GenomeNet

Database: UniProt
Entry: H0WHU7_OTOGA
LinkDB: H0WHU7_OTOGA
Original site: H0WHU7_OTOGA 
ID   H0WHU7_OTOGA            Unreviewed;       549 AA.
AC   H0WHU7;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   SubName: Full=Tripartite motif containing 55 {ECO:0000313|Ensembl:ENSOGAP00000000967.2};
GN   Name=TRIM55 {ECO:0000313|Ensembl:ENSOGAP00000000967.2};
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:ENSOGAP00000000967.2, 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:ENSOGAP00000000967.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   EMBL; AAQR03133692; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAQR03133693; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAQR03133694; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; H0WHU7; -.
DR   STRING; 30611.ENSOGAP00000000967; -.
DR   Ensembl; ENSOGAT00000001083.2; ENSOGAP00000000967.2; ENSOGAG00000001083.2.
DR   eggNOG; KOG2177; Eukaryota.
DR   GeneTree; ENSGT00940000154004; -.
DR   HOGENOM; CLU_013137_5_3_1; -.
DR   InParanoid; H0WHU7; -.
DR   OMA; CDIHEDE; -.
DR   TreeFam; TF331669; -.
DR   Proteomes; UP000005225; Unassembled WGS sequence.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0030674; F:protein-macromolecule adaptor activity; IEA:Ensembl.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:Ensembl.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0050904; P:diapedesis; IEA:Ensembl.
DR   GO; GO:0002523; P:leukocyte migration involved in inflammatory response; IEA:Ensembl.
DR   GO; GO:1905517; P:macrophage migration; IEA:Ensembl.
DR   GO; GO:1901224; P:positive regulation of non-canonical NF-kappaB signal transduction; IEA:Ensembl.
DR   GO; GO:0070936; P:protein K48-linked ubiquitination; IEA:Ensembl.
DR   CDD; cd19832; Bbox2_MuRF2_C-II; 1.
DR   CDD; cd16760; RING-HC_MuRF2; 1.
DR   Gene3D; 1.20.5.170; -; 1.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR017903; COS_domain.
DR   InterPro; IPR027370; Znf-RING_euk.
DR   InterPro; IPR000315; Znf_B-box.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR24103; E3 UBIQUITIN-PROTEIN LIGASE TRIM; 1.
DR   PANTHER; PTHR24103:SF640; TRIPARTITE MOTIF-CONTAINING PROTEIN 55; 1.
DR   Pfam; PF00643; zf-B_box; 1.
DR   Pfam; PF13445; zf-RING_UBOX; 1.
DR   SMART; SM00336; BBOX; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF57845; B-box zinc-binding domain; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS51262; COS; 1.
DR   PROSITE; PS50119; ZF_BBOX; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005225};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00024}.
FT   DOMAIN          26..84
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          121..163
FT                   /note="B box-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50119"
FT   DOMAIN          271..329
FT                   /note="COS"
FT                   /evidence="ECO:0000259|PROSITE:PS51262"
FT   REGION          328..431
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          448..534
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        329..357
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        376..390
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        415..431
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        449..463
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        495..527
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   549 AA;  60516 MW;  955D3EAFBCE7AE86 CRC64;
     MSASLNYKSF SKEQQTMDNL EKQLICPICL EMFTKPVVIL PCQHNLCRKC ASDIFQEQAS
     NPYLPTRGGT TVASGGRFRC PSCRHEVVLD RHGVYGLQRN LLVENIIDIY KQESTRPEKK
     SDQPVCEEHE EERINIYCLN CEVPTCSLCK VFGAHKDCQV APLTHVFQRQ KSELSNGIAV
     LVGSNDRVQG VISELEDTCK IIEECCRKQK QELCEKFDYL YGILEERKNE MTQVITRTQE
     EKLEHVRALI KKYSDHLENV TKLVESGIQF MDEPEMAVFL QNAKTLLQKI SEASKAFQME
     KIEHGYENMN HFTVNLNREE KIIREIDFYR EEEEEEEEGG EGEREEGEEE GEVEVEEVEN
     GPTVAPGEDA SLGRALEPSQ LSSELQAATG ALPASSPEPP PALPPAADAP VTQGEVVPTG
     SQQTTESETP VLAAADTADP LFYPSWYKGQ TRKATTNPPC TPGSEVLGQI GPPGSEDSNV
     QNAEVAGAAS QERAAVSGKE TSAPAATSQI GFETPPLQGQ AAASGSGNGA DSEPARHVFS
     FSWLNSLNE
//
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