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Database: UniProt
Entry: A0A0N5D2V9_THECL
LinkDB: A0A0N5D2V9_THECL
Original site: A0A0N5D2V9_THECL 
ID   A0A0N5D2V9_THECL        Unreviewed;       516 AA.
AC   A0A0N5D2V9;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN   ORFNames=TCLT_LOCUS7225 {ECO:0000313|EMBL:VDN04661.1};
OS   Thelazia callipaeda (Oriental eyeworm) (Parasitic nematode).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Thelazioidea; Thelaziidae; Thelazia.
OX   NCBI_TaxID=103827 {ECO:0000313|Proteomes:UP000046394, ECO:0000313|WBParaSite:TCLT_0000723601-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:TCLT_0000723601-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDN04661.1, ECO:0000313|Proteomes:UP000276776}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
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DR   EMBL; UYYF01004487; VDN04661.1; -; Genomic_DNA.
DR   STRING; 103827.A0A0N5D2V9; -.
DR   WBParaSite; TCLT_0000723601-mRNA-1; TCLT_0000723601-mRNA-1; TCLT_0000723601.
DR   OMA; RNCMHRF; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000046394; Unplaced.
DR   Proteomes; UP000276776; Unassembled WGS sequence.
DR   GO; GO:0000151; C:ubiquitin ligase complex; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR043540; RING1/RING2.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR46076:SF3; E3 UBIQUITIN-PROTEIN LIGASE RING1; 1.
DR   PANTHER; PTHR46076; E3 UBIQUITIN-PROTEIN LIGASE RING1 / RING 2 FAMILY MEMBER; 1.
DR   Pfam; PF13923; zf-C3HC4_2; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000276776};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          52..92
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          194..234
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        215..234
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   516 AA;  57436 MW;  6365CA61B30DD414 CRC64;
     MVSGRGDGQH TSRRSTLPLL TSYDKSRKPH VLRTGINTGT IHFDWISKEL ECGICEKTIQ
     NTMVVRNCMH RFCADCILQR IHTGTRKCPL CHKLLPKKTP LKSDTNFDAI IKKFSLSAER
     RCVKRPITES GTLYFKNKAV YDNKSSNKRV ANTTLITPSP FGEQTSSKRV QIPMKYIPVM
     SSNVNATLEA KQPLLPSTHS DTSDPPLTID EGLSDDSYPN LQQPTTSSFS RDESKLNGNV
     SIAGSCEVTP VVWQKSCNYE KFNGMVIKSP QFNGSNVHVK CFPVSANLGI SPHLANQAPI
     TRATNGCFIH LNGNAKRTNN TKIGDGLHLP PSLENSISME DKVVASPRTS EFLLITGKQR
     LYPGIESQLV LNPDASVVTD DSLPTAAKHL RYIVTCSATT VGHLCEYILQ RIRIESFDEK
     DRKPSEDFFT RRVLLCPVKS DLALDDVLVV NETGEGQFTT MNVGERNSDS RSTSVFTINS
     PFVALDESVT VEQLKAEHWS NKKKPLKLIF KFQRKS
//
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