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
//