ID A0A1V6RFU9_9EURO Unreviewed; 778 AA.
AC A0A1V6RFU9;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 08-NOV-2023, entry version 16.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN ORFNames=PENVUL_c052G02788 {ECO:0000313|EMBL:OQE00420.1};
OS Penicillium vulpinum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=29845 {ECO:0000313|EMBL:OQE00420.1, ECO:0000313|Proteomes:UP000191518};
RN [1] {ECO:0000313|Proteomes:UP000191518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 29486 {ECO:0000313|Proteomes:UP000191518};
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:OQE00420.1}.
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DR EMBL; MDYP01000052; OQE00420.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6RFU9; -.
DR STRING; 29845.A0A1V6RFU9; -.
DR OrthoDB; 1508at2759; -.
DR Proteomes; UP000191518; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR032682; Cnd1_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR PANTHER; PTHR12984:SF3; N-TERMINAL KINASE-LIKE PROTEIN; 1.
DR PANTHER; PTHR12984; SCY1-RELATED S/T PROTEIN KINASE-LIKE; 1.
DR Pfam; PF12717; Cnd1; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000191518}.
FT DOMAIN 20..312
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 596..706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 722..778
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 596..626
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 655..679
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 733..752
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 757..771
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 778 AA; 84676 MW; 1227F120923B3061 CRC64;
MDFLKSAIGS AIAKGGGLPF SLGDRVDIGD SVWALHNGTK RDDGSACSVF AFDVNANKSR
LPLAKNAVRK FRTLRHPGVI KVLDTIETEH NLYIVTERVV PLSWPVKRKS LSEETAKWGL
YTVASTLKFI NDDASSVHGA VRASSVFIGE SGEWKLGGFE ILSSMKEDDA IIYTYGSSVP
DAGRYTPPEV VKTGWDTIKR NPLAAVDAYG LGILIFEVFN GGFSGGDQAG KTTNIPPSMQ
QSYKRLCAAN PKLRLSPGHF VEQGKKHGGF FQTPLIRMTE DIDSLGLKSD EEREEFINEL
DNLSDDFPEE FFKMKVLPEL LKSVEFGGGG PKVLAATMKI GAKLSADEFN AKLTPVVVRL
FGNPDRALRV CLLDNLPLMI DNLPQKIVND KIFPQMTSGF TDVAPVVREQ TVKAVLTIIN
KLNDRIVNGE LLKFLARTAN DEQPGIRTNT TICLGRIAKN LNQSTRSKVL IAAFTRAVRD
PFVHARNAGF LALSATIDVF TEEDCAVRIL PAVCPGLLDK EKLIRDQANK TFDVYVHRIR
KHASTMADTV IPVAAPAEVN KPDARVGTPN DNSWAGWAIS SFTNKIATAN GEIEPTANTI
KTIDPDTTRS ASVPRSTKTS PSTPLELPKQ VLRPKAQPPL NRLMSDRPAP VVHDEPEEEG
DDVFDAWGAM DDDENDDDPF TAAVASPKPT SPVPSSKKAP AVPYDDGGEP DFAGWLAAKS
QTKAKNPLPK GLHKAASTNS VTTRSTSSVA KPRTVIAPKK IDIKPKDEET DDWGDAWD
//