ID A0A3P9PXF2_POERE Unreviewed; 831 AA.
AC A0A3P9PXF2;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
OS Poecilia reticulata (Guppy) (Acanthophacelus reticulatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=8081 {ECO:0000313|Ensembl:ENSPREP00000026587.1, ECO:0000313|Proteomes:UP000242638};
RN [1] {ECO:0000313|Proteomes:UP000242638}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Guanapo {ECO:0000313|Proteomes:UP000242638};
RA Kuenstner A., Dreyer C.;
RT "The genomic landscape of the Guanapo guppy.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPREP00000026587.1}
RP IDENTIFICATION.
RC STRAIN=Guanapo {ECO:0000313|Ensembl:ENSPREP00000026587.1};
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 -!- SIMILARITY: Belongs to the TRIM/RBCC family.
CC {ECO:0000256|ARBA:ARBA00008518}.
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DR RefSeq; XP_008419685.1; XM_008421463.2.
DR AlphaFoldDB; A0A3P9PXF2; -.
DR STRING; 8081.ENSPREP00000026587; -.
DR Ensembl; ENSPRET00000026864.1; ENSPREP00000026587.1; ENSPREG00000017981.1.
DR GeneID; 103472086; -.
DR KEGG; pret:103472086; -.
DR CTD; 131405; -.
DR GeneTree; ENSGT00940000159099; -.
DR OMA; GRCDTHA; -.
DR OrthoDB; 2901369at2759; -.
DR Proteomes; UP000242638; Unassembled WGS sequence.
DR GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0010172; P:embryonic body morphogenesis; IEA:Ensembl.
DR GO; GO:0031047; P:regulatory ncRNA-mediated gene silencing; IEA:UniProtKB-KW.
DR CDD; cd19812; Bbox1_TRIM71_C-VII; 1.
DR CDD; cd19796; Bbox2_TRIM71_C-VII; 1.
DR CDD; cd14954; NHL_TRIM71_like; 1.
DR Gene3D; 4.10.830.40; -; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR017868; Filamin/ABP280_repeat-like.
DR InterPro; IPR001298; Filamin/ABP280_rpt.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR001258; NHL_repeat.
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; PTHR24104; E3 UBIQUITIN-PROTEIN LIGASE NHLRC1-RELATED; 1.
DR PANTHER; PTHR24104:SF47; E3 UBIQUITIN-PROTEIN LIGASE TRIM71; 1.
DR Pfam; PF00630; Filamin; 1.
DR Pfam; PF01436; NHL; 6.
DR Pfam; PF00643; zf-B_box; 2.
DR SMART; SM00336; BBOX; 2.
DR SMART; SM00557; IG_FLMN; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57845; B-box zinc-binding domain; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF101898; NHL repeat; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50194; FILAMIN_REPEAT; 1.
DR PROSITE; PS51125; NHL; 6.
DR PROSITE; PS50119; ZF_BBOX; 2.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000242638};
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 12..81
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 152..194
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT DOMAIN 235..276
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT REPEAT 441..543
FT /note="Filamin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00087"
FT REPEAT 556..599
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 603..646
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 650..693
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 697..740
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 744..787
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 791..831
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT COILED 298..325
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 831 AA; 91415 MW; 941DAC21DE710FE4 CRC64;
MASFPDSDLQ TCPLCKELCG SSAPISSNSS TSSSSSQTSV SSNHATKKLH VLPCLHTFCR
QCLEGQRSPS DPLKLCCPTC DQKVSISEAG VDSLPSSNFL FSNLLDVVVS SDDQMQNKNG
HHHLGGLIGG SSGFHPSHGG LLHVQHMGEP QCSSCDEENP ATSHCLDCEE YLCDNCVRAH
QRVRLTKDHY IDPLGESLHL SRVNSISSGT GQPGVSVSLA QSLQNNFALL SLFQGRMSFC
QNHDGEVFLF FCETCSVPIC RECSVGRHIG HTYVYLQDAV QDCRAITIQL LADAQQGRQA
VQQSMEKVQA MAEQVEIKAK VVQTEVKALV LRHKKALEER ECELLWKVDK IRQVKAKTLY
LQVEKLHQSL TKLDSTIAAV SQMLDEGHHL DVLLARERML TQIHELKTLR GLMQPQDDDR
IMFTPPDQAL YVAIQSMGLI SSSAFAPVTK VHGEGLKNVL CGKPASFTVI GYDHDGEPCL
SGGDTVSAMV MSVADGSPSA VEVTDRKNGS YTVCFLPKME GEHLVSVLVC HQHVQGSPFK
VTVKSRRNYR SLGSQMSSFG CEGEGDGQLC RPWGISVDRE GYVVVADRSN NRIQIFKPCG
AFHHKFGSLG SRPGQFDRPA GVACDSQRRI IVADKDNHRV QVFTFEGQFL LKFGEKGTKN
GQFNYPWDVA VNSEGKILVS DTRNHRVQLF APDGSFLNKY GFEGTLWKHF DSPRGVAFNH
EDHLVVTDFN NHRLLVIRPD CQAARFLGSE GTKDGQFLRP QGVAVDQENR IIVADSRNHR
IQVFEASGSF LCNFGSQGSG YGQMDRPSGV AVMPDGIIVV VDFGNNRILK F
//