ID A0A3R7K6C0_9STRA Unreviewed; 373 AA.
AC A0A3R7K6C0;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-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=BBI17_000578 {ECO:0000313|EMBL:RLN26069.1}, BBO99_00000539
GN {ECO:0000313|EMBL:RLN85445.1};
OS Phytophthora kernoviae.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=325452 {ECO:0000313|EMBL:RLN26069.1, ECO:0000313|Proteomes:UP000285883};
RN [1] {ECO:0000313|Proteomes:UP000285624, ECO:0000313|Proteomes:UP000285883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Chile2 {ECO:0000313|EMBL:RLN26069.1}, and Chile4
RC {ECO:0000313|EMBL:RLN85445.1};
RA Studholme D.J., Sanfuentes E., Panda P., Hill R., Sambles C., Grant M.,
RA Williams N.M., Mcdougal R.L.;
RT "Genome sequencing of oomycete isolates from Chile give support for New
RT Zealand origin for Phytophthora kernoviae and make available the first
RT Nothophytophthora sp. genome.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
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:RLN26069.1}.
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DR EMBL; MAYM02001187; RLN26069.1; -; Genomic_DNA.
DR EMBL; MBDN02000008; RLN85445.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3R7K6C0; -.
DR STRING; 325452.A0A3R7K6C0; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000285624; Unassembled WGS sequence.
DR Proteomes; UP000285883; Unassembled WGS sequence.
DR GO; GO:0000151; C:ubiquitin ligase complex; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd16531; RING-HC_RING1-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR043540; RING1/RING2.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR46076:SF3; E3 UBIQUITIN-PROTEIN LIGASE RING1; 1.
DR PANTHER; PTHR46076; E3 UBIQUITIN-PROTEIN LIGASE RING1 / RING 2 FAMILY MEMBER; 1.
DR Pfam; PF13923; zf-C3HC4_2; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000285624};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 77..117
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
SQ SEQUENCE 373 AA; 42603 MW; 7F879D55BE8CB707 CRC64;
MSNQAPQNPY EFTREAYDAL VKGTPNCHVS QRSKYEEMEL VDDCTLFDIY RQPRAPVTDP
KVTKSLPVRV LNADLTCPIC LGIIKETMVV MECLHRFCGE CISTAIRQSK RECPSCRIHI
PSKRSLRPDT NFDALITKIH PNLAEFERNE DRIIEQLNRS KHFNNAYTES TRMGVLSQAA
SRRNVRWKEE VGGGINVRVR IFITYSFPVE RIQRIVAFNE SSRKKPRVAT STLSTSTVTD
RVNLRVLLHQ EEQPHAPKLQ RTLFTTSSKL KIRHLKKHLC NLLKLDSYHN MCIVLPKVNC
KLSGLSSSTK TLSSSGVRQD LQCDQELEDF VTVKDIYQQY GMGTEWELRL LYHFSPGTIV
NGLAQFVSVP SGV
//
