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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//