ID A0A1B8CP34_9PEZI Unreviewed; 777 AA.
AC A0A1B8CP34;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=CAMK/CAMKL/AMPK protein kinase {ECO:0000313|EMBL:OBT48567.1};
GN ORFNames=VE00_01344 {ECO:0000313|EMBL:OBT48567.1};
OS Pseudogymnoascus sp. WSF 3629.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1622147 {ECO:0000313|EMBL:OBT48567.1, ECO:0000313|Proteomes:UP000091997};
RN [1] {ECO:0000313|EMBL:OBT48567.1, ECO:0000313|Proteomes:UP000091997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WSF 3629 {ECO:0000313|EMBL:OBT48567.1,
RC ECO:0000313|Proteomes:UP000091997};
RA Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT "Comparative genomics of Pseudogymnoascus destructans, the fungus causing
RT white-nose syndrome of bats.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000091997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WSF 3629 {ECO:0000313|Proteomes:UP000091997};
RX PubMed=29295979; DOI=10.1038/s41467-017-02441-z;
RA Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT "Extreme sensitivity to ultraviolet light in the fungal pathogen causing
RT white-nose syndrome of bats.";
RL Nat. Commun. 9:35-35(2018).
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; KV454569; OBT48567.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B8CP34; -.
DR STRING; 1622147.A0A1B8CP34; -.
DR OrthoDB; 5475340at2759; -.
DR Proteomes; UP000091997; 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; 2.
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; 2.
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:OBT48567.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000091997};
KW Transferase {ECO:0000313|EMBL:OBT48567.1}.
FT DOMAIN 60..311
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 503..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 611..653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..51
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 503..549
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 611..645
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 94
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 777 AA; 85882 MW; 86F468AB39538BC7 CRC64;
MQPSQGYDDE ELSISLAPSN NRRTQNKPPD ASSGRSNRPR EEVRRPTVPA RKAEQRIGAY
DIKGTLGEGS FGKVKLAVHR VTQQQVALKI IARKKLISRD MAGRVEREIE YLQLLRHPHI
IKLYTVIKTQ TEIIMVLEFA GGELFNYIVQ HGKMTETKAR RFFQQIICAV EYCHRHKIVH
RDLKPENLLL DNDLNVKIAD FGLSNIMTDG NFLKTSCGSP NYAAPEVING KLYAGPEVDV
WSCGVILYVL LVGRLPFDDD NIPALFAKIA KGHYVVPNYM TPGAASLIKK MLAVNPVHRV
TIDEIRQDPW FLLDLPAYLM PPVEEFMDTG VDSGKAINPQ GIAPGASRAV QEKLHDAVTE
KLGKKMGYGK QDVQEALEAD EPSAIKDAYL IVRENTIAQA NPNINALLGS SPPAWDEPLS
SLRDKSIATV SQNVVGSGDV DEMSLRASLG GLTIQPSAEQ ASSRSGSINT VLSGDRPVRP
FISKIGILPS SLPAYHRAYM EARKTGKDVP SSSPKVDVDH VETNRAKSSE EQAETARRLN
PHSRNQLKLD EGNNKPAAMT PVPQKKSKPT KWQFGIRSRN QPLEAIGCIY RALKKLGAEW
VVDENYRSVA QKNNDNERQQ KRSFGSNESD SDDGGSLHRF DSQDNLAKDF PYPPGAQYKL
PADPWVLRVR WRKGGMYAPG TVPPGSTHSS QIDLRRQSLA SMSSVSGSGP LNDPEEGVIM
HLDIQLYEME QGVYLVDFKC AGYETAAGVM LEEKDVTSPF PFLDLSSTLI IALAEAD
//
