ID A0A3B3U8S9_9TELE Unreviewed; 382 AA.
AC A0A3B3U8S9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=E3 ubiquitin-protein ligase TRIM21-like {ECO:0000313|Ensembl:ENSPLAP00000009049.1};
OS Poecilia latipinna (sailfin molly).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48699 {ECO:0000313|Ensembl:ENSPLAP00000009049.1, ECO:0000313|Proteomes:UP000261500};
RN [1] {ECO:0000313|Ensembl:ENSPLAP00000009049.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR RefSeq; XP_014881624.1; XM_015026138.1.
DR AlphaFoldDB; A0A3B3U8S9; -.
DR STRING; 48699.ENSPLAP00000009049; -.
DR Ensembl; ENSPLAT00000001866.1; ENSPLAP00000009049.1; ENSPLAG00000011720.1.
DR GeneID; 106942799; -.
DR KEGG; plai:106942799; -.
DR GeneTree; ENSGT01040000240400; -.
DR OrthoDB; 5343342at2759; -.
DR Proteomes; UP000261500; Unplaced.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd13733; SPRY_PRY_C-I_1; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR003879; Butyrophylin_SPRY.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR006574; PRY.
DR InterPro; IPR003877; SPRY_dom.
DR InterPro; IPR027370; Znf-RING_euk.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR24103:SF691; B30.2_SPRY DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24103; E3 UBIQUITIN-PROTEIN LIGASE TRIM; 1.
DR Pfam; PF13765; PRY; 1.
DR Pfam; PF00622; SPRY; 1.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR PRINTS; PR01407; BUTYPHLNCDUF.
DR SMART; SM00589; PRY; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50188; B302_SPRY; 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 Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 15..55
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 182..377
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000259|PROSITE:PS50188"
SQ SEQUENCE 382 AA; 42607 MW; 18B7ADF9BA48FDED CRC64;
MSTASCLLSE DQFRCFICQN VFTDPVSTPC GHNFCKNCVT ENVCDDVPFQ CPACEKMFFP
RPELEVNTLI AELLDEFRRS ALRQNAEAEI PGPVSGNLFT KNRKIAILCG MVLLFILSSQ
VNHSPPLTEE TEGNAKGIME DIWSWSPAKR CQNLTSGQNW TAVGPLSASQ LEQIFTEVMN
KETPRLLIRA ELMRAKHYAV DVTLDPDTVH PKLILSDDGK QVSCCNPTGN LPHDPNRFRY
LKYVLGEQSF SSGRFYFEVQ VKGKTNWTIG VAKESVSRTD RVRLIPRSGF WSLTVRNQNE
FFGLSSPPVP LSLKSGLEKV GVFVDYEEGL VFFYDVDAAA LIFSFTGCHF TERLHPLFGP
GHNNDGTNGA PLIITPVSIV PQ
//
