ID M1CS99_SOLTU Unreviewed; 385 AA.
AC M1CS99;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN Name=102585008 {ECO:0000313|EnsemblPlants:PGSC0003DMT400073577};
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:PGSC0003DMT400073577, 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:PGSC0003DMT400073577}
RP IDENTIFICATION.
RC STRAIN=DM1-3 516 R44 {ECO:0000313|EnsemblPlants:PGSC0003DMT400073577};
RG EnsemblPlants;
RL Submitted (JUN-2015) 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}.
CC -!- SIMILARITY: Belongs to the RING-type zinc finger family. LOG2
CC subfamily. {ECO:0000256|ARBA:ARBA00025721}.
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DR RefSeq; XP_006361866.1; XM_006361804.2.
DR AlphaFoldDB; M1CS99; -.
DR EnsemblPlants; PGSC0003DMT400073577; PGSC0003DMT400073577; PGSC0003DMG400028580.
DR GeneID; 102585008; -.
DR Gramene; PGSC0003DMT400073577; PGSC0003DMT400073577; PGSC0003DMG400028580.
DR KEGG; sot:102585008; -.
DR HOGENOM; CLU_016631_0_0_1; -.
DR OrthoDB; 383715at2759; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR ExpressionAtlas; M1CS99; baseline.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR CDD; cd16789; mRING-HC-C3HC5_MGRN1-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR045195; LOG2-like_mRING_C3HC5.
DR InterPro; IPR045194; MGRN1/RNF157-like.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR22996; MAHOGUNIN; 1.
DR PANTHER; PTHR22996:SF4; RING-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR Pfam; PF13920; zf-C3HC4_3; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Reference proteome {ECO:0000313|Proteomes:UP000011115};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT DOMAIN 330..369
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..76
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 385 AA; 43188 MW; 19953593871C92A6 CRC64;
MGISWSKRHQ NHHLHHHPPP PVLPLPSSSI APPFPSLSPP PLPPPHPTYS LPPPSTTPPP
SRNPYPLLTP PPPPNYPPPS NSNYHFCFSQ SSYGTRPVVY HNQYPPYYHP HSNNGWGGFR
PPPPPPPPLP AVPYVDHQNA KKIKNDVNLH KDTIRVHVDE FNKDFHLVSF TFDALVDGSI
TIFYFAKEGP NCKFNPVYPE IKPVQIPFVK GLGQKFCQPS GTGIDLGFFD VNDLSKPLQG
EEIFPLVISA ESCLPSTPLD EKYDGQSLDK SPHSQITEAV LVKNNEDHFQ VKVIKQILWI
EGVRYELREI YGINNSEETN VNDEESGKEC VICMTEPKDT AVLPCRHMCL CGECAKELRH
QSNKCPICRQ PIEELLEIKV NEAAS
//
