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Database: UniProt
Entry: S7ZLA6_PENO1
LinkDB: S7ZLA6_PENO1
Original site: S7ZLA6_PENO1 
ID   S7ZLA6_PENO1            Unreviewed;      1024 AA.
AC   S7ZLA6;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=Protein kinase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PDE_06360 {ECO:0000313|EMBL:EPS31405.1};
OS   Penicillium oxalicum (strain 114-2 / CGMCC 5302) (Penicillium decumbens).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=933388 {ECO:0000313|EMBL:EPS31405.1, ECO:0000313|Proteomes:UP000019376};
RN   [1] {ECO:0000313|EMBL:EPS31405.1, ECO:0000313|Proteomes:UP000019376}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=114-2 / CGMCC 5302 {ECO:0000313|Proteomes:UP000019376};
RX   PubMed=23383313; DOI=10.1371/journal.pone.0055185;
RA   Liu G., Zhang L., Wei X., Zou G., Qin Y., Ma L., Li J., Zheng H., Wang S.,
RA   Wang C., Xun L., Zhao G.-P., Zhou Z., Qu Y.;
RT   "Genomic and secretomic analyses reveal unique features of the
RT   lignocellulolytic enzyme system of Penicillium decumbens.";
RL   PLoS ONE 8:E55185-E55185(2013).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC       protein kinase family. CHEK2 subfamily.
CC       {ECO:0000256|ARBA:ARBA00005575}.
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DR   EMBL; KB644413; EPS31405.1; -; Genomic_DNA.
DR   AlphaFoldDB; S7ZLA6; -.
DR   STRING; 933388.S7ZLA6; -.
DR   eggNOG; KOG0615; Eukaryota.
DR   HOGENOM; CLU_003637_1_0_1; -.
DR   OrthoDB; 2045964at2759; -.
DR   PhylomeDB; S7ZLA6; -.
DR   Proteomes; UP000019376; Unassembled WGS sequence.
DR   GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR   CDD; cd05117; STKc_CAMK; 1.
DR   Gene3D; 2.60.200.20; -; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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   PANTHER; PTHR44167; OVARIAN-SPECIFIC SERINE/THREONINE-PROTEIN KINASE LOK-RELATED; 1.
DR   PANTHER; PTHR44167:SF18; SERINE_THREONINE-PROTEIN KINASE RAD53; 1.
DR   Pfam; PF00498; FHA; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00240; FHA; 1.
DR   SMART; SM00220; S_TKc; 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.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000019376}.
FT   DOMAIN          91..145
FT                   /note="FHA"
FT                   /evidence="ECO:0000259|PROSITE:PS50006"
FT   DOMAIN          239..522
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          734..793
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1005..1024
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        755..769
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        770..793
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         268
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1024 AA;  113868 MW;  AEE1BE82F2C191A2 CRC64;
     MEATQESTQP CADPRRMGLD NSGLHEQDLA DIICILHPNS HAAHDAVAAT ATRGTQHILQ
     QDVLDYEQSE TAALDIALRL SSQVCDLGVG FCFGRNPTRC DVLLAVNDQA KRVSNTHFRI
     YLTGDGIIML QDTSTNGTIV DNCRLRKNQK ENSRMLTNGS VIQVVAGDQG SDEVRFVVRI
     PSREGFALQY TQNILRYFER VQKAAGALQL KNRNAPTTSS LSWSVANTYG MHWTGGSVYN
     VTGQIGKGAF ATVYKLATKQ HGAIYAAKEL DKRRFMKNGI LDQKVDNEMK IMRDLQHPNI
     VQYIDHHEYD RWIYIIMEYV PGGELSTYLS SHGKIAEDMV RTIARQLLRA LHYLHKRRIT
     HRDIKPDNIL IASLDPLRVK LSDFGLSKVT QEETFLKTFC GTLLYCAPEV YPDYETYRRG
     EFRKRRRLGD PPPKTSPYSQ SVDMWSLGAV LYHILCGVPP YSGRAEDRGV AMLRSIMESE
     ADFDVLRREG VSETGVDFVA RLLNRDPFSR PTEKQCFQHP WIADVPDVDE YEEDDILTDV
     RDALSVIGEA EEELDASQLS IHEEAEYTLS AGEEESESSE ALAKKPRIEY IAQDIRYPSL
     PKIESFQDGQ IVAETHARRL FGEVTSSALR SSYCLGHTGS LEEENDYDHE EFLSSGESVS
     DERSVYSIIS LPEHPVGGVA PSLMGAEGLV GRLNMNSSHP AYPAQMTPFV HIGSRQTSPG
     LFPTNVSTDL AIGRDTPRVG APLSSSASEI TPKAPKVSRR IDLELPETAS ERSDSSAPVS
     RAQSANPPEA QAQADYDVNL ATTLDAQTGQ VILDHMRSAD EEPSEPVVHK QPDGPGLALS
     MPATEFAKPP KLLGRLKSLP GSMLDLKIRL EDRMTSWGRG PNATIRHPDN LDVRIPAYAL
     EITFWAPGLE RRIAEGQDWT QVPGVMAVLS TKTSKCIWVN DVPLRKGGPD GLQFGKLYTG
     DIITIYKHRD NGEFLQLKCE FYHGESAQPR PEGETGFVVR QALVSKSDSS NRQPVRSQRL
     KTAV
//
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