ID A0A093ZBA0_9PEZI Unreviewed; 1139 AA.
AC A0A093ZBA0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU361162};
DE EC=2.7.11.21 {ECO:0000256|RuleBase:RU361162};
GN ORFNames=V491_05964 {ECO:0000313|EMBL:KFY14636.1};
OS Pseudogymnoascus sp. VKM F-3775.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420901 {ECO:0000313|EMBL:KFY14636.1, ECO:0000313|Proteomes:UP000029338};
RN [1] {ECO:0000313|EMBL:KFY14636.1, ECO:0000313|Proteomes:UP000029338}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-3775 {ECO:0000313|EMBL:KFY14636.1,
RC ECO:0000313|Proteomes:UP000029338};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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:KFY14636.1}.
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DR EMBL; JPJT01003717; KFY14636.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093ZBA0; -.
DR HOGENOM; CLU_000288_46_0_1; -.
DR Proteomes; UP000029338; 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; 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; 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 Pfam; PF00659; POLO_box; 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}; Kinase {ECO:0000256|RuleBase:RU361162};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000029338};
KW Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU361162};
KW Transferase {ECO:0000256|RuleBase:RU361162}.
FT DOMAIN 219..481
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 963..983
FT /note="POLO box"
FT /evidence="ECO:0000259|PROSITE:PS50078"
FT REGION 175..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 618..691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..210
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 618..636
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 655..682
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 248
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1139 AA; 128430 MW; E28E225019FA8EDA CRC64;
MEGESCLPPV GWLLYDDMRL PQRIIEHNNK KKREVEQLYD SSSYSDSELD LEPPRDPWYQ
EIGPVHDICY QEDDEEAHHI AGSILCQALS IPRDCIYCAH DSNEKQLFDT LAYLDFEFHD
REEENQLEED ETYEATTKEA FAIVKPYIAW ECLYPEGIDM AALSPLDINA NLRPRQAAHK
ERSKAPPTKV SPREKDHPPP PPDEVREPPS SDRPNGATYK TGKLLGKGGF AICHDGVLAG
TREKYALKIV KSVMPQKKME QKFQTELQIH SKMRHANIVQ FHRAFTYQES TYIVLELCPN
GSLMDMVKKR RFVTEPEVRF YTIQIAGAIK YMHSKGIIHR DLKMGNIFLD KDMNVKVGDF
GLAALLMSGK DMTACRRTTL CGTPNYIAPE ILEKGKGGHD HAVDIWSLGI IIFAMLTGRP
PFQSTTQEEI YRKAREREYD WPSLDKSNNY VSQEAKDLVA LLLQSPEERP DCDTIVQHPF
FSCGWVPQEE EMTPSLRENS PDPNQFATLS LRGGRASLYA RNLKALCVKS DVGPWSTTQK
VHSSTYREVA AEEKAGLTPA VPLADNVVYR PFDEVVREHK ATLAREESIV ATKPKEYDQK
PLTHRPVTVA TASKTVPRSF AAQQRAQNQP PSISATARRP RAQAESGPST RRANPHDQGS
EEEEILTETR TRSRREPSRS QSKGKAVSES VVATEARLGA DMVQQLGKSR SETSMPSIKA
PPRDPAFASI FSPSENAEFL HRSKPRHVTK NLQVLYAEIE RALNSRSVGP AREAPDSDPT
IVVKWVDYTN KFGLGYILND GGVGCIFKSL PVSGNSNTQI PPTCVIVRNA EKHLQNRRNP
NYPDRNQLVP VSGADIEFFE NNGDEGIYCV KVNPREFAAS EEYGVAGKLG RGKDEWEDRK
REKIVLWRKF ANYMTVFGRD QDHPYDDALN RMLLDGDSDS SGPNKSNVVT FYQRFGDVGC
WGFCNGSFQF NFPDHTKILL SADGTWCDFY HLPLEAARDL ALTGNLPSAA LDDRQHLSFP
LQAFLNFMTK PSARNGMTSR RRAIQVDPMI QGIPAANDFR RKVEFIKAIV GEWITNGGIG
RSAMEPESRL RWLGNRELVN VKVPFKHVWV TVGAYGGDDR RVAWFDPREP SQVVPDIEA
//
