ID A0A1B8EPH7_9PEZI Unreviewed; 913 AA.
AC A0A1B8EPH7;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=AGC/AKT protein kinase {ECO:0000313|EMBL:OBT73245.1};
GN ORFNames=VF21_08859 {ECO:0000313|EMBL:OBT73245.1};
OS Pseudogymnoascus sp. 05NY08.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1622149 {ECO:0000313|EMBL:OBT73245.1, ECO:0000313|Proteomes:UP000092096};
RN [1] {ECO:0000313|EMBL:OBT73245.1, ECO:0000313|Proteomes:UP000092096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=05NY08 {ECO:0000313|EMBL:OBT73245.1,
RC ECO:0000313|Proteomes:UP000092096};
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:UP000092096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=05NY08 {ECO:0000313|Proteomes:UP000092096};
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).
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DR EMBL; KV458867; OBT73245.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B8EPH7; -.
DR STRING; 1622149.A0A1B8EPH7; -.
DR OrthoDB; 10768at2759; -.
DR Proteomes; UP000092096; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd05586; STKc_Sck1_like; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 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; IPR017892; Pkinase_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24351:SF245; AGC_AKT PROTEIN KINASE SCK2; 1.
DR PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 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; 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.
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:OBT73245.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000092096};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 309..485
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 520..781
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 782..865
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT REGION 25..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 232..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 275..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 893..913
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..41
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..83
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..299
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..428
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 549
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 913 AA; 101246 MW; 69198B0895AA96B0 CRC64;
MYLSPRSENG ELRRIYLDDQ ADKTMFFSKP GEDDANDHID SDTPRSGVAT PKPDPSDKRL
PGIMHSYFQV GLNSGSSENP ISVPLETPAI GTEAENPPVL HVRETTTELD ENLSATGSSS
RENSSGDSEG SPYLLPHEKT ERRASSAADG ASHNPHPYPT PPVSKPPSVR KLKFNDSTAE
DGEAANPELA SPTSQISLPH HKTISESILP KFGASSMLKT LSNILTPSNV LASHISTPKE
PTPTTTEPDT PIHSRIASGS VSDSLSYDML KKLTIGDEKS HPATPTRALS NNTSTSDTSD
HGHEQVHKRP SGLSETKSSS SDIGGAPVRA PRGKLTVKIA EARGLRRSKD PYVVAVFQRN
ELVSKGPRSE DEDDEDEDAT ISPPPGGIPI SRQPSDSGRP MAIPMKSRQS SNTSDPEPRD
FKVKSRRSMT NPKWDTEAVF DVVGDDSRVS ISVYDRGTLT EDFLGHVDFN PELSEYDTAP
VKGWYPLRDR KGEEDSSIGE VYVEISFERT DKRHYGPEDF QILKLIGKGT FGQVYQVRKK
DTKRIYAMKV LQKKVIVQKK EVAHTVGERN ILVRTAMTES PFIVGLKFSF QTPTDLYLVT
DYMSGGELFW HLQKEGRFDE KRAKFYIAEL ILALQHLHVH DIVYRDLKPE NILLDANGHI
ALCDFGLSKA NLTKNDTTNT FCGTTEYLAP EVLLDEAGYT KMVDFWSLGV LVFEMCCGWS
PFYAEDTQQM YKNIAFGKVR FPRDTLSTEG RNFVKGLLNR NPKHRLGAID DAEELKRHPF
FADIDWEALT KKLITPPFKP KLKSETDTSN FDPEFTNALN GASSLNARAA ALAAGIVTST
PLSPGMQANF KGFTFVDENS IDDHFQDRTK YDIDEMDEAW DDTKTKRMSG MSGIVKSHNN
EDSSMINGEH FDM
//
