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Database: UniProt
Entry: DRIPH_ARATH
LinkDB: DRIPH_ARATH
Original site: DRIPH_ARATH 
ID   DRIPH_ARATH             Reviewed;         480 AA.
AC   Q9LS86;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 139.
DE   RecName: Full=Probable E3 ubiquitin protein ligase DRIPH;
DE            EC=2.3.2.27 {ECO:0000250|UniProtKB:Q9M9Y4};
DE   AltName: Full=DREB2A-interacting protein homolog;
DE   AltName: Full=RING-type E3 ubiquitin transferase DRIPH {ECO:0000305};
GN   OrderedLocusNames=At3g23060; ORFNames=MXC7.9;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA   Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT   features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT   clones.";
RL   DNA Res. 7:131-135(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
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:0000250|UniProtKB:Q9M9Y4};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- INTERACTION:
CC       Q9LS86; Q9LEZ3: BIM1; NbExp=3; IntAct=EBI-4445671, EBI-617095;
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DR   EMBL; AB026655; BAB02097.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE76711.1; -; Genomic_DNA.
DR   EMBL; AY099845; AAM20696.1; -; mRNA.
DR   EMBL; BT006623; AAP31967.1; -; mRNA.
DR   RefSeq; NP_188946.2; NM_113206.5.
DR   AlphaFoldDB; Q9LS86; -.
DR   SMR; Q9LS86; -.
DR   BioGRID; 7212; 6.
DR   IntAct; Q9LS86; 6.
DR   STRING; 3702.Q9LS86; -.
DR   iPTMnet; Q9LS86; -.
DR   PaxDb; 3702-AT3G23060-1; -.
DR   ProteomicsDB; 224306; -.
DR   EnsemblPlants; AT3G23060.1; AT3G23060.1; AT3G23060.
DR   GeneID; 821880; -.
DR   Gramene; AT3G23060.1; AT3G23060.1; AT3G23060.
DR   KEGG; ath:AT3G23060; -.
DR   Araport; AT3G23060; -.
DR   TAIR; AT3G23060; ATBM1C.
DR   eggNOG; KOG2660; Eukaryota.
DR   HOGENOM; CLU_039235_1_0_1; -.
DR   InParanoid; Q9LS86; -.
DR   OMA; NAYIRTD; -.
DR   OrthoDB; 688423at2759; -.
DR   PhylomeDB; Q9LS86; -.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:Q9LS86; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9LS86; baseline and differential.
DR   Genevisible; Q9LS86; AT.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   CDD; cd17087; RAWUL_DRIP_like; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR044768; DRIP-like_RAWUL.
DR   InterPro; IPR044807; DRIP1-like.
DR   InterPro; IPR018957; Znf_C3HC4_RING-type.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR46293; E3 UBIQUITIN PROTEIN LIGASE DRIP1; 1.
DR   PANTHER; PTHR46293:SF3; E3 UBIQUITIN PROTEIN LIGASE DRIPH-RELATED; 1.
DR   Pfam; PF00097; zf-C3HC4; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   1: Evidence at protein level;
KW   Metal-binding; Reference proteome; Transferase; Ubl conjugation pathway;
KW   Zinc; Zinc-finger.
FT   CHAIN           1..480
FT                   /note="Probable E3 ubiquitin protein ligase DRIPH"
FT                   /id="PRO_0000397044"
FT   ZN_FING         16..57
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   REGION          93..133
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          167..193
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          241..261
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          280..356
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        115..129
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        171..193
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   480 AA;  53664 MW;  4E656E20E7A01E7E CRC64;
     MLTKVLSKEV KPCLACPICT NPFKDATTIS ECLHTFCRSC IRNKFINERV NACPVCNVNL
     GVFPLEKLRS DCTWQDLKLK IYRAMMESLK KAGPKTVAAS VKSSKKKRKS RTSLRVSSSR
     VSSSPDTPLE PANVVVEPPN VVVEEKHRET VLALQSTRKP IITFQKRGRK ASLPKKIDSK
     PEPELPPKEP KIKNLFDLNN EPEDNGLDEA EGSTFQEVVP KEKDLCKPIF SLSVTLNIND
     TPPDIVEPEI SSDDDTEESV EPIQNKCVVN RETKEVPVQV NQNSLLISSD RDREDNSGQK
     LKTNGAATSR SRKKKGKKPV EKSYSLRPRI GRRTVNPAAG TTTPEAPVSV EEEMKVEEGR
     NNNPVWFSLK PSKTQNIEML LPPITACCIR VKDSNMTVSY LKKYLMVKLG LESEDQVEIW
     LRDEPVCSSL TLHNLVDWWV QTTPLPERQS AMVGSSAAEF IMDLYYSFKS DASDSGSASE
//
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