(data stored in SCRATCH zone)

SWISSPROT: B6H1E8_PENRW

ID   B6H1E8_PENRW            Unreviewed;       894 AA.
AC   B6H1E8;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   08-MAY-2019, entry version 73.
DE   RecName: Full=Non-specific serine/threonine protein kinase {ECO:0000256|SAAS:SAAS01060667};
DE            EC=2.7.11.1 {ECO:0000256|SAAS:SAAS01060667};
GN   ORFNames=Pc13g02620 {ECO:0000313|EMBL:CAP91331.1}, PCH_Pc13g02620
GN   {ECO:0000313|EMBL:CAP91331.1};
OS   Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 /
OS   Wisconsin 54-1255) (Penicillium chrysogenum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum species complex.
OX   NCBI_TaxID=500485 {ECO:0000313|EMBL:CAP91331.1, ECO:0000313|Proteomes:UP000000724};
RN   [1] {ECO:0000313|EMBL:CAP91331.1, ECO:0000313|Proteomes:UP000000724}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255
RC   {ECO:0000313|Proteomes:UP000000724};
RX   PubMed=18820685; DOI=10.1038/nbt.1498;
RA   van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA   Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA   Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA   Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A.,
RA   van der Klei I.J., van Peij N.N.M.E., Veenhuis M., von Doehren H.,
RA   Wagner C., Wortman J.R., Bovenberg R.A.L.;
RT   "Genome sequencing and analysis of the filamentous fungus Penicillium
RT   chrysogenum.";
RL   Nat. Biotechnol. 26:1161-1168(2008).
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,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1; Evidence={ECO:0000256|SAAS:SAAS01127769};
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|SAAS:SAAS01127730};
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; AM920428; CAP91331.1; -; Genomic_DNA.
DR   RefSeq; XP_002558702.1; XM_002558656.1.
DR   STRING; 1108849.XP_002558702.1; -.
DR   EnsemblFungi; CAP91331; CAP91331; PCH_Pc13g02620.
DR   GeneID; 8314717; -.
DR   KEGG; pcs:Pc13g02620; -.
DR   eggNOG; KOG0598; Eukaryota.
DR   eggNOG; ENOG410XNPH; LUCA.
DR   HOGENOM; HOG000233033; -.
DR   KO; K19800; -.
DR   OMA; SRLEGWF; -.
DR   OrthoDB; 614710at2759; -.
DR   BioCyc; PCHR:PC13G02620-MONOMER; -.
DR   Proteomes; UP000000724; Contig Pc00c13.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR000008; C2_dom.
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   Pfam; PF00168; C2; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00433; Pkinase_C; 1.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 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   4: Predicted;
DR   PRODOM; B6H1E8.
DR   SWISS-2DPAGE; B6H1E8.
KW   ATP-binding {ECO:0000256|SAAS:SAAS00593399};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000724};
KW   Kinase {ECO:0000256|SAAS:SAAS00593820};
KW   Nucleotide-binding {ECO:0000256|SAAS:SAAS00593601};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000724};
KW   Serine/threonine-protein kinase {ECO:0000256|SAAS:SAAS00593706};
KW   Transferase {ECO:0000256|SAAS:SAAS00592725}.
FT   DOMAIN      494    755       Protein kinase. {ECO:0000259|PROSITE:
FT                                PS50011}.
FT   DOMAIN      756    840       AGC-kinase C-terminal.
FT                                {ECO:0000259|PROSITE:PS51285}.
SQ   SEQUENCE   894 AA;  99686 MW;  6916500E002A0E07 CRC64;
     MAAQSGPVLH GDDMKTMNSG LEDDSQDQIR SNDSTPTPTG IATPEPDPVD KRLPSIMHNY
     FQVGSFSGDK ASLPRLWSCL SKPSEDSQSN AHTQHSSDSS ESFVMMEQED GPDKMEEHPS
     LHTPPHSLLQ HESDEMELGT SPGVSSIFTT LKSYLISPTQ TPPEDHPSRR QTSLPVSSIS
     DDPVLATHFS NPSLPPTSDA FSLIEAPLLD HEKPHVPISS ENLAKLTESV PDGLRLKNTP
     PLTPRAMSNE VPAAQEKNAT SAPQESAQET PPSESKPEDM ESSTDEITMK LDEAFPSQSQ
     SEDAPASPTS TSPANGAPTG PINGKLFVKI TDGRGLRPSF DPYVVCVFEW NEYISKGARD
     GEEEKKRRQQ ESDAEEAAGR PMAIPLKTRS SSHNSAVEGD HKGRTPVTDP HWDHEATLYV
     TPTQLFTWVY DRNNQEAFLG HVRLRVNLKE DHSRLEGWFP LVARGAGDNQ VSGEIHLDMK
     FEKTDRKQVG PNDFLVLKLI GKGTFGQVYQ VKKKDTQRIY AMKVLSKKVI IQKKEVVHTL
     GERNILVRTA MTASPFIVGL KFSFQTPTDL YLVTDYMSGG ELFWHLQREG RFQEARAKFY
     IAELILALQH LHEHDIVYRD LKPENILLDA NGHIALCDFG LSKANLSQND TTNTFCGTTE
     YLAPEVLLDE QGYTKMVDFW SLGVLVFEMC CGWSPFYAED TQQMYKNIAF GKVRFPRDAL
     STEGRNFVKG LLNRNPKHRL GANGDAKELM AHPFFHDINW DTLCRKEVIP PFKPQLQSET
     DTSNFDPEFT NAMELNNSLN LRAANVANGL MPASTPLSPG MQANFKGFTF VNESSIDHHL
     MDDSDHMEDD AMHDDHWQRG HRSGNSVDQR MTGVQKTHDG TEPGIFNVDD TFDM
//

If you have problems or comments...

PBIL Back to PBIL home page