ID   A0A067EMV8_CITSI        Unreviewed;      1122 AA.
AC   A0A067EMV8;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   08-OCT-2025, entry version 43.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN   ORFNames=CISIN_1g041480mg {ECO:0000313|EMBL:KDO56433.1};
OS   Citrus sinensis (Sweet orange) (Citrus aurantium var. sinensis).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Sapindales; Rutaceae; Aurantioideae; Citrus.
OX   NCBI_TaxID=2711 {ECO:0000313|EMBL:KDO56433.1, ECO:0000313|Proteomes:UP000027120};
RN   [1] {ECO:0000313|EMBL:KDO56433.1, ECO:0000313|Proteomes:UP000027120}
RP   NUCLEOTIDE SEQUENCE.
RG   International Citrus Genome Consortium;
RA   Gmitter F., Chen C., Farmerie W., Harkins T., Desany B., Mohiuddin M.,
RA   Kodira C., Borodovsky M., Lomsadze A., Burns P., Jenkins J., Prochnik S.,
RA   Shu S., Chapman J., Pitluck S., Schmutz J., Rokhsar D.;
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; KK784973; KDO56433.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A067EMV8; -.
DR   STRING; 2711.A0A067EMV8; -.
DR   PaxDb; 2711-XP_006492727.1; -.
DR   KEGG; cit:102631331; -.
DR   eggNOG; KOG0167; Eukaryota.
DR   OrthoDB; 10064100at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000027120; Unassembled WGS sequence.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   CDD; cd16664; RING-Ubox_PUB; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR055566; ARM_LIN.
DR   InterPro; IPR056512; LIN_N.
DR   InterPro; IPR045210; RING-Ubox_PUB.
DR   InterPro; IPR003613; Ubox_domain.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR35549; OS04G0584500 PROTEIN; 1.
DR   PANTHER; PTHR35549:SF1; OS04G0584500 PROTEIN; 1.
DR   Pfam; PF23568; ARM_LIN; 1.
DR   Pfam; PF23628; ARM_LIN_C; 1.
DR   Pfam; PF04564; U-box; 1.
DR   SMART; SM00504; Ubox; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS51698; U_BOX; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000027120};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT   DOMAIN          643..718
FT                   /note="U-box"
FT                   /evidence="ECO:0000259|PROSITE:PS51698"
FT   REGION          14..177
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          960..981
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        53..62
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        66..78
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        81..117
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        120..129
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        147..170
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        964..981
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1122 AA;  125826 MW;  CE2712B88F4131BE CRC64;
     MASLEELLLA DGFKGRRSSV TSSRPSFREE AMSMPVYPFG DKNKAASSSS SRIKTERARS
     DLSRYTLKSD SPRISNLSGR RPRDSLVRRE KVDSGSMKEH RERLAGRRSV DVQERRRSNA
     KSSETSQENE IVEVSGEESQ RVSINLDTRH SNVDNRKSMK ENEPGNDRYN RSSMSRKSIK
     ENYRKHESVL APASEPALDE VAVQAIVSIL SGYVKSFLKN EDFRATLRRK CFSSLNFIEP
     EDEGNSNESK VIASLEQAIE TVQRAAEESA SSKELKKASL QLSMITGMSA NDLKDGSTSG
     VPNSKLSACA HLYLSVIYKI QKKDRVSAKH LLQVFCDSPF MARTTLLPEL WDYLISPHLA
     HLKAWYKQEA DSLADESNKP RKMKLLEKVY NEILDSGTYQ FAVYYKDWLT EGIEDPSVPT
     IQIPSLSVQR HQRKGSFGNS SEVASPAAAF SPQPTVSKKL YDAVFERASK PRVDAAEDDG
     EMENFDNYAR SSGGSTVEKR TLTYSSEIVK CTYQDTEDDS PKIAQDDLFH PEDELLLAAE
     EGWRLPGVKY PAERNINSNI NICCTSKKIQ TIKLYTPPDT KANELTLKRL AKSAFEQQQT
     EGCTALTISS PPSTSEAPVN LRPSFEELHE NDEYFDKGSF LTSIPQDFIC PLTGQLFEEP
     VTLESGQTFE CEAIKEWIEQ GNRTCPVTGK YLACPSLPLT NFILKRVIDG WKSENCMHLL
     AFAFQIVEKS RMNESKNGDE TAIFILEQLL TVFSDQERIT NAKHLISIGG LQFLICRFES
     GKLEEKARVA ALMCCCIEAD AGCRNQMARN INVYSLLELL HSKQVKPRTN TVLLLIDLIC
     LSRRRDVSTL LRNVQNEELV NAMHVLLLYL QRSPPEQRPL FSILLLHLDL LVEPRKYSIY
     REAAVDAITV ALEESLTDEK IQEKCCRALL ILGGRFSFSR EVANESWILK PAGFNDRCEG
     NSLDNDENDL PVDDSTPLDD EEQASEEWLR KLSASLLGNR KRSFLETVSK ILGSRNSDLV
     SVCLTTVAWL SHALSAQPDA EFQLSAFSAV ISQLKEILQN GEQPQQKVLA SMSLLNFSKI
     PECGAVLKTI AAEIRIPLQS LTEVTWTTQE LCAIIAGRSL IS
//