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Database: UniProt
Entry: W9SBM0_9ROSA
LinkDB: W9SBM0_9ROSA
Original site: W9SBM0_9ROSA 
ID   W9SBM0_9ROSA            Unreviewed;       703 AA.
AC   W9SBM0;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   SubName: Full=E3 ubiquitin-protein ligase SINA-like 2 {ECO:0000313|EMBL:EXC20577.1};
GN   ORFNames=L484_027132 {ECO:0000313|EMBL:EXC20577.1};
OS   Morus notabilis.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Moraceae; Moreae; Morus.
OX   NCBI_TaxID=981085 {ECO:0000313|EMBL:EXC20577.1, ECO:0000313|Proteomes:UP000030645};
RN   [1] {ECO:0000313|Proteomes:UP000030645}
RP   NUCLEOTIDE SEQUENCE.
RA   He N., Zhao S.;
RT   "Draft Genome Sequence of a Mulberry Tree, Morus notabilis C.K. Schneid.";
RL   Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination and
CC       subsequent proteasomal degradation of target proteins. E3 ubiquitin
CC       ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the
CC       form of a thioester and then directly transfers the ubiquitin to
CC       targeted substrates. It probably triggers the ubiquitin-mediated
CC       degradation of different substrates. {ECO:0000256|ARBA:ARBA00024004}.
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DR   EMBL; KE345919; EXC20577.1; -; Genomic_DNA.
DR   RefSeq; XP_010108937.1; XM_010110635.1.
DR   AlphaFoldDB; W9SBM0; -.
DR   STRING; 981085.W9SBM0; -.
DR   eggNOG; KOG3002; Eukaryota.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000030645; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   CDD; cd00084; HMG-box_SF; 1.
DR   Gene3D; 1.10.30.10; High mobility group box domain; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR019557; AminoTfrase-like_pln_mobile.
DR   InterPro; IPR009071; HMG_box_dom.
DR   InterPro; IPR036910; HMG_box_dom_sf.
DR   InterPro; IPR044286; SINL_plant.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR013010; Znf_SIAH.
DR   PANTHER; PTHR46632; E3 UBIQUITIN-PROTEIN LIGASE SINA-LIKE 4; 1.
DR   PANTHER; PTHR46632:SF13; RING-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR   Pfam; PF00505; HMG_box; 1.
DR   Pfam; PF10536; PMD; 1.
DR   Pfam; PF21361; Sina_ZnF; 1.
DR   SMART; SM00398; HMG; 1.
DR   SUPFAM; SSF47095; HMG-box; 1.
DR   SUPFAM; SSF49599; TRAF domain-like; 1.
DR   PROSITE; PS50118; HMG_BOX_2; 1.
DR   PROSITE; PS51081; ZF_SIAH; 1.
PE   4: Predicted;
KW   DNA-binding {ECO:0000256|PROSITE-ProRule:PRU00267};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00455};
KW   Nucleus {ECO:0000256|PROSITE-ProRule:PRU00267};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030645};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00455};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00455}.
FT   DOMAIN          118..187
FT                   /note="HMG box"
FT                   /evidence="ECO:0000259|PROSITE:PS50118"
FT   DOMAIN          518..576
FT                   /note="SIAH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51081"
FT   DNA_BIND        118..187
FT                   /note="HMG box"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00267"
FT   REGION          1..81
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   703 AA;  79361 MW;  EAE4829D8A723429 CRC64;
     MAEYAAGGDD DGEGTTSPRC KRRRLPIFVT NSTQENPEPP REDERHTDSE DDQWEEEGDR
     AQRVSQEGPV SSEPDRNRST IPVFKVSGEG DLQVVKGNIE KHNVLEGKRR KKTKQVTTPR
     PACSWVYFSR EFIKEYSASH PESSGLKAAT KAASETWKSM SLDEKAKFTT RAREVWDNYL
     SAAPPRTPKP RKQTKLVTRC SPGRLFNVLQ HLTAEQKDAV KIMGFGSLLG LRCRTLRRSL
     CLWLLERFNT MQRSLEICGG HIHLYPKDVE LVMGLAASGK DVVNSGPDDL IADLRNNYNA
     TNRGISVRLL EERLSAPEAG DDFKRSFVLY ALGTLLSPTA RLDVSPSFLH FLTNMSVVHQ
     YNWGKFLLDR LVREISRFRQ GKQQAVGGCL LFLQLFYYER ISIEGTRDLS SAVSPCLSSW
     GEDEITEREK QERERGGYGC GQVVFKDRCL GVETSEDRPP ACSIINGVEH DPLLLHKANQ
     VDEEGMSGEI IQEVENNMPI FLKSKDVVCG DIELIVESVR TPCQNKEYGC NERVDCVRNN
     DHEGTCMYAP CACPLPGCNF VSSFYQLSLH FSTKHWDSGR RFRYKSEFAV SLKMNEQVLV
     LQAEDDGTLF LLNKGIESIG HTVMLTCIAP SSSKRRFMYD LVLKRGSSSL RLNSLAECFP
     GRVEGFPQMD FFFAPYRFLD STGQLNLDVC IRNCEEELSG DYS
//
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