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Database: UniProt
Entry: A0A397YNW5_BRACM
LinkDB: A0A397YNW5_BRACM
Original site: A0A397YNW5_BRACM 
ID   A0A397YNW5_BRACM        Unreviewed;       272 AA.
AC   A0A397YNW5;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN   ORFNames=BRARA_G01016 {ECO:0000313|EMBL:RID53634.1};
OS   Brassica campestris (Field mustard).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=3711 {ECO:0000313|EMBL:RID53634.1, ECO:0000313|Proteomes:UP000264353};
RN   [1] {ECO:0000313|EMBL:RID53634.1, ECO:0000313|Proteomes:UP000264353}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. B-3 {ECO:0000313|Proteomes:UP000264353};
RA   Bowman J., Kohchi T., Yamato K., Jenkins J., Shu S., Ishizaki K.,
RA   Yamaoka S., Nishihama R., Nakamura Y., Berger F., Adam C., Aki S.,
RA   Althoff F., Araki T., Arteaga-Vazquez M., Balasubrmanian S., Bauer D.,
RA   Boehm C., Briginshaw L., Caballero-Perez J., Catarino B., Chen F.,
RA   Chiyoda S., Chovatia M., Davies K., Delmans M., Demura T., Dierschke T.,
RA   Dolan L., Dorantes-Acosta A., Eklund D., Florent S., Flores-Sandoval E.,
RA   Fujiyama A., Fukuzawa H., Galik B., Grimanelli D., Grimwood J.,
RA   Grossniklaus U., Hamada T., Haseloff J., Hetherington A., Higo A.,
RA   Hirakawa Y., Hundley H., Ikeda Y., Inoue K., Inoue S., Ishida S., Jia Q.,
RA   Kakita M., Kanazawa T., Kawai Y., Kawashima T., Kennedy M., Kinose K.,
RA   Kinoshita T., Kohara Y., Koide E., Komatsu K., Kopischke S., Kubo M.,
RA   Kyozuka J., Lagercrantz U., Lin S., Lindquist E., Lipzen A., Lu C.,
RA   Luna E., Martienssen R., Minamino N., Mizutani M., Mizutani M.,
RA   Mochizuki N., Monte I., Mosher R., Nagasaki H., Nakagami H., Naramoto S.,
RA   Nishitani K., Ohtani M., Okamoto T., Okumura M., Phillips J., Pollak B.,
RA   Reinders A., Roevekamp M., Sano R., Sawa S., Schmid M., Shirakawa M.,
RA   Solano R., Spunde A., Suetsugu N., Sugano S., Sugiyama A., Sun R.,
RA   Suzuki Y., Takenaka M., Takezawa D., Tomogane H., Tsuzuki M., Ueda T.,
RA   Umeda M., Ward J., Watanabe Y., Yazaki K., Yokoyama R., Yoshitake Y.,
RA   Yotsui I., Zachgo S., Schmutz J.;
RT   "WGS assembly of Brassica rapa FPsc.";
RL   Submitted (JUN-2018) 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}.
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   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
CC   -!- SIMILARITY: Belongs to the SINA (Seven in absentia) family.
CC       {ECO:0000256|ARBA:ARBA00009119}.
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DR   EMBL; CM010634; RID53634.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A397YNW5; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000264353; Chromosome a7.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   CDD; cd16571; RING-HC_SIAHs; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR049548; Sina-like_RING.
DR   InterPro; IPR044286; SINL_plant.
DR   InterPro; IPR001841; Znf_RING.
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:SF24; RING-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR   Pfam; PF21362; Sina_RING; 1.
DR   Pfam; PF21361; Sina_ZnF; 1.
DR   SUPFAM; SSF49599; TRAF domain-like; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
DR   PROSITE; PS51081; ZF_SIAH; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00455};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00455};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00455}.
FT   DOMAIN          31..67
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          84..144
FT                   /note="SIAH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51081"
SQ   SEQUENCE   272 AA;  30436 MW;  533E35BC79E1137A CRC64;
     MAEQQTPSAE NQSSSTTPVS LTLLDPDVLE CPICCEPLKV PIFQCENGHL ACSQCCEKVK
     KICPSCKSPN GYSRCRSMER VIEACRVSCP NSKYGCKENT SFGNRSSHEK QCLFAPCFCP
     VPLNDCNYVG SDKNLRNHIR AKHKDHVIPI VFDTPLTLVM GSSEKIVCFQ EKKDGELFVV
     QAFRKSYGLA VSVNCIARSA HGLGRFSCCM DVIIDPCIKL KQAFTVREIQ KKIHEEPKDS
     FMLIPSHMLM LTDWSFGIDI CFSRGMDSFI RA
//
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