ID A0A397ZBP0_BRACM Unreviewed; 1242 AA.
AC A0A397ZBP0;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=BRARA_F03724 {ECO:0000313|EMBL:RID60576.1};
OS Brassica campestris (Field mustard).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=3711 {ECO:0000313|EMBL:RID60576.1, ECO:0000313|Proteomes:UP000264353};
RN [1] {ECO:0000313|EMBL:RID60576.1, ECO:0000313|Proteomes:UP000264353}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. B-3 {ECO:0000313|Proteomes:UP000264353};
RA Bowman J., Kohchi T., Yamato K., Jenkins J., Shu S., Ishizaki K.,
RA Yamaoka S., Nishihama R., Nakamura Y., Berger F., Adam C., Aki S.,
RA Althoff F., Araki T., Arteaga-Vazquez M., Balasubrmanian S., Bauer D.,
RA Boehm C., Briginshaw L., Caballero-Perez J., Catarino B., Chen F.,
RA Chiyoda S., Chovatia M., Davies K., Delmans M., Demura T., Dierschke T.,
RA Dolan L., Dorantes-Acosta A., Eklund D., Florent S., Flores-Sandoval E.,
RA Fujiyama A., Fukuzawa H., Galik B., Grimanelli D., Grimwood J.,
RA Grossniklaus U., Hamada T., Haseloff J., Hetherington A., Higo A.,
RA Hirakawa Y., Hundley H., Ikeda Y., Inoue K., Inoue S., Ishida S., Jia Q.,
RA Kakita M., Kanazawa T., Kawai Y., Kawashima T., Kennedy M., Kinose K.,
RA Kinoshita T., Kohara Y., Koide E., Komatsu K., Kopischke S., Kubo M.,
RA Kyozuka J., Lagercrantz U., Lin S., Lindquist E., Lipzen A., Lu C.,
RA Luna E., Martienssen R., Minamino N., Mizutani M., Mizutani M.,
RA Mochizuki N., Monte I., Mosher R., Nagasaki H., Nakagami H., Naramoto S.,
RA Nishitani K., Ohtani M., Okamoto T., Okumura M., Phillips J., Pollak B.,
RA Reinders A., Roevekamp M., Sano R., Sawa S., Schmid M., Shirakawa M.,
RA Solano R., Spunde A., Suetsugu N., Sugano S., Sugiyama A., Sun R.,
RA Suzuki Y., Takenaka M., Takezawa D., Tomogane H., Tsuzuki M., Ueda T.,
RA Umeda M., Ward J., Watanabe Y., Yazaki K., Yokoyama R., Yoshitake Y.,
RA Yotsui I., Zachgo S., Schmutz J.;
RT "WGS assembly of Brassica rapa FPsc.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000256|ARBA:ARBA00008684}.
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DR EMBL; CM010633; RID60576.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A397ZBP0; -.
DR Proteomes; UP000264353; Chromosome a6.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd14066; STKc_IRAK; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 6.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR013210; LRR_N_plant-typ.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR48053; LEUCINE RICH REPEAT FAMILY PROTEIN, EXPRESSED; 1.
DR PANTHER; PTHR48053:SF118; OS07G0498400 PROTEIN; 1.
DR Pfam; PF00560; LRR_1; 15.
DR Pfam; PF13855; LRR_8; 2.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR00019; LEURICHRPT.
DR SMART; SM00365; LRR_SD22; 8.
DR SMART; SM00369; LRR_TYP; 14.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF52047; RNI-like; 2.
DR PROSITE; PS51450; LRR; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1242
FT /note="non-specific serine/threonine protein kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017211980"
FT TRANSMEM 873..896
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 941..1227
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 970
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1242 AA; 135776 MW; C7D622D11D65896C CRC64;
MQRLSLFVLF FLCFLVGSGS GQPGQSNDLQ TLLELKKSLV ANPKDETVLR SWNSDDPNYC
NWTGVTCGGR EVIGLNLSGL NLTGSISPSI GRFDNIIDLD LSSNSLVGPI PAALSNLSSS
LETLHLFSNL LSGEIPSQLG SLVNLKSLKI GNNDLAGSIP ETLGNLANLQ TLGLAACRLT
GPIPSQLGRL VQMQYLYLRH NYLEGPIPPE LGNCANLVTF SAEVNSLNGS LPAELSRLGN
LESLNLANNS LSGEIPSQLG DLRSLNHLYL IGNKLQGSIP KTLTELKNLR ILDLSKNSLT
GGIHEEFWNM NQLEYLVLEY NPLSGSLPKS LCSNNTNLKL LLLSETQLSG EIPTEISKCR
SLQELNLSNN TLTGLIPDSL FHLVELTVLY INNCSLRGTL SPSISNLTNL QEFGPSHNAL
EGKLPKEIGF LSKLERLLLH DNRFSGEIPV EIGNCTSLQE IDMYGNHFSG EIPSWIGRLK
DLTWLHLREN EFSGNVPATL GNCQQLTLLD LADNHLTGSI PSSFGFLTAL DQLHLYNNSL
QGNLPSSLIN LKKLTRINFS NNTLNGSISP LCGSSSYLSF DLTDNRFEGD VPLELGKSPS
LNRLRLGKNQ FTGRIPWTLG KINALSVLDI SSNSLTGIIP VELGLCTNLT LIDLSNNFLS
GVIPPWLGKL PFLGELKLSS NQLTGSLPSE IFNLSNLLVL SLDGNSLNGS IPQEIGNLEA
LNVLNLDKNQ ISGQLPSAIG KLSKLYELRL SRNSLIGDIP VEIGQLQDLQ SALDLSYNNF
TGHIPSTIST LHKLESLDLS HNHLVGDVPG PIGDMKSLGY LNLSYNNLTG RLKKPFYKWH
ADAFVGNADL CGSPLSPCKR VGSKQQGLSA KTVVIISALS SVAAIALTVL VVVLFCKQGH
DLLNSTFSSN SSPSSQAPLF RNGAAKTDIK WEDIMEATHR LDDEFMIGSG GSGKVYKADL
KNGETIAVKK ILWKDDLMSN KSFNREVKTL GTIRHRHLVK LMGYCTSKEE GLNLLIYEYM
ENGSVWDWLH EKKKQVLGWE TRLKIALGLA QGVEYLHFDC APPIVHRDIK TSNVLLDSNM
EAHLGDFGLA KILTEESNDT NTGSHSLFAG SYGYIAPEYA YSLKATEKSD VYSMGIVLME
IVTGKKPTDE VFDEETNMVR WVETCLEMPP GSRAREKLID SELKPLLPCE EAAAYQLLEI
AIQCTKTYPR ERPSSRQACD CLLNVFNNRA ASYGEMQTGS EK
//