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Database: UniProt
Entry: A0A1J1HTF8_9DIPT
LinkDB: A0A1J1HTF8_9DIPT
Original site: A0A1J1HTF8_9DIPT 
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
//
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