ID Q2UCW5_ASPOR Unreviewed; 2055 AA.
AC Q2UCW5;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 111.
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=AO090012000420 {ECO:0000313|EMBL:BAE60600.1};
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516 {ECO:0000313|EMBL:BAE60600.1, ECO:0000313|Proteomes:UP000006564};
RN [1] {ECO:0000313|EMBL:BAE60600.1, ECO:0000313|Proteomes:UP000006564}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40 {ECO:0000313|Proteomes:UP000006564};
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00169}.
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DR EMBL; AP007161; BAE60600.1; -; Genomic_DNA.
DR RefSeq; XP_001727439.1; XM_001727387.2.
DR STRING; 510516.Q2UCW5; -.
DR EnsemblFungi; BAE60600; BAE60600; AO090012000420.
DR GeneID; 5987913; -.
DR KEGG; aor:AO090012000420; -.
DR VEuPathDB; FungiDB:AO090012000420; -.
DR HOGENOM; CLU_000709_0_0_1; -.
DR OMA; HNRRFVG; -.
DR OrthoDB; 1968985at2759; -.
DR Proteomes; UP000006564; Chromosome 4.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00130; PAS; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR CDD; cd05611; STKc_Rim15_like; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR24356; SERINE/THREONINE-PROTEIN KINASE; 1.
DR PANTHER; PTHR24356:SF1; SERINE_THREONINE-PROTEIN KINASE GREATWALL; 1.
DR Pfam; PF00069; Pkinase; 2.
DR Pfam; PF00072; Response_reg; 1.
DR SMART; SM00091; PAS; 1.
DR SMART; SM00448; REC; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000006564};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 47..98
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 745..1180
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1181..1299
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT DOMAIN 1558..1672
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 26..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 135..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 312..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 518..739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 907..951
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 963..987
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1003..1039
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1220..1241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1253..1287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1310..1494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1506..1547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1703..1727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1752..1793
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1807..1925
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1973..2055
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..357
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..583
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 921..948
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1266..1280
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1310..1403
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1418..1432
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1439..1462
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1476..1494
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1532..1546
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1763..1792
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1821..1841
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1888..1925
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1999..2023
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2055 AA; 224230 MW; BD2A18F190654F15 CRC64;
MAGNGTQSPQ FLAPPAVTAL RQEARSIVPS LTPSNRSLSD DNDMQEERAE LKQAAEQTLN
VIVDLDLDGR IKWVSPSWRQ VVGTDPESVE GRMISDLIVD NKNAFQDAVE AMKEDDSRSR
FIRFSLLMGP DSVLKYAPEP RPVEAETTGT DETEGAGGQE EPLAETEEHN HDILSMEAQG
IMAYDRTADG VSHTMWMLRP FTEPREVTID LPPLLVESLG VGAEVLASYL TTLAEAAANE
PDPSKHPAPN PVLCRICERQ ITPWWFEKHS DLCLQEHRAE MDVQIAQENL NEHRHAIVKV
LDALEARQGR PLVLGESNPP LPQPEYKGLP IGPSPVASAP SSGSVSNSSS APATPPRSRD
HSVSGMGHSR GRSFAVRRPL SRVVELILDL CDTALEINMP VLKETRVDNN DEFRTLSPQS
ESRISQVYQW QSPSTNTLEQ EQGLAALCTD TEQVAKAKVD ATVRYRRIVE YAERIRIEYT
VLVEECITAA LSKAERIAAG QLSDSSSSED EQVPDILDSN IVTGPIPSPA QSRESIPLPR
PMSALTMSMR NSPDRHQSPH SSEGKLSSVA VSTGSNSPME CPTPRSHKSV AGVLGTSQPS
RRGLASADFD AGEMSDSSVL SSAFPGAMRT DSPCSDRSLD RKRRSLVPPG LSSSPRRGHS
PARVSGPHSP LRMPKPRLSS GAESLPSPIV SPSTNAGELA HHHFRHHRRQ SSATSSDAPR
PPVSPHLASA SQPQPRPAPV SIKDFEVIKP ISKGAFGSVY LSKKKTTGEH FAIKVLKKAD
MVAKNQVTNV KAERAIMMWQ GESDFVAKLY WTFSSKDYLY LVMEYLNGGD CASLVKILGE
LPEDWAKKYV AEVVLGVEHL HSRGIVHRDL KPDNLLIDQT GHLKLTDFGL SRMGLVGRQK
RVLKSMNNEP APDLLKQGPF PRATSITSSR SASFDFQGSG SPGSTPLMTP DVAGSMPQPS
YFNLNQSGIS RQTSRRASGY RSDSVGSEGL NSVFRSLSLH DPSEVQGSLP VPVPGAHNLT
EAEGQSEAGE SPHLYPLQPT PSNSVPHDIG PQQGMMPPLM ALFDPEDHNR RFVGTPDYLA
PETINGAGQD EMSDWWSLGC IMFEFLFGYP PFNASSPDEV FDNILHRRIN WPDHVEELTS
PEAIDLMNKL MTTDPAQRIG ANVDEKYPNG GAEIRSHPWF SDINFDTLLD DKAQFVPNLE
NPEDTEYFDA RGATLQAFSE ELEDGDSPRP VTTGPYPDRP HDALFKVRSQ VNASKRPLMP
LHIPPHVRES RSRRLSEPSL EDDFGSFSFK NLPMLEKANK DVIQKLRQEA MQAQQRPFAA
SGPQQQPPGK DQGQAQGQGQ NQAQTPAPSS SGPSLEGSPL PMSLQRTMSQ NKGNNRPSSP
SSQANSSPSR PSQPSSPLLV QFSTGHHNHE RRKTSGSSST NSHHSSASGP PASAEQARMA
SLKISSSASS PVKTSRAITH SPDKTPSGPP RHGSVPTRAR SQTIGSQDGD LSSSLARESY
VAGHYKRRSQ RFNDISPSSS DNEDPRTKQL FKNQRQRQSS RRLSQLNYPD GPFFRPLDVL
ICEDHPVSRM VMERLFEKLR CRTITAVNGA EAMRYALSQV QFDIIMTEFK LPQVNGADVA
RMVRETRSAN RHTPIIAVTG YLKDFPETHH FDGLIEKPPT LTKLTQALCK HCQWKPPPND
SILSQPLAVP SATPRQIPIA AEHSPSSVTS SNFAPVPTSS YQGSSRADSI GSSYFGDMES
VKAEDAPVVG GRKYDEWSSG QGGLGISGDT GTTQVESTQA TVDSNNKSSS DPAPLLHLLH
AVSAPASMNA SGTLTPRKQR SSEAIRAKRE SLERKRYEGA ESGDDEDEEL GRSNSRTQSP
RNRSTRPGSK LGIEMMRTNS RGSVVSGSEE LLKKERESLE RRRSGGSESI SEERAESPGI
DGKFEGLHFP EDAIVLSEDN YSPRQSPTLS VSQMSPSFST MSRLEPSFAH GITETGFGVS
PDTSTETLKK GHITPPIVFT TEEGSSSVDP NTPFIQTSSV EDDTETIPDS EATPRPVHTP
SLGLDSEITP RQGGR
//
