ID A0A0M9WE13_9EURO Unreviewed; 1625 AA.
AC A0A0M9WE13;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
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=ACN38_g7949 {ECO:0000313|EMBL:KOS41202.1};
OS Penicillium nordicum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=229535 {ECO:0000313|EMBL:KOS41202.1, ECO:0000313|Proteomes:UP000037696};
RN [1] {ECO:0000313|EMBL:KOS41202.1, ECO:0000313|Proteomes:UP000037696}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAOMC 185683 {ECO:0000313|EMBL:KOS41202.1,
RC ECO:0000313|Proteomes:UP000037696};
RA Nguyen H.D., Seifert K.A.;
RT "Genome sequencing of Penicillium nordicum.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
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:KOS41202.1}.
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DR EMBL; LHQQ01000139; KOS41202.1; -; Genomic_DNA.
DR STRING; 229535.A0A0M9WE13; -.
DR OrthoDB; 179130at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000037696; 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:UP000037696};
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 1573..1619
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
SQ SEQUENCE 1625 AA; 180314 MW; 8ECB7D08DE0B271C CRC64;
MSKKFKSQAS SSRAAASAFG SFGGFSGGLS SEGKEPSALT YIAAPPDLSR IAEQQLVIAF
KNLLKKDDIT RLKALEELRD HISTVQETKR TLDDGFLDAW VRIYPRLSID LSRRVRQIAH
PIQGTISGLV GKRIVPNLPK TIGAWIAGIY DNDRPVHRAA LESFTKVFTT EEKRNNVWKI
YQSSILDFVE DVILHQTALT LSDERTVKRD DAEGKYARVA GAAILLFNRV LGNASDEDLQ
KNLPEIENLL ASKNLWALCY HDDPYVRRSI YILLRSAVSR EPGWIDWKTL SSAVIGKSLS
LQQIGSATEL SESLLSLSSL RPQIWTDDYT GKSSASKRLR QYMQKGSQGG HCNFWSNLDQ
LLRIIPQEVL AGADKAAADH GITSTSAIAL SEALQEGLNS REEPRSNLAI GWKSYTQIGT
WLATLVPQEQ KSEFIAKRLS PLVVQYVKID PELTQWSLPA ELAEGICVDY VFTLASTKQA
QELQSLCTFL SDGLLEAVKL SSPEQSKDFL ESQDSICAQA KRLLDLKSAV LSRVADIEVE
SQVSEIFERT STSLLEGCLE VLRSRNGKPY GAAATVVECV RSLPSVAKRS QDLQYFVQND
APELLLSPSA DRLISIILQC REWDGFASSF ENVVERALAL ELEPSNVHVL QSLLSSLDFN
HAEHKDKINS LVVRALGKAC QGSHVHWPII TAVLQNKTSH GVLMDQIFLS LIEALSSDDK
VFYALHGLSH IGKSAPSSVR VFQNGSLGSK LAGKLLFLTE SPSEEVASLA EALLKSLKES
GIGDTSAKSG IEILQHGFSH VDEESLSIES LLAIAEELLP GLTAERATNT AKDILPSRRS
WEESLTPFLQ LPPRPSIAIT SPLGGAVHLI QRELSDSFKA LWPTIPRDSD HRSSAFRLAI
FTISILSTSE LSKHLDQEDL ETLFHFLPLA IQLIDDDLSI ENCNGISGLE LADQREEYME
IVFAGRKVLG NWIRDNEPVN FAPERTISSS FAEFWETRLE ELKGTSPLDY RVGEAFVKIM
AVTDSLQKSK SSEDVAKICR EARTANLIRS ASLFAVLRNS ILSNPIGNRI CNELVADSTG
LKPQDPSQVG LRKLALLNIL LSGEEDVVST IPTQRLVFLT KNLIECLQSG SMALGLKSEV
IQTLSIVLPA LGEIYGSHWE ESMGILNSVL RETNGGEEAL PLLVSSFRLF ARLKSTAESD
SNDDVQDAWL DRKAGLFNAL ASTIDSFDSS TTFHQPRDVA VDLLRRLINT IPIDSLEDVS
ETFHLLTAHS RAVQRTAYTI LHHYIPHAQE KVSFEVALSK TAVSLPDELV SLLLEPPTMK
MVSAAYGDDK MWTSMRAYLL SWKVVFDHFS TASLPVQEYY LSSIRENNIL IPLLEFTFDF
LQKSHGKMID ASKLNIRSFE PDESESAEKE TQWLLVHLYY LCLRYSANMT KNWWIDTKKR
IKGPVEAWSE RYVSPLVVED ALKSVTDWIA TQDANEERAL EVKISPKTGE IIASIPVDEE
SPPVAISITL PPAYPLQPAL VVGRSRVLVD EKKWKSWLLT IQGVIMFANG NLVDGLLAFR
RNVQGALKGQ SECAICYSVI STDMQTPNKR CATCKNTFHS VCLFRWFKSS NQSTCPLCRN
NFVYV
//
