ID A0A022RFK0_ERYGU Unreviewed; 191 AA.
AC A0A022RFK0;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
DE Flags: Fragment;
GN ORFNames=MIMGU_mgv1a0110002mg {ECO:0000313|EMBL:EYU38533.1};
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:EYU38533.1, ECO:0000313|Proteomes:UP000030748};
RN [1] {ECO:0000313|EMBL:EYU38533.1, 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};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SIMILARITY: Belongs to the RING-type zinc finger family. LOG2
CC subfamily. {ECO:0000256|ARBA:ARBA00025721}.
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DR EMBL; KI630480; EYU38533.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A022RFK0; -.
DR STRING; 4155.A0A022RFK0; -.
DR eggNOG; KOG4265; Eukaryota.
DR Proteomes; UP000030748; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR CDD; cd16789; mRING-HC-C3HC5_MGRN1-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR045195; LOG2-like_mRING_C3HC5.
DR InterPro; IPR045194; MGRN1/RNF157-like.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR22996:SF27; E3 UBIQUITIN-PROTEIN LIGASE LOG2-RELATED; 1.
DR PANTHER; PTHR22996; MAHOGUNIN; 1.
DR Pfam; PF13920; zf-C3HC4_3; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
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 135..174
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EYU38533.1"
SQ SEQUENCE 191 AA; 21271 MW; BEF8B4EA651FCE33 CRC64;
GEDCCLTPTK ENLHPPIVVQ FEQGLAQKFK QPSGTGIDLS MFEDGELSKE LDMDVYPLAV
KAEASPDNQN ESSDSGSTNS QITQAVFEKD KGEYQLRVVK QILWVNGMRY ELQEIYGIGN
SVEGEFDAND PGKECVICLS EPRDTTVLPC RHMCMCSECA KVLRFQTNRC PICRQPVERL
LEIKVSSGGD E
//
