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Database: UniProt
Entry: A0A0D2BXE9_9EURO
LinkDB: A0A0D2BXE9_9EURO
Original site: A0A0D2BXE9_9EURO 
ID   A0A0D2BXE9_9EURO        Unreviewed;       887 AA.
AC   A0A0D2BXE9;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KIW23803.1};
GN   ORFNames=PV07_11975 {ECO:0000313|EMBL:KIW23803.1};
OS   Cladophialophora immunda.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC   Cladophialophora.
OX   NCBI_TaxID=569365 {ECO:0000313|EMBL:KIW23803.1, ECO:0000313|Proteomes:UP000054466};
RN   [1] {ECO:0000313|EMBL:KIW23803.1, ECO:0000313|Proteomes:UP000054466}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 83496 {ECO:0000313|EMBL:KIW23803.1,
RC   ECO:0000313|Proteomes:UP000054466};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Cladophialophora immunda CBS83496.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KN847046; KIW23803.1; -; Genomic_DNA.
DR   RefSeq; XP_016244019.1; XM_016399457.1.
DR   AlphaFoldDB; A0A0D2BXE9; -.
DR   GeneID; 27351169; -.
DR   VEuPathDB; FungiDB:PV07_11975; -.
DR   HOGENOM; CLU_000288_52_1_1; -.
DR   OrthoDB; 10768at2759; -.
DR   Proteomes; UP000054466; Unassembled WGS sequence.
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   Gene3D; 2.60.40.150; C2 domain; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
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:SF245; AGC_AKT PROTEIN KINASE SCK2; 1.
DR   PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00433; Pkinase_C; 1.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 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:UP000054466};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          500..761
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          762..846
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51285"
FT   REGION          1..174
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          200..327
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          384..413
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        74..92
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        94..111
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        145..159
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        211..243
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        295..311
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         529
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   887 AA;  97810 MW;  5AFE5A0EE9348794 CRC64;
     MAQTGVNPHA AAAADLLRQA MAQNSARHEN REDFHDQIGS NSPTPSGVET PRPDLHDKRL
     PGIIHGYFGQ VGRDPSQRTP SRSSQAATNP EPETDQHDMG EPAKESERRR SSSASLGSMV
     MVEREQASIQ TPPPDEPPEE SAPPVSDGGT SQLPPTPISS AASVVHRDGE VAENGGSLLD
     GGIASITQAL RNFVLPKSVS GVKDRRHQSL PVSGVTKSTV SAAHISNPAS STHSSRPQSP
     KSPSPSHAKL PPSAILKGSD ELTSNVADGP REKSTPPHTP RALSQEDHRR ADTRSPLSSA
     STTVSEANSQ VEKRSLAKDE IPNSTPRGKL SIKIAEGRDL KPSFDPYVVC QFEWNEYVSK
     GPRHDKMDVD VDDRKGPVGQ LQSVRRTDSD MGKPMAIPMR SRQSSTNGDG RVSDPQWDHE
     AIFDVVSDQS ELDVTVYDRH AETFLGHIRL CLKLTEQNPT LEGFFKLEPR SPEDHDITGE
     IHIRMHFSPV EKKHVGPNDF QILKLIGKGT FGQVYQVRKK DTGRIYAMKV LSKKVIIQKK
     EIQHTIGERN ILVRTATTES PFIVGLKFSF QTPTDLYLVT DFMSGGELFW HLQKEGRFKE
     DRAKFYIAEL ILALKHLHQS DIVYRDLKPE NILLDANGHI ALCDFGLSKA NLAQDDTTNT
     FCGTTEYLAP EVLLDEQGYT KMVDFWSLGV LVFEMCCGWS PFYAEDTQQM YKNIAFGKVR
     FPRDALSTEG RNFVKGLLNR NPKHRLGAHG DAEELMQHPF FADIDWDALG KKNLVPPFKP
     KLASIADTSN FDPEFTNALN TSSSLNARAA ALAAGAAPAS TPLSPTMQNA FQGFTFVDES
     TMEQQFGGAR DAEDHRVDDN FLARTKTLEH RMSGVQKTGE DGFFFEE
//
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