ID A0A7N2MC94_QUELO Unreviewed; 1212 AA.
AC A0A7N2MC94;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 28-JAN-2026, entry version 18.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
OS Quercus lobata (Valley oak).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fagales; Fagaceae; Quercus.
OX NCBI_TaxID=97700 {ECO:0000313|EnsemblPlants:QL08p046141:mrna, ECO:0000313|Proteomes:UP000594261};
RN [1] {ECO:0000313|EnsemblPlants:QL08p046141:mrna, ECO:0000313|Proteomes:UP000594261}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. SW786 {ECO:0000313|EnsemblPlants:QL08p046141:mrna,
RC ECO:0000313|Proteomes:UP000594261};
RX PubMed=27621377; DOI=10.1534/g3.116.030411;
RA Sork V.L., Fitz-Gibbon S.T., Puiu D., Crepeau M., Gugger P.F., Sherman R.,
RA Stevens K., Langley C.H., Pellegrini M., Salzberg S.L.;
RT "First Draft Assembly and Annotation of the Genome of a California Endemic
RT Oak Quercus lobata Nee (Fagaceae).";
RL G3 (Bethesda) 6:3485-3495(2016).
RN [2] {ECO:0000313|EnsemblPlants:QL08p046141:mrna}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (JAN-2021) 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 EMBL; LRBV02000008; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A7N2MC94; -.
DR EnsemblPlants; QL08p046141:mrna; QL08p046141:mrna; QL08p046141.
DR Gramene; QL08p046141:mrna; QL08p046141:mrna; QL08p046141.
DR InParanoid; A0A7N2MC94; -.
DR OMA; VKMIMAK; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000594261; Chromosome 8.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd21037; MLKL_NTD; 1.
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; 4.
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; IPR059179; MLKL-like_MCAfunc.
DR InterPro; IPR045210; RING-Ubox_PUB.
DR InterPro; IPR052608; U-box_domain_protein.
DR InterPro; IPR003613; Ubox_domain.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45958; RING-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR PANTHER; PTHR45958:SF5; RING-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR Pfam; PF00514; Arm; 1.
DR Pfam; PF04564; U-box; 1.
DR SMART; SM00185; ARM; 7.
DR SMART; SM00504; Ubox; 1.
DR SUPFAM; SSF48371; ARM repeat; 3.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51698; U_BOX; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Reference proteome {ECO:0000313|Proteomes:UP000594261};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT DOMAIN 261..335
FT /note="U-box"
FT /evidence="ECO:0000259|PROSITE:PS51698"
FT DOMAIN 597..611
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT REGION 559..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 196..223
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 565..579
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1212 AA; 134366 MW; 5A6D80FB1D4C779D CRC64;
MMSLDMATSA SVGPASEAVT QTVEAILEIV LAANDVLVKK ESFKELATYL ERIVPILKEL
NRKNVSDSES LNNAIEILNR EIRAAKQLTL ECSKRNKVYL LMNCRTIVKR LEDTVKEISR
ALDLIPMASL DLTSGISEEI GELCDKMQRA EFRAAMAEEE ILEKIESGIQ ERNVDRSYAN
NLLVLIAEAV GIPTDRSALK KEFEEFKNEI ESTRLRKDEA EAIQMDQIMA LLERADATSS
PREKEIKHFS KRKSLGSQPL EPLQSFYCPI TRDVMEDPVE TSSGQTFERR AIEKWFADGN
KLCPLTMTSL NTSILRPNKT LRQSIEEWKD RNTMITIGSI KPKLNSEEED EVLHSLEQLQ
ELCEQRDLNR EWVILEDYVP TLIQLLAKNR DIRNHSLVIL CILAKDSDDA KERIVKADNA
IESIVRSLGR RVGERKLAVE LLLELSKCHL ARDCIGKVQG CILLLVTMSS SDDSQAARDA
QALLENLSFS DQNIIQMAKA NYFRHLLQRL STAAMRLNAN RNREGNKDDG ASLKFSIQEK
MDLQPVWTVD EAHNLVSKAE RRQGTEGSSR TVPRQTGGVN NRDAAKNPCT RPTAKHCYRC
DEPGHSSNAC PACKPVHLAN HADEYGGELE EGYGDDNLLD AEIADKEAEF LCGVDCTLLT
PKQEELSQHH SIFHSLWCFY LDIETLEGNF FNFLVSKPEG QCPSKPEAMI GVRSDNEGPE
DVKLIMATTL AEMELTDHNK ESLFEGGVLG PLLHFVSHGD PHMKNVAAKA LRNLSSLPKI
GLQMIKEAAV RPLLDILFSH SASSSSLREH AAGTIMHLAV STMSQESSQI PVSLLECDED
ILRLFSLINL TGPEIQQSII QTFQALCQSP SAPMIKTKLS QCAAIQVLVQ LCEHDDPCVR
ANVVKLFCCL AEGGDEVTLA EHVNQKCIET LLKIIKSSKD EEEIASVMGI VSNLPELPQI
TQWLLDAGAL PIIFSHLHNG KQNNLYKNQL IENAVGAICR FIVPTNLEWQ KSAAGTGIIP
VLVQLLESGT TLTKKRAAIS LCRFSESSLV LSRLIPKRKG FLCFSAPPET VCPVHGGICS
IESSFCLIEA DAVRPLVRIL GEHDPGACEA SLDALLTLIE GERLQSGSKV LGEANAIPPI
IKFLGSPSPS LLEKALNALE RIFRLVDFKM KYGALAQMPL VDITQRGSGS VKSLAARILA
HLNVLHDQSS YF
//
