ID A0A388M933_CHABU Unreviewed; 828 AA.
AC A0A388M933;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=CBR_g51805 {ECO:0000313|EMBL:GBG91071.1};
OS Chara braunii (Braun's stonewort).
OC Eukaryota; Viridiplantae; Streptophyta; Charophyceae; Charales; Characeae;
OC Chara.
OX NCBI_TaxID=69332 {ECO:0000313|EMBL:GBG91071.1, ECO:0000313|Proteomes:UP000265515};
RN [1] {ECO:0000313|EMBL:GBG91071.1, ECO:0000313|Proteomes:UP000265515}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S276 {ECO:0000313|EMBL:GBG91071.1,
RC ECO:0000313|Proteomes:UP000265515};
RX PubMed=30007417; DOI=10.1016/j.cell.2018.06.033;
RA Nishiyama T., Sakayama H., Vries J.D., Buschmann H., Saint-Marcoux D.,
RA Ullrich K.K., Haas F.B., Vanderstraeten L., Becker D., Lang D.,
RA Vosolsobe S., Rombauts S., Wilhelmsson P.K.I., Janitza P., Kern R.,
RA Heyl A., Rumpler F., Villalobos L.I.A.C., Clay J.M., Skokan R., Toyoda A.,
RA Suzuki Y., Kagoshima H., Schijlen E., Tajeshwar N., Catarino B.,
RA Hetherington A.J., Saltykova A., Bonnot C., Breuninger H., Symeonidi A.,
RA Radhakrishnan G.V., Van Nieuwerburgh F., Deforce D., Chang C., Karol K.G.,
RA Hedrich R., Ulvskov P., Glockner G., Delwiche C.F., Petrasek J.,
RA Van de Peer Y., Friml J., Beilby M., Dolan L., Kohara Y., Sugano S.,
RA Fujiyama A., Delaux P.-M., Quint M., TheiBen G., Hagemann M., Harholt J.,
RA Dunand C., Zachgo S., Langdale J., Maumus F., Straeten D.V.D., Gould S.B.,
RA Rensing S.A.;
RT "The Chara Genome: Secondary Complexity and Implications for Plant
RT Terrestrialization.";
RL Cell 174:448-464(2018).
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:GBG91071.1}.
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DR EMBL; BFEA01000868; GBG91071.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A388M933; -.
DR STRING; 69332.A0A388M933; -.
DR EnsemblPlants; GBG91071; GBG91071; CBR_g51805.
DR Gramene; GBG91071; GBG91071; CBR_g51805.
DR Proteomes; UP000265515; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR23328:SF0; RING-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR23328; UNCHARACTERIZED; 1.
DR Pfam; PF00097; zf-C3HC4; 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 Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000265515};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 476..515
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 71..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 124..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 282..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 392..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 619..694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 747..828
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..111
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..147
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..450
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 629..653
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 764..819
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 828 AA; 89484 MW; 6CAAEB8F930CEB8C CRC64;
MDAIGSEVAV LREETCRSCV HCGVTHCRQT EPDCTCSSPL WKSEHRGLDK AGVEEDGEDV
EARVSGECQK LVRSKESEAQ GGGSGSVCER GEEAGQEQAA DPEDQQRRRQ QEQGFHSVVM
NGYGSAELGS AGEGEDDEED VDDDEEEETI HLVHNGSGGS VFTPRFRRRA EEAGWDENAL
LMGMGALDEM TEAGVGGGPL FPEEVTVAAV GTTARSEVVG EGGWRRREEA VPSAAIARES
TLSPGRNHGA DEVVIDNDEG VEEDHGNHAV SVVMDGAVTS RQSPREMARG AEDASAGNGV
AASERDRERK REVRTPGLAR TPVSAERRYR RMRHTADEVN ENEGMQSTSS EALRRIREGG
DVEACLERSR REFGRRLEAI QASRRIVLER AEERTGVSTS SAVVGPSDPC EFQGSSARAG
EGGTSPRSGE GGKDQEKERA PSEKDRKQGV ASRIAQSNGR PLELPCLEQL RQELSCAVCL
EICVEPSTTT CGHSFCSSCL RSSIQRCGPK CPKCRHPLGA DAALHCPVNT VLWNTIQLLF
PEVSAAMSPR KCSTSAMSPG NQLSSLVIPG PHPLMHMLPT NARTRHHTRG LARIAAHLVT
GEGHAVHSHF VHNTPRLRSA ARVPSNNPFR EPRSATSMSM PSTLVTSDSH RPAMHSVSLR
RGGSNIGPIP SSVANTRVVP DRNIEEDDES ENDDMDLFSG AAARLTESNA EGHNPVRARF
QAYMRTRRND RDDRTDRHEQ LERLDALLLG TRLQRPDMSR DDDSPPSPSL SSPSSLPQVL
ITSASAAAAS NQLASVRSDT TRSGVSRSAT SSRSAVGQTP QLRHGRHP
//
