ID W2ZFC3_PHYPR Unreviewed; 862 AA.
AC W2ZFC3;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=AGC/AKT protein kinase, variant 2 {ECO:0000313|EMBL:ETP44879.1};
GN ORFNames=F442_08578 {ECO:0000313|EMBL:ETP44879.1};
OS Phytophthora parasitica P10297.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=1317064 {ECO:0000313|EMBL:ETP44879.1, ECO:0000313|Proteomes:UP000018948};
RN [1] {ECO:0000313|EMBL:ETP44879.1, ECO:0000313|Proteomes:UP000018948}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P10297 {ECO:0000313|EMBL:ETP44879.1,
RC ECO:0000313|Proteomes:UP000018948};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA Machado M., Johnson C.S., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Phytophthora parasitica P10297.";
RL Submitted (NOV-2013) 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:ETP44879.1}.
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DR EMBL; ANIY01001791; ETP44879.1; -; Genomic_DNA.
DR AlphaFoldDB; W2ZFC3; -.
DR EnsemblProtists; ETP44879; ETP44879; F442_08578.
DR Proteomes; UP000018948; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00030; C2; 1.
DR CDD; cd00065; FYVE_like_SF; 1.
DR CDD; cd05123; STKc_AGC; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR045270; STKc_AGC.
DR InterPro; IPR000306; Znf_FYVE.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR24351:SF247; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ETP44879.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000018948};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Synapse {ECO:0000256|ARBA:ARBA00023018};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00091}.
FT DOMAIN 245..356
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 410..466
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 517..786
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 787..855
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT BINDING 549
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 862 AA; 97175 MW; 04666EB749CE3CA3 CRC64;
MQTLVAQIHA KLKNELNLRE IFIPNSKAEA RCSIFVSHNY AACPKLCIFM QPGEGMQPGM
WSRTIHPKTG FQGSMIPYLK TAIQGGYGVV ILNPSTNFCM VNGHRAKILH SSTPEAHVSY
VWKNYVVPNA AQEISFIVHD NAGVLLKTFL SSLSGHEQQR VGGIAFIESA HQVSSGDSNA
LREMLREKAV NFEASTEPMF TVIGSSKARL GCTSLSVGRT SGEANNREWT VHSVQTSAFV
FLQSIANGIE ESLHAIRATF PNKLIVTVNR ARLTGQPYNN PFAVVQCAGQ KKETVGSHKH
TMDPEWNQTF SFPVTSSEAK VVIIVKDRSF PMNTSLGQVV VTMSEVGLNR ADRRWFALRD
EKVATSHGNG EVELTLEWVH DTFVARSDSF IRGNRMPTLE AQQRPRNGTG DGENCCYLCK
TTFVLHRRRY CRMCLRLVCT SCSDRLFLPG FSEPKRVCSG CCDLQMMLHN KLPRMGGPGG
PGSKVPSQDK LDEHAQRMEA MRKREEAEKR PLSINDFDLL KVVGRGAFGK VLLVRKKEGK
NSGQIYAMKI LVKSHIIKND QIENTKAEQH ILKEISHPYV VRLRYAFQNA DKLYLIMDYY
PGGSMFYHLR KSKRFSEERT RLYMAQLLTA LMHLHSKQIA YRDLKLENIL MDPKGNIALT
DFGLSKEGQM VEGAIRASQA DTGMKTICGT AEYMAPELLR HQPYGKVVDW WSYGILLFEM
LTGRTPFVDR NRRQMFKNIM QSEVIYPSHI SPVARSLISK LLNRDPARRL GGGPNGGRDI
MAHPFFESID WDKLMRKEIE PPFVPDVSSV DDITNVPEMF QNMAAVDSPV NKKNGEGHHF
DDFTYQEDGY IMRATHNLNQ HQ
//
