ID A0A022QJ92_ERYGU Unreviewed; 352 AA.
AC A0A022QJ92;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=RING-type domain-containing protein {ECO:0000259|PROSITE:PS50089};
GN ORFNames=MIMGU_mgv1a009116mg {ECO:0000313|EMBL:EYU27634.1};
OS Erythranthe guttata (Yellow monkey flower) (Mimulus guttatus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Phrymaceae; Erythranthe.
OX NCBI_TaxID=4155 {ECO:0000313|EMBL:EYU27634.1, ECO:0000313|Proteomes:UP000030748};
RN [1] {ECO:0000313|EMBL:EYU27634.1, ECO:0000313|Proteomes:UP000030748}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DUN x IM62 {ECO:0000313|Proteomes:UP000030748};
RX PubMed=24225854; DOI=10.1073/pnas.1319032110;
RA Hellsten U., Wright K.M., Jenkins J., Shu S., Yuan Y., Wessler S.R.,
RA Schmutz J., Willis J.H., Rokhsar D.S.;
RT "Fine-scale variation in meiotic recombination in Mimulus inferred from
RT population shotgun sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:19478-19482(2013).
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; KI631456; EYU27634.1; -; Genomic_DNA.
DR RefSeq; XP_012848831.1; XM_012993377.1.
DR AlphaFoldDB; A0A022QJ92; -.
DR STRING; 4155.A0A022QJ92; -.
DR GeneID; 105968727; -.
DR KEGG; egt:105968727; -.
DR eggNOG; KOG1327; Eukaryota.
DR OMA; PICWNQA; -.
DR OrthoDB; 3641271at2759; -.
DR PhylomeDB; A0A022QJ92; -.
DR Proteomes; UP000030748; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR010734; Copine_C.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45751; COPINE FAMILY PROTEIN 1; 1.
DR PANTHER; PTHR45751:SF47; RING-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF07002; Copine; 1.
DR Pfam; PF13920; zf-C3HC4_3; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00327; VWA; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF53300; vWA-like; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Reference proteome {ECO:0000313|Proteomes:UP000030748};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT DOMAIN 305..338
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
SQ SEQUENCE 352 AA; 38829 MW; 7CEB8277F14AF92E CRC64;
MGGEQSKHSR IGDNYKSLDQ VTKAVLDAGL ESSNFIVGID FTKSNENAGK KSFNGKCLHH
ISDVVNPYEH AISIIGRTLS AFDEDNLIPC FGFGDVTTHD EAVFSFYPDH RPCNGFDEVL
SRYREIVPNV QLAGPSSFAP IIETAMEITD QSGGKYHILL VLVDGQVTRS ADTKPGELST
QERSTFNAIV KASKYPLSII FVGVGDGPWQ MLKRMDDNIP GRAFDNIQFV NFTEIMSRNK
PMAEKEAEFA LAAVMEVPMQ YKATIELKLL SKQVGGDSAK VPLPPPPPNL YPHLGGGFFP
TFPTCPVCLR SKRNLALGCG HQTCHECGSD LNWCPVCHTR ITNKIRLYDQ DQ
//
