ID A0A2U9BN84_SCOMX Unreviewed; 866 AA.
AC A0A2U9BN84;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, 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};
GN ORFNames=SMAX5B_016229 {ECO:0000313|EMBL:AWP04902.1};
OS Scophthalmus maximus (Turbot) (Psetta maxima).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC Scophthalmus.
OX NCBI_TaxID=52904 {ECO:0000313|EMBL:AWP04902.1, ECO:0000313|Proteomes:UP000246464};
RN [1] {ECO:0000313|EMBL:AWP04902.1, ECO:0000313|Proteomes:UP000246464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Martinez P.;
RT "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT evaluation of genetic and physical mapping variation across individuals.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
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 EMBL; CP026249; AWP04902.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U9BN84; -.
DR STRING; 52904.ENSSMAP00000033859; -.
DR Proteomes; UP000246464; Chromosome 7.
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: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 CDD; cd16589; RING-HC_TRIM71_C-VII; 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; 3.
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; 5.
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; SSF63829; Calcium-dependent phosphotriesterase; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50194; FILAMIN_REPEAT; 1.
DR PROSITE; PS51125; NHL; 5.
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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000246464};
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 161..203
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT DOMAIN 243..284
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT REPEAT 449..551
FT /note="Filamin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00087"
FT REPEAT 564..607
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 611..654
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 658..701
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 705..748
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 752..795
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REGION 117..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 809..866
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..135
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 817..831
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 845..859
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 866 AA; 95524 MW; CC2FE338C2E779E7 CRC64;
MASFPDSDLQ TCPLCKELCG SSAPISSSSS TSSSSSHTSS SSSQTSRRLH VLPCLHAFCR
QCLEGQRSPG EPLKLRCPTC DQKVSISEAG VDSLPSSNFL FSNLLDVVVS SEEQIHNKNG
HHHPHQQHHH HHRGGLGGGS SSFRHPHGGL LHQHHLAEPQ CSSCDEENPA TSHCLDCQEY
LCDNCVRAHQ RVRLTKDHFI ERLGESLHMG RVNANSNQGQ PGVSVSLAQS LQNNFALLSL
FQDRMSFCQH HDNEVFLFFC ETCSLPICRE CSVGRHMGHT FVYLQDAVQD CRAITIQLLA
DGQQGRQAVQ LSMEKVQAMA EQVEIKAKVV QTEVKALVLR HKKALEEREC ELLWKVEKIR
QVKAKSLYLQ VEKLHQSLTK LDSTIAAVSQ VLDEGHHLDV LLARERMLTQ IHELKALRGL
LQAQEDDRFM FTPPDQALCI AIQSMGLISS GAFALVTKAH GEGLKSGLRG KPTSFTVIGY
DHDGEPRLSG GDSVSAIVMS AGDGTLSAAD VTDHQNGSYT ISYVPKCEGE HLVSVLVCNQ
HIQGSPFKVI VKSGRSYGSL GSHMSSFGCE GEGDGQLCRP WGISVDKEGY VAVADRSNNR
IQIFKPCGAF HHKFGSLGSR PGQFDRPAGV ACDSQRRIIV ADKDNHRVQV FTFEGQFLLK
FGEKGTKNGQ FNYPWDVAVN SEGKILVSDT RNHRVQLFAP DGSFLNKYGF EGALWKHFDS
PRGVAFNHED HLVVTDFNNH RLLVIRPDCQ SARFLGSEGT GNGQFLRPQG VAVDQENRII
VADSRNHRVQ VFEPNGNFLC KFGTQGSGFG QMDRPSEMFE SRTDDARTKE HQSGPFPPPS
HLSHQPSNDA PTSINCRRPV GSSEHH
//
