ID F2U867_SALR5 Unreviewed; 1632 AA.
AC F2U867;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-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=PTSG_04311 {ECO:0000313|EMBL:EGD72575.1};
OS Salpingoeca rosetta (strain ATCC 50818 / BSB-021).
OC Eukaryota; Choanoflagellata; Craspedida; Salpingoecidae; Salpingoeca.
OX NCBI_TaxID=946362 {ECO:0000313|Proteomes:UP000007799};
RN [1] {ECO:0000313|Proteomes:UP000007799}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50818 {ECO:0000313|Proteomes:UP000007799};
RA Russ C., Cuomo C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA Lang F.B.F., Roger A.J., Ruiz-Trillo I., Young S.K., Zeng Q., Gargeya S.,
RA Alvarado L., Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C.,
RA Birren B.;
RT "Annotation of Salpingoeca rosetta.";
RL Submitted (AUG-2009) 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; GL832964; EGD72575.1; -; Genomic_DNA.
DR RefSeq; XP_004994398.1; XM_004994341.1.
DR STRING; 946362.F2U867; -.
DR EnsemblProtists; EGD72575; EGD72575; PTSG_04311.
DR GeneID; 16074988; -.
DR KEGG; sre:PTSG_04311; -.
DR eggNOG; KOG0803; Eukaryota.
DR InParanoid; F2U867; -.
DR OrthoDB; 179130at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000007799; 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; 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:UP000007799};
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 1582..1629
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 375..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 515..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 632..687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 826..850
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1090..1133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1146..1169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1228..1250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..530
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1106..1130
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1147..1169
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1632 AA; 174499 MW; 58A5F6BAF7CD6216 CRC64;
MDSNRRIREL TQRAWSIMVD RAQKKILPAL KPIMGAWLCA MRDTHAEAAN LATRAFETAF
PEDKRTKSIV FCQHDILLAL THNIMEVTLE SLRAAGTGED DVELTEKLER IQATSVMALH
HLITTLPLKS LMEEEDAYMS LLRASRLWKL SKATKPLVHR AVCDLACAVL TEHRVWVDGL
EKRILSACIK GMTAANPTTV AASLLLVFTM SKTPDVLWPN VNVLADVIAP ICVMLNDGGG
PAHHTLFPLL PKIVAALPDS VQGDTKLEVL SAISSAVTSP SVAMQPRRFD LWLAAFADTL
ALLRDDPTLA SSHEVIEEAA RSALAHVLTQ HQLQPQLGRL LTALAETALV EDAYVRVVQQ
LRDQVVQQWC TLITPPASSS SSSSSSSSSS SSSSSTTRAA VVAAASPLVS ALGRISDQAV
HEAVQHVAAT TAAAMAVAGM KADTLQQQQQ GSEETTPPSS STMLKAVMTA RLVLACRLTT
LATNGDGGAD DTAAVVHVLL ALLRQAVDAL AGNCDDTDDT DNNGGNADGS GDGGATTAPV
SAATVRDDVR DLLAAALQLN CDATSDAVHA LLLHMAAQLQ LTHVAVAAEA MAACTNVAQW
VRGLPNPLTA RIVQLASALI SDDAQAAMLI TASSSSGRRH HQQQQQRQRR PRRCSDTTDS
GAGEGGPQRR QWRQEERTGL GSVNPSTGAA ACDGPDDLLS FLLSHRTVGG RAVVAVPDSA
CAELVAAIRA RLMLLRYLHA DTTSSTATAS SWLVAALPSL LTAVMTRLTS SPAGAADLRV
VEEVAATVAR MLDAVNVNEA GVLTETILPS CVAVAAAGGA AASVVSAEAP STTTTTTTAT
STPSSSTTSS AVPVHEVMPF IRRACLDGLA STLTGDSVAA GGVWTHERLD GFNSHLQMLE
ALGCFDDHAD VDDSRVCAFI TNLPQLRQPL HAAHARIASL PPRATLAVES GLTFAGCELG
QDADTYAPAQ WRAMAGGVKK KAAAAYGAEE QQHALINTIQ AWVSLLTCTP LQVVWQHHPD
THMRCLYTAL MATEAAQAVL AGEAAVHAPI SHTLADCMDA LVETTLTLDG THMQQLVATL
ARRAVAGVKG TSGDTADADG HDDKDTNQDD GDDDDDDDGD DDDDDEETPG LSSELLVLST
ILSASTHQDH DHSHVDDNGD ANGDEHEHGA GADVSEWLYV DGSPEQSLSG GRTRLIQTLL
TTFDAAAADM KRIRNSVTHA LEMLTAPADR ADGDVHDSDD GSDDDDDEDD LTRTVYPLAA
AISYANTLCQ LEFLQQQTVD HDKMAKMSMA GRRAFERQQQ LNAIFGCASA STWQLLQRII
AVFEQWEAAD AELLDLEDFE PEELPREQER RKLAICTEYA KLCHVIVDSC ARHLSSEQWE
LMLCRLVEWM QIPVSCGYTA ALACAATQAC TAIAALMTRL AQAGSVAPNL SPVLAKILPE
WQNFFVPQIA VALITAIQQA GHILDVQAPQ YALTKILASD VATLCPDKFM HEHARMSAVV
PLLYHGESAV RGTAFFILCH LIAGDNENKV QCGQRLGVSA ALWRSWMLQL SMYMTNQNGS
ILDALKTWKR NVDKKFEGME ECTVCFSIVH GTNYQLPTIK CPTCRKLFHA DCIARWFSSS
GNNTCPMCRS LM
//
