ID A0A135LLE3_PENPA Unreviewed; 1582 AA.
AC A0A135LLE3;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=PGRI_057550 {ECO:0000313|EMBL:KXG49787.1};
OS Penicillium patulum (Penicillium griseofulvum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=5078 {ECO:0000313|EMBL:KXG49787.1, ECO:0000313|Proteomes:UP000070168};
RN [1] {ECO:0000313|EMBL:KXG49787.1, ECO:0000313|Proteomes:UP000070168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PG3 {ECO:0000313|EMBL:KXG49787.1,
RC ECO:0000313|Proteomes:UP000070168};
RX PubMed=26729047; DOI=10.1186/s12864-015-2347-x;
RA Banani H., Marcet-Houben M., Ballester A.R., Abbruscato P.,
RA Gonzalez-Candelas L., Gabaldon T., Spadaro D.;
RT "Genome sequencing and secondary metabolism of the postharvest pathogen
RT Penicillium griseofulvum.";
RL BMC Genomics 17:19-19(2016).
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:KXG49787.1}.
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DR EMBL; LHQR01000048; KXG49787.1; -; Genomic_DNA.
DR STRING; 5078.A0A135LLE3; -.
DR OMA; EFYHRSG; -.
DR OrthoDB; 8734at2759; -.
DR Proteomes; UP000070168; 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:SF91; EUKARYOTIC TRANSLATION INITIATION FACTOR 2-ALPHA KINASE; 1.
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:KXG49787.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR000660-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000070168};
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 212..529
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 569..941
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 681..728
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 158..215
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 788
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 1582 AA; 179194 MW; 97CF547AC11BF1C4 CRC64;
MSPKQRKKPS RQKKQTSESP VTSPIFTTNY REIHQTEVEA LRSIYGDDFE EVENRRSAWQ
QSSDVTFKLH LRSSSNPDIL LILLVELPAT YPKTIPNLSP GNLDGFRDGA RSRIQEILRN
KPKSLLGSEM IYELAVSIQD VLEDVAQAQA QDKDLPSLEE ERMEQEAAAL QRADLEKQEE
IRKQKAAAVE EERALQEMLQ DKMRQRNKAR ILRRKSRTGG ADMSYVDDLV ENTPGAICFD
PPLAVNDTDE QPLVFRAVHG KTLLQSKQCK KTFTVRPVVS ESRCHVPMLV LKELCLGEKD
SEGLAFREQM RTSEDKLEGI KRLRHPNLVE FVGFKINRPI GQLDSPDNSW TVFALLEHAN
KGSLSELLDI VGTVAVDMLR GWMIQLLEAL EFYHRSGFVH GNIHCGRVFL FRTPSGETIV
KLQSSIEEAL PYSPCGKPSF AASKSPLWLP PELTEDSSPP SMKTDVWDLG IVLLQMGFGK
DVLLRYTSAN QLMVSMGLSP PLQDLLCEFF RPDPRKRPTA FQLQPSEFFR VDAPLKTRER
ASGSVSMQRR PRLDSFGAMP AFSRYHQDFD ETGQLGRGGF GQVVKARNKL DGRLYAIKKI
SQTSAAALKD TLSETMLLSR LNHSYVVRYY TAWLEEDFNH IDEEAMSSTE GDPFASHDHH
GFSTGGLDFI SSSGYPKIEF AASDSDDENE GTLSDPAHPR TPDRNGVNDA SVDSGYTEEV
ELSRPRSGSY SRPILTTLYI QMEYCEKHTL RDLIRDDLCD DNERVWRLFR QILDGLSHIH
SHGIIHRDLK PDNIFIDVAN NPRIGDFGLA TSGQFTTAVR SSAAADFEGD FTRSLGTTYY
VAPEMKSVVS GHYNEKVDMF SLGVIFFEMC HPLPTGMERD QTLRAIREKN HTLPPTFQQS
DKLLQGEIIE SLLSHNPNER PTASELLSSG KIPLQVEEET FRRAIVHLLS DPNSPDYKKI
LSAIFSQSPK KFEDIAWDID SHAVPAANEL LVQGLVKKKL TSIFRRHGAV ESTRQMLFPR
SQHYNSGAVR VLDASGNLLQ LPYDLTLPNA RAIPRQDHSL EKTFAFGTVY RESTHGGEPR
THREVDFDIV SYNTLDLALK EAEVIKVLDE IIEEFPPLRS TPMCFLVNHS DLLQLIMEFC
RITPIQIPKA KEVLSKLNVG KYSMQKIRSE LRAPGIGVAS TSLDDLARFD FRDSLKETQR
RLQNIMEGTE YAERIAPIFA RLNVLMTYLQ SFGVKRKIYI NPLSSVQDKF YRGSILFQCI
FDSKRRDVFA AGGRYDRLIQ EFSPNVLSNR PQAHAVGFNL GSDRLRSSMI DYLKAKAPSK
DPETGAELYW GARRCDVLVA SFDPTVLRTT GVKLIEELWS NNISAELAVD ASSLEELLAK
YKDSNHRWIV IAKQDSKERG FKVRNLMRKE EFDIRAAELV LWLRSEVQAR NPREGTADPR
QSRQLSQQEA FAFQERANDV RILVPQHRSK KTNRRNIVES ALLSSREVAE NARNGPVAAI
DTRDEVLDAI RNTRLSDAES WRSVIQNAPL TERKYLSQVH ELLTDLAMES RTNDATESYT
NAFIYNYRTG SCVYYDLGPS EK
//
