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Database: UniProt
Entry: A0A094BAZ6_9PEZI
LinkDB: A0A094BAZ6_9PEZI
Original site: A0A094BAZ6_9PEZI 
ID   A0A094BAZ6_9PEZI        Unreviewed;       738 AA.
AC   A0A094BAZ6;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=Protein kinase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=V493_00086 {ECO:0000313|EMBL:KFY32535.1};
OS   Pseudogymnoascus sp. VKM F-4281 (FW-2241).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420906 {ECO:0000313|EMBL:KFY32535.1, ECO:0000313|Proteomes:UP000029327};
RN   [1] {ECO:0000313|EMBL:KFY32535.1, ECO:0000313|Proteomes:UP000029327}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4281 (FW-2241) {ECO:0000313|Proteomes:UP000029327};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:KFY32535.1}.
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DR   EMBL; JPJV01000041; KFY32535.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094BAZ6; -.
DR   STRING; 1420906.A0A094BAZ6; -.
DR   HOGENOM; CLU_332915_0_0_1; -.
DR   OrthoDB; 2474457at2759; -.
DR   Proteomes; UP000029327; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0006811; P:monoatomic ion transport; IEA:UniProtKB-KW.
DR   CDD; cd06186; NOX_Duox_like_FAD_NADP; 1.
DR   Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR013112; FAD-bd_8.
DR   InterPro; IPR017927; FAD-bd_FR_type.
DR   InterPro; IPR013130; Fe3_Rdtase_TM_dom.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   PANTHER; PTHR32361:SF26; FAD-BINDING 8 DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR32361; FERRIC/CUPRIC REDUCTASE TRANSMEMBRANE COMPONENT; 1.
DR   Pfam; PF08022; FAD_binding_8; 1.
DR   Pfam; PF01794; Ferric_reduct; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51384; FAD_FR; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   4: Predicted;
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029327};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00023065}.
FT   TRANSMEM        339..362
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        374..392
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        404..424
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        431..448
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        460..482
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1..348
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          472..594
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   REGION          1..83
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        45..65
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        66..82
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   738 AA;  82143 MW;  AD5AD643751239F8 CRC64;
     MSSGKRGTKI DMLAGSAQLL PTQHPKASAT LPALSRSPVG DTPESASKKL KRSRSPKDDT
     DHTSSVKISK PPSISESKPS PFTARKESPW EIYKIHFDLD LNGPVTVAQG KAGLVAVRTF
     TVAAAEKALY MHGRVRHPNI VNALEAFTTE TSFYIVLEYM PISLYQIVES AKYPTESELA
     AILRQVLDGL IYLESEGLEH GSINCRNILL STGGDVKIAN QQCCEKTEKT QRNREPQDVR
     ALGIITMELM QKYTQDNGAV GVENLDRWPS DSDAVTFLSE TTSAASAREL RKILQRHSHL
     GPWTPAGVVL HTGYIAANVS CLEFWRLTTT KVGFRAANLA LINMMPLFLG AHISFLSDLF
     GVSLKSWRLV HRSAGIMSFS LMLLHILIVV ASRVSFSLSV PENLYGLIGG SALCLVILLS
     IPFFRKPSYE IFLRMHQAVA SLVVYSIVRH LISQSNFKWS YVYIFAGVFV ALLAFQCGVV
     MFRNKAWGRR FPRAFITHID QTVMIRMTMS RPIEIKAGQY INLWIPSVSF WSFLQSHPFV
     VTNWADGKQD TLELFTQPRR GLTRELFSHG TLDERGSVPR LALFSGPHGI SVPVGEYETV
     LMVATGFGIA AQLPYLRKLI HGYNNCKAHT RRVHLVWQLQ TFDIGLAAES LLNSALVDDT
     LDDGYILCIS IYLESGNGDK VPFGKRATMY PGTANLEEIL QVELTGKHIR RVQETQERGK
     MLVMGKTPYI TIDNAYKT
//
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