ID A0A176VDB5_MARPO Unreviewed; 1458 AA.
AC A0A176VDB5;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN ORFNames=AXG93_1783s1000 {ECO:0000313|EMBL:OAE18372.1};
OS Marchantia polymorpha subsp. ruderalis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE18372.1, ECO:0000313|Proteomes:UP000077202};
RN [1] {ECO:0000313|EMBL:OAE18372.1, 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:OAE18372.1};
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 -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000256|ARBA:ARBA00008684}.
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:OAE18372.1}.
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DR EMBL; LVLJ01004075; OAE18372.1; -; Genomic_DNA.
DR OrthoDB; 455055at2759; -.
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 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; PTHR48056:SF81; LEUCINE-RICH REPEAT CONTAINING PROTEIN; 1.
DR PANTHER; PTHR48056; LRR RECEPTOR-LIKE SERINE/THREONINE-PROTEIN KINASE-RELATED; 1.
DR Pfam; PF00560; LRR_1; 10.
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; 5.
DR SMART; SM00369; LRR_TYP; 12.
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}; Reference proteome {ECO:0000313|Proteomes:UP000077202};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
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 TRANSMEM 1033..1059
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1101..1393
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 1128
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1458 AA; 159833 MW; B38602F5A7F87FAA CRC64;
MDETMSHTRE HAPMGVRGAV GDTVVSAEAK SKLARCCEVR TSEAGSSVLV FRQTNPIQSS
RRTYYSMSFW GLTGTPSGIR QATYSGSQEF RVPITEDEEE KKSCRGSRKE SSSAMLKVHP
RAMVRNQSHL RNRIYEIHHL DVPDFGALLW SDLPCRDVLQ IWKREIEDGA QALRDWDNPS
SAGYCQYTGV QCGATGRVRS LNISGLGLSG PITTFIGDLT ELDNLDLSNN NFDGAIPTEI
GRLLSLQVMA LQVNNLTSSI PDSLGNLTRL KSLTLGNNSL TGGVPEALTK LTSLEVLSVP
ANQLEGQLTE DLGNLGNLTH LILESNKLNG SIPQSLGRLT NLRVLNLGNN SMSGEVPWGN
LTRLREMQEL TLYSNSFSGN LADNFGQLSN LQILNLHGNG FNGTIPDNIC VALVNLRMLQ
LNKNEFQGEL PIGIGRCSRL ETVDINSNHL FGSIPTSIGN CSSLRQIIAW NNNFTGQIPH
QVGDLTQLVD FNFDVNNLVG VLPSELGNLT QLRTLQLSLN AFTGNIPKEL GRLSNLKFLN
LGSSFLNGSI PPELFDSTFS LEEIHLDLNL LTGNIPATIG KARSLTILWL HYNQLNGSIP
DEIGNLTSLT TLSLGNNSLS GKIPDALGKL TNLMNFDLAL NEFTGEIPPF LQNFSQLKAI
WLHDNKLHGE IPVWLASLTN LQYLYLGENS LNGIIPEGLG QLTNLISLGL NECNLTGSIP
RSLSNLTKLE FLNLEYNSLQ GNITVDFSNF SSPAFSLILA GNELTGNFPA SLQDCSLYIL
DLSSNQLDGL LPNVAPNSLM LNISVFSIRS NNFSGPVPAW IWTLQNVTIL DLSDNKFTSP
MPSSFLSLQA LQQSTQSYDS SLDKVTDDEH KPMLVFDVEF HVKGGLVTYT YVLASNTLLD
LSNNKFSGQI PSNLGDLRGL RLLNFSRNQL DGAIPGTLGL LEDLEQLDLS DNNLSGEIPS
TLSELHSLAV LDLSNNNLSG AIPQTDNFNT RFLASAFAGN SLLCGFPLAA CIVDGSDGND
TGSSCSGSLC HAWARAVLGT FLALIVATVA ATVAMILLLR RQRRSSESDF TTYLFRDHHE
YDAILKVDFK GLAYHTNGFE FSNYETLGVG GSSVVYKVPL PETTIALKKL NLERHEHLKK
IATLEFDREL ETLGSLRHRN LVKLLGFCST STMKAIMLEY MENGSLDKHL YGPGNKPLSW
KTRLDIASGV VEALYYLHHG CQFPVIHLDL KPSNILLNYD MIPKVGDFGL AKFVKSGAGT
GDVTASNVCG STGYIPPEYA STMKVSTKGD VYSFGVVLLE LLSRKRPTDL GGDMTIRQWF
VGAFPMNLSL VLDQQLLEES ETMSDVQLKQ ISLLTRIGLL CTVPQPSDRP TMVDVKAMLE
QIRAENGFTH ASLVKYPSLQ ELAAVDHEPR TIRRRESLFP MQIQDKNCTS AKKFPGFTGN
VTRTTQRVAK EHEENQED
//
