(data stored in SCRATCH zone)

SWISSPROT: Q4WDC1_ASPFU

ID   Q4WDC1_ASPFU            Unreviewed;       620 AA.
AC   Q4WDC1;
DT   05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2005, sequence version 1.
DT   11-DEC-2019, entry version 95.
DE   RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|SAAS:SAAS01037474};
DE            EC=2.3.2.31 {ECO:0000256|SAAS:SAAS01037474};
GN   ORFNames=AFUA_6G04230 {ECO:0000313|EMBL:EAL85617.1};
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=330879 {ECO:0000313|EMBL:EAL85617.1, ECO:0000313|Proteomes:UP000002530};
RN   [1] {ECO:0000313|EMBL:EAL85617.1, ECO:0000313|Proteomes:UP000002530}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100
RC   {ECO:0000313|Proteomes:UP000002530};
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.,
RA   Fedorova N., Fedorova N., Feldblyum T.V., Fischer R., Fosker N., Fraser A.,
RA   Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B., Haas H., Harris D., Horiuchi H.,
RA   Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K.,
RA   Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafon A., Latge J.P.,
RA   Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y.,
RA   Molina M., Monod M., Mouyna I., Mulligan S., Murphy L., O'Neil S.,
RA   Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A.,
RA   Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H.,
RA   Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M.,
RA   Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D.,
RA   Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G.,
RA   Vazquez de Aldana C.R., Weidman J., White O., Woodward J., Yu J.H.,
RA   Fraser C., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.,
RA   Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.;
CC         EC=2.3.2.31; Evidence={ECO:0000256|SAAS:SAAS01116878};
CC   -!- SIMILARITY: Belongs to the RBR family. {ECO:0000256|SAAS:SAAS00692262}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EAL85617.1}.
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DR   EMBL; AAHF01000012; EAL85617.1; -; Genomic_DNA.
DR   RefSeq; XP_747655.1; XM_742562.1.
DR   STRING; 746128.CADAFUBP00009144; -.
DR   EnsemblFungi; EAL85617; EAL85617; AFUA_6G04230.
DR   GeneID; 3505156; -.
DR   KEGG; afm:AFUA_6G04230; -.
DR   EuPathDB; FungiDB:Afu6g04230; -.
DR   HOGENOM; HOG000201485; -.
DR   InParanoid; Q4WDC1; -.
DR   KO; K11971; -.
DR   OMA; HTSPCPT; -.
DR   OrthoDB; 1188714at2759; -.
DR   Proteomes; UP000002530; Chromosome 6.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0000151; C:ubiquitin ligase complex; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IBA:GO_Central.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR   GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR031127; E3_UB_ligase_RBR.
DR   InterPro; IPR002867; IBR_dom.
DR   InterPro; IPR006575; RWD-domain.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR11685; PTHR11685; 1.
DR   Pfam; PF01485; IBR; 1.
DR   Pfam; PF05773; RWD; 1.
DR   SMART; SM00647; IBR; 2.
DR   SUPFAM; SSF54495; SSF54495; 1.
DR   PROSITE; PS50908; RWD; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q4WDC1.
DR   SWISS-2DPAGE; Q4WDC1.
KW   Metal-binding {ECO:0000256|SAAS:SAAS00468077};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002530};
KW   Repeat {ECO:0000256|SAAS:SAAS01001854};
KW   Transferase {ECO:0000256|SAAS:SAAS01110310};
KW   Ubl conjugation pathway {ECO:0000256|SAAS:SAAS01110306};
KW   Zinc {ECO:0000256|SAAS:SAAS00468092};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175,
KW   ECO:0000256|SAAS:SAAS00099736}.
FT   DOMAIN          13..162
FT                   /note="RWD"
FT                   /evidence="ECO:0000259|PROSITE:PS50908"
FT   DOMAIN          202..236
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          514..546
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          570..595
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   620 AA;  69941 MW;  9D41E30F2A561ABF CRC64;
     MTGSDLSEDE RSVELSSITA IYPEIKIDPT SPFKASLDIP VKPSTPLPVC FEQQLDAGFP
     EVLTPPTSLD ASDVELGFAT KDDGRDVHTL SYLPPLRLEI DLPEGYPSEK APIFRLETNP
     PWLSHSIILR LTEDGNRLWE DCGRDLVVYT YIDHLQQLAE TAFSVSDTAD QEVRLPRDIK
     IALLDFNNKA EREKFEQETF ECGVCLEPKK GSVCHRLLLC SHVFCVSCLQ DFYNNCITEG
     DVDSVKCLSP DCGKKKNDIA EAGNQLKKRK KHDRTLSPSE LLQIPLDQET VQRYVSLKRK
     KKLESDKSTV YCPRQWCQGA ARSKKHPKPI DPMSDDVESS DEEEGFVFDP NGDEAQLPPM
     ADRVAICEDC NYAFCSVCKK GWHGELVRCF PRREAELSAE EKATEEYLRL YTSPCPTCDA
     PCQKRMGCNH MICFKCRTHF CYLCSSWLSE DNPYRHFNDI NSRCYNRLWD LEGGDGIDPE
     GPEALHRIPN DLVVFDEPSD DEGAPILEFR EAEVAHRRRP PPPAPVPPQV NQAAGGHGHR
     NRGNDANVLD AAGRAAAAER QAQARAIAEV RARPRQHDGP VAVQPPRPGR IHRPGLQRFL
     DLVQNDREDE WDSDELDDDF
//

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