ID F7W226_SORMK Unreviewed; 1546 AA.
AC F7W226;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 24-JAN-2024, entry version 56.
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};
GN ORFNames=SMAC_04659 {ECO:0000313|EMBL:CCC11676.1};
OS Sordaria macrospora (strain ATCC MYA-333 / DSM 997 / K(L3346) / K-hell).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Sordaria.
OX NCBI_TaxID=771870 {ECO:0000313|EMBL:CCC11676.1, ECO:0000313|Proteomes:UP000001881};
RN [1] {ECO:0000313|EMBL:CCC11676.1, ECO:0000313|Proteomes:UP000001881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-333 / DSM 997 / K(L3346) / K-hell
RC {ECO:0000313|Proteomes:UP000001881};
RC TISSUE=Mycelium {ECO:0000313|EMBL:CCC11676.1};
RX PubMed=20386741; DOI=10.1371/journal.pgen.1000891;
RA Nowrousian M., Stajich J., Chu M., Engh I., Espagne E., Halliday K.,
RA Kamerewerd J., Kempken F., Knab B., Kuo H.C., Osiewacz H.D., Poeggeler S.,
RA Read N., Seiler S., Smith K., Zickler D., Kueck U., Freitag M.;
RT "De novo assembly of a 40 Mb eukaryotic genome from short sequence reads:
RT Sordaria macrospora, a model organism for fungal morphogenesis.";
RL PLoS Genet. 6:E1000891-E1000891(2010).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CCC11676.1}.
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DR EMBL; CABT02000021; CCC11676.1; -; Genomic_DNA.
DR RefSeq; XP_003346486.1; XM_003346438.1.
DR STRING; 771870.F7W226; -.
DR GeneID; 10803877; -.
DR KEGG; smp:SMAC_04659; -.
DR VEuPathDB; FungiDB:SMAC_04659; -.
DR eggNOG; KOG0803; Eukaryota.
DR HOGENOM; CLU_000471_0_0_1; -.
DR InParanoid; F7W226; -.
DR OMA; IYGSHWE; -.
DR OrthoDB; 179130at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000001881; Unassembled WGS sequence.
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; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
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; SM01197; FANCL_C; 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:UP000001881};
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 1484..1530
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
SQ SEQUENCE 1546 AA; 171586 MW; 1DE0995978564268 CRC64;
MKKGAFGSGG FGAFSSSTAS LSYVAPPPDL SSLPQDVIVP FKNLLKRDST TKSKALEEIL
ACVKKSDEPV DDSVIDLVKS AKKRIEKTLP KLVGPWVAGT FDKDKGVARA ALAVSAHILD
SDQKKAKFWI AFQGKLLEYA NEAIRETVDS LSDERTTSKE DMEAKYYRVL GSSMAMIQHL
LPTIKDDQYP DELKRFFDAD TLWTLAASDD ASVRRAFYQL VASYLDNKPS LLEPKLKDVG
RALVAESPKK DQRGSAVDLL RALISVTKRF PKVWGSKSPL DRLRPLVQKG SQGGSDEYWT
ELDQLLVVLS TSSPDYAATT SAFLKSMRTA ITSREERRQN TASAWACYLN TVDRFTASST
PSPEFLQENL YPLTQEYLLP SDKTSAWASA QPPHLLKAWK IVPYTTSEEV RSSAKEEWQK
LGDDFATDLS NSLPEVSPDY EKSQWELAAI GERWFNLVEG FLRGAPSQQT FDGDSDLPSL
VASTSSKLLD SAQDLLYRRN YKPFCAAAVL KAAFTKVPGL CAKSDLIKKI FPLGDQEAFE
KIVVSRSFPY LASCLAAVTQ DQPDFSDQVW AKLIDAALSR GFPSGAPIVK DLVSVPLPQA
VAQKNESLQK FIVEAWHDFA QEEPSSPVVA QLCKASISHS ILDGSAIQSL ASSFAQDVDV
PGKYDPEFKA LELLLRSNSA LFGDAPVDLF MKLLSLEETS DSEKASKVAA IRSLIQKQYG
ADKLWLEVIR RSLADAEPSS LDINTLVRHA KDMLRSDPSL SITSSFGGAY FLATEGKGST
PTTQKRDRQG RSIPARMAVY TTQLLRDVEV EKLPVDLLEL IFLTGVLAND DLTVMKENGL
WSLHATEETR TERSDEIQSF LGLGTTLLAR VAGASTAWKD GDLNGNSLAE TLIQSLLQKA
VDLSFKSLYA SKALTELLQA LVSVHGYPVG VKCDEWFNKL GVMKATPQTV FAAIAFLIGL
DEGLSSSRAV ANLYNRLVSD IVGCFPSSPK TLYNMVLLTV CLSVYPPAKT PVEQRKLVFA
LKQFSTWVQT SDEMTFGLTA EVCKGIHRIL PNVAQVYGPY WREAIDYCLL LWEKARSDTP
QRWPAYVLPS IRLISAMETL EDANDDLVEA LEETALDRSK ALIRLLELPH DVVNTARRIL
DETLCRVVQK IPLKHLTSEE DLLSNLYGLL SSGSRDVQTA AFSLLHRALP AKQEEEVLET
LLEEKAAKLP DELLALVQSV PALEKYTDEE LAVFPVDIRA YLLGWHLVFD AYNQAPLQVR
KQYTEYLKAD NSLNTLLELM FDILGHSAGQ ALNLDKSTFS VEHIRSYDIT QSDEGSPERD
MQWLLVHLFY LSLKFLPGLV KSWYLDLRSK QTKIALDSWM AKYYAPLLIS DALDEVNDWA
SSQEAPQEDE KELRVRVNRM AKEISAGYEI DEEFASIAIK IPAGYPLESV EVIGENRVAV
NEKKWQSWVR ATQGVITFAN GSITDGLAAF RRNIIGALKG HTECPICYAV VSADKKLPDK
RCGTCNNLFH RLCLYKWFQN SNKNTCPLCR NPIDYLGSST RRGGGD
//
