GenomeNet

Database: UniProt
Entry: H0WMJ5_OTOGA
LinkDB: H0WMJ5_OTOGA
Original site: H0WMJ5_OTOGA 
ID   H0WMJ5_OTOGA            Unreviewed;       612 AA.
AC   H0WMJ5;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU369081};
DE            EC=2.3.2.27 {ECO:0000256|RuleBase:RU369081};
DE   AltName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|RuleBase:RU369081};
GN   Name=RNF157 {ECO:0000313|Ensembl:ENSOGAP00000002965.2};
OS   Otolemur garnettii (Small-eared galago) (Garnett's greater bushbaby).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lorisiformes;
OC   Galagidae; Otolemur.
OX   NCBI_TaxID=30611 {ECO:0000313|Ensembl:ENSOGAP00000002965.2, ECO:0000313|Proteomes:UP000005225};
RN   [1] {ECO:0000313|Proteomes:UP000005225}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   The Broad Institute Genome Sequencing Platform;
RA   Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K., Jaffe D.B.,
RA   Gnerre S., MacCallum I., Przybylski D., Ribeiro F.J., Burton J.N.,
RA   Walker B.J., Sharpe T., Hall G.;
RT   "Version 3 of the genome sequence of Otolemur garnettii (Bushbaby).";
RL   Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSOGAP00000002965.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: E3 ubiquitin ligase. {ECO:0000256|RuleBase:RU369081}.
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:RU369081};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU369081}.
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DR   EMBL; AAQR03041406; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAQR03041407; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAQR03041408; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; H0WMJ5; -.
DR   STRING; 30611.ENSOGAP00000002965; -.
DR   Ensembl; ENSOGAT00000003325.2; ENSOGAP00000002965.2; ENSOGAG00000003319.2.
DR   eggNOG; KOG4265; Eukaryota.
DR   GeneTree; ENSGT00390000009925; -.
DR   HOGENOM; CLU_016631_2_0_1; -.
DR   InParanoid; H0WMJ5; -.
DR   OMA; EDSCPVH; -.
DR   TreeFam; TF314969; -.
DR   Proteomes; UP000005225; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion 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-UniRule.
DR   CDD; cd16817; mRING-HC-C3HC5_RNF157; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR045194; MGRN1/RNF157-like.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR22996:SF1; E3 UBIQUITIN LIGASE RNF157; 1.
DR   PANTHER; PTHR22996; MAHOGUNIN; 1.
DR   Pfam; PF13920; zf-C3HC4_3; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Cytoplasm {ECO:0000256|RuleBase:RU369081};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU369081};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005225};
KW   Transferase {ECO:0000256|RuleBase:RU369081};
KW   Ubl conjugation pathway {ECO:0000256|RuleBase:RU369081};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU369081};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          208..247
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          269..292
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          365..536
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          586..612
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        270..292
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        373..387
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        388..471
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   612 AA;  66587 MW;  660723AB2A825D99 CRC64;
     FPYAAPPPQE PVKTLRSLIN IRKDTLRLVK CAEEVKSPGE EASKAKVYYN VEFTFDTDAR
     VAITIYYQAT EEFQNGIASY IPKDNSLQSE TVHYKRGVCQ QFCLPSHTVD PSEWAEEELV
     FDLDREVYPL VVHAVVDEGD EYFGHCHVLL GTFEKHTDGT FCVKPLKQKQ VVDGVSYLLQ
     EIYGIENKYN TQDSKVAEDE VSDNSAECVV CLSDVRDTLI LPCRHLCLCN TCADTLRYQA
     NNCPICRLPF RALLQIRAMR KKLGPLSPPN FNPIISSQTS DSEEHSSSEN IPPGYEVVSL
     LEALNGPLTP SPAVPPLHVL GDGHLSGMLP SYGSDGHLPP ARTLSPLDRL SDCSSQGLKL
     KKSLSKSISQ NSSVVHEEED ERSCSESETQ LSQRPSAQHL TEECGVTPES ENLTLSSSGA
     IDQSSCTGTP LSSTISSPEG PASSSLAQSV MSMASSQIST DTVSSMSGSY IAPGTEEEGE
     ALPSSRAASR DPSEEGEGLP AESPESNFAG LPAGEQDAEG NDVMEEEDES PTQEDGQRTC
     AFLGMECDNN NDFDIASVNA LDNTLCSEVC LPGTWHADDN IVSRRNTPRR RLSSSSLEDS
     ENRPCVWGPL AV
//
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