ID A0A1V6SKD4_9EURO Unreviewed; 883 AA.
AC A0A1V6SKD4;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN ORFNames=PENFLA_c040G06519 {ECO:0000313|EMBL:OQE14199.1};
OS Penicillium flavigenum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=254877 {ECO:0000313|EMBL:OQE14199.1, ECO:0000313|Proteomes:UP000191342};
RN [1] {ECO:0000313|Proteomes:UP000191342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 14082 {ECO:0000313|Proteomes:UP000191342};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
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:OQE14199.1}.
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; MLQL01000040; OQE14199.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6SKD4; -.
DR STRING; 254877.A0A1V6SKD4; -.
DR OrthoDB; 1366859at2759; -.
DR Proteomes; UP000191342; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd16018; Enpp; 1.
DR CDD; cd00180; PKc; 1.
DR Gene3D; 3.30.1360.180; -; 1.
DR Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR002591; Phosphodiest/P_Trfase.
DR InterPro; IPR000719; Prot_kinase_dom.
DR PANTHER; PTHR10151:SF120; BIS(5'-ADENOSYL)-TRIPHOSPHATASE; 1.
DR PANTHER; PTHR10151; ECTONUCLEOTIDE PYROPHOSPHATASE/PHOSPHODIESTERASE; 1.
DR Pfam; PF01663; Phosphodiest; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 4: Predicted;
KW GPI-anchor biosynthesis {ECO:0000256|ARBA:ARBA00022502};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000191342};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 154..173
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 730..883
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 86..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 596..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..662
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 883 AA; 99440 MW; F365653D8B014C3F CRC64;
MRHPDTSPSL LSPGNYDNDA SSLRSPSEQD SDSDDDALLG QNRSTLEIAE HDRAVLEAEE
ELENLLIRRG SAHGLRRIFS PNGSRVKIGK TKKERRQRRG SRRERVSEDG ELMYEMEEGI
GDDNASLLSG SSLDLDQKGE YTYEPPPRPS WRKILFIIAL IAILFVILLL GAYKASSGFR
ASRAHFPPLL SNGTALFAPT TIVISLDGFR ADFLDRGLTP ALNSLVANGV SPQYMNPSFP
SVTFPNHFTL MTGLYPESHG IVGNTFWDPK INEEFYYTHP AVSMQPKWWM AEPLWVTAEK
QGVKTAIHMW PGSEAHIGDR EPTFLDKYNG TEVLSRKVDR VLEFLDLPGL EDKSQVTPER
PQFIIAYVPD VDRDGHTFGP NSTEIRKTIS EADSMVANIM TGLEQRNLTE VVNIVVVSDH
GMATTSAERL IQLDDLIDYN LIEHIDGWPS AGLRPKRPED LETLRKQLEK VAPDYEHAFE
FYTRETMPER YHFSNNERIA PLWVIPKTGW AIVNRSEFDV KEDLKTGKEY HPRGIHGYDH
EHPLMRAIFI ARGPAFPHKP NSRVEVFQNI EVYNIVCDSL GVDPLPGNGT LRLPLKPVGL
HSDENAPVLD TPPDPPAQTS ATAVPAQPAP PQPTLPQPSP PQPKPAQPAQ PAPKPSPAPE
TPPATDHQSD DEKGSTWWGT IWHKFEDLKS WAGGVADAVQ GKHPDKYETV HNYYKQESLS
QRPIKKSEHW QRERKIGGGG FGEVWLEKCT KGKNNGHHVR ATKQMEVGRQ IDYARELEAI
AKFSHPKARL PATQYQQYER CFVKSFGWYQ NEASLFIAME YLELGDLHDY LLDKNQPLPE
IEVRCVMSQI LESLGLIHDN GFAQRDLKPR NILQEPVHQM TGG
//