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Database: UniProt
Entry: A0A1V6QZ77_9EURO
LinkDB: A0A1V6QZ77_9EURO
Original site: A0A1V6QZ77_9EURO 
ID   A0A1V6QZ77_9EURO        Unreviewed;       649 AA.
AC   A0A1V6QZ77;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 28.
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=PENSOL_c025G07823 {ECO:0000313|EMBL:OQD94488.1};
OS   Penicillium solitum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=60172 {ECO:0000313|EMBL:OQD94488.1, ECO:0000313|Proteomes:UP000191612};
RN   [1] {ECO:0000313|Proteomes:UP000191612}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 29525 {ECO:0000313|Proteomes:UP000191612};
RX   PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA   Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA   Frisvad J.C., Workman M., Nielsen J.;
RT   "Global analysis of biosynthetic gene clusters reveals vast potential of
RT   secondary metabolite production in Penicillium species.";
RL   Nat. Microbiol. 2:17044-17044(2017).
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   -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC       protein kinase family. COT1 subfamily. {ECO:0000256|ARBA:ARBA00038271}.
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:OQD94488.1}.
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DR   EMBL; MDYO01000025; OQD94488.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V6QZ77; -.
DR   STRING; 60172.A0A1V6QZ77; -.
DR   OrthoDB; 10768at2759; -.
DR   Proteomes; UP000191612; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd21776; MobB_Sid2p-like; 1.
DR   CDD; cd05600; STKc_Sid2p_like; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR017892; Pkinase_C.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24356:SF417; CELL CYCLE PROTEIN KINASE DBF2-RELATED; 1.
DR   PANTHER; PTHR24356; SERINE/THREONINE-PROTEIN KINASE; 1.
DR   Pfam; PF00069; Pkinase; 2.
DR   Pfam; PF00433; Pkinase_C; 1.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 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}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000191612};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          246..549
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          550..629
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51285"
FT   REGION          1..153
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          625..649
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        31..49
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        68..85
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        97..138
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         275
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   649 AA;  74228 MW;  966BC5D8365A819E CRC64;
     MAIISEDHLG LRLPNPPPLL HTRGQFDRPS TPADGFTSPP QTPQGSPSKS RLPPGALDLP
     NVFDKAMKLT PTSPSKSTYN HYNHPMFSAG KSGEDFNESV IHQTPSSPTR RANKENTPPN
     PTRLTKDLGS TPTAAALSRQ EPYQPRDETT RRQVQMRGLT PEEMEKLAQP KVKRLVNVTQ
     LYFLDHYFDL LSYVHNRQTR HTQFKAAYPD PPATPNEEHE PALLKYLGRE RAHLRKRRTR
     LRQGDFQILT QVGQGGYGQV YLAQKKDTRE VCALKVMSKK LLFKLDEIRH ILTERDILTA
     AKSEWLVKLL YAFQDDTQIY LAMEYVPGGD FRTLLNNTGV LHNRHARFYI AEMFSCIDAL
     HVLGYIHRDL KPENFLIDST GHVKLTDFGL AAGMLSPGKI ESMRVKLEEV GNTPVPFGRP
     MEQRTMAERR QGYQSLRQRE VNYAKSIVGS PDYMAPEVLK GDQYDFTVDY WSLGCMLFEA
     LAGYPPFAGA TVEETWQNLK RWQKVLRKPV YEDPNYFLSR RTWDLITKLV AGKEQRFKNI
     KEIHSHDYFA EVDFESLRDQ RAPFVPELDS ETDAGYFDDF SNEADMAKYK EVHDKQRALE
     DMADRDDKMG KGLFVGFTFR HRKPAVDSNG RSSSPRKPIA TDGTFGTMF
//
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