ID A0A1V9YMZ4_9STRA Unreviewed; 1012 AA.
AC A0A1V9YMZ4;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Protein kinase {ECO:0008006|Google:ProtNLM};
GN ORFNames=ACHHYP_09562 {ECO:0000313|EMBL:OQR87089.1};
OS Achlya hypogyna.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Achlya.
OX NCBI_TaxID=1202772 {ECO:0000313|EMBL:OQR87089.1, ECO:0000313|Proteomes:UP000243579};
RN [1] {ECO:0000313|EMBL:OQR87089.1, ECO:0000313|Proteomes:UP000243579}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 48635 {ECO:0000313|EMBL:OQR87089.1,
RC ECO:0000313|Proteomes:UP000243579};
RX PubMed=25527045; DOI=10.1093/gbe/evu276;
RA Misner I., Blouin N., Leonard G., Richards T.A., Lane C.E.;
RT "The secreted proteins of Achlya hypogyna and Thraustotheca clavata
RT identify the ancestral oomycete secretome and reveal gene acquisitions by
RT horizontal gene transfer.";
RL Genome Biol. Evol. 7:120-135(2014).
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:OQR87089.1}.
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DR EMBL; JNBR01001469; OQR87089.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V9YMZ4; -.
DR STRING; 1202772.A0A1V9YMZ4; -.
DR OrthoDB; 5635964at2759; -.
DR Proteomes; UP000243579; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0043229; C:intracellular organelle; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR CDD; cd00030; C2; 1.
DR CDD; cd00992; PDZ_signaling; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR44329:SF214; ANKYRIN REPEAT-CONTAINING PROTEIN KINASE A-RELATED; 1.
DR PANTHER; PTHR44329; SERINE/THREONINE-PROTEIN KINASE TNNI3K-RELATED; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00248; ANK; 2.
DR SMART; SM00239; C2; 1.
DR SMART; SM00228; PDZ; 2.
DR SMART; SM00233; PH; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF50156; PDZ domain-like; 2.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00022527};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000243579};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022527};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 8..90
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 223..326
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 380..499
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REPEAT 576..598
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 649..910
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 676
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1012 AA; 111232 MW; BA6AE9CCA945861E CRC64;
MAETAPRLLP LELPSGSKLG IAITPPKHGV TVRGLVIDKV QNELFIGQIS HGDLLLEIGG
IPLDGMKFAY AVDLLKTMPR PLQLTFEIVP MSLKRMATTT EVDSLDVNVP SYNVVFDNAK
MGLNLDDGMR FGIDGAIVKG VRDFAEDAGI SVGDILYKVN GTEVLFMSLK QANLDEVQRI
SLNMSVAEKN DRVARAKPTK DPPEQLIAPE KSITEIIQEN RSTVIKEGPM YKQGQMVKNW
KKRHFVLAVS KLEYFKDSKD KISQGVVYFE NCRCTVRSLP STAAKLTGAP GDYVLELMAG
DRQFIMSCTS EDERMEWLEA LKVAIDASKA LSGTSSEVDA LRRTSFLLSS RRLGQGMSSI
SEDAPMPRST TRHMSISTGL NASMQTTPEK SLDTLVGIGA TVDIEVLSIQ NLTKAFFHVM
NPFCEVTFGS ETFKTPTVKD SLNPRWTQDN KVTFSVSSVD TLIEVRVFDE RMIRAPELLS
TFTIPLQSLP RKTRLEQTYS LILADRTAYA SITLGLRYNN GDLDQEVTPT SQCKTAVTKF
TATDLRHFFE AVASGDEARA NEWLAQGINP NVANDAGETP LHVAVRCDHR KLLELLLQAT
GVDATVCNKH GDTPLIAAIK QGHRRFAARI YTHLDSKQPM SKVEDTDVIV ERTILGHGTF
GVVFKGIFDN QPVAVKTFLG AFASNTFTYE MEAMELCKSP YLLRLLAVTG QNTSSPQLVL
EYMDGGDLRG YLDKKRDDLP VAVEYSALEV AWVIANALAD LHLNNLLHRD LKSHNVLLSS
THYIKVADLG TVRACATVMT QGKGTPFWTA PEVLADEGNY DYAADVYSFG VILTELSTLQ
LPYAGLQLSQ SIILERVRKG TLRPDVGVSS PTWLRDLATD CMKYDPNERP NVQAILQRLT
DRRRLEASFV STSIECLKCK ASHPIVAAAC PECGEPTLPP TTKLTNLLER VAVAKKRGIA
VNASLTCAVC DMANSVSATA CAECESELPD DVEKLQRLVK SVNWAMKVAV AA
//
