ID A0A1S4D9X1_TOBAC Unreviewed; 892 AA.
AC A0A1S4D9X1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN Name=LOC107827584 {ECO:0000313|RefSeq:XP_016510245.1};
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_016510245.1};
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_016510245.1}
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_016510245.1; XM_016654759.1.
DR GeneID; 107827584; -.
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 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 527..804
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 821..892
FT /note="U-box"
FT /evidence="ECO:0000259|PROSITE:PS51698"
FT REGION 274..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 329..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 352..498
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 554
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 892 AA; 99909 MW; D92E7DF7648DE281 CRC64;
MALESPVPEI RQSPVRYPEV DLSGLNLNEE IESPLTPPAR VADDMIYVAV GKDLKESEPT
LKWALHKSGG RRICILHVHT PAQKIPMMGT KFNIDQLDVH QVRAYHEKER QDMHKILEKY
ILICGRAGVR ADKLVVEMDS IETGIVELVS QRGIGKLVMG AAANKCYSKK MTDLRSKKAI
YVRLQAPTFC CIWFVCKGNL IYTRESESER PNTDSVSPPI PVSPENDTVL RSRSVTEGYN
EQVGLRGPFN EYRRVASDNH RIIFSGPPSG GTLRANFPSM SSDRSPSVAS RFSSSSYGEM
VGDSPTISLA RTEGNETAID SSTLHHFILG HHQPSSPSIA ESLNDEPAGS MNDELLDRLD
QYVAEAEDAR REAFEESIKR RKAEKDAIEA RRRAKASETI YADELRQRRD IEEALAKSKE
EANQMKSKLN KMLADLQAAQ AQTSSLERQL LNSDTTVQEL EQKMFSAVDL LQKYRKERDE
LQVERDDALN IAEALREQHS NGSSTTSASV LFAEFYFHEI EEATRRFDPA LKIGEGGYGS
IYRGLLRHTH VAIKMLHPHS SQGPSEFQQE VNILSKLRHP NIVTLIXPNI VTLIGACPEA
WALVYEYLPN GSLEDRLTCK DNTPPLSWQT RIRVASELCS ALIFLHSCTA RGIIHGDLKP
ANILLDANFV SKLSDFGICR VLPEDEFSEK STSLCYRTDP KGTFAYLDPE FLDTGELTPK
SDVYSFGIIL LRLLTGRPAL GINNEVQYAL DKGNLKDLLD PTAGDWPFVQ AKQLAHLAMN
CCEKNRRLRP ELSSEVWKVL EPMRASCGAS SFRMSSEERC EIPSYFICPI FQETMQDPVV
AADGFTYEAE ALRGWLDSGH DTSPMTNLAL SNTNLVPNHA LRSAIQEWLQ QH
//
