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Database: UniProt
Entry: M1BAI5_SOLTU
LinkDB: M1BAI5_SOLTU
Original site: M1BAI5_SOLTU 
ID   M1BAI5_SOLTU            Unreviewed;       441 AA.
AC   M1BAI5;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN   Name=102605657 {ECO:0000313|EnsemblPlants:PGSC0003DMT400040842};
OS   Solanum tuberosum (Potato).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX   NCBI_TaxID=4113 {ECO:0000313|EnsemblPlants:PGSC0003DMT400040842, ECO:0000313|Proteomes:UP000011115};
RN   [1] {ECO:0000313|Proteomes:UP000011115}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. DM1-3 516 R44 {ECO:0000313|Proteomes:UP000011115};
RX   PubMed=21743474; DOI=10.1038/nature10158;
RG   The Potato Genome Sequencing Consortium;
RT   "Genome sequence and analysis of the tuber crop potato.";
RL   Nature 475:189-195(2011).
RN   [2] {ECO:0000313|EnsemblPlants:PGSC0003DMT400040842}
RP   IDENTIFICATION.
RC   STRAIN=DM1-3 516 R44 {ECO:0000313|EnsemblPlants:PGSC0003DMT400040842};
RG   EnsemblPlants;
RL   Submitted (JUN-2015) to UniProtKB.
CC   -!- FUNCTION: Functions as an E3 ubiquitin ligase.
CC       {ECO:0000256|ARBA:ARBA00003861}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
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DR   AlphaFoldDB; M1BAI5; -.
DR   EnsemblPlants; PGSC0003DMT400040842; PGSC0003DMT400040842; PGSC0003DMG400015790.
DR   Gramene; PGSC0003DMT400040842; PGSC0003DMT400040842; PGSC0003DMG400015790.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; M1BAI5; baseline.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   CDD; cd16655; RING-Ubox_WDSUB1-like; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR003613; Ubox_domain.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR45647; OS02G0152300 PROTEIN; 1.
DR   PANTHER; PTHR45647:SF22; U-BOX DOMAIN-CONTAINING PROTEIN 32; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF04564; U-box; 1.
DR   SMART; SM00504; Ubox; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS51698; U_BOX; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011115}.
FT   DOMAIN          89..349
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          370..441
FT                   /note="U-box"
FT                   /evidence="ECO:0000259|PROSITE:PS51698"
FT   COILED          34..61
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         116
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   441 AA;  49742 MW;  94B7C45BA4660054 CRC64;
     MIQEKKPVLE SQITESSYAG KELEEKIIQA VELLISFRKQ RDEMQIERDN AIKEVNRFRK
     LVQDDADEYC IKNFFSISFS DIIEATRNFD PSSKIGEGKF GSVYKGIIHH VKVAIKMLPA
     CGSFSDSDFQ HKAESLSRVR HPNLVTLIGI CSESRSLAYE FLENGNLEDH LACCKKSRPL
     HWQHRIRIAV EICSALIFVH ANDPCIVHGN LRPTNILLDA KFVSKISDFG VHLLISQTEN
     SNNDDPEASI YVDPEYIDNG QFTVESDVYS FGVILLRLLT ARPALGIVRD VKCALESGNL
     GSVLDSSAGD WPIEQAELLA YLALSCCEKD PLNRPNMLSE VWPTIEPMRD ICKPHSDLNT
     SSQGSKGQKR IPPHFVCPIF QDVMEDPHIA ADGYTYEGDA IKGWLYSGHD TSPMTNLKLD
     TCDLIPNYAL YRAIQEWQQQ F
//
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