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Database: UniProt
Entry: A0A1V6SKD4_9EURO
LinkDB: A0A1V6SKD4_9EURO
Original site: A0A1V6SKD4_9EURO 
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}.
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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
//
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