ID A0A1D6LR13_MAIZE Unreviewed; 770 AA.
AC A0A1D6LR13;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=ZEAMMB73_Zm00001d036765 {ECO:0000313|EMBL:AQK81893.1};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577 {ECO:0000313|EMBL:AQK81893.1};
RN [1] {ECO:0000313|EMBL:AQK81893.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Seedling {ECO:0000313|EMBL:AQK81893.1};
RG Maize Genome Sequencing Project;
RA Ware D.;
RT "Update maize B73 reference genome by single molecule sequencing
RT technologies.";
RL Submitted (DEC-2015) 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 -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CM000782; AQK81893.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1D6LR13; -.
DR ExpressionAtlas; A0A1D6LR13; baseline and differential.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd16702; RING_CH-C4HC3_MARCH6; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR011016; Znf_RING-CH.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR13145:SF0; E3 UBIQUITIN-PROTEIN LIGASE MARCHF6; 1.
DR PANTHER; PTHR13145; SSM4 PROTEIN; 1.
DR Pfam; PF12906; RINGv; 1.
DR SMART; SM00744; RINGv; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
DR PROSITE; PS51292; ZF_RING_CH; 1.
PE 4: Predicted;
KW Ligase {ECO:0000313|EMBL:AQK81893.1};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT DOMAIN 27..88
FT /note="RING-CH-type"
FT /evidence="ECO:0000259|PROSITE:PS51292"
FT DOMAIN 35..82
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
SQ SEQUENCE 770 AA; 85629 MW; 146C26D4CBDADD32 CRC64;
MAEIAERAVA GEVPEEPRPP HGEEDDEGEE EGDVCRICRN HGDEDHPLRY PCACSGSIKF
VHQDCLLQWL DHSNSRQCEV CKHAFSFSPV YADNAPTRLP FQELMVGVGM KACHVFQFIL
RLAFVLSVWL MIIPFITYWI WRLTFVRSLS EAQRLFLSHI SAQLILSDCL HGFLLSAIIV
LIFLGATSLR DYIRHLRELG GHDAERDDGG RERHGARAVR RLAGPNNRVP ADGNVDELAE
AQGIGAGELL RRNAENVAAR LERLEAQVEQ MLDGLDDADG AEDVPFDELV GMQGPVFHLV
ENAITVLASN AIFLIVVIFV PFSLGRIILY YLSWFFSSAS TPMLAKVMPF TETAISIAND
TLKSALNVVK NFSSDSNNEG VIGHVIEVVT QSLKINATGL SVIQGTGKNS LMKGTTIASS
YLSDLTTLAV GYMFIFCLVF LYIGSLALLR YARGERFTIG RLYGIATILE AIPSLCRQFF
AGMKHLMTMV KVAFLLVIEL GVFPLMCGWW LDVCTLKMLG TTIAQRVEFF TMSPLASSSI
HWLVGIVYML QISIFVSLLR GVLRNGVLYF LRDPADPNYN PFRDLIDDPV HKHARRVLLS
VAVYGSLIVM LVFLPVKVAM RVAPSMFPLD ITIFDPFTEI PVDVLLFQIC IPFAIEHFKP
RATIKALLHH WFSVVGWGLG LTDFLLPKSE ENGGQENLNA RAERRDRGHG GREMVAPQVE
QLMIQHVAAE DNGRGDSNEA NDVTEDSDVD DQGDCMALCF GSCSCLYWHG
//