ID   A0CFD2_PARTE            Unreviewed;       281 AA.
AC   A0CFD2;
DT   28-NOV-2006, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2006, sequence version 1.
DT   27-MAR-2024, entry version 79.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN   ORFNames=GSPATT00037938001 {ECO:0000313|EMBL:CAK69499.1};
OS   Paramecium tetraurelia.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC   Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX   NCBI_TaxID=5888 {ECO:0000313|EMBL:CAK69499.1, ECO:0000313|Proteomes:UP000000600};
RN   [1] {ECO:0000313|EMBL:CAK69499.1, ECO:0000313|Proteomes:UP000000600}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK69499.1,
RC   ECO:0000313|Proteomes:UP000000600};
RX   PubMed=17086204; DOI=10.1038/nature05230;
RG   Genoscope;
RA   Aury J.-M., Jaillon O., Duret L., Noel B., Jubin C., Porcel B.M.,
RA   Segurens B., Daubin V., Anthouard V., Aiach N., Arnaiz O., Billaut A.,
RA   Beisson J., Blanc I., Bouhouche K., Camara F., Duharcourt S., Guigo R.,
RA   Gogendeau D., Katinka M., Keller A.-M., Kissmehl R., Klotz C., Koll F.,
RA   Le Moue A., Lepere C., Malinsky S., Nowacki M., Nowak J.K., Plattner H.,
RA   Poulain J., Ruiz F., Serrano V., Zagulski M., Dessen P., Betermier M.,
RA   Weissenbach J., Scarpelli C., Schachter V., Sperling L., Meyer E.,
RA   Cohen J., Wincker P.;
RT   "Global trends of whole-genome duplications revealed by the ciliate
RT   Paramecium tetraurelia.";
RL   Nature 444:171-178(2006).
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};
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DR   EMBL; CT868069; CAK69499.1; -; Genomic_DNA.
DR   RefSeq; XP_001436896.1; XM_001436859.1.
DR   AlphaFoldDB; A0CFD2; -.
DR   STRING; 5888.A0CFD2; -.
DR   EnsemblProtists; CAK69499; CAK69499; GSPATT00037938001.
DR   GeneID; 5022681; -.
DR   KEGG; ptm:GSPATT00037938001; -.
DR   eggNOG; KOG4642; Eukaryota.
DR   HOGENOM; CLU_056455_1_0_1; -.
DR   InParanoid; A0CFD2; -.
DR   OMA; WAGVEHD; -.
DR   Proteomes; UP000000600; Partially assembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0051087; F:protein-folding chaperone binding; IBA:GO_Central.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR   GO; GO:0071218; P:cellular response to misfolded protein; IBA:GO_Central.
DR   GO; GO:0045862; P:positive regulation of proteolysis; IBA:GO_Central.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR   GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IBA:GO_Central.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR013105; TPR_2.
DR   InterPro; IPR019734; TPR_repeat.
DR   InterPro; IPR003613; Ubox_domain.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR46803; E3 UBIQUITIN-PROTEIN LIGASE CHIP; 1.
DR   PANTHER; PTHR46803:SF2; E3 UBIQUITIN-PROTEIN LIGASE CHIP; 1.
DR   Pfam; PF07719; TPR_2; 1.
DR   Pfam; PF04564; U-box; 1.
DR   SMART; SM00028; TPR; 2.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000000600};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT   DOMAIN          189..265
FT                   /note="U-box"
FT                   /evidence="ECO:0000259|Pfam:PF04564"
SQ   SEQUENCE   281 AA;  32958 MW;  7927F4D5DC04F787 CRC64;
     MQTTTKAQQF KVKGNEAFQS KNYLEAIQFY SQAIAEDNTE SIFFSNRSNC YYQLRRYQEA
     CNDATEALEL DEKNIKAHMI AGQSICMLAK ERQESSKIDT GIQRILKART LCAGQKKSEY
     EKEIDEKIHK AKKLKWFIQQ EEEKIKNQEI VQQLQDLVKS DVKLTQQEKQ ITLAQIDKYI
     TNEKPKLEIP EYLQCHISKK LLIDPYTTEV GYSYEKALLF SKLHLNQDPY TKYMSHQISK
     PINPQIIYPN INLKQAASEF LAQNPWAYDY NPDQNYKDIE I
//