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Database: UniProt
Entry: A0A1D6LR13_MAIZE
LinkDB: A0A1D6LR13_MAIZE
Original site: A0A1D6LR13_MAIZE 
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
//
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