ID A0A0N0DFZ6_FUSLA Unreviewed; 711 AA.
AC A0A0N0DFZ6;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Camk camkl ampk protein kinase {ECO:0000313|EMBL:KPA43344.1};
GN ORFNames=FLAG1_03723 {ECO:0000313|EMBL:KPA43344.1};
OS Fusarium langsethiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=179993 {ECO:0000313|EMBL:KPA43344.1, ECO:0000313|Proteomes:UP000037904};
RN [1] {ECO:0000313|EMBL:KPA43344.1, ECO:0000313|Proteomes:UP000037904}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fl201059 {ECO:0000313|EMBL:KPA43344.1,
RC ECO:0000313|Proteomes:UP000037904};
RA Lysoe E., Divon H.H., Terzi V., Orru L., Lamontanara A., Kolseth A.-K.,
RA Frandsen R.J., Nielsen K., Thrane U.;
RT "The draft genome sequence of Fusarium langsethiae, a T-2/HT-2 mycotoxin
RT producer.";
RL Submitted (APR-2015) 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};
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:KPA43344.1}.
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DR EMBL; JXCE01000044; KPA43344.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N0DFZ6; -.
DR OrthoDB; 5475340at2759; -.
DR Proteomes; UP000037904; 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; 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:KPA43344.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000037904};
KW Transferase {ECO:0000313|EMBL:KPA43344.1}.
FT DOMAIN 66..317
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 418..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 466..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 568..599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 624..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..439
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..505
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..582
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..599
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 624..642
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 100
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 711 AA; 79757 MW; C6D3B45E26ADCB2E CRC64;
MAPRGFEDEE LTISLSSSHV RRPQQTQSQP QSQQQDDSHD APQAASRPAD APLKERIKTE
QRIGAYKVLR TLGEGSFGKV KLAIHNGTGQ QVALKIIARK KLISRDMAGR VEREIEYLQL
LRHPHIIKLF TVIKTPNEII MVLEYAGGEL FDYIVQHGRM KEPEARRFFQ QMLCAVEYCH
RHKIVHRDLK PENLLLDENL NVKIADFGLS NIMTDGNFLK TSCGSPNYAA PEVIGGKLYA
GPEVDVWSCG VILYVLLVGR LPFDDEHIPS LFAKIAKGTY SIPQWMPTGA ANLIKKMLVV
NPVHRATIED IRADPWFTTD LPVYLQLPVE EFFNTGVDPN KAIKKNDIAP NASEKVQERL
HNEVTEKISK TMGYGKSDVE EALQAAEPSA IKDAYMIVRE NKMMQVNHNS EALLAEPEGS
SPMLSMSSAR STTSQVTTTP RPYVSKVGIL PSSLPAYHKD YMEREKAGSV ENSPPKVLIN
DEPQLNRTDA EKEETARRLR PHSRSQLRID EANARPQGMT PINPPKKTKP VRWQFGIRSR
NSPWEALLCI HKALYKLGAT YIPDEDYESR TAEERAEASG DSSFVDSHDS YRGSTSSIDP
KKRYNLPADP WHINVRWDTS AIKKKAGNTP SAPSTPSSPS TPDGHHAKEP FVALHLDIQI
YEMEHGVYLV DFKCSGYETA HGRLLEEKDV TSPFPFLDMA AKLIMQLAEA D
//
