ID A0A229WK54_9EURO Unreviewed; 284 AA.
AC A0A229WK54;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=CDV55_100477 {ECO:0000313|EMBL:RHZ44193.1}, CFD26_100497
GN {ECO:0000313|EMBL:RLL92894.1};
OS Aspergillus turcosus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1245748 {ECO:0000313|EMBL:RHZ44193.1, ECO:0000313|Proteomes:UP000215394};
RN [1] {ECO:0000313|Proteomes:UP000215289, ECO:0000313|Proteomes:UP000215394}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMR AF 1038 {ECO:0000313|EMBL:RLL92894.1}, and HMR AF 23
RC {ECO:0000313|EMBL:RHZ44193.1};
RA Parent-Michaud M., Dufresne P.J., Fournier E., Martineau C., Moreira S.,
RA Perkins V., De Repentigny L., Dufresne S.F.;
RT "Draft genome sequences of two Aspergillus turcosus clinical strains
RT isolated from bronchoalveolar lavage fluid: one azole-susceptible and the
RT other azole-resistant.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900};
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:RHZ44193.1}.
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DR EMBL; NKHV02000566; RHZ44193.1; -; Genomic_DNA.
DR EMBL; NIDN02000728; RLL92894.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A229WK54; -.
DR STRING; 1245748.A0A229WK54; -.
DR OrthoDB; 313431at2759; -.
DR Proteomes; UP000215289; Unassembled WGS sequence.
DR Proteomes; UP000215394; Unassembled WGS sequence.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR InterPro; IPR003613; Ubox_domain.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR46803; E3 UBIQUITIN-PROTEIN LIGASE CHIP; 1.
DR PANTHER; PTHR46803:SF2; E3 UBIQUITIN-PROTEIN LIGASE CHIP; 1.
DR Pfam; PF04564; U-box; 1.
DR SMART; SM00504; Ubox; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS50005; TPR; 1.
DR PROSITE; PS51698; U_BOX; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000215289};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT REPEAT 2..35
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 208..281
FT /note="U-box"
FT /evidence="ECO:0000259|PROSITE:PS51698"
FT COILED 150..195
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 284 AA; 32016 MW; 563DA42D03C9FF06 CRC64;
MSFELKEKGN QLFKEGDYNG AEELYSQAIQ KNPREPTFFT NRALTRIRLE KWAGVEHDAR
AAIELYGPKN PSSLKSCWYL AQALLGLQRP QEAYEVAIDA YRASLAAKSP QTENLSKTVL
RAKQQIWAAK ETSRLREMSD TLATVEALIE ADLNRELAEL QARLDKGEIG QTGFVEDQKA
LHADAEKHIQ NVREAFRIAS NGDIQERVVP DYLVDGITFE IMHDPVITPS GTSFDRIGIV
KYVEQSGVDP ITRTPMTVND LRPNYALKAA CEEFLNKNGW AVDW
//
