ID A0A1V6S9C9_9EURO Unreviewed; 1143 AA.
AC A0A1V6S9C9;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU361162};
DE EC=2.7.11.21 {ECO:0000256|RuleBase:RU361162};
GN ORFNames=PENFLA_c085G03560 {ECO:0000313|EMBL:OQE10627.1};
OS Penicillium flavigenum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=254877 {ECO:0000313|EMBL:OQE10627.1, ECO:0000313|Proteomes:UP000191342};
RN [1] {ECO:0000313|Proteomes:UP000191342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 14082 {ECO:0000313|Proteomes:UP000191342};
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-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=2.7.11.21; Evidence={ECO:0000256|RuleBase:RU361162};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. CDC5/Polo subfamily. {ECO:0000256|RuleBase:RU361162}.
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:OQE10627.1}.
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DR EMBL; MLQL01000085; OQE10627.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6S9C9; -.
DR STRING; 254877.A0A1V6S9C9; -.
DR OrthoDB; 5471704at2759; -.
DR Proteomes; UP000191342; 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; cd13118; POLO_box_1; 1.
DR CDD; cd13117; POLO_box_2; 1.
DR CDD; cd14099; STKc_PLK; 1.
DR Gene3D; 3.30.1120.30; POLO box domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR033701; POLO_box_1.
DR InterPro; IPR033695; POLO_box_2.
DR InterPro; IPR000959; POLO_box_dom.
DR InterPro; IPR036947; POLO_box_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24345; SERINE/THREONINE-PROTEIN KINASE PLK; 1.
DR PANTHER; PTHR24345:SF0; SERINE_THREONINE-PROTEIN KINASE PLK1; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF82615; Polo-box domain; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50078; POLO_BOX; 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 Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU361162};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000191342};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000256|RuleBase:RU361162};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361162}.
FT DOMAIN 61..322
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 944..963
FT /note="POLO box"
FT /evidence="ECO:0000259|PROSITE:PS50078"
FT REGION 24..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 461..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 499..707
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..477
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 589..624
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 668..705
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 90
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1143 AA; 127423 MW; 5353BEBCF9113C6D CRC64;
MEALSPRTTN QMIKPKLAMD RKAFDKNAAL PSNKQKSATS KSYADPPPSI VSEPEDGGER
YSIGAFLGKG GFAVCYEGSL ARNGRVYAMK VVKSAMPQKK MEEKFRTELQ IHSKMRHPFI
VQFYRAFAFE SSTYVVLELC PNGSVMDMFR KRRCFSLPEV RRYMIQLCAA VKYLHKRFVA
HRDLKMGNLF LDHNMNIKVG DFGLAAMILS DKDAKRRNTL CGTPNYIAPE VLDKSKGGHT
QKVDIWSVGV ICFAMLAGYL PFQSKTQDEV YKRVQNLNYV WPKESESGNY IPEEAKDLVG
RCLNLVDEER PDPDDIVEHP FFNMYDGCIP RQLDPSCRFN KPLWLKDASP QGDCVVSGYG
LDSDEKLRAY VYQVDDPAQR YHSCKAAFYS LCGVGRKPDG TARKSVGRNC SKSAFSECDV
EDSRGLRPVI PLSPDYVYRW PHDLEGDWCL ESSRKVIRSE ESMLNSSTMS QRSAPIRPNP
MAASRTNAAL AAAQQRRMEG QSHAATLRQQ ARVPPISPRR APGISDPAVL PSRPYRDVPQ
AEPKPSAAEV PTGGLADRPI RTRRMVSASQ ATTLRSKDKD IAPQLAKSIS MPSGLTVGKT
RSQSRRLAAA DQELMQPSFQ TRERQPSARP EERKVVTRQT SLRSTSRADL YACVGQGERR
RDSPTEESAR SSLAQSKSSA ESNGLGRSDS NGVARSNSKT AGGRARSSLG LSPLFHAEDT
CKLLPGTSLT EVNTDLRLML TNLVNHAPSR RRGGARKQPH AYVIKWVDYT NRYGIGYVLD
DGSVGCVFKG ENGQPATSVV VRDGERHIRR KARSVADGKQ QPIYYSEADQ LVPRTGNPVE
FYENRDDDLL GCRGIRRALI PPSLFDVKTS KAMRIRSNTG TEIERADAEK IKRMKLVDQF
GKYMIGALGR HGDEGIMDED LPEHNSAQFV KFYQRLGNVG IWGFGDGAFQ FNFPDHTKLV
ISPGRTRSSS PWIDFYHLSS SAARFFAAKG KMHPAGFDTR AVASDEAATF LSIANGDSIN
STEDRIRDIL DANAFIQKIA FIKDTLRVWI KFGRLGGRPP SVDSSADESM PDEAFWQGTQ
ERSQPNSPGT KFVWVTVGAP DGDGQYRSMM LKDSDREPKR APAAMEYDKE MDLLKDRLRA
LGR
//
