ID A0A2N3N350_9PEZI Unreviewed; 1251 AA.
AC A0A2N3N350;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 08-NOV-2023, entry version 25.
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=jhhlp_006942 {ECO:0000313|EMBL:PKS06866.1};
OS Lomentospora prolificans.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Microascales; Microascaceae; Lomentospora.
OX NCBI_TaxID=41688 {ECO:0000313|EMBL:PKS06866.1, ECO:0000313|Proteomes:UP000233524};
RN [1] {ECO:0000313|EMBL:PKS06866.1, ECO:0000313|Proteomes:UP000233524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JHH-5317 {ECO:0000313|EMBL:PKS06866.1,
RC ECO:0000313|Proteomes:UP000233524};
RX PubMed=28963165; DOI=10.1534/g3.117.300107;
RA Luo R., Zimin A., Workman R., Fan Y., Pertea G., Grossman N., Wear M.P.,
RA Jia B., Miller H., Casadevall A., Timp W., Zhang S.X., Salzberg S.L.;
RT "First Draft Genome Sequence of the Pathogenic Fungus Lomentospora
RT prolificans (Formerly Scedosporium prolificans).";
RL G3 (Bethesda) 7:3831-3836(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. AGC Ser/Thr
CC protein kinase family. PDPK1 subfamily.
CC {ECO:0000256|ARBA:ARBA00010006}.
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:PKS06866.1}.
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DR EMBL; NLAX01001033; PKS06866.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N3N350; -.
DR STRING; 41688.A0A2N3N350; -.
DR VEuPathDB; FungiDB:jhhlp_006942; -.
DR InParanoid; A0A2N3N350; -.
DR OrthoDB; 208777at2759; -.
DR Proteomes; UP000233524; 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-EC.
DR CDD; cd05581; STKc_PDK1; 1.
DR CDD; cd10568; SWIB_like; 1.
DR Gene3D; 1.10.245.10; SWIB/MDM2 domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR039046; PDPK1.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR019835; SWIB_domain.
DR InterPro; IPR036885; SWIB_MDM2_dom_sf.
DR InterPro; IPR003121; SWIB_MDM2_domain.
DR PANTHER; PTHR24356:SF163; 3-PHOSPHOINOSITIDE-DEPENDENT PROTEIN KINASE 1-RELATED; 1.
DR PANTHER; PTHR24356; SERINE/THREONINE-PROTEIN KINASE; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF02201; SWIB; 1.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00151; SWIB; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF47592; SWIB/MDM2 domain; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS51925; SWIB_MDM2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000233524}.
FT DOMAIN 261..537
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1018..1096
FT /note="DM2"
FT /evidence="ECO:0000259|PROSITE:PS51925"
FT REGION 1..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 149..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 408..441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 584..612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 804..829
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1200..1251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..60
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..228
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..601
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 812..829
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1200..1218
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1223..1251
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 290
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1251 AA; 138777 MW; 89072DDAD29A43E8 CRC64;
MSGDLSLSRA LGGLRIANPD DAPPASSLDQ SPPGQPREPA RLPDSNHRFS IGDESATVHE
SRRTVISTPY EQEDRSTPPP FTLSSRQFRN DGERSSESRA HYAETLSHIA NDASPDIQPT
EGPPHTSHTL SHPSHYVSVV RDAQTPTRTD ITAPGYYHQP SATATANHSG QSDGSYGASY
HASAPASSGP LPPRRSSRGM GGGYLSSSQA GNPPQSLNPE THVPMSSQEW QERGAAVGVR
REIDANGQTV LRHVKKGVRD FTFGRILGEG SYSTVYLATD RQTLKEYAIK VLEKKHIIKE
KKIKYVNIEK NTLNRLTEHP GIVRLYYTFQ DETCLYYALD FCSGGELLGA LKRTGTFDVE
CARFYGAQIL DAIEYMHSRG VLHRDLKPEN VLLDDHMHIK ITDFGTAKML PDPRAPKSQG
GGDRGVPEGT QTGKEDDSRA PSFVGTAEYV SPELLTNKNS CKASDLWAFG CIIYQLLAGR
PPFKAGSEYL TFQKIVGLDY EYPPGFPPAA RDLVERLLVL DPARRLTIEH IKNHEFFDGQ
QFGKSLWRSK APRLRPFVPP SQEPHIIQLN GYSSTTKPIA GVRPLPQSHQ GTPTTNSGAT
RPPLPIAELP PPTQLDFEWS SVLTRTNERI LKLGDLMVIS APLPNSPQGK NGEHGDGHKK
LSRFFGGSTT KKRQRLVMIT SSGRIILAPA GGEEKRAKQD ISLLAPDCVW RSQIDAKGQP
VWCVDTAGTH YTFEEPRSAS TSGNPANTGA VDEWIDSLQR ARELAVSQSV VGSSGSDNGF
GPMMSAGPHP SVPLTQAQIA QQQQAQAQAN ELAKRRSRKP TDKAMPEGVE DTTIDPELVA
LYSNLRAYER RLDATLARKR LDIIDNASRY LKHRRTLRIW ISNSVEDQPW QSNDLNVDSF
DFSDNLEPTY RVRIEGRLLD DEFDLALRQS GGSEDGDAST SGLAVSTGSA YKLSHFFKSI
NVDFHAPGRR PDQGVEWKKS ERSPASANIQ QHTDFDEFTF KRNGDDNMNV SINLVRHEEP
ERFLLTPELA SVVDMEEATR QEAMMGIWEY IRYNGLQEDE EKRNFRCDDM LKRVINRGDV
GHIPLLGDYI APHLRPLPPI SLPYTIRVDE DFHKNPKPTI YDIQVTVENP LRAKMIGFIT
DPGYAGMLKE VAGLDDQLAR LVQAVSMSKS KHAFFSSLSE DPVTFFRNWL SSQKRDLEVI
DGEAPRGGGE HASGDEWRRG GENSVWTTEN AKETVNVILS RPRQQAQPRQ A
//
