ID K9G188_PEND2 Unreviewed; 1578 AA.
AC K9G188;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=PDIG_30950 {ECO:0000313|EMBL:EKV14642.1};
OS Penicillium digitatum (strain PHI26 / CECT 20796) (Green mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1170229 {ECO:0000313|EMBL:EKV14642.1, ECO:0000313|Proteomes:UP000009882};
RN [1] {ECO:0000313|Proteomes:UP000009882}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHI26 / CECT 20796 {ECO:0000313|Proteomes:UP000009882};
RX PubMed=23171342; DOI=10.1186/1471-2164-13-646;
RA Marcet-Houben M., Ballester A.-R., de la Fuente B., Harries E.,
RA Marcos J.F., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome sequence of the necrotrophic fungus Penicillium digitatum, the main
RT postharvest pathogen of citrus.";
RL BMC Genomics 13:646-646(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001433};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
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:EKV14642.1}.
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DR EMBL; AKCT01000131; EKV14642.1; -; Genomic_DNA.
DR STRING; 1170229.K9G188; -.
DR eggNOG; KOG1035; Eukaryota.
DR HOGENOM; CLU_001222_2_0_1; -.
DR InParanoid; K9G188; -.
DR OMA; EFYHRSG; -.
DR OrthoDB; 8734at2759; -.
DR Proteomes; UP000009882; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004694; F:eukaryotic translation initiation factor 2alpha kinase activity; IEA:InterPro.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; IEA:InterPro.
DR CDD; cd14012; PK_eIF2AK_GCN2_rpt1; 1.
DR CDD; cd14046; STKc_EIF2AK4_GCN2_rpt2; 1.
DR Gene3D; 3.40.50.800; Anticodon-binding domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR036621; Anticodon-bd_dom_sf.
DR InterPro; IPR016255; Gcn2.
DR InterPro; IPR041715; HisRS-like_core.
DR InterPro; IPR024435; HisRS-related_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR006575; RWD_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR PANTHER; PTHR11042; EUKARYOTIC TRANSLATION INITIATION FACTOR 2-ALPHA KINASE EIF2-ALPHA KINASE -RELATED; 1.
DR Pfam; PF12745; HGTP_anticodon2; 1.
DR Pfam; PF00069; Pkinase; 3.
DR Pfam; PF05773; RWD; 1.
DR Pfam; PF13393; tRNA-synt_His; 1.
DR PIRSF; PIRSF000660; Ser/Thr_PK_GCN2; 1.
DR SMART; SM00591; RWD; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 2.
DR SUPFAM; SSF54495; UBC-like; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50908; RWD; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR000660-
KW 2}; Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EKV14642.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR000660-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000009882};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 36..145
FT /note="RWD"
FT /evidence="ECO:0000259|PROSITE:PS50908"
FT DOMAIN 248..529
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 569..940
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 681..725
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 158..215
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 690..724
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 787
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000660-1"
FT BINDING 575..583
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000660-2"
FT BINDING 598
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000660-2"
FT BINDING 599
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1578 AA; 179090 MW; 85220AA913C9F815 CRC64;
MSPKQRKKPS RQKNQPSDSS VTFPIFTTNY REIHQTEVEA LCSIYGDDFE EVENRRSAWQ
QSSDVAFKLH LRSSSNPDIL LILLVELPAT YPKTVPNLSP GNLDGFRDGA RSRIQEILHN
KPKSLLGSEM IYELAVSIQD VLEDVAQAQA QDKDLPSLEE ERMEQEAAAL HRADLEKQEE
LRKQKAAAAE EERALQEMLQ DKMRQRNKAR ILRRKSRTGG ADVSYIDDLV ENTPGAICFD
PPLAVNDTDE QPLVFRAVHG KTLLQSKQCK KTFTVRPVVS EDRCYVPLLV LKEFCLDENN
SEGLKFREQM RTSEDKLECI KRLRHPNLVD FVGFKINRPI SHLDSLDNSW TVFALLEYAN
KGSLSELLDI VGTVAVDMLR GWMIQLLEAL EFYHRSGFVH GNIHCGRVFL FRTPSGETIV
KLQSNVEEAL PDPLCGRPSF VASKSPLWVP PELTQDSSAP SMKTDVWDLG IVLLQMGFGK
DVLLRYTSAN QLMVSMGLSP PLQDLLCEFF RPDPRKRPTA FQLQPSEFFR VDAPLKMRER
ASGSLSLQRR PRLDSFGAMP AFSRYHQDFD EAGQLGRGGF GQVVKARNKL DGRLYAIKKI
SQSSAAALKD TLSETMLLSR LNHSYVVRYY TAWLEEDFNH IEEETMSSTE GDPFASHDHG
FSTGGLDFIS SSGYPKIEFA ASDSDDENEG TLSDPAHPET PERNRVHDAG VDSGSEEDVE
LSRPRSSSYA RPILTTLYIQ MEYCEKHTLR DLIKDDLCDD NERSWRLFRQ ILDGLSHIHS
HGIIHRDLKP DNIFIDVANN PRIGDFGLAT SGQFTTAVRS SAAADFEGNF TRSLGTTYYV
APEMKSVVSG HYNEKVDMFS LGVIFFEMCH PLPTGMERDQ TLRQIREKNH TLPPTFQQSD
KLLQGQIIES LLSHTPSERP TASDLLSSGK IPLQVEEETF RRAIVHLLSD PNSPDYKNIL
SAIFSQSPKK FEDIAWDIDS HAVPAANELL VQGLVKKKLT SIFRRHGAVE STRQMLFPRS
QHYNVGAVRV LDASGNLLQL PYDLTLPNAR AIPRQDHSLE KTFAFGTVYR DSPHGSEPRT
HREVDFDIVS YNTLDLALKE AEVIKVLDEI IEEFPPLRST PMCFLVNHSD LLQLIMEFCR
VTPTQIPKAK EVLSKLNVGK YTMQKIRSEL RAPAIGVAST SLDDLARFDF RDSLKETQRR
LQSIMEGTEY AERISPIFAR LNVLMTYLQT FDVKRKIYIN PLSSVHDKFY RGSVLFQCIF
DSKRRDVFAA GGRYDRLIQE FSPNVLSNRP QAHAVGFNLG SDRLRSSMID YLKAKAPSKD
SETNTESYWA ARRCDVLVAS FDPTVLRTTG VKLIEELWSN KISAELAVDA SSLEELLAKY
KDSNHRCIVI AKQDSKERGF KVRNLMRKEE FDIRTPELVL WLRSEVQARN HREGTADPRQ
SRQLSQQEAL AFQERANDVR ILVPQHRSKK TNRRNIVESA LLSAREVAEN ARNGPIAAID
TRDEVLDAIR DTRLSDAESW RSVIQNVPLT ERKYLSQVFE LLTDLAVENR TNDNTESYTN
AFIYNYRTGS CVYYDLGT
//
