ID A0A1Y2E0Y9_9PEZI Unreviewed; 503 AA.
AC A0A1Y2E0Y9;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=BCR38DRAFT_408759 {ECO:0000313|EMBL:ORY65014.1};
OS Pseudomassariella vexata.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Pseudomassariaceae; Pseudomassariella.
OX NCBI_TaxID=1141098 {ECO:0000313|EMBL:ORY65014.1, ECO:0000313|Proteomes:UP000193689};
RN [1] {ECO:0000313|EMBL:ORY65014.1, ECO:0000313|Proteomes:UP000193689}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 129021 {ECO:0000313|EMBL:ORY65014.1,
RC ECO:0000313|Proteomes:UP000193689};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) 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:ORY65014.1}.
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DR EMBL; MCFJ01000006; ORY65014.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2E0Y9; -.
DR STRING; 1141098.A0A1Y2E0Y9; -.
DR InParanoid; A0A1Y2E0Y9; -.
DR OrthoDB; 5474929at2759; -.
DR Proteomes; UP000193689; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd16454; RING-H2_PA-TM-RING; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR15710; E3 UBIQUITIN-PROTEIN LIGASE PRAJA; 1.
DR PANTHER; PTHR15710:SF228; FINGER DOMAIN PROTEIN, PUTATIVE-RELATED; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000193689};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 332..373
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 72..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 227..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 381..503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..406
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..483
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 503 AA; 54154 MW; 36EB8D2D651D7749 CRC64;
MESNSSDRGG RHLDASADRE VVYCHQCEHE WYRDQGGLIC PNCDGEATEI VTPENDPRNM
EDDFALPGFD HHHRHLHDTD SDPEEDDIEE HLAHGPGGFF GRRTLFRAPG DPEAVYRSRA
HPENSDDIIR RFTEMLGDIG GPNLGPPAVT GRSGPATLFS GPGGQGGPGL GEPRVSYTTF
HGPGFTGNVS SYTITSSSGG QSRTIRGGNR LGGAEDPFQS IFGNIFGHVG PPPGARNDPT
SPDAPGGPGA PQEGRVDLAA ALNQLFASVL NPTAVHGDAV YSQEALDRII TNLMEANPQS
NAPPPASPET IAKLPRKKLD EQMLGPELKG ECTICIDEMH VEDEVIVLPC KHWFHEACVT
LWLKEHNTCP ICRTAIDGSV ASESGATPSS ARPQVSSSSS SRVNMSSDRS ERLRSNLQQR
GEARLNSIRD MASPYDRGGS SRGNSNSPPL NSAFAQSSRD RSPSPATRRS TQSDQTRESS
GSGSGGPLHW LRDQFSRGER RRS
//
