ID A0A176WAG9_MARPO Unreviewed; 642 AA.
AC A0A176WAG9;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN ORFNames=AXG93_4295s1010 {ECO:0000313|EMBL:OAE30148.1};
OS Marchantia polymorpha subsp. ruderalis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE30148.1, ECO:0000313|Proteomes:UP000077202};
RN [1] {ECO:0000313|EMBL:OAE30148.1, ECO:0000313|Proteomes:UP000077202}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Tak-1 and cv. Tak-2 {ECO:0000313|Proteomes:UP000077202};
RC TISSUE=Whole gametophyte {ECO:0000313|EMBL:OAE30148.1};
RA Honkanen S., Jones V.A., Morieri G., Champion C., Hetherington A.J.,
RA Kelly S., Saint-Marcoux D., Proust H., Prescott H., Dolan L.;
RT "Mechanisms controlling the formation of the plant cell surface in tip-
RT growing cells are functionally conserved among land plants.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OAE30148.1}.
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DR EMBL; LVLJ01001351; OAE30148.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A176WAG9; -.
DR OrthoDB; 1219660at2759; -.
DR Proteomes; UP000077202; Unassembled WGS sequence.
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 Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 2.
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; IPR032675; LRR_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR PANTHER; PTHR45974:SF242; LEUCINE-RICH REPEAT PROTEIN KINASE FAMILY PROTEIN; 1.
DR PANTHER; PTHR45974; RECEPTOR-LIKE PROTEIN 55; 1.
DR Pfam; PF00560; LRR_1; 3.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00365; LRR_SD22; 2.
DR SUPFAM; SSF52058; L domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Reference proteome {ECO:0000313|Proteomes:UP000077202};
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 349..373
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 411..642
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 439
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 642 AA; 71066 MW; BE60A239D69C8B2B CRC64;
MLFSNVVHGD ANPDQTAVLI DGDQSWFWKL FKVPGSPGFF QLLSNDQVIR SDWFTLRIGP
NGTTEAPVLL NAAEIHGEFA AVSVRTSKLD VDAVRKVYTE TALSSVDTAG DPCLPVPWDW
LVCSIELPPT ITQINLTGEG VSGVLPNELG NLSQLTILDL SENNYSDSFP DSLGRIRTLR
ELNLRHNKLS GELPLFSPKS LDNLEMLSLS SNMFNGTLIS LMGALDESIQ NLDLSNNKFV
GPVPGNIEML KNLENLDMSN NQLSSELAVN FTKLRNLKNL NLSLNNLNGT VPDSIWNSSN
LQFVLGDNPW CLNDTEGVNL KFIKKYMCRS DEHENFWPSP SKDGVQTGVV IAVGVVSGIF
VLLMSCLVIF FTWKMRRSSR ELQQLKEDLA KDNVKSPFFS YQELKTATNN FSSSNELGKG
GFGTVFKAVL ADGSVVAVKR LTPTKQSPSD FLKEMVNIMG IKHKHLIQLK GCCVKENQER
MLIYEYAENK SLAEALFDSG PQCVTFLNWK QRYNICLGIA RGLAYLHEGL QPGMIHRLEG
DYDEEEVLLV VNMALSCLQA DPKKRATMSQ LVNELLKNAN ASVAVDIVNE LKSQTVYLCS
IPEDEHYVDT YAGSQGVQGE SVELALLSSF AIDSQVSDMV PR
//
