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Database: UniProt
Entry: A0A3B3DKG1_ORYME
LinkDB: A0A3B3DKG1_ORYME
Original site: A0A3B3DKG1_ORYME 
ID   A0A3B3DKG1_ORYME        Unreviewed;       759 AA.
AC   A0A3B3DKG1;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
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:ENSOMEP00000030608.1, ECO:0000313|Proteomes:UP000261560};
RN   [1] {ECO:0000313|Ensembl:ENSOMEP00000030608.1}
RP   IDENTIFICATION.
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   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
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DR   AlphaFoldDB; A0A3B3DKG1; -.
DR   STRING; 30732.ENSOMEP00000030608; -.
DR   PaxDb; 30732-ENSOMEP00000030608; -.
DR   Ensembl; ENSOMET00000033163.1; ENSOMEP00000030608.1; ENSOMEG00000014980.1.
DR   GeneTree; ENSGT00530000063836; -.
DR   OMA; RMMSGNR; -.
DR   Proteomes; UP000261560; Unplaced.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd16812; RING_CH-C4HC3_MARCH7; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR011016; Znf_RING-CH.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR14471:SF1; E3 UBIQUITIN-PROTEIN LIGASE MARCHF7; 1.
DR   PANTHER; PTHR14471; MARCH7/10 E3 UBIQUITIN PROTEIN LIGASE FAMILY MEMBER; 1.
DR   Pfam; PF12906; RINGv; 1.
DR   SMART; SM00744; RINGv; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS51292; ZF_RING_CH; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          593..663
FT                   /note="RING-CH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51292"
FT   REGION          39..135
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          166..228
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          241..284
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          297..518
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          732..759
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        39..120
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        166..198
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        199..220
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        297..329
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        359..444
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        489..512
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        732..749
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   759 AA;  84636 MW;  975504B7D3887F1B CRC64;
     MDSRSRRLPF CLSGSRSSYT FSTPSPPVSS SLSSTRLYNR ETMLNNDRIP RASSPFKTDM
     DKPTSRLLSS SRDYSSADAR SSSWKLPSLS SSTRSYDRPY ESSYSSRSKM TNSEERLGTR
     SGLLNASDDA DSKRAKLSYS NRGLYPRTAS TSMTASTYFN SAVGSSRGTQ HLIDPLDSSR
     SSSHLFSQPS SSSPKTLLSR REQEAKEEAS LSRLRERRVR TPGLVPSLYQ TDRVMSTYAQ
     GARPKETAYT SSSFSSSSSS SSSSTVRDSS LNRHMSSSTP QRVSPLVHNF SSRAAAHFTN
     DSPTRYSSRQ QTGNSESSSI SSSYSSPPWH TPPLARPEPV PSRSTPDVGE PEGRSSTRRL
     LSRLFSRRSS QDSSSGSSSV RSLDDDSSET ALGSLRNHRA DLSTIQEGNS YNSGPPRPTR
     PTWNVGGSSS STNGRWSPSW LSSSLRGRCP PLLSRLRRHA RQGSSHSASS LEEGSSHTLL
     RRWDEHQSSQ EEDEEDEEEE EEEEEDDEVE GAVGLEALST GRSCRLERES LPELEDAPVS
     FLPRSRAGLF ERITASMVQL GDVESKPEDP KSISSRDQEK LLKIKERLLL EDSDEEEGDL
     CRICQMGEES SSNPLIQPCR CTGSLQYVHQ ECIKRWLRSK ISSGTNLEAI TTCELCKEKL
     RLNIDNFDIH ELYRTHVQSE YDEFISSGLY LVVLLHFCEQ RFSDVLGAVD AAGLFNLVRI
     LHEHMDNLEI PHEESDEEVQ DNRPSVDFSD LDDDLEEEY
//
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