ID A0A1E3HML1_9TREE Unreviewed; 667 AA.
AC A0A1E3HML1;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, 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=L202_04737 {ECO:0000313|EMBL:ODN77568.1};
OS Cryptococcus amylolentus CBS 6039.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus.
OX NCBI_TaxID=1295533 {ECO:0000313|EMBL:ODN77568.1, ECO:0000313|Proteomes:UP000094065};
RN [1] {ECO:0000313|EMBL:ODN77568.1, ECO:0000313|Proteomes:UP000094065}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 6039 {ECO:0000313|EMBL:ODN77568.1,
RC ECO:0000313|Proteomes:UP000094065};
RA Cuomo C., Litvintseva A., Heitman J., Chen Y., Sun S., Springer D.,
RA Dromer F., Young S., Zeng Q., Chapman S., Gujja S., Saif S., Birren B.;
RT "Evolution of pathogenesis and genome organization in the Tremellales.";
RL Submitted (JUN-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:ODN77568.1}.
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; AWGJ01000007; ODN77568.1; -; Genomic_DNA.
DR RefSeq; XP_018992804.1; XM_019138861.1.
DR AlphaFoldDB; A0A1E3HML1; -.
DR STRING; 1295533.A0A1E3HML1; -.
DR GeneID; 30156046; -.
DR OrthoDB; 383715at2759; -.
DR Proteomes; UP000094065; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR045194; MGRN1/RNF157-like.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR22996; MAHOGUNIN; 1.
DR PANTHER; PTHR22996:SF0; RING-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR Pfam; PF13920; zf-C3HC4_3; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000094065}.
FT DOMAIN 429..522
FT /note="RING-type"
FT /evidence="ECO:0000259|SMART:SM00184"
FT REGION 47..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 195..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 255..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 466..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 541..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 589..667
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..79
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..273
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 541..567
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 619..633
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 650..667
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 667 AA; 72002 MW; C3EDF2232806F3CF CRC64;
MTSLNSVSGW YTNAYSGPFR TSRLRAPSLL PGARIPAPVQ QTLVVDAAHN NSPSADDANP
EGKDGVRNVR RRETVFGPDV GEDDEPGWGE GGKEKISVDV VKKWVEKAKT DEGIHPTTTL
QALVNLKRPS LLLQQVDQPQ PKADKYEDIA PYPTAAQSDY PISPTSLLPT PPLHTLKFTY
DATTPAARIT LLLYPNPRPR PTIPEGGGKA SFEEGEEEEQ EPTVIYTGLH AGGFGQVFDL
PKEWAMDLSS AIRLEEEDQP NKPEVKEEPG EQVQELNEQP EEQQGRRRFG IFGRRRGESD
VEAGNANIEM TSPVTQSEEK EAPKQVEYGM RVLIKIEAAG PEGQPLKRRN AQLTHILITG
TWVNDPNSGD DAGPGGKRVW VVKVARREAV IGSHTFLLKE IFGLSATSST ATSYPPTADD
PYASTPNECI VCLTSPRDVV LLPCRHLVVC RDCAVGMVEF GAGGKVARRE ETPATGTGAG
GGGDSEAGGE GGTDTPAAAP ATTTTHRERR KKKVKGWYCP VCRQPYTSLL RLALPQAKAS
EAQSHQELSR QPSRASVRTT RTTKSLAPTL PDGAERFLEG LRPEGADADL ELEEDEDKEA
GSDSVRPGWV GGGAGTPDVE KPEVEHKEVE ESELTGPSPT PATMETPPHP EGDVADEGKG
KGWKEVA
//
