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DEF1_ZYGRC
ID   DEF1_ZYGRC              Reviewed;         757 AA.
AC   C5E4K0;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   25-MAY-2022, entry version 52.
DE   RecName: Full=RNA polymerase II degradation factor 1;
GN   Name=DEF1; OrderedLocusNames=ZYRO0E06754g;
OS   Zygosaccharomyces rouxii (strain ATCC 2623 / CBS 732 / NBRC 1130 / NCYC 568
OS   / NRRL Y-229) (Candida mogii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Zygosaccharomyces.
OX   NCBI_TaxID=559307;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2623 / CBS 732 / BCRC 21506 / NBRC 1130 / NCYC 568 / NRRL
RC   Y-229;
RX   PubMed=19525356; DOI=10.1101/gr.091546.109;
RG   The Genolevures Consortium;
RA   Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA   Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P., Jubin C.,
RA   Poulain J., Barbe V., Segurens B., Artiguenave F., Anthouard V.,
RA   Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R., Durrens P.,
RA   Jean G., Marck C., Martin T., Nikolski M., Rolland T., Seret M.-L.,
RA   Casaregola S., Despons L., Fairhead C., Fischer G., Lafontaine I., Leh V.,
RA   Lemaire M., de Montigny J., Neuveglise C., Thierry A., Blanc-Lenfle I.,
RA   Bleykasten C., Diffels J., Fritsch E., Frangeul L., Goeffon A.,
RA   Jauniaux N., Kachouri-Lafond R., Payen C., Potier S., Pribylova L.,
RA   Ozanne C., Richard G.-F., Sacerdot C., Straub M.-L., Talla E.;
RT   "Comparative genomics of protoploid Saccharomycetaceae.";
RL   Genome Res. 19:1696-1709(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; CU928181; CAR30961.1; -; Genomic_DNA.
DR   RefSeq; XP_002499216.1; XM_002499171.1.
DR   AlphaFoldDB; C5E4K0; -.
DR   SMR; C5E4K0; -.
DR   STRING; 559307.C5E4K0; -.
DR   EnsemblFungi; CAR30961; CAR30961; ZYRO0E06754g.
DR   GeneID; 8204771; -.
DR   KEGG; zro:ZYRO0E06754g; -.
DR   HOGENOM; CLU_023119_0_0_1; -.
DR   InParanoid; C5E4K0; -.
DR   Proteomes; UP000008536; Chromosome E.
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   CDD; cd14368; CUE_DEF1_like; 1.
DR   InterPro; IPR003892; CUE.
DR   InterPro; IPR041803; DEF1_CUE.
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..757
FT                   /note="RNA polymerase II degradation factor 1"
FT                   /id="PRO_0000405673"
FT   DOMAIN          21..63
FT                   /note="CUE"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00468"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          69..521
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          556..575
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          664..703
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        69..86
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        87..103
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        118..166
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        194..212
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        213..262
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        312..329
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        342..385
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        400..521
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   757 AA;  83228 MW;  4BBF5D50E71C9175 CRC64;
     MSAQSRKSNS HNGKNSRVNP EIKFKLETLT ELFPDWTNDD LIDLVHEYDD LETIIDKITS
     GAVTRWDEVK KPSKKERLEK RLEQQQQLQK EQQQHQLQQQ HYHAQDLDGH HGGSSSHHHT
     KAGQGSGSRY SRDNNGTHSS SGGSNAKSKK QQQQQQQQQN GKPSLPSDNA RAAISRGKPA
     SGGGSWAAVA SSDSKKHQQE EEEEEDQQQQ RPESSPEEPS ATTVQASETK TDGVEASASA
     TSTAQSSTHA TATASTGNAA HNEKPKKMSW AAIAAPKPKV VQKKQSSLNN VGGLKKEINE
     VAKETETPAA GQAQREPVSE TNDKATNNQG KKADAQHEDT ASKLSEQQQQ QQEQLQAQQQ
     EQQQTQQQDQ SPIEFQSQGT NQEDTAQHNR PEEQKDTREI TSNQVQIDEQ EVAATSEPQE
     PSQTAQAVAT EVNDGSKVKQ QQQQPTVGVE AGKPQQQQQQ EAYYQQQQQQ QQQQQQQYFA
     QQQQYAQSQT PQHAPQQLSG QQAAVGQPNA NANASANANA AAAATAAQQQ YYMYQNQFPG
     YTYPGMFDSP SYAYGQQQAY QQPSQPSAQA GFGTGTASQY SIPQGYAAAP AADMTTASTA
     TASPVAGHAQ PQQQQPYGGS FLPYYAHFYQ QSFPYAQPQY GMAGQYPYQV PKAGYNYYQP
     QRQTQGRNVQ QGQQSPGHSP SQQGEDVQQQ SQPTQQNQLQ NGQQPLNPQQ LQFQQYYQFQ
     QQQQAAAAAA AAAAAQQGLP YGYTGYDYTS QASRGFY
 
 
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