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Database: UniProt
Entry: G4ZTL0_PHYSP
LinkDB: G4ZTL0_PHYSP
Original site: G4ZTL0_PHYSP 
ID   G4ZTL0_PHYSP            Unreviewed;       707 AA.
AC   G4ZTL0;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   SubName: Full=Cyclic AMP-dependent protein kinase-like protein regulatory subunit {ECO:0000313|EMBL:EGZ12921.1};
GN   ORFNames=PHYSODRAFT_262016 {ECO:0000313|EMBL:EGZ12921.1};
OS   Phytophthora sojae (strain P6497) (Soybean stem and root rot agent)
OS   (Phytophthora megasperma f. sp. glycines).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=1094619 {ECO:0000313|EMBL:EGZ12921.1, ECO:0000313|Proteomes:UP000002640};
RN   [1] {ECO:0000313|EMBL:EGZ12921.1, ECO:0000313|Proteomes:UP000002640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P6497 {ECO:0000313|EMBL:EGZ12921.1,
RC   ECO:0000313|Proteomes:UP000002640};
RX   PubMed=16946064; DOI=10.1126/science.1128796;
RA   Tyler B.M., Tripathy S., Zhang X., Dehal P., Jiang R.H., Aerts A.,
RA   Arredondo F.D., Baxter L., Bensasson D., Beynon J.L., Chapman J.,
RA   Damasceno C.M., Dorrance A.E., Dou D., Dickerman A.W., Dubchak I.L.,
RA   Garbelotto M., Gijzen M., Gordon S.G., Govers F., Grunwald N.J., Huang W.,
RA   Ivors K.L., Jones R.W., Kamoun S., Krampis K., Lamour K.H., Lee M.K.,
RA   McDonald W.H., Medina M., Meijer H.J., Nordberg E.K., Maclean D.J.,
RA   Ospina-Giraldo M.D., Morris P.F., Phuntumart V., Putnam N.H., Rash S.,
RA   Rose J.K., Sakihama Y., Salamov A.A., Savidor A., Scheuring C.F.,
RA   Smith B.M., Sobral B.W., Terry A., Torto-Alalibo T.A., Win J., Xu Z.,
RA   Zhang H., Grigoriev I.V., Rokhsar D.S., Boore J.L.;
RT   "Phytophthora genome sequences uncover evolutionary origins and mechanisms
RT   of pathogenesis.";
RL   Science 313:1261-1266(2006).
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DR   EMBL; JH159156; EGZ12921.1; -; Genomic_DNA.
DR   RefSeq; XP_009530350.1; XM_009532055.1.
DR   AlphaFoldDB; G4ZTL0; -.
DR   STRING; 1094619.G4ZTL0; -.
DR   EnsemblProtists; EGZ12921; EGZ12921; PHYSODRAFT_262016.
DR   GeneID; 20639341; -.
DR   KEGG; psoj:PHYSODRAFT_262016; -.
DR   InParanoid; G4ZTL0; -.
DR   Proteomes; UP000002640; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   CDD; cd00038; CAP_ED; 2.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 2.
DR   Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR   InterPro; IPR018488; cNMP-bd_CS.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR018490; cNMP-bd_dom_sf.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   PANTHER; PTHR24353:SF37; CAMP-DEPENDENT PROTEIN KINASE CATALYTIC SUBUNIT PRKX; 1.
DR   PANTHER; PTHR24353; CYCLIC NUCLEOTIDE-DEPENDENT PROTEIN KINASE; 1.
DR   Pfam; PF00027; cNMP_binding; 2.
DR   PRINTS; PR00103; CAMPKINASE.
DR   SMART; SM00100; cNMP; 2.
DR   SUPFAM; SSF51206; cAMP-binding domain-like; 2.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR   PROSITE; PS00888; CNMP_BINDING_1; 2.
DR   PROSITE; PS00889; CNMP_BINDING_2; 2.
DR   PROSITE; PS50042; CNMP_BINDING_3; 2.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002640};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          306..415
FT                   /note="Cyclic nucleotide-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50042"
FT   DOMAIN          429..536
FT                   /note="Cyclic nucleotide-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50042"
FT   REGION          1..289
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          564..598
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        28..60
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        69..85
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        94..111
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        169..201
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        234..273
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        564..592
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   707 AA;  76643 MW;  6D581013D837D27A CRC64;
     MGQHLSTGRE SDVSAGDAAE GPPSSTLSAA FPAASPSSAS YSVTSNAADS SANGPSLLSA
     QRPTLEPHKV DTVQQDEREG SVRLGDVVRD TLGSSSGAHD QEPSAHQLQP LELQSDDEDG
     GFPRVSSVDS FPSPPCNVKT DDAHPLKRRS SMSRTPAPPK LSRFRPSMDI VQSPKSPQSG
     YLSSSDSRSV DSSSSSSDED LVGSGEELVS DWLDEPEDAV LSPPSIPKRA RHASACSSVS
     SHTGNSVSFS AMHSSGGRNS NSSQHSMTGW ASWLSSPDDV EEEEDADDEP VALTPFLRDN
     MPVQMQQEQV VRALKPCKFS DGEVIVAQGT RGSRFYMIAK GEAVVTKKVV ASSNSMTGST
     PTGAGQTQER MITHLRAGHY FGELALIYDD PRTATVRAVG DVELLYLTQE DFQHIGQVHL
     SLMLQQVPLL ARLSAQDQDI VLKCLRPANF SDGEYIVHQG DEGTRFYMIT RGEAIVSEKA
     VGPDKKPYEK ELTRLYEGHV FGEMSLIYSE PRTASVRAVG PVKCLYLSKE DFDKCLLSDH
     FQRFIQEAYV EKATRRAMRL RLQQRANSAA SNAPTPQAEG SGANSSSGSI VAPPPAPISP
     VKATETKKLL LPALLGLVER FHRSWKDMVA MYVAEAQDDW DQWLHCSAYA YNGARHSGTG
     YSPNELMMGR KLRAPSELLR SSGVTQTGPF AVYYRKLVDN MARVLSL
//
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