ID A0A1J1HTF8_9DIPT Unreviewed; 1994 AA.
AC A0A1J1HTF8;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 30.
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|ARBA:ARBA00032366, ECO:0000256|RuleBase:RU367090};
GN ORFNames=CLUMA_CG005016 {ECO:0000313|EMBL:CRK91343.1};
OS Clunio marinus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Chironomoidea; Chironomidae;
OC Clunio.
OX NCBI_TaxID=568069 {ECO:0000313|EMBL:CRK91343.1, ECO:0000313|Proteomes:UP000183832};
RN [1] {ECO:0000313|EMBL:CRK91343.1, ECO:0000313|Proteomes:UP000183832}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Syromyatnikov M.Y., Popov V.N.;
RL Submitted (APR-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}.
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DR EMBL; CVRI01000020; CRK91343.1; -; Genomic_DNA.
DR STRING; 568069.A0A1J1HTF8; -.
DR OrthoDB; 179130at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000183832; Unassembled WGS sequence.
DR GO; GO:0005680; C:anaphase-promoting complex; IEA:InterPro.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:1990112; C:RQC complex; IEA:UniProtKB-UniRule.
DR GO; GO:0097602; F:cullin family protein binding; IEA:InterPro.
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:0031145; P:anaphase-promoting complex-dependent catabolic process; IEA:InterPro.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
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; IPR006578; MADF-dom.
DR InterPro; IPR039804; RING-CH-C4HC3_LTN1.
DR InterPro; IPR001841; Znf_RING.
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; PF10545; MADF_DNA_bdg; 1.
DR SMART; SM00595; MADF; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51029; MADF; 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:UP000183832};
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 5..94
FT /note="MADF"
FT /evidence="ECO:0000259|PROSITE:PS51029"
FT DOMAIN 1944..1991
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
SQ SEQUENCE 1994 AA; 231121 MW; A2C944120C5FC084 CRC64;
MDTKVLIETI KLYPTLYDRK HSSINIEHKN LIWNEISQKI DQPVEKCKAK WRNLRDSYQK
AMKWKHELEA IGKLSSYHPY KHEYLLEFLE VRPKRKISDG SRRSKFKVSN YMLKKQKLED
YNTSQDAHGL SSHAVEFLVE NEKQNIQNDD SNADIVEAVD EQDQYEEITE EEQIYQETSE
HQEESVDSNN KVEEKPFLLS YDCAHETALQ SSEETREEIT YQDTYPNESE TSYTLELDSC
YQIIIMGGKA KQAQRTKGNL KPASSSKASE QLDTLSFTPL DMTITSSIVS GFTEDPFDID
SRIDPNFQMV LRKMGKKDPT TKIKALKEFI DLVGQADNDT LTAVLPFFPK VYIQLSCDVD
ARVRESSQSA LQSIVNKVGK NLAMILKQIF PAWVCGQYDT HPTAASIATN CFEKAFPAKK
ISDVFVFCET ETLDYITKNL TVLTAQTACN PKIYSPEECE AKYQRIVISS LRGYALYLEK
MSSDKLESSM NKNFLLIEND RFWSYHKSKV PQIKSAFFEA LSSLLQHASY LLVNFEEQMT
AIVFKSIDET DAALLSHIWT CVVLVQVKVE NWYKYVNFNK AVFPKLWKIL HSSMCPCVIF
PNLLPFLSKF NKSVLPDDQL QIFYLKFYEN IKFGLINNQM GKSETSAVSS AYFETLQYII
IQIANDSESI ETDKLSFCLG LLDEHVIAVI FWCINAEGFF GKFVFHHIAN MINYFSKTSS
TSKIFESLLN RFWSELYQVL SNSLETTTNI EKIANSHVEL IKSMKSCQQR IRTTKIKFDD
VVEDSPSSSP TKVVENSKNR AYEDELNKLV YKICNVYTER ISSTHEIGFV ENLEILIKEY
QSEELFRHLA KWNNPDEVDI CSLYDTFSAW LLVKELRCES IVEIILVLYK YLKPSEKIDL
LNRWIRVPSV QSWIIMRALS YPLCIEPDIS KLLQMQEVKD HMIHCARQAS NGIYKENLII
LQKYFFQTED SQSNLIDSET CEKIIEIMCE PLTDVARISQ MDQCGSFLAQ ILPVVCADSD
KKSLQEKIFL ALYEFSMIKE VSDDLSEDTL WEVTTAWQDA LSSRDLILDE FLLNSCTKII
QNKLENLSME KISMNDMERV AEVGSKLIMC STEQETPDEK KKIVDMLIKK ILKHNEDENV
NYMENLCLCI ELMHGDIIST TIFDTPPMNF TNTLDTFLKH KIFNLDVITK LSCNIKKVSK
QMMKVEDDND DVEQPGYEIE FSELQNQALE EEATEDYCDM DENLLKEWSD AIYEKFHDIC
YSESILNVIL TRGRNIQSEL ENWIIYLQER LETLMKNLPE NISVIVKEKL FELANVRGGF
WTRSLMNLLN LKCYNVESGI SLLLNDLSKP SSQDEITNNY LNIIQSFSER IDKKSLTIAS
NLFENHSNLI VKVSIIRSLM RNHLNVGDFN EMNDRRIVGN ALNLMNEILS KQKSDPFLLY
NKDISMDGEE SILIACEIAN FLSDVLSYFP NEVDVKRWDF IRIALSSWVL SVSKSCHKFH
ENKVKIFISS IFRLNATLFK FITIEKTKSS TEILQNVIDE WEKVFAKEVN LVLIKSFILI
IKQLDYQSKH QECFVDSLCP SIDYIDFNYI LQSQKVDSTF SLKDLIVFSL ENLSNNYRTI
CVTSATIIKK LTFGLIKLDQ DVLIQRNSED DTGRNDDDEN LGNYRWHILD TFRDTLEGYQ
DVMKEFIEDF NFKLSDMDEL SSISQNVAFS YLLLWDCILN FCSKAPAELR SIYAKWITVH
HFEDVFLVSL FKLMPRDIVR NPEAQMKSGH VVFSSLEWKE IEDLSVDIDR YAAFLYAESL
RTVPAVVRKW WHVSNTRQAQ IVEKITQNYV SPILCQQDLT VLMNRKEKDG KDNMQVKVLM
QSREIFATYS LEEAKMELTI SLPANYPLGA IKIESTKHIA GKFQAREIVK QLSIYLTHQN
GRLYDGISLW KRNLDRKYEG VEECYVCYSV INQDTCQLPR LTCKTCKKKF HSNCLYKWFT
SSNKSTCPLC RNVF
//