ID A0A061D611_BABBI Unreviewed; 1788 AA.
AC A0A061D611;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 42.
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=BBBOND_0300510 {ECO:0000313|EMBL:CDR96146.1};
OS Babesia bigemina.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC Babesiidae; Babesia.
OX NCBI_TaxID=5866 {ECO:0000313|EMBL:CDR96146.1, ECO:0000313|Proteomes:UP000033188};
RN [1] {ECO:0000313|Proteomes:UP000033188}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bond {ECO:0000313|Proteomes:UP000033188};
RX PubMed=24799432; DOI=10.1093/nar/gku322;
RA Jackson A.P., Otto T.D., Darby A., Ramaprasad A., Xia D., Echaide I.E.,
RA Farber M., Gahlot S., Gamble J., Gupta D., Gupta Y., Jackson L.,
RA Malandrin L., Malas T.B., Moussa E., Nair M., Reid AJ., Sanders M.,
RA Sharma J., Tracey A., Quail M.A., Weir W., Wastling J.M., Hall N.,
RA Willadsen P., Lingelbach K., Shiels B., Tait A., Berriman M., Allred D.R.,
RA Pain A.;
RT "The evolutionary dynamics of variant antigen genes in Babesia reveal a
RT history of genomic innovation underlying host-parasite interaction.";
RL Nucleic Acids Res. 42:7113-7131(2014).
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; LK391709; CDR96146.1; -; Genomic_DNA.
DR RefSeq; XP_012768332.1; XM_012912878.1.
DR STRING; 5866.A0A061D611; -.
DR EnsemblProtists; CDR96146; CDR96146; BBBOND_0300510.
DR GeneID; 24564687; -.
DR KEGG; bbig:BBBOND_0300510; -.
DR VEuPathDB; PiroplasmaDB:BBBOND_0300510; -.
DR OMA; VRLICAC; -.
DR OrthoDB; 179130at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000033188; Chromosome 3.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:1990112; C:RQC complex; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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: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; 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 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:UP000033188};
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 1732..1779
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1405..1427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1788 AA; 200786 MW; A4435CA6386B00D1 CRC64;
MTRKGKKQEE RKVRSSDFAM YQTANSRPTG LHHIFDSFYH DATAYGTGDQ SRDGRSDDAS
SAFSQSQAEL LKALEKLTKK DGTTKLKAIE HLISLLDDTP DYVLEGLVPD FMHLFKRIAV
VEPSRKIRLH LGQALSRIAK TLKKRMQVHM DGIVTYWWMA MHDDAPDVAS AYIEAFHSLF
SAPDAERTEL DRKTFRVLTH YIQTIANTSL MLLSRNIEEY KRDWMDTFGK TCDNSATISD
MHNRLVCSLL QGIVNLMTQQ RLFANEVDGD KLPVTVFVND ELVNRIGSLC LNGTFRQRLA
SARLLVELVK VLPAGKLPIA RKLFGIGMKR VHEDEEAHIS YQHVRLICAC ARYNSACWEP
SILGNYASFV KRVLEQHTGD SAVTAELYSL CPCLVSYLPQ EWLRSPSGEQ AVLEVIKYVL
HLLSEKLQAN YEKSYAYDVK MLSQVGSSML YCYYRILMLL EGNCETIAQH AIAPILELPY
ESTSLAKHLL SQLPRIFTEF IEEAEAMKSS EAIDTILTML RKVDEKQVNG VLMTRIFDSL
SKGGHNDVED VEPRDSIKSY VRNAQKGLKS RIMEDELPSV LMEFLAEPQS PSCVERMDEM
LSVADSITTL SKDSGILVAP RFFMERKYHD SWEFEGAFAK LSRVLKLFEP LLNEPEKYYP
EETDAKSVLL VSLVALQNTD SDDKAVNIAK KVYSCLTELG DGNCLAVFLK FVNASQRFSH
CLSQTMLGWL MQPEHLNVAT CEAVYSAVDV SSLDAEGLLK YELLHTVLRF ERKTAVKGYK
PKEHGMVDDV VAFYLVGYYT NLLVRIDTLL NFSVALLPEW QQGKSTADSD RLKSFLQLLQ
RGKDTFKYSH DTSSEVVLNK DLVNAMISLQ STPCRCTVSI SRTISALTQA SVLVDAVIHH
RNAVLFAQLW YMNCEAYLFV ADETSKLHRD TEAVNGTATQ SDDDTAKGDE VAASKIHGDK
VDLQNFASVL VPTLVNDGFN YPLFEKLVEK VLKSCACSDT ITTTLVKYIC SKTWKSKFEY
TNKIQLFNSY LHKLGAYDES VVALFKQQYC SNQFVGGFVA TSKRMGNVAI TTADDILSAV
ELCGEDDIVL MTNYLLELAP LFGNSFVNGD GKFDVKEGCD VSYLTEKMVS VPLAVLGKLR
ILKHKDACTS FWLHSALLDL FHACSCLVKA LSLDSAAFLK FVEGGWIMSA LSFCCRNLSA
PSHLVINLFA EIMHLCISNE IVSLKVLRVD RGAYDFSLSS LREYADVMEA LSAENVAQAL
AEGPFGTTVD SIDPHYFVSM VVYFVESVDS QKTVVGHDAD DIQRALKTLK AATYEFVSFL
SKSQSCYIYS LAFVSRLWCC SFLFSHIAEY SGTLCNVDLE HNSVYLLLPG KFAAVETSPD
VHNAVNQEGV PIDISQLLLN ALQDPEENGH PGDAEEPSTD NPEEVPVGPT REEIAYFGRK
AISFYFNVLF GPHITGALFK TYDVFGDSCH HQDLELCLTS WLSAFMLLQH LVESNQLTLK
NAILKVLTAN PSEAGGAMYE SIKAQVSNAV ADEGKEYVSA WWLSDAPAIP EHADESALHV
LLNVLILCLE NLYLKEERYR HLVKTLYYKV SKVFPEEVNH VWNQCKSVYV KKQIKKFTKT
EITQRLIADE LRALKACKSS ALHITHDADY RNLYASLDTK AEVSIKLTVK IPKAFPLEPL
SFTSTEDAAT FKNKHLRWLM MAQSAANRGG ISQGLLLWSD NITKFFDGIE ECPICYSIVH
LQFNSIPGKT CKVCKHKFHT ECLYKWFRNA QKAKCPLCQS TSSFTSYN
//
