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DEF1_CLAL4
ID   DEF1_CLAL4              Reviewed;         671 AA.
AC   C4Y1P0;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   25-MAY-2022, entry version 31.
DE   RecName: Full=RNA polymerase II degradation factor 1;
GN   Name=DEF1; ORFNames=CLUG_02122;
OS   Clavispora lusitaniae (strain ATCC 42720) (Yeast) (Candida lusitaniae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Metschnikowiaceae; Clavispora.
OX   NCBI_TaxID=306902;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42720;
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: RNA polymerase II degradation factor recruits the
CC       ubiquitination machinery to the RNA polymerase II for
CC       polyubiquitination, removal and degradation, when RAD26 fails to
CC       efficiently displace stalled RNA polymerase II. Also involved in
CC       telomere length regulation (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome, telomere
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DEF1 family. {ECO:0000305}.
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DR   EMBL; CH408077; EEQ37999.1; -; Genomic_DNA.
DR   RefSeq; XP_002618663.1; XM_002618617.1.
DR   AlphaFoldDB; C4Y1P0; -.
DR   SMR; C4Y1P0; -.
DR   STRING; 306902.C4Y1P0; -.
DR   EnsemblFungi; EEQ37999; EEQ37999; CLUG_02122.
DR   GeneID; 8499323; -.
DR   KEGG; clu:CLUG_02122; -.
DR   VEuPathDB; FungiDB:CLUG_02122; -.
DR   HOGENOM; CLU_438800_0_0_1; -.
DR   InParanoid; C4Y1P0; -.
DR   OMA; EPANVHV; -.
DR   Proteomes; UP000007703; Unassembled WGS sequence.
DR   GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0043130; F:ubiquitin binding; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   InterPro; IPR003892; CUE.
DR   Pfam; PF02845; CUE; 1.
DR   PROSITE; PS51140; CUE; 1.
PE   3: Inferred from homology;
KW   Chromosome; DNA damage; DNA repair; DNA-binding; Nucleus;
KW   Reference proteome; Telomere; Ubl conjugation pathway.
FT   CHAIN           1..671
FT                   /note="RNA polymerase II degradation factor 1"
FT                   /id="PRO_0000405666"
FT   DOMAIN          22..65
FT                   /note="CUE"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00468"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          66..266
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          294..439
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          480..516
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          546..577
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          601..651
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        12..27
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        67..85
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        138..158
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        164..189
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        222..236
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        331..373
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        400..414
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        424..439
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        495..515
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        546..564
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        610..627
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   671 AA;  72398 MW;  28C271010BC248AF CRC64;
     MSQRKNHRGQ QKKAAASPSK SAASSQLQTL SEMFPAWEAD ELAALLSEHH DDVEIVIDLI
     VNNKVSKWEP IKKEPKPKKR EEVITDSNAT QTSHAHNDAK PKHSRERPKN EKRRERKPVQ
     RKEPSAAVQA AQAASPAPAA AASTSSTSSA SVPSNSWAAA LSKDAKPKQK KEEPEVKEPA
     QEQEQPKEEQ EPAVAAATAA AASAASAPQE TQAAPAAPAA PVAPTTTTTN DHAEKPATTW
     ASAIKPKAKP IKKKAPEHVP EEEVSEVVVV ETEVSDVVLP QQVAEVGVSF GSLALETEDV
     PESQPEAQPK PEAQPESQPE PEVQPEAEPE IQQEPVQQEQ VQPQQVQQQV QSQPEQPQQP
     VPVQTQEQPQ QPQQPQQPQQ PQQPQAQQPQ QPQQPQQPQQ PQQQPQQQGQ QPPHFEKPAQ
     GYDYYPQFQQ TQQYQQAAGS VPGQYAYPSF DYSAAYGQLG QAGLGSVASP GYYPAAVNGA
     AKPAAPAPAS AEIGQSPLVQ PNNMGQQSMQ SGQAQVPGAA PFGYPNYYNY FYNTPFYGNG
     GMAASTTSYG AQQQPQSQQA AGENAPASGE PETNGVPAQA QANNQYYAQY YGQPNQFGSR
     GGYPYSGYPA SQPYPQSAGQ EQPEGAQPSA PQGAPVPGVP SYPQQMPQYG AYQQFPQYGS
     YQDSNQYRGW Y
 
 
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