ID W6KTN5_9TRYP Unreviewed; 291 AA.
AC W6KTN5;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=GSEM1_T00005062001 {ECO:0000313|EMBL:CCW64944.1};
OS Phytomonas sp. EM1.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Phytomonas.
OX NCBI_TaxID=479712 {ECO:0000313|EMBL:CCW64944.1, ECO:0000313|Proteomes:UP000027080};
RN [1] {ECO:0000313|EMBL:CCW64944.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=EM1 {ECO:0000313|EMBL:CCW64944.1};
RA Genoscope - CEA;
RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CCW64944.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EM1 {ECO:0000313|EMBL:CCW64944.1};
RX PubMed=24516393; DOI=10.1371/journal.pgen.1004007;
RA Porcel B.M., Denoeud F., Opperdoes F., Noel B., Madoui M.A.,
RA Hammarton T.C., Field M.C., Da Silva C., Couloux A., Poulain J.,
RA Katinka M., Jabbari K., Aury J.M., Campbell D.A., Cintron R., Dickens N.J.,
RA Docampo R., Sturm N.R., Koumandou V.L., Fabre S., Flegontov P., Lukes J.,
RA Michaeli S., Mottram J.C., Szoor B., Zilberstein D., Bringaud F.,
RA Wincker P., Dollet M.;
RT "The Streamlined Genome of Phytomonas spp. Relative to Human Pathogenic
RT Kinetoplastids Reveals a Parasite Tailored for Plants.";
RL PLoS Genet. 10:e1004007-e1004007(2014).
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; HF955094; CCW64944.1; -; Genomic_DNA.
DR AlphaFoldDB; W6KTN5; -.
DR EnsemblProtists; CCW64944; CCW64944; GSEM1_T00005062001.
DR OrthoDB; 383715at2759; -.
DR Proteomes; UP000027080; 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:SF3; RING-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR Pfam; PF13920; zf-C3HC4_3; 1.
DR SUPFAM; SSF57850; RING/U-box; 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:UP000027080};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT DOMAIN 234..273
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
SQ SEQUENCE 291 AA; 32483 MW; 369C438A7738FE46 CRC64;
MQLQNPQLSQ TNNRGVQEGQ MVKMLGTIEA STVTYNPSTQ LLTFYITTIA PSLTYEIHTG
VKEFVKGGDV FYMPNKPKME PTRILIEGPH ENRKIAVKLD ISKLEEKEKV FNKHYPKQMP
CVIVLRYRTT EFRKKENADN NIISNESNND DKGDTEDVEE VVVEHTEHTA VDLAERPKRR
VISQIVTTGG SAYVVENLYG AGHENATGVS EGTELMVGST IVPHEGEEEE EGLCVICLMN
SKDTAVMPCR HMCMCKDCGE QLLKHKPVCP VCRAPISTLL HMPSFTNGGS K
//
