ID A0A0E0B667_9ORYZ Unreviewed; 1506 AA.
AC A0A0E0B667;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
OS Oryza glumipatula.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=40148 {ECO:0000313|EnsemblPlants:OGLUM09G19320.1};
RN [1] {ECO:0000313|EnsemblPlants:OGLUM09G19320.1}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.A., Panaud O., Oliveira A.C.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OGLUM09G19320.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001433};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
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DR STRING; 40148.A0A0E0B667; -.
DR EnsemblPlants; OGLUM09G19320.1; OGLUM09G19320.1; OGLUM09G19320.
DR Gramene; OGLUM09G19320.1; OGLUM09G19320.1; OGLUM09G19320.
DR eggNOG; ENOG502QSWF; Eukaryota.
DR HOGENOM; CLU_000288_178_6_1; -.
DR Proteomes; UP000026961; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030553; F:cGMP binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0048544; P:recognition of pollen; IEA:InterPro.
DR GO; GO:0051707; P:response to other organism; IEA:UniProt.
DR CDD; cd00028; B_lectin; 2.
DR CDD; cd01098; PAN_AP_plant; 2.
DR CDD; cd14066; STKc_IRAK; 1.
DR Gene3D; 2.90.10.10; Bulb-type lectin domain; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR InterPro; IPR001480; Bulb-type_lectin_dom.
DR InterPro; IPR036426; Bulb-type_lectin_dom_sf.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR003609; Pan_app.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR000858; S_locus_glycoprot_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR32444; BULB-TYPE LECTIN DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR32444:SF139; OS09G0551150 PROTEIN; 1.
DR Pfam; PF01453; B_lectin; 2.
DR Pfam; PF08276; PAN_2; 2.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 2.
DR Pfam; PF00954; S_locus_glycop; 2.
DR SMART; SM00108; B_lectin; 2.
DR SMART; SM00473; PAN_AP; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF51110; alpha-D-mannose-specific plant lectins; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 2.
DR PROSITE; PS50927; BULB_LECTIN; 2.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
DR PROSITE; PS50948; PAN; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 2.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; EGF-like domain {ECO:0000256|ARBA:ARBA00022536};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000026961};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..1506
FT /note="non-specific serine/threonine protein kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002354176"
FT DOMAIN 25..161
FT /note="Bulb-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50927"
FT DOMAIN 352..451
FT /note="Apple"
FT /evidence="ECO:0000259|PROSITE:PS50948"
FT DOMAIN 538..824
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 875..1002
FT /note="Bulb-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50927"
FT DOMAIN 1195..1280
FT /note="Apple"
FT /evidence="ECO:0000259|PROSITE:PS50948"
FT DOMAIN 1269..1309
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 1333..1506
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 566
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 1360
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1506 AA; 164496 MW; 0DA3EF796C236D19 CRC64;
MDWSSCAFTC IAAFLLLSPA LCAADDRIVS GKPLSPGAAV ISDGGDFALG FFAPSNSTPA
KLHLGIWYNN IPRRTVVWVA NRATPIIVNG SSNSSLPSLA MTNTSDLVLS DASGQIVWTT
NLTAVESSSS LSPSPSTAVL MNTGNLVVRS QNGTVLWQSF SQPTDTLLPG MKVRLSYRTL
AGDRLVSWKS PEDPSPGSFS YGGDSDTFFQ FFIWNGSRPA WRAGVWTGYM VTSSQFQANA
RTAVYLALVD TDNDLSIVFT VADGAPPTRF LLSDSGKLQL LGWNKEASEW MMLATWPAMD
CFTYEHCGLG GSCDATAAVP TCKCLDGFEP VSAEWNSGLF SRGCRRKEAL RCGGDGHFVA
LPGMKVPDRF VHVGNRSLDE CAAECGGDCN CMAYAYATLN SSAKSRGDVT RCLVWAGDGE
LVDTGRLGPE QVWGTVGAGG DSRETLYLRV AGMPNSGKRK QGNAVKIAVP VLVIVTCISL
SWFCIFRGKK RSVKEHKKSQ VQGVLTATAL ELEEASTTHD HEFPFVKFDD IVAATNNFSK
SFMVGQGGFG KVYKGMLQGC QEVAVKRLSR DSDQGIVEFR NEVTLIAKLQ HRNLVRLLGC
CVEGHEKLLI YEYLPNKSLD VAIFKSERSV TLDWPARFRI IKGVARGLVY LHHDSRLTII
HRDLKTSNVL LDSEMRPKIA DFGMARIFGD NQQNANTRRV VGTYGYMAPE YAMEGMFSVK
TDVYSFGVLL LEVISGVKIS NIDRIMDFPN LIVYAWSLWM EGRAKELVDL NITESCTLDE
ALLCIHVGLL CVQENPDDRP LMSSVVSILE NGSTTLPTPN HPAYFAPRKN GADQRRDNVF
NSGNEMTLTN CCCTCTQAVT AIFLFLLSLP LSASDDRLAV GKTLSPGATL VSDGGAFAMG
FFSPSNSSGL YLGIWYNNVP KLTVVWVADQ LAPITDHPSS SKLAMADDSS NLVLSDAAGR
VLWRTNVTAG GVNSSGVVAV LVNSGNLVLR LPDDTALWQT FEHPSDVFMA GMKLGIDYRS
HSGMRIVSWK GAGDPSPGSF SFGVDPERPL QAKIWNGSRV HWRSSMWTGY MVDSNYQKGG
SSAIYTAVVY TDDEIYASFT LSAGAPPMHY LMSYSGDLHL QSWSNVSSAW VTNARFPRRD
CSLFGYCGAF GYCGNSTGGG VSTCHCLEGF EPASGADWSR GDFSLGCRRK EAARCGDGFA
EFPDTKLPDG YALVGNMNAG ECAAACRRNC SCVAYAYADL SSSTRRDPTR CLMWGGELLD
MEKVNESWGD LGETLYLRMA GAEMIVKYDG KNNKKRALRV LSVSDEFGKE IPAQDLDFPF
VEYNEIAAAT DNFSEASMIG KGSFGKVYKG VIGGRKVAIK RLSRCSEQGV VKFRNEVLLI
AKLQHRNLVR LVGCSIEGDE KLLIYEFMTN KSLDASLFNS ERKSSLNWST RFKIIKGVAR
GLLYLHQDSR LTVIHRDLKA SNILLDTEMN PKISDFGMAR IFEDNQQNRI TRRVVGTVSN
ARTILN
//