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Database: UniProt
Entry: H2T9V0_TAKRU
LinkDB: H2T9V0_TAKRU
Original site: H2T9V0_TAKRU 
ID   H2T9V0_TAKRU            Unreviewed;       371 AA.
AC   H2T9V0;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 3.
DT   27-MAR-2024, entry version 63.
DE   SubName: Full=Tripartite motif containing 55 {ECO:0000313|Ensembl:ENSTRUP00000021440.3};
GN   Name=trim55 {ECO:0000313|Ensembl:ENSTRUP00000021440.3};
OS   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000021440.3, ECO:0000313|Proteomes:UP000005226};
RN   [1] {ECO:0000313|Ensembl:ENSTRUP00000021440.3, ECO:0000313|Proteomes:UP000005226}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21551351;
RA   Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA   Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT   "Integration of the genetic map and genome assembly of fugu facilitates
RT   insights into distinct features of genome evolution in teleosts and
RT   mammals.";
RL   Genome Biol. Evol. 3:424-442(2011).
RN   [2] {ECO:0000313|Ensembl:ENSTRUP00000021440.3}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   AlphaFoldDB; H2T9V0; -.
DR   Ensembl; ENSTRUT00000021528.3; ENSTRUP00000021440.3; ENSTRUG00000008556.3.
DR   GeneTree; ENSGT00940000154004; -.
DR   InParanoid; H2T9V0; -.
DR   OMA; CDIHEDE; -.
DR   Proteomes; UP000005226; Chromosome 10.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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, ECO:0000256|SAM:Coils};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005226};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00024}.
FT   DOMAIN          13..68
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          109..151
FT                   /note="B box-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50119"
FT   DOMAIN          259..317
FT                   /note="COS"
FT                   /evidence="ECO:0000259|PROSITE:PS51262"
FT   REGION          319..371
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          173..229
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        319..338
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        342..371
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   371 AA;  42127 MW;  056181371AB43B0A CRC64;
     MNNMDNLEKQ LICPICLEMF TKPVVILPCQ HNLCRKCAND IFQASNPYLP TRAGSLTSGG
     RFRCPSCRHE VVLDRHGVYG LQRNLLVENI IDMFKQESSS GKPVEERKEQ MPMCDVHEGE
     KINIYCITHA VPTCSMCKIF GAHKDCEVSP ITSIYQTKKM ELSDGIAMMV GNNDRMQGII
     SQLEETCRAI EENGRRQKTM VCEKFDQLYS VLEEKKREMS QKVTDEQEEK LSYIRSLTRK
     YGDHLEQSCK VVEMGIQNME EPEMALFLQN TKPLLKKITD ATSTAHLDKV ERGYENMDHF
     HVEFKKVGQA LRSIDFIQEE EEEEHDDEEG EAEDEEAAQT VSEGSAVPTA SLQPPEPQQT
     NPSTVTSATS S
//
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