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
//