ID A0A2K1JM08_PHYPA Unreviewed; 1982 AA.
AC A0A2K1JM08;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN ORFNames=PHYPA_017413 {ECO:0000313|EMBL:PNR42583.1};
OS Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae; Physcomitrium.
OX NCBI_TaxID=3218 {ECO:0000313|EMBL:PNR42583.1};
RN [1] {ECO:0000313|EMBL:PNR42583.1, ECO:0000313|Proteomes:UP000006727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004 {ECO:0000313|EnsemblPlants:Pp3c13_15270V3.1,
RC ECO:0000313|Proteomes:UP000006727};
RX PubMed=18079367; DOI=10.1126/science.1150646;
RA Rensing S.A., Lang D., Zimmer A.D., Terry A., Salamov A., Shapiro H.,
RA Nishiyama T., Perroud P.-F., Lindquist E.A., Kamisugi Y., Tanahashi T.,
RA Sakakibara K., Fujita T., Oishi K., Shin-I T., Kuroki Y., Toyoda A.,
RA Suzuki Y., Hashimoto S.-I., Yamaguchi K., Sugano S., Kohara Y.,
RA Fujiyama A., Anterola A., Aoki S., Ashton N., Barbazuk W.B., Barker E.,
RA Bennetzen J.L., Blankenship R., Cho S.H., Dutcher S.K., Estelle M.,
RA Fawcett J.A., Gundlach H., Hanada K., Heyl A., Hicks K.A., Hughes J.,
RA Lohr M., Mayer K., Melkozernov A., Murata T., Nelson D.R., Pils B.,
RA Prigge M., Reiss B., Renner T., Rombauts S., Rushton P.J., Sanderfoot A.,
RA Schween G., Shiu S.-H., Stueber K., Theodoulou F.L., Tu H., Van de Peer Y.,
RA Verrier P.J., Waters E., Wood A., Yang L., Cove D., Cuming A.C., Hasebe M.,
RA Lucas S., Mishler B.D., Reski R., Grigoriev I.V., Quatrano R.S.,
RA Boore J.L.;
RT "The Physcomitrella genome reveals evolutionary insights into the conquest
RT of land by plants.";
RL Science 319:64-69(2008).
RN [2] {ECO:0000313|EMBL:PNR42583.1, ECO:0000313|Proteomes:UP000006727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004 {ECO:0000313|EnsemblPlants:Pp3c13_15270V3.1,
RC ECO:0000313|Proteomes:UP000006727};
RX PubMed=29237241; DOI=10.1111/tpj.13801;
RA Lang D., Ullrich K.K., Murat F., Fuchs J., Jenkins J., Haas F.B.,
RA Piednoel M., Gundlach H., Van Bel M., Meyberg R., Vives C., Morata J.,
RA Symeonidi A., Hiss M., Muchero W., Kamisugi Y., Saleh O., Blanc G.,
RA Decker E.L., van Gessel N., Grimwood J., Hayes R.D., Graham S.W.,
RA Gunter L.E., McDaniel S.F., Hoernstein S.N.W., Larsson A., Li F.W.,
RA Perroud P.F., Phillips J., Ranjan P., Rokshar D.S., Rothfels C.J.,
RA Schneider L., Shu S., Stevenson D.W., Thummler F., Tillich M.,
RA Villarreal Aguilar J.C., Widiez T., Wong G.K., Wymore A., Zhang Y.,
RA Zimmer A.D., Quatrano R.S., Mayer K.F.X., Goodstein D., Casacuberta J.M.,
RA Vandepoele K., Reski R., Cuming A.C., Tuskan G.A., Maumus F., Salse J.,
RA Schmutz J., Rensing S.A.;
RT "The Physcomitrella patens chromosome-scale assembly reveals moss genome
RT structure and evolution.";
RL Plant J. 93:515-533(2018).
RN [3] {ECO:0000313|EnsemblPlants:Pp3c13_15270V3.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (DEC-2020) to UniProtKB.
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DR EMBL; ABEU02000013; PNR42583.1; -; Genomic_DNA.
DR PaxDb; 3218-PP1S158_132V6-1; -.
DR EnsemblPlants; Pp3c13_15270V3.1; Pp3c13_15270V3.1; Pp3c13_15270.
DR Gramene; Pp3c13_15270V3.1; Pp3c13_15270V3.1; Pp3c13_15270.
DR InParanoid; A0A2K1JM08; -.
DR Proteomes; UP000006727; Chromosome 13.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0043531; F:ADP binding; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR CDD; cd13999; STKc_MAP3K-like; 1.
DR Gene3D; 1.10.8.430; Helical domain of apoptotic protease-activating factors; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 7.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR042197; Apaf_helical.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR006553; Leu-rich_rpt_Cys-con_subtyp.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR002182; NB-ARC.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR48051; -; 1.
DR PANTHER; PTHR48051:SF1; ZGC:77287; 1.
DR Pfam; PF00560; LRR_1; 2.
DR Pfam; PF00931; NB-ARC; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR00364; DISEASERSIST.
DR SMART; SM00367; LRR_CC; 14.
DR SMART; SM00369; LRR_TYP; 18.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52058; L domain-like; 4.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
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};
KW Plant defense {ECO:0000256|ARBA:ARBA00022821};
KW Reference proteome {ECO:0000313|Proteomes:UP000006727};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 238..521
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
SQ SEQUENCE 1982 AA; 221458 MW; 3EB5B69FAD944A6F CRC64;
MEYFLELFKY YIITIWSFLH GFFMSRFSST MEKYDKISSM QGIFGDTWKG SEVYIGAFEV
LLNKNNLLNK NQCAHLCKKI EHVTKVFDHL MTCTNGGLEF RLLMSELFFI LNKSFFLVEN
CGRPNWCKEA ILQLNNKETF RELLLDLKCC CDIASDILLK NYSKKLEDIS FATFNVATYD
EVEGDVKVVY ERLNNVNGID DFEYCGLANH LLKRLEDLLH IDDEELDDLK LSSNIESLQF
IKRISEGSFG AVYESKWLGV LCAIKKMDVA FNKFFKREVT ILANLSHPNL ITYYFAMKGH
ANESGESFEL VFKKDYLYIG MELMQTNLND MLENTKQTSY VFLIDIIYQI AKGMCYLHDM
HIAHRDLKPQ NILVNVIEIK VMNKVIQHAI VKVIDFGISK IEVGSNPETT KNEVPYGTVA
YMAPEVLKSK FETITMCPFE ADVYSFAMVC SKILSKRDPF DGVYKMEAIL ERIEKGERPK
LPSNCNELIE LIQECWMLNP LHRPKFANIC KRLDLIKKKF LVGIEVANAP YFGESNKNCH
QSKRFQPIHN ELPLVESSGE EIFGRAQYLS QIRKLCANKV KVLYLVGMGG IGKTTIAKTT
LINVKNMYNA SCFVECIESG GDCYTTSCNI LEQFQVKEKP KDVKEAHKIL KSFLTKNKTI
LVFDNIKNQS QIEDVVPMDD IFASNGSTLI ATTRDSNVMK DCGKEIYKIN IEELDEETSM
KMFITHSCGQ KSLPIELVEV GKKIVRACNG LPLSLKVMGA FLREKKRLRC WERALQKLKR
GRKLDGDENN SNYKIWKILR VSFDNLKVEE KKMFLDICCF FCNDVCPQGM SKERALRIWV
NNQNNILEHE MEFTLNTLIY QSLIKLDKDG IIRVHDQLRD MSRNIVEEEM EYKYTRMWNL
NIDPFYGLSN KLEGLFYNNI NNNNIGKVRS ASFSSLQFLS CNIGVFAPKI VIKILSIFFV
LVKNSLNLRC FLLNMPLEYE FKKEEAHKAL QMLHDKDVWK KFGSLNVLQL RNCSFIEIPP
NLFYKITTLL ELDLGGCSNL TMLPNELEYM TSLKILNLQY CERLKLLPTS IGSLISLKDL
NIENCQSLTS LPNELGNLTS LTFLNMKGCS SLTSLPNELG NLTSLTTLNM KGCSSLTSLP
NELGNLTSLT TLNTEGCSRL TSLPNEFGNL TSLTTLNMTG CSSLTSLPNE LDNLTSLTTL
NISWCSSLTS LPNELGNLTS LTTLNMWGCF RLTSMPNELG NLTSLTSLNM KGCSRLTSLP
KELENLTSLT TLNMWGCSSL RSLPNELSNL TSLTTLYMEG CSRLTSLPNE LGNLTSLTTL
SIGRCSSLTS LPKELDNLTS LTTLSLRRCS SLTSLPNELG NLTSLTTLDI SWCSRLTSLP
NELGNLTSLT TLNISWCSSL TSLPNELGNL TSLTTLSIGR CSSLTSLPNE LGNLTSLTTL
NMERCFRLTS MPNELGNLTS LTSLNMKGCS RLTSLPKELE NLTSLTTLNM WGCSSLRSLP
NELSNLTSLT TLYMEGCSRL TSLPNELGNL TSLTTLSIGR CSSLTSLPKE LDNLTSLTTL
SLRRCSSLTS LPNELGNLTS LTTLDISWCS RLTSLPNELG NLTSLTTLNI SWCSSLTSLP
NELGNLTSLT TLSIGRCSSL TSLPNELGNL TSLTTLNMER CSRLTSLPKE LGNLTSLTTL
DINWCSSLTS LPNELGNLTS LTILNMMECS SLTSLPNELG NLTSLTTLSI GRCSSLTSLP
NELGNLTSLT TLNMERCSRL TSLPKELGNL TSLTTLDINW CSSLTSLPNE LGNLTSLTIL
NMMECSSLTS LPNELGNLTS LTTLNFERCS RLTSLPKELD NLTSLTTLNI KGCTRLTSLP
NELGNLTSLT TLNMEGCSSL ISLPNELGNL TSLTTLNISW CSSLRSLPNE LGNLTSLTIL
NISWCSSLTS LPNELGNLTS LFFLNTEGCS SLTSLPNELD NLTSLIILNM EGCSSLTSLP
NE
//