ID B9SGB3_RICCO Unreviewed; 398 AA.
AC B9SGB3;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Copine, putative {ECO:0000313|EMBL:EEF37359.1};
GN ORFNames=RCOM_0881500 {ECO:0000313|EMBL:EEF37359.1};
OS Ricinus communis (Castor bean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae; Acalypheae;
OC Ricinus.
OX NCBI_TaxID=3988 {ECO:0000313|Proteomes:UP000008311};
RN [1] {ECO:0000313|Proteomes:UP000008311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Hale {ECO:0000313|Proteomes:UP000008311};
RX PubMed=20729833; DOI=10.1038/nbt.1674;
RA Chan A.P., Crabtree J., Zhao Q., Lorenzi H., Orvis J., Puiu D.,
RA Melake-Berhan A., Jones K.M., Redman J., Chen G., Cahoon E.B., Gedil M.,
RA Stanke M., Haas B.J., Wortman J.R., Fraser-Liggett C.M., Ravel J.,
RA Rabinowicz P.D.;
RT "Draft genome sequence of the oilseed species Ricinus communis.";
RL Nat. Biotechnol. 28:951-956(2010).
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; EQ973951; EEF37359.1; -; Genomic_DNA.
DR AlphaFoldDB; B9SGB3; -.
DR eggNOG; KOG1327; Eukaryota.
DR InParanoid; B9SGB3; -.
DR Proteomes; UP000008311; 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; SM00327; VWA; 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:UP000008311};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT DOMAIN 354..387
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 398 AA; 44444 MW; DEAA48136794878E CRC64;
MGVKQSRHKS HYGAPSLPSS SPYSFHSSRY VDYDGRSKLQ SMYSRIGDDY HSLEQVTRAL
AQAGLESSNL IVGIDFTKSN EWTGARSFNR KSLHHLGDTP NPYEQAISII GRTMSEFDED
NLIPCYGFGD ATTHDQEVFS FHPDDHPCNG FEEVLSRYRD IIPNVNLAGP TSFAPIIETA
IGIVDSSGGQ YHVLMIIADG QVTRSVDTGY AQLSPQEQST INAIVKASEY PLSIVLVGVG
DGPWDMMHKF DDNIPSRTFD NFQFVNFTQI MLKDTPMSKK ETEFALSALM EIPSQYRATI
GLHLLGCQRG TPKRFPLPPP VGNRLVNLYA KHIRPNSNQQ RIGFHNNPSA PDNCPVCLWS
KKDFVFGCGH QACFDCGRDL HLCPICQTSI ITRIRLYD
//
