ID X0CB03_FUSOX Unreviewed; 710 AA.
AC X0CB03;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=CAMK/CAMKL/AMPK protein kinase {ECO:0000313|EMBL:EXK91296.1};
GN ORFNames=FOQG_06714 {ECO:0000313|EMBL:EXK91296.1};
OS Fusarium oxysporum f. sp. raphani 54005.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=1089458 {ECO:0000313|EMBL:EXK91296.1, ECO:0000313|Proteomes:UP000030663};
RN [1] {ECO:0000313|EMBL:EXK91296.1, ECO:0000313|Proteomes:UP000030663}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=54005 {ECO:0000313|EMBL:EXK91296.1,
RC ECO:0000313|Proteomes:UP000030663};
RG The Broad Institute Genome Sequencing Platform;
RA Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Fusarium oxysporum PHW815.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001433};
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DR EMBL; JH658373; EXK91296.1; -; Genomic_DNA.
DR AlphaFoldDB; X0CB03; -.
DR eggNOG; KOG0583; Eukaryota.
DR Proteomes; UP000030663; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd12122; AMPKA_C; 1.
DR CDD; cd14079; STKc_AMPK_alpha; 1.
DR CDD; cd14334; UBA_SNF1_fungi; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR Gene3D; 3.30.310.80; Kinase associated domain 1, KA1; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR032270; AMPK_C.
DR InterPro; IPR028375; KA1/Ssp2_C.
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; IPR013896; SNF1_UBA.
DR PANTHER; PTHR24346; MAP/MICROTUBULE AFFINITY-REGULATING KINASE; 1.
DR PANTHER; PTHR24346:SF82; SERINE_THREONINE-PROTEIN KINASE MARK-A-RELATED; 1.
DR Pfam; PF16579; AdenylateSensor; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF08587; UBA_2; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF103243; KA1-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.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:EXK91296.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000030663};
KW Transferase {ECO:0000313|EMBL:EXK91296.1}.
FT DOMAIN 67..318
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 418..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 466..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 569..604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 625..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..443
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..510
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 569..583
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..602
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 101
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 710 AA; 79605 MW; 4B359B1E5E2B6328 CRC64;
MAPRGFEDEE LTISLSSSHV RRPQQQQQQQ SQQQQQHASS DAPTPGSRPA DAPLKERIKT
EQRIGAYKVL RTLGEGSFGK VKLAIHNGTG QQVALKIIAR KKLISRDMAG RVEREIEYLQ
LLRHPHIIKL FTVIKTPNEI IMVLEYAGGE LFDYIVQHGR MKEPEARRFF QQMLCAVEYC
HRHKIVHRDL KPENLLLDEN LNVKIADFGL SNIMTDGNFL KTSCGSPNYA APEVIGGKLY
AGPEVDVWSC GVILYVLLVG RLPFDDEHIP SLFAKIAKGT YSIPQWMPAG AANLIKKMLV
VNPVHRATIE DIRADPWFTT DLPAYLQLPV EEFFNTGVDP NKAIKKNDIA PNASEKVQER
LHNEVTEKIS KTMGYGKSDV EEALQAAEPS AIKDAYMIVR ENKMMQVNHN PEALLAEPEG
SSPMLSMSSA RSTTSQATTT PRPYVSKVGI LPSSLPAYHK DYMEREKAGS VENSPPKVLI
NDEPPSNRTD AEKEETARRL RPHSRSQLRM DEANTRPQGM TPINPPKKNK PVRWQFGIRS
RNSPWEALLC IHKALHKLGA TYIPDEDYES RTAEERAEAS GEGSFADSHD NNRGSSSSID
PKKRYNLPAD PWHINVRWDT SAIKKKAASV PGTPSSPSTP EGQHHPKEPF VALHMDIQIY
EMEHGVYLVD FKCSGYETAH GRLLEEKDVT SPFPFLDMAA KLIMQLAEAD
//
