ID J3L8F4_ORYBR Unreviewed; 1887 AA.
AC J3L8F4;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE RecName: Full=E3 ubiquitin-protein ligase listerin {ECO:0000256|ARBA:ARBA00017157, ECO:0000256|RuleBase:RU367090};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483, ECO:0000256|RuleBase:RU367090};
DE AltName: Full=RING-type E3 ubiquitin transferase listerin {ECO:0000256|RuleBase:RU367090};
OS Oryza brachyantha (malo sina).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4533 {ECO:0000313|EnsemblPlants:OB01G55100.1};
RN [1] {ECO:0000313|EnsemblPlants:OB01G55100.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IRGC 101232 {ECO:0000313|EnsemblPlants:OB01G55100.1};
RX PubMed=23481403;
RA Chen J., Huang Q., Gao D., Wang J., Lang Y., Liu T., Li B., Bai Z.,
RA Luis Goicoechea J., Liang C., Chen C., Zhang W., Sun S., Liao Y., Zhang X.,
RA Yang L., Song C., Wang M., Shi J., Liu G., Liu J., Zhou H., Zhou W., Yu Q.,
RA An N., Chen Y., Cai Q., Wang B., Liu B., Min J., Huang Y., Wu H., Li Z.,
RA Zhang Y., Yin Y., Song W., Jiang J., Jackson S.A., Wing R.A., Wang J.,
RA Chen M.;
RT "Whole-genome sequencing of Oryza brachyantha reveals mechanisms underlying
RT Oryza genome evolution.";
RL Nat. Commun. 4:1595-1595(2013).
RN [2] {ECO:0000313|EnsemblPlants:OB01G55100.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2013) to UniProtKB.
CC -!- FUNCTION: E3 ubiquitin-protein ligase. Component of the ribosome
CC quality control complex (RQC), a ribosome-associated complex that
CC mediates ubiquitination and extraction of incompletely synthesized
CC nascent chains for proteasomal degradation.
CC {ECO:0000256|RuleBase:RU367090}.
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 ECO:0000256|RuleBase:RU367090};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|RuleBase:RU367090}.
CC -!- SUBUNIT: Component of the ribosome quality control complex (RQC).
CC {ECO:0000256|RuleBase:RU367090}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000256|ARBA:ARBA00004514}.
CC -!- SIMILARITY: Belongs to the LTN1 family. {ECO:0000256|ARBA:ARBA00007997,
CC ECO:0000256|RuleBase:RU367090}.
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DR STRING; 4533.J3L8F4; -.
DR EnsemblPlants; OB01G55100.1; OB01G55100.1; OB01G55100.
DR Gramene; OB01G55100.1; OB01G55100.1; OB01G55100.
DR eggNOG; KOG0803; Eukaryota.
DR HOGENOM; CLU_002223_0_0_1; -.
DR OMA; EAIHTWK; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000006038; Chromosome 1.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:1990112; C:RQC complex; IEA:UniProtKB-UniRule.
DR GO; GO:0043023; F:ribosomal large subunit binding; IEA:UniProtKB-UniRule.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0072344; P:rescue of stalled ribosome; IEA:UniProtKB-UniRule.
DR GO; GO:1990116; P:ribosome-associated ubiquitin-dependent protein catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd16491; RING-CH-C4HC3_LTN1; 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; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR039795; LTN1/Rkr1.
DR InterPro; IPR039804; RING-CH-C4HC3_LTN1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR011016; Znf_RING-CH.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR12389:SF0; E3 UBIQUITIN-PROTEIN LIGASE LISTERIN; 1.
DR PANTHER; PTHR12389; ZINC FINGER PROTEIN 294; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00744; RINGv; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU367090};
KW Reference proteome {ECO:0000313|Proteomes:UP000006038};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU367090};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU367090};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU367090};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 1837..1884
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
SQ SEQUENCE 1887 AA; 212602 MW; AF4F288571800AC1 CRC64;
MGKNKGRAAS SGLAASLLPH AQGAVPTDVD SEVLQHLKRL GRKDPTTKLK ALSTLSMLFA
QKPGDEVVQI VPQWAFEYKR LLLDYNREVR RATHETMSSL VKTVKKGLAP HLKSLMGPWW
FSQFDPALEV AQAARHSFEA AFPQADKRLD ALMLCVKEIF LHLNENLKLT TQALSDKATP
VDELEDMHQR VISSSLLSMA TLIDILLGVK LQKCGHDCSN PENKSLSRVL SAMLSSAESA
FSMHKHFLDF LKSKSVIIRS ATYSLLTSYI KYVSHVFNEE TMKVLSPALL GAFHEKDPSC
HSSMWDAFLA LSRRFPEAWS YCNIHKVVFS RFWHFLQNGC YGSKQASYPL LVQFLESVPS
EDVTAEQFVF DFLHNLWAGR NQCQLSAADS LAFFSAFKQS FLWLLKVRSR HSERDSSDDI
PIKLINSILA KIVWHDYLLI SSAENQAISL SGLSDEATSD DHHLSRKESL LASNMRYPTY
YLQDLGKFII EMLDEISAME DHLLKIACET LLKDCLDIIH QRERLSNFQN HVEQVVSFFI
SLDQLVVQKG ETWPLERLAR PLVEQSVPAI KSMDTPVLIK LLSVLVEIFR PAPLFLKIAH
RESKESVQAY LDVFNEFVPW CLNGEHSTCS SKIDLLLSLT IDECFFDQWC SIIKYTRAKQ
KHSVDDNNSH VEDQFELLTL ILQKVRQRIA GGKLRNLQKN GCLPEHWQHD LLDSAAESVF
CDLPATDSHV HFVCAALGGS DQDDQICFLS ADTVKKILES ILKCLTSVLM GSAFEWARSV
YVVLLPTEAE HLKVIGANSS LSNIEIAHFA FKILEGSLFA LKMLEEDSLF PSILAALFVI
EWECSMTLTL DEEHDLEGYK EDYVGYSVRN NSDGHLDEKM HLKANLAESI HTFRQSLSSS
FWSDLHPCTL NSLVNILART VRCALFQTVE LPTASTSSLC SEWVMNMLKF ICLDHVKLQS
FFDLLLSEGE HWPLWVKPSL QNGNAPMKIQ LEPVITYETG LKHHQFVAFV DKLVLNLGFG
EVILGVPGST CYNRAQSFGA TSSVPSFSRA WVAAEILCTW KWKEGSVFST FLPSLIQHLK
MESCAEVSIL SLLLDTLLEG AFHECNEWVL FDAWHISENE IEKIQDNFLR ALVALLFSTN
NINDCIWRES DALVFFEKVL SNLFIGSTVN RKCVTTLPFV MSTIIKPLSG ELKLNEASSY
TDLVGKSILS WLDVAISCLS SSPREVAQQG IIDWMQVVLS CFPLNIIGGA QKLEVKIERK
ISDVERSLLL TLFQKYQIFT METRSLSTSG TILSTMVELL GVKLIAVVVG YCWTELQEDD
LYFVYHSVQK WIESAVLLGE EMTDAINDAV IYKKSNEDAL EKLKVVVSAI DELTLNFSQT
ALVTLYHLNH LVNLQETENF HSLQIIRSED YAERNNKMME SMLRLFLASG VSEAIAKSCC
EEASSIIASS RVAYMHFWEL VASFVIHASP QTRRCALESM ELWGLAKGSI SGLYSILFSS
QQISHLQFAA YSLLLSEPLC QFSLVKECSL GLNRPLTQES DMGQSIELMP DAERTLDLRE
ELSSLIEMPT SELLQTDLLA QDRVDAFIAW SLLLSHLQLL PPSSITREKV LQYIQDKISP
CILDCIFQHI PLRTGALSGK KKDAELMPEA EVAAIASKNA ITACSLFSCI ESLWPVGTSQ
MASLAGGLYG MMIRLLPSYV RTWFTSLRDR SLSNSIESLT RVWCSPPLLL DEFSQVRDSL
YADDSFSVSV NRSAYEIVAT YKKEETGIDL VIRLPSCYPL RHVDVECTRS LGISEVKCRK
WLLSLTAFVR NQNGAIAEAI HTWKSNFDKE FEGVEECPIC YSILHTSNHS LPRLACKTCR
HKFHGACLYK WFSTSNKSTC PLCQTPF
//
