(data stored in ACNUC7421 zone)

SWISSPROT: Q4W9M4_ASPFU

ID   Q4W9M4_ASPFU            Unreviewed;       333 AA.
AC   Q4W9M4;
DT   05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2005, sequence version 1.
DT   11-DEC-2019, entry version 86.
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_4G04415 {ECO:0000313|EMBL:EAL84589.1};
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:EAL84589.1, ECO:0000313|Proteomes:UP000002530};
RN   [1] {ECO:0000313|EMBL:EAL84589.1, 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:EAL84589.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AAHF01000016; EAL84589.1; -; Genomic_DNA.
DR   RefSeq; XP_746627.1; XM_741534.1.
DR   EnsemblFungi; EAL84589; EAL84589; AFUA_4G04415.
DR   GeneID; 3503986; -.
DR   KEGG; afm:AFUA_4G04415; -.
DR   EuPathDB; FungiDB:Afu4g04415; -.
DR   HOGENOM; HOG000170497; -.
DR   InParanoid; Q4W9M4; -.
DR   OMA; TAMANEQ; -.
DR   OrthoDB; 1140368at2759; -.
DR   Proteomes; UP000002530; Chromosome 4.
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; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR11685; PTHR11685; 1.
DR   Pfam; PF01485; IBR; 2.
DR   SMART; SM00647; IBR; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q4W9M4.
DR   SWISS-2DPAGE; Q4W9M4.
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          104..148
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          39..61
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   333 AA;  36658 MW;  8FB7345FE652E553 CRC64;
     MPSITLSSFI SGLIHSRAEE ERLHASDVEK IAPLGAASDK KAISTGARRA ASRRNMDVRP
     APGKSDLHLQ AHIAGLKNLC VFPRLGVIDN MARLYQGIRK KERCTVCFNS ESIKNVEILP
     CQHIYCDYCF SRLALTAMAN EQLFPPRCCS QMIPTEQVLS KLTEKEKALF KLKAREYATS
     ARERRYCPAM KCGKWIPLEK LEGQSTTQLC PYCGTAICPG CKDKAHAPGK CSFDPGLTEF
     LELARTQGWQ RCFHCGAMVE LNEGCPRITC RCGADLCYNC GGPWLICHHN ALGNVIAECQ
     TGAPLGDGMG THDAVELAAI VAAMKFAERE LEE
//

If you have problems or comments...

PBIL Back to PBIL home page