ID D8RFG5_SELML Unreviewed; 740 AA.
AC D8RFG5;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=SELMODRAFT_410663 {ECO:0000313|EMBL:EFJ28864.1};
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:EFJ28864.1, 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 -!- 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; GL377578; EFJ28864.1; -; Genomic_DNA.
DR RefSeq; XP_002969740.1; XM_002969694.1.
DR AlphaFoldDB; D8RFG5; -.
DR STRING; 88036.D8RFG5; -.
DR EnsemblPlants; EFJ28864; EFJ28864; SELMODRAFT_410663.
DR GeneID; 9646032; -.
DR Gramene; EFJ28864; EFJ28864; SELMODRAFT_410663.
DR KEGG; smo:SELMODRAFT_410663; -.
DR eggNOG; KOG0167; Eukaryota.
DR HOGENOM; CLU_006348_5_1_1; -.
DR InParanoid; D8RFG5; -.
DR OrthoDB; 2721872at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000001514; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd16664; RING-Ubox_PUB; 1.
DR Gene3D; 1.20.930.20; Adaptor protein Cbl, N-terminal domain; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR036537; Adaptor_Cbl_N_dom_sf.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000225; Armadillo.
DR InterPro; IPR045210; RING-Ubox_PUB.
DR InterPro; IPR003613; Ubox_domain.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR23315; U BOX DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR23315:SF7; U-BOX DOMAIN-CONTAINING PROTEIN 4; 1.
DR Pfam; PF00514; Arm; 3.
DR Pfam; PF04564; U-box; 1.
DR SMART; SM00185; ARM; 6.
DR SMART; SM00504; Ubox; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50176; ARM_REPEAT; 3.
DR PROSITE; PS51698; U_BOX; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Ligase {ECO:0000313|EMBL:EFJ28864.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001514}.
FT DOMAIN 242..316
FT /note="U-box"
FT /evidence="ECO:0000259|PROSITE:PS51698"
FT REPEAT 493..535
FT /note="ARM"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
FT REPEAT 574..616
FT /note="ARM"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
FT REPEAT 615..657
FT /note="ARM"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
FT REGION 336..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 183..210
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 367..381
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 740 AA; 81136 MW; 7BCAAC64289706EF CRC64;
MENGTLLVDI ALSIRMIIHM CESAKSQQGN CLALAAQLRL LKQLFDELRQ SKFPLSDATI
EAFGSLQSAL QGAKEVLGQC SKGSKIYSFL KSPQCVDQFQ ELSAEIETIL SASRLALPRV
SKQVQCMAEN CVLELRKASY SKDVLEEQIR QEIEALLCDH REGRKASREK LDKLAGCLGI
TTKEQISEEL NALEKDRGEA GRNKDKLEEE FIDQVISLFM QLAEDNFDDG NVKGETQSQE
VQIPADFRCP LSLELMYDPV IVASGQTYER AYIQHWLDQG NTRCPKTGKP LAHINLIPNY
TVKALIASWC QTNDVPLPKV DAVKSTNWLP PTFSEAEEAR EDTSVIPSGL DTDCEERSSD
HGSSTGIVSG RRKDKDDVYE KRMPSGPVMR VRSSSTYSSE LSGEVEALGL SPSRNSPDHF
PIFTRQMQSS KQKERKSYKS VYAGGDKVAD AGIERLVQNL ASTDLEVQRS AASELRVMTK
NSIEDRNRIA HAGGITPLIA LLSSGDAQTQ ENAVTALLNL SLNEHNKAEI AEAGAIDPLI
DVLKSGTSDA RENAAATLCS ISVEDYKEKI GARGAIPPLV DLLRTGTPRG KKDAALALHN
LSLFRENKVR IVAAGGVKPL INLICEPRMG MVDRAVDVLV TLSSIPEGRM AIGEEGGIPP
LVEVVEAGSP LAKERAAAAL LQLCTNNPKY RRTTLQEGAL PPLYILSQIG TSRAKEKAAG
ILRLFREQRQ ASMSRRNRHM
//
