDRV LSILRNYKDQ GFWYLDACTE
     LAHVFLRMLE QYSKQNVDMQ VRSRRRARRK QAQAAVPNQN ETEAGGEHDS DTEDIAEAHQ
     TVTERSFDFK RFSVRFCTQK SVDTFVALTK YYRELDSEQL KRAHRFFYRV AFKQDMSVLL
     FRVDIISLLF KMIKGPEGLD PSKPPFKDWE ELIRQIFKKL VRKLGERPEL VVELLFSKIN
     ATVFYLEYGH EKQTMSESRP ATELELKPGS ASTLDEKIRI VVSALIQEDK KPLVKWLSQV
     LGSAASERLS WEMEAEARAT SSPQEQSDRS KAPSIAVLPE DDGCRTAMFR NARLRLLMRL
     AGLERLDEDV LGASWMIPSS VPSSNLKEYH ELIEKHCESP AEDIDGVDPR DLMRRKRTAA
     DTDSSRHEFT ENVNFGSDSE GEDDGVLFPP NLPERSKALK TLKQRRRRRR RSDDAEESGP
     DEAVLEARRT AREKNALERQ RKIKSDLYVH ASDDESDEEA DIEFFAKEEM RRQAQARRVA
     EALETGMPEN NTTKKKSKAS AGRKRKVKPV LELDDDDSEA SPPKRRRSDE VIESDSDGEL
     MVGIGSTSPR RSQTPPTSAD NIFGSEKSPS PMFPWSVGVD QMMAKLQGKD EASADNGESN
     EDEGEDVLSG TGRTRRRRTM GGFVIGSDSD S
 
 
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