ID   A0A1S4EBE6_DIACI        Unreviewed;       240 AA.
AC   A0A1S4EBE6;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN   Name=LOC103509109 {ECO:0000313|RefSeq:XP_017299531.1};
OS   Diaphorina citri (Asian citrus psyllid).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Paraneoptera; Hemiptera; Sternorrhyncha; Psylloidea; Psyllidae;
OC   Diaphorininae; Diaphorina.
OX   NCBI_TaxID=121845 {ECO:0000313|Proteomes:UP000079169, ECO:0000313|RefSeq:XP_017299531.1};
RN   [1] {ECO:0000313|RefSeq:XP_017299531.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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   RefSeq; XP_017299531.1; XM_017444042.2.
DR   AlphaFoldDB; A0A1S4EBE6; -.
DR   STRING; 121845.A0A1S4EBE6; -.
DR   PaxDb; 121845-A0A1S4EBE6; -.
DR   GeneID; 103509109; -.
DR   KEGG; dci:103509109; -.
DR   OrthoDB; 276791at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000079169; Unplaced.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:InterPro.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:0060255; P:regulation of macromolecule metabolic process; IEA:UniProt.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR045103; RNF5/RNF185-like.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR12313; E3 UBIQUITIN-PROTEIN LIGASE RNF5-RELATED; 1.
DR   PANTHER; PTHR12313:SF0; RING-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR   Pfam; PF13920; zf-C3HC4_3; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000079169};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   TRANSMEM        220..239
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          37..78
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          97..130
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        97..111
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   240 AA;  26401 MW;  0573379D872A650C CRC64;
     MATTSSGSKQ TPPNRDEGSG DQKKTDGGND KSQIYDCNIC FDTAKDAVIS MCGHLFCWPC
     LHQWLETCPN RQTCPVCKAA IDKEVLKFFY WPGRGGSEID PRDEVPPRPQ GQRTERENSS
     IPPEQRGMFD DAITRRSESN SMWSLGESGF SIGEFLLGLF SSTSSLGDQR LRSGNGFRGA
     DYGYTSPGGL FSAGGAQGRP GEAHAHGGAR FDANVEIEDM FFKLFLIFAA LCLFYILFVF
//