ID D8SKS5_SELML Unreviewed; 281 AA.
AC D8SKS5;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 24-JAN-2024, entry version 59.
DE SubName: Full=Ubiquitin-protein ligase, PUB61 {ECO:0000313|EMBL:EFJ15030.1};
GN ORFNames=SELMODRAFT_119447 {ECO:0000313|EMBL:EFJ15030.1};
OS Selaginella moellendorffii (Spikemoss).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Lycopodiopsida; Selaginellales; Selaginellaceae; Selaginella.
OX NCBI_TaxID=88036 {ECO:0000313|Proteomes:UP000001514};
RN [1] {ECO:0000313|EMBL:EFJ15030.1, ECO:0000313|Proteomes:UP000001514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551031; DOI=10.1126/science.1203810;
RA Banks J.A., Nishiyama T., Hasebe M., Bowman J.L., Gribskov M.,
RA dePamphilis C., Albert V.A., Aono N., Aoyama T., Ambrose B.A., Ashton N.W.,
RA Axtell M.J., Barker E., Barker M.S., Bennetzen J.L., Bonawitz N.D.,
RA Chapple C., Cheng C., Correa L.G., Dacre M., DeBarry J., Dreyer I.,
RA Elias M., Engstrom E.M., Estelle M., Feng L., Finet C., Floyd S.K.,
RA Frommer W.B., Fujita T., Gramzow L., Gutensohn M., Harholt J., Hattori M.,
RA Heyl A., Hirai T., Hiwatashi Y., Ishikawa M., Iwata M., Karol K.G.,
RA Koehler B., Kolukisaoglu U., Kubo M., Kurata T., Lalonde S., Li K., Li Y.,
RA Litt A., Lyons E., Manning G., Maruyama T., Michael T.P., Mikami K.,
RA Miyazaki S., Morinaga S., Murata T., Mueller-Roeber B., Nelson D.R.,
RA Obara M., Oguri Y., Olmstead R.G., Onodera N., Petersen B.L., Pils B.,
RA Prigge M., Rensing S.A., Riano-Pachon D.M., Roberts A.W., Sato Y.,
RA Scheller H.V., Schulz B., Schulz C., Shakirov E.V., Shibagaki N.,
RA Shinohara N., Shippen D.E., Soerensen I., Sotooka R., Sugimoto N.,
RA Sugita M., Sumikawa N., Tanurdzic M., Theissen G., Ulvskov P., Wakazuki S.,
RA Weng J.K., Willats W.W., Wipf D., Wolf P.G., Yang L., Zimmer A.D., Zhu Q.,
RA Mitros T., Hellsten U., Loque D., Otillar R., Salamov A., Schmutz J.,
RA Shapiro H., Lindquist E., Lucas S., Rokhsar D., Grigoriev I.V.;
RT "The Selaginella genome identifies genetic changes associated with the
RT evolution of vascular plants.";
RL Science 332:960-963(2011).
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
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DR EMBL; GL377625; EFJ15030.1; -; Genomic_DNA.
DR RefSeq; XP_002984018.1; XM_002983972.1.
DR AlphaFoldDB; D8SKS5; -.
DR STRING; 88036.D8SKS5; -.
DR EnsemblPlants; EFJ15030; EFJ15030; SELMODRAFT_119447.
DR Gramene; EFJ15030; EFJ15030; SELMODRAFT_119447.
DR KEGG; smo:SELMODRAFT_119447; -.
DR eggNOG; KOG4642; Eukaryota.
DR HOGENOM; CLU_056455_0_0_1; -.
DR InParanoid; D8SKS5; -.
DR OMA; WAGVEHD; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000001514; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
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 CDD; cd16654; RING-Ubox_CHIP; 1.
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; IPR045200; CHIP.
DR InterPro; IPR045202; CHIP_RING-Ubox.
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; PF13414; TPR_11; 1.
DR Pfam; PF07719; TPR_2; 1.
DR Pfam; PF04564; U-box; 1.
DR SMART; SM00028; TPR; 3.
DR SMART; SM00504; Ubox; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS50005; TPR; 2.
DR PROSITE; PS51698; U_BOX; 1.
PE 4: Predicted;
KW Ligase {ECO:0000313|EMBL:EFJ15030.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001514};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT REPEAT 12..45
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 80..113
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 202..276
FT /note="U-box"
FT /evidence="ECO:0000259|PROSITE:PS51698"
SQ SEQUENCE 281 AA; 32268 MW; 64ECE7EA5D51B3AC CRC64;
MSAKIVSAAK QAELLKEQGN LYFKKERLSA AIDAYTEAIT LCPDVPVYWT NRALCYQRKG
DWERVEADCW KALELDKASV KAHYMLGLAL LNSQHYAEAI KQLEKALDLG RGANPAAYMV
EQIWQELSKA RYTQWEVATA ARRAKQKEIR YSAETPMEDD DIVESDESEW KAISRLREIY
QEKLRTIADI FNKAAESDIP SEIPEHLCCK ITMDVFRDPV ITPSGVSYER AVLLEHLRKV
GKFDPWTRAP LEPEQIVSNL ALKEAVQAYM LDHGWAYKPY Y
//