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Database: UniProt
Entry: A0A3B3CY74_ORYME
LinkDB: A0A3B3CY74_ORYME
Original site: A0A3B3CY74_ORYME 
ID   A0A3B3CY74_ORYME        Unreviewed;       771 AA.
AC   A0A3B3CY74;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-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   Name=TRIM3 {ECO:0000313|Ensembl:ENSOMEP00000022566.1};
GN   ORFNames=FQA47_004581 {ECO:0000313|EMBL:KAF6724952.1};
OS   Oryzias melastigma (Marine medaka).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC   Oryzias.
OX   NCBI_TaxID=30732 {ECO:0000313|Ensembl:ENSOMEP00000022566.1, ECO:0000313|Proteomes:UP000261560};
RN   [1] {ECO:0000313|Ensembl:ENSOMEP00000022566.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:KAF6724952.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Bigg-433 {ECO:0000313|EMBL:KAF6724952.1};
RX   PubMed=32938378;
RA   Liang P., Saqib H.S.A., Ni X., Shen Y.;
RT   "Long-read sequencing and de novo genome assembly of marine medaka (Oryzias
RT   melastigma).";
RL   BMC Genomics 21:0-0(0).
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   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
CC   -!- SIMILARITY: Belongs to the TRIM/RBCC family.
CC       {ECO:0000256|ARBA:ARBA00008518}.
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DR   EMBL; WKFB01000381; KAF6724952.1; -; Genomic_DNA.
DR   STRING; 30732.ENSOMEP00000022566; -.
DR   PaxDb; 30732-ENSOMEP00000022566; -.
DR   Ensembl; ENSOMET00000014415.1; ENSOMEP00000022566.1; ENSOMEG00000002196.1.
DR   Ensembl; ENSOMET00000014426.1; ENSOMEP00000022579.1; ENSOMEG00000002196.1.
DR   Ensembl; ENSOMET00000014438.1; ENSOMEP00000022596.1; ENSOMEG00000002196.1.
DR   GeneTree; ENSGT00940000158173; -.
DR   OrthoDB; 5387006at2759; -.
DR   Proteomes; UP000261560; Unplaced.
DR   Proteomes; UP000646548; Unassembled WGS sequence.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:Ensembl.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd14960; NHL_TRIM2_like; 1.
DR   CDD; cd16768; RING-HC_TRIM3; 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; IPR003649; Bbox_C.
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; 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; PTHR24104; E3 UBIQUITIN-PROTEIN LIGASE NHLRC1-RELATED; 1.
DR   PANTHER; PTHR24104:SF21; TRIPARTITE MOTIF-CONTAINING PROTEIN 3; 1.
DR   Pfam; PF00630; Filamin; 1.
DR   Pfam; PF01436; NHL; 6.
DR   Pfam; PF00643; zf-B_box; 1.
DR   Pfam; PF13445; zf-RING_UBOX; 1.
DR   SMART; SM00502; BBC; 1.
DR   SMART; SM00336; BBOX; 1.
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; 1.
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   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000646548};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00024}.
FT   DOMAIN          27..68
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          118..159
FT                   /note="B box-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50119"
FT   REPEAT          335..426
FT                   /note="Filamin"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00087"
FT   REPEAT          482..523
FT                   /note="NHL"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT   REPEAT          527..570
FT                   /note="NHL"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT   REPEAT          571..612
FT                   /note="NHL"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT   REPEAT          647..679
FT                   /note="NHL"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT   REPEAT          683..726
FT                   /note="NHL"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT   REPEAT          727..770
FT                   /note="NHL"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT   REGION          433..469
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   771 AA;  84316 MW;  6EB13BC79235C38D CRC64;
     MVVIMAKCET GSTSPVVRQI DKQFLVCSIC LDRYHNPKVL PCLHTFCEKC LQNYIPPQSL
     TLSCPVCRQT SILPEKGVAA LQNNFFITNL MEVLQRDPEC SRPEATNVLE SANAATTCQS
     LSCPNHEGKV MEFYCESCET AMCLECTEGE HREHVTVPLR DVLEQHKSAL KNQLDTVCNR
     LPQLTVAIDH VNDISKQLTE RKSEAVMEIS NTFDELEKAL HQRKNALITE VENICSSKQK
     VLQAQLTSLL QGKENIQSSC SFTEHALSHG SATEILLVQK QMGERVSALA RHSFPVHPHE
     NGHLECQVET DGLRRSIQNL GVLITTGAVG HTSVATGEGL RHALVGQHTS ITVTTKDKDG
     ELVKSGNAAL RAEIVSADGG RTEAEVVDNK NGTYEVGYTV RSEGEFTFSL LLYGQPVRGS
     PFRLRAVKPS DVLQSPEDVK RRVKSPSGGG GHVRQKAVRR PSSMYSTTKK KENPIEDELI
     YRVGTRGRDK GEFTNLQGIS ASSNGRIVVA DSNNQCIQVF SNDGQFKMRF GVRGRSPGQL
     QRPTGVTVDV NGDIIVADYD NRWISIFSSD GKFKNKIGAG RLMGPKGVAV DKNGHIITAD
     NKACCVFIFQ SNGKLVTKFG ARGTSDRHFT EKSGANIVLE TKISKSGPVF SPHFVAVNNK
     NEIVVTDFHN HSVKVYNADG EFLFKFGSHG EGNGQFNAPT GVAVDANGNI IVADWGNSRI
     QVFDSSGSFL SYINTSADPL YGPQGLALTS DGHVAVADSG NHCFKVYRYL Q
//
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