ID Q54XG4_DICDI Unreviewed; 563 AA.
AC Q54XG4;
DT 24-MAY-2005, integrated into UniProtKB/TrEMBL.
DT 24-MAY-2005, sequence version 1.
DT 27-MAR-2024, entry version 129.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN ORFNames=DDB_G0278981 {ECO:0000313|EMBL:EAL67912.1};
OS Dictyostelium discoideum (Social amoeba).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689 {ECO:0000313|EMBL:EAL67912.1, ECO:0000313|Proteomes:UP000002195};
RN [1] {ECO:0000313|EMBL:EAL67912.1, ECO:0000313|Proteomes:UP000002195}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4 {ECO:0000313|EMBL:EAL67912.1,
RC ECO:0000313|Proteomes:UP000002195};
RX PubMed=15875012; DOI=10.1038/nature03481;
RG The Dictyostelium discoideum Sequencing Consortium;
RA Eichinger L., Pachebat J.A., Glockner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M., Spiegler S., Tivey A., Sugano S.,
RA White B., Walker D., Woodward J., Winckler T., Tanaka Y., Shaulsky G.,
RA Schleicher M., Weinstock G., Rosenthal A., Cox E.C., Chisholm R.L.,
RA Gibbs R., Loomis W.F., Platzer M., Kay R.R., Williams J., Dear P.H.,
RA Noegel A.A., Barrell B., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.;
CC EC=2.3.2.31; Evidence={ECO:0000256|ARBA:ARBA00001798};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EAL67912.1}.
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DR EMBL; AAFI02000026; EAL67912.1; -; Genomic_DNA.
DR RefSeq; XP_641886.1; XM_636794.1.
DR AlphaFoldDB; Q54XG4; -.
DR SMR; Q54XG4; -.
DR STRING; 44689.Q54XG4; -.
DR PaxDb; 44689-DDB0233057; -.
DR GeneID; 8621812; -.
DR KEGG; ddi:DDB_G0278981; -.
DR dictyBase; DDB_G0278981; -.
DR eggNOG; KOG1815; Eukaryota.
DR HOGENOM; CLU_009823_4_1_1; -.
DR InParanoid; Q54XG4; -.
DR OMA; ICKVCHT; -.
DR PhylomeDB; Q54XG4; -.
DR Reactome; R-DDI-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS:dictyBase.
DR GO; GO:0000151; C:ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR CDD; cd20360; Rcat_RBR_TRIAD1; 1.
DR CDD; cd16773; RING-HC_RBR_TRIAD1; 1.
DR CDD; cd14298; UBA2_scUBP14_like; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR045840; Ariadne.
DR InterPro; IPR048962; ARIH1-like_UBL.
DR InterPro; IPR031127; E3_UB_ligase_RBR.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR047556; Rcat_RBR_TRIAD1.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR033864; UBA2_scUBP14-like.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR11685:SF212; E3 UBIQUITIN-PROTEIN LIGASE ARIH1; 1.
DR PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR Pfam; PF21235; ARI1_UBAl; 1.
DR Pfam; PF19422; Ariadne; 1.
DR Pfam; PF01485; IBR; 2.
DR Pfam; PF00627; UBA; 1.
DR SMART; SM00647; IBR; 2.
DR SMART; SM00165; UBA; 1.
DR SUPFAM; SSF57850; RING/U-box; 3.
DR SUPFAM; SSF46934; UBA-like; 1.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS50030; UBA; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Ligase {ECO:0000313|EMBL:EAL67912.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000002195};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
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 DOMAIN 1..42
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT DOMAIN 211..413
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 215..265
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 60..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 563 AA; 64486 MW; B3479019CF08D035 CRC64;
MDKDLILAQL LEFGYDPVVA QTALEQTNWK DIDKAIDYIY THFGEGMNKA ATAMEYTQNK
NNSTTKPTST QAPISRSNSK LKTSGKRIKS SITISTGSEE YNSDNEYEDY DEENEYYQDV
DDYEFDIAVV DAFPKTNTVI QAVDIVKTAL SEIDKIASIT ETSPSAATLL LCHFQWNGNK
LLERYYEDPE KVIAQAGIKK IDQFFTHQNV KGESCSVCAD DLDSLNGSYL PCKHYSCNDC
WNQYLSLKVL EGGATSITCM GLKCPSVIPD EFINLVAPTV YPKYLERLAQ TYVDQNPNMR
WCPAPKCGNA LKADSQTEAT ALCSCGFKIC FKCKQESHFP ADCEKMKHWK KKCEDDSETA
NWISTNTQDC PKCHSAIEKN GGCMHMTCKK CKHEFCWICL GNWIGHSNCN SYKKEENSNK
SESKKQLERY LFYFHRFNTH EQAKKFETKL RTAALETIIS FQNKTDKRWI DIKFVETSTE
ILIQCRRTLK YTYVYGYFME DGPEKNLFEY IQSDLEKTTE QLSFLLSQAH QDLKIFDLKE
MTNLASTKLK HLLEGVEDGF INQ
//
