ID A0A1D6MLE5_MAIZE Unreviewed; 1979 AA.
AC A0A1D6MLE5;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU366018};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU366018};
GN ORFNames=ZEAMMB73_Zm00001d039860 {ECO:0000313|EMBL:ONM30036.1};
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:ONM30036.1};
RN [1] {ECO:0000313|EMBL:ONM30036.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Seedling {ECO:0000313|EMBL:ONM30036.1};
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 -!- FUNCTION: Ubiquitin ligase protein which is a component of the N-end
CC rule pathway. Recognizes and binds to proteins bearing specific N-
CC terminal residues that are destabilizing according to the N-end rule,
CC leading to their ubiquitination and subsequent degradation.
CC {ECO:0000256|RuleBase:RU366018}.
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 ECO:0000256|RuleBase:RU366018};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|RuleBase:RU366018}.
CC -!- SIMILARITY: Belongs to the UBR1 family. {ECO:0000256|ARBA:ARBA00009750,
CC ECO:0000256|RuleBase:RU366018}.
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DR EMBL; CM007649; ONM30036.1; -; Genomic_DNA.
DR UniPathway; UPA00143; -.
DR ExpressionAtlas; A0A1D6MLE5; baseline and differential.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniRule.
DR GO; GO:0071596; P:ubiquitin-dependent protein catabolic process via the N-end rule pathway; IEA:UniProtKB-UniRule.
DR CDD; cd16482; RING-H2_UBR1-like; 1.
DR CDD; cd19673; UBR-box_UBR3; 1.
DR Gene3D; 2.10.110.30; -; 1.
DR Gene3D; 1.10.10.2670; E3 ubiquitin-protein ligase; 1.
DR InterPro; IPR042065; E3_ELL-like.
DR InterPro; IPR044046; E3_ligase_UBR-like_C.
DR InterPro; IPR039164; UBR1-like.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR InterPro; IPR003126; Znf_UBR.
DR PANTHER; PTHR21497:SF53; E3 UBIQUITIN-PROTEIN LIGASE PRT6; 1.
DR PANTHER; PTHR21497; UBIQUITIN LIGASE E3 ALPHA-RELATED; 1.
DR Pfam; PF18995; PRT6_C; 1.
DR Pfam; PF02207; zf-UBR; 1.
DR SMART; SM00396; ZnF_UBR1; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS51157; ZF_UBR; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU366018};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU366018};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366018};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU366018};
KW Zinc-finger {ECO:0000256|RuleBase:RU366018}.
SQ SEQUENCE 1979 AA; 221163 MW; DA7788797AD78CB9 CRC64;
MAGIDAGEGA AAAPPPEMSP QQRIEQKLIL YGVPEEQLQE HQQSLVQYTE EHKEQIPDIV
RHILSAGTDI SEARKVSKKD ANSSSNGDAY RESLSWLQWL MFKNEPAAML DDLERSNAGE
RAVCGSVWGH NDVAYRCRTC ESDPTCAICV PCFQNGNHKD HDYSIIYTGG GCCDCGDATA
WKREGFCSKH KGAEQIKPLP VELACSVGPV LDVLLQFWKE RICLLEPHHA KGSDGSSCKR
IAEELTTSIS SMLLEFCTRS ENLLSFLSLR IREFPDMLDA LIRSDRLLDK KVARKLHEFL
LKLISDPAFK YEFAKVFIHY YPITFGEVIK GCNDSLLEDY PLMTTFSVQI FTVPTLTPRL
VREVDLLGVL LGCLTDLFLS CIGEDGRLQT NKWGNLFDAS IRLLDDTRYV LSHEEVSKHV
AYGRPDLTRS WIKLLSLVQG MDPQKRVTSI HAEDENEHLS APFVLGHYLG IVQNLLMRGS
FSPPDQHEST DVTVCSTAIK GVESAENQRH AKVGRVSQES SVSDLSSRDS SLCCGLPSPA
AWLVLQCLKA IESWLWLEND IALRSKLSSL DASSNDSHKL MALLEDPLTS LTGNSSNTNM
CVMDVKINEG SQTDCTADYY EASSSPVQGQ GQEAMPLVSN STGKGKMHGS SNSTVVQLHP
EDAITYTLTD GSILYAHPDS RIEELGILNT RGWPHVVFDV SSQETSFHIP LHRMLSLLLR
KAMKKCFGED GHSDVQSNEF FPQILRGCEP YGFASIVMEH PLRVRVFCAQ VRAGMWRKNG
DAAILSAEWY RSVQWFESVL MQEMLIFLIQ LVKERRFCGL STADNLRREL IYKLAIGDAT
HSQIVKSLPR DLSSSDQLQN VLDSLAAYSN PSGMKQGKYV LRKSCWKELD LYHPRWNSRE
LQIAEERYYR FCEISALNAQ LPRWTHVFNP LRSISNIATS KAVLQIVRAV LFYAVYSDAS
SASRAPDNVL VTGLHLLWLA LDICESERQI HADQYDMDVM QHDDESWVVL SSTEEAIPLL
TYSTELVSPV SDKVKKESML TLLVSLMHKY KEENDGTFSG SKYCNIPSLI EILLKKFAKL
SKECLLRLRQ MAPHIVPSTP DHTSIKEGPG SSSDSMEKKA KARQRQAAIM AKMRAEQSKF
AQSMKSSENE GHDITMLEAD VSSSTGVVSE ESLPVCSLCR DSDSKSPLCY LILLQKSRLA
TFVEMGNPSW ENPAQVNKTG SVKREGSVDC CVSGSSTSEE LVNDTTVEPS FDIDNMEVDA
FLDFSNEQHP LIRYISSFPT GHSNINADEN VSLEAIEADI YNSILNDLFG SRNAHIQDSD
QMLPSNTSNI TIDTKRTRSP KRSVLGTYVS CLSSKHRHSS LYDVASKSSA SVTTRNRFGP
VDCDGIHISS CGHAVHQECH DRYLFSLKQR YVRRLGFEGG HIVDPDLGEL LCPVCRRFAN
SILPASPDFS GKTSMMLRPF VQTLTPQVVT TTSDVNRNCL QFARALSLFE SAGKIVGETK
FLKAISGKLN ETTNPALDPC LRRLAMLYYP RSHSSFSPSK RLNPSLFLWD TLRYSLVSTE
IASRGRMSSH SAESKSCLES LRGELNSSSG FILSLLFHAA HSARNLNRLE VLLRFEGIQL
LAGSICSCIS GYKDILNATK RKGSLPSMVD PASEGALFPD VQFWKQCADP VLAQDPFSSL
MSALFCLPVQ FLSSAEFFIP FVHLFYVVCA IQALVTCYGE ETFDRSNFND CLLNDVCKTM
SGYDIARDYF VSKYIDPSCH PKDMVRRLTY PYLRRCALLW ELLRSSATSP LYDGSNIWEG
SHLYLSNSTQ DDSSSLAMEL AGLRELEDLF QIQSLDLILQ DESVHMLALK WSQHFCEEYN
PRKYRGTLFS TPAVPFRLMQ LPDVYQVLLE RYIKMQCPDC GSVPDEPALC LLCGKLCSPS
WKPCCRTGKC QNHALQCGAG IGIFLLVRVC SSSLLLFLEH TGELRVLYII KKGGMRNLK
//
