ID A0A1S4CT11_TOBAC Unreviewed; 885 AA.
AC A0A1S4CT11;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN Name=LOC107822250 {ECO:0000313|RefSeq:XP_016504258.1};
OS Nicotiana tabacum (Common tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4097 {ECO:0000313|Proteomes:UP000084051, ECO:0000313|RefSeq:XP_016504258.1};
RN [1] {ECO:0000313|Proteomes:UP000084051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. TN90 {ECO:0000313|Proteomes:UP000084051};
RX PubMed=24807620; DOI=10.1038/ncomms4833;
RA Sierro N., Battey J.N., Ouadi S., Bakaher N., Bovet L., Willig A.,
RA Goepfert S., Peitsch M.C., Ivanov N.V.;
RT "The tobacco genome sequence and its comparison with those of tomato and
RT potato.";
RL Nat. Commun. 5:3833-3833(2014).
RN [2] {ECO:0000313|RefSeq:XP_016504258.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Functions as an E3 ubiquitin ligase.
CC {ECO:0000256|ARBA:ARBA00003861}.
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}.
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DR RefSeq; XP_016504258.1; XM_016648772.1.
DR AlphaFoldDB; A0A1S4CT11; -.
DR SMR; A0A1S4CT11; -.
DR STRING; 4097.A0A1S4CT11; -.
DR PaxDb; 4097-A0A1S4CT11; -.
DR GeneID; 107822250; -.
DR KEGG; nta:107822250; -.
DR OMA; CKNNSPP; -.
DR OrthoDB; 37517at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000084051; Unplaced.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd16655; RING-Ubox_WDSUB1-like; 1.
DR CDD; cd01989; STK_N; 1.
DR CDD; cd14066; STKc_IRAK; 1.
DR Gene3D; 3.40.50.620; HUPs; 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; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR003613; Ubox_domain.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45647; OS02G0152300 PROTEIN; 1.
DR PANTHER; PTHR45647:SF100; U-BOX DOMAIN-CONTAINING PROTEIN 33; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF04564; U-box; 1.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00504; Ubox; 1.
DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 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; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS51698; U_BOX; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000084051};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 528..797
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 814..885
FT /note="U-box"
FT /evidence="ECO:0000259|PROSITE:PS51698"
FT REGION 206..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 277..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 321..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 353..499
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 212..226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..347
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 555
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 885 AA; 98939 MW; 141F12E83DB357F7 CRC64;
MALESPVPEI RQSPVRYPEV DLSGLNLNEE IESPLTPPAR VAGDMIYVAV GKDLKESEPT
LKWALHKSGG SRICILHVHT PAQKIPMMGT KFNIDQLDVH QVRTYHEKER QDMHKILEKY
VLICGRAGVR ADKLVVEMDS IEKGIVELVS QRGIGKLVMG AAANKCYSKK MTDLRSKKAI
YVRLQAPTFC CIWFVCKGNL VYTRESKSER PNTDSVSPSI PVSPENDTVL RSRSVTEGYN
EQVGLRGPFN EYRRVASDNH RIIFSGPTSG GTLRANFPSM SSDRSPSVAS RFSSSSYGEM
VGDSPTISLA RTEGNDTAID SSTLHHFIPG HHQPSSPSIQ AESLNDEPAG SMNDELLDRL
EQYVAEAEDA RREAFEESIK RRKAEKDAIE ARRRAKASET IYADELRQRR DIEEALAKGK
EEANQMKSKL NKMLADLQAA QAQTSSLEHQ LLNSDTTVQE LEQKMFSAVD LLQKYRKERD
ELQVERDDAL NIAEALRKQH SNGSSTTSAF VLFAEFYFHE IEEATRRFDP ALKIGEGGYG
SIYRGLLRHT HVAIKMLHPH SSQGPSEFQQ EVNILSKLRH PNIVTLIGAC PEAWALVYEY
LPNGSLEDRL TCKDNTPPLS WQTRIRVASE LCSALIFLHS CTARGIIHGD LKPANILLDA
NFVSKLSDFG ICRVLSEDEF SEKSTSLCYR TDPKGTFAYL DPEFLDTGEL TPKSDVYSFG
IILLRLLTGR PALGIKNEVQ YALDKGNLKD LLDPTAGDWP FVQAKQLAHL AMNCCEKNGR
LRPELSSEVW KVLEPMRASC GASSFRMGSE ERCEIPSYFI CPIFQETMQD PVVAADGFTY
EAEALRGWLD SGHDTSPMTN LALSNTNLVP NHALRSAIQE WLQQH
//
