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Database: UniProt
Entry: B6HRL8_PENRW
LinkDB: B6HRL8_PENRW
Original site: B6HRL8_PENRW 
ID   B6HRL8_PENRW            Unreviewed;       642 AA.
AC   B6HRL8;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   24-JAN-2024, entry version 89.
DE   SubName: Full=Pc22g20830 protein {ECO:0000313|EMBL:CAP99371.1};
GN   ORFNames=Pc22g20830 {ECO:0000313|EMBL:CAP99371.1}, PCH_Pc22g20830
GN   {ECO:0000313|EMBL:CAP99371.1};
OS   Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS   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:CAP99371.1, ECO:0000313|Proteomes:UP000000724};
RN   [1] {ECO:0000313|EMBL:CAP99371.1, 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., van der Klei I.J.,
RA   van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA   Bovenberg R.A.L.;
RT   "Genome sequencing and analysis of the filamentous fungus Penicillium
RT   chrysogenum.";
RL   Nat. Biotechnol. 26:1161-1168(2008).
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DR   EMBL; AM920437; CAP99371.1; -; Genomic_DNA.
DR   RefSeq; XP_002565982.1; XM_002565936.1.
DR   AlphaFoldDB; B6HRL8; -.
DR   STRING; 500485.B6HRL8; -.
DR   GeneID; 8305225; -.
DR   KEGG; pcs:Pc22g20830; -.
DR   VEuPathDB; FungiDB:PCH_Pc22g20830; -.
DR   eggNOG; KOG0598; Eukaryota.
DR   HOGENOM; CLU_000288_120_0_1; -.
DR   OMA; HGRYSAK; -.
DR   OrthoDB; 10768at2759; -.
DR   BioCyc; PCHR:PC22G20830-MONOMER; -.
DR   Proteomes; UP000000724; Contig Pc00c22.
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; cd11651; YPK1_N_like; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR000961; AGC-kinase_C.
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   PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR   PANTHER; PTHR24351:SF234; SERINE/THREONINE-PROTEIN KINASE YPK2/YKR2; 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; Protein kinase-like (PK-like); 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;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000724};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          299..556
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          557..628
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51285"
FT   REGION          18..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          107..145
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          236..259
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        19..55
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        107..144
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        236..255
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         332
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   642 AA;  71323 MW;  E1166E64F3725B88 CRC64;
     MSSWKLTKKL KETHLAPLTA SFGRSSSTST IKGDSNGEEA PTPVSSNPPS ATPSVNGIAA
     SESLVSPPVA PVNPGILIVT LHEGRNFSLS PHFQQIFNSH FQNNSYAPSS LRPSTSSSSH
     STQNQAGSFV PSGRPQSTSG GINAAPTIHG RYSTKYLPYA LLDFEKNQVF VDAVSGTPEC
     PLWAGDNTAF KFDVSRKTEL NVQLYLRNPA ARPGAGRSED IFLGACKVNP RFEESQPYVE
     DPKLSKKDNQ KAAAAHDEQG RQLGQQGAEW LDLQFGVGSV KIGISFVENK QRSLKLEDFD
     LLKVVGKGSF GKVMQVMKKD TGRIYALKTI RKAHIISRSE VTHTLAERSV LAQINNPFIV
     PLKFSFQSPE KLYFVLAFVN GGELFHHLQR EQRFDINRAR FYTAELLCAL ECLHGFKVIY
     RDLKPENILL DYTGHIALCD FGLCKLDMKD EDRTNTFCGT PEYLAPELLL GNGYTKTVDW
     WTLGVLLYEM LTGLPPFYDE NTNEMYRKIL QEPLTFPSSD IVPPAARDLL SRLLDRDPVR
     RLGANGAAEI KSHHFFANID WRKLLQRKYE PSFRPNVVDA RDTENFDVEF TREAPQDSYV
     DGPVLSQTMQ QQFAGWSYNR PVAGLGDAGG SVKDPSFGSI PE
//
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