ID A0A2V5HZW0_9EURO Unreviewed; 284 AA.
AC A0A2V5HZW0;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=BP00DRAFT_448535 {ECO:0000313|EMBL:PYI29341.1};
OS Aspergillus indologenus CBS 114.80.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1450541 {ECO:0000313|EMBL:PYI29341.1, ECO:0000313|Proteomes:UP000248817};
RN [1] {ECO:0000313|EMBL:PYI29341.1, ECO:0000313|Proteomes:UP000248817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 114.80 {ECO:0000313|EMBL:PYI29341.1,
RC ECO:0000313|Proteomes:UP000248817};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (FEB-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};
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DR EMBL; KZ825533; PYI29341.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V5HZW0; -.
DR Proteomes; UP000248817; 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 CDD; cd16654; RING-Ubox_CHIP; 1.
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; IPR045202; CHIP_RING-Ubox.
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; SM00028; TPR; 2.
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 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"
SQ SEQUENCE 284 AA; 32038 MW; 0F2DB1E8D5959528 CRC64;
MAFELKEKGN QLYKAGDYAS AEEMFSQAIQ KNPKEPTFFS NRAITRMKLE NWAGVEHDAR
AAIDLYGAKN PASLKSRYYL AQALLELQRP QEAHEIATEA YQASLAAKNV QSENLSRAVL
RAKQQLWAAK EAARVREMNG TLASVERLIE ADLQRALDDL QGQLDRGEIG QIGFSEDQKA
LRDDTEKTLQ VLRETFAIAS KGEVQERVVP DYLIDPITFE IMHDPVITPS GTSFERVAIT
KYVEQSKVDP ITRVPMTADD LRPNYALRGV CEEFLEKNGW AVDW
//
