ID A0A094JAI6_9PEZI Unreviewed; 1120 AA.
AC A0A094JAI6;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=V501_07828 {ECO:0000313|EMBL:KFZ05988.1};
OS Pseudogymnoascus sp. VKM F-4519 (FW-2642).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420914 {ECO:0000313|EMBL:KFZ05988.1, ECO:0000313|Proteomes:UP000029315};
RN [1] {ECO:0000313|EMBL:KFZ05988.1, ECO:0000313|Proteomes:UP000029315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4519 (FW-2642) {ECO:0000313|Proteomes:UP000029315};
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 -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. CHEK2 subfamily.
CC {ECO:0000256|ARBA:ARBA00005575}.
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:KFZ05988.1}.
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DR EMBL; JPKD01002231; KFZ05988.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094JAI6; -.
DR STRING; 1420914.A0A094JAI6; -.
DR HOGENOM; CLU_009254_0_0_1; -.
DR Proteomes; UP000029315; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR CDD; cd00180; PKc; 1.
DR Gene3D; 2.60.200.20; -; 1.
DR Gene3D; 1.10.1280.10; Di-copper center containing domain from catechol oxidase; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR008922; Di-copper_centre_dom_sf.
DR InterPro; IPR000253; FHA_dom.
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; IPR008984; SMAD_FHA_dom_sf.
DR InterPro; IPR002227; Tyrosinase_Cu-bd.
DR PANTHER; PTHR11474:SF125; TYROSINASE COPPER-BINDING DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR11474; TYROSINASE FAMILY MEMBER; 1.
DR Pfam; PF00498; FHA; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00264; Tyrosinase; 1.
DR PRINTS; PR00092; TYROSINASE.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF48056; Di-copper centre-containing domain; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS00497; TYROSINASE_1; 1.
DR PROSITE; PS00498; TYROSINASE_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000029315};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1120
FT /note="Protein kinase domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001905028"
FT DOMAIN 407..460
FT /note="FHA"
FT /evidence="ECO:0000259|PROSITE:PS50006"
FT DOMAIN 532..766
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 788..827
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 976..1010
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1065..1102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 976..992
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 566
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1120 AA; 122634 MW; 71786A972AF1E2AC CRC64;
MLASVSNILV ASLFATTVVG SSVYRPENSN HGGDAVDAIS AKGLAKLKAW TKSNPPAGNC
TLENAVIRRE WSAFSRQERL DYIDAVLCLQ KKPPTTPLSI IPGVRSRYDD FVGTHINQTL
FIHSTGNFLG WHRYYVWTYE QALRNECNYQ GHQPYWNWGK YALDPVNSLL FDGSDESLSG
DGSCFEHTPV AVAGAPPPFD VIIPGNGGGC VTSGPFKDMV VSLGPVAGTL DGVTPNPTPD
GYSYNPRCLR RDISENAAVS TRTNATVSLL TTRDNISDFQ DYMQGVFAEG ILGVHAGGHF
TVGGDPGGDF FASAGDPAFW LHHASVDRIW WIWQNQDLAT RQNAIAGQTH MAGDGVPTTL
EDDQFFQVNG KPRSPPSLGF DSTPRNDSLG FVFGRFDVAS STNNEIDDVG QGPSVPDIII
PPPNSDVGRM QFRIHYNLST GVLMITESSS RGTWVGQKRI RKTATTIMIG TTIYFGSGGR
IGFQVYIPDH SRNHDLYQRN YRQYAALLGC TPSAYIPTPT PALQDMPLGR DYSILEYIGR
GSFGTVNTVC RNKDGYIFAA KGIAGKTIGD DIVFPQEVEK MRRLSHAHIV KFVDAFIWGK
GIQVIMERLS MHLEDYRLTR PRQQLSLAAI QSVTRQSLCG LEYLHENGVT HRDLKPENIL
IAEQNSLEMH GTNRLNQALR REHRRAGSPP PQNLHTYTPA IDIWAIGMIL HKLLGGEFQQ
INDRWYAEER DFSSAKRPAA RLAVKMLAID PKQRLTAAEC LQDPWLAIAD DIPAQSLEKR
VRSFSPITQN EEQARKKAQF SIPNTQAGYS GTETSSAPQT SLNSADDVTP LGTVRQVEGL
IQAFQEAHGR NESGPDDVTM LLNWVNDQSS FRSGFSKIVI TSQASGSIIV TLGSSVWQID
ICSPTLVPSN GASHVSAGAQ GNNDATLNNT ESMQMVIDQM LAAFEASGFY NPALQEQNEL
AQFPGLTARQ AAWQSQNDPG STITNANANK APHHQNMALP GEDVPDDGPS ESPEWVIKLV
NRIFAQRDDC YSAIYYWQRP AHETHGSIIH HPVSDPFFPQ PSLSAAMKSR VQSDTGSKQG
GSSGKSKYGD SSGKSSSDDS AWNRTTLPVT LSLYDDLAGC
//
