ID A0A0D2BWB9_9EURO Unreviewed; 1075 AA.
AC A0A0D2BWB9;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN ORFNames=PV07_10963 {ECO:0000313|EMBL:KIW22690.1};
OS Cladophialophora immunda.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=569365 {ECO:0000313|EMBL:KIW22690.1, ECO:0000313|Proteomes:UP000054466};
RN [1] {ECO:0000313|EMBL:KIW22690.1, ECO:0000313|Proteomes:UP000054466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 83496 {ECO:0000313|EMBL:KIW22690.1,
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; KIW22690.1; -; Genomic_DNA.
DR RefSeq; XP_016242906.1; XM_016398344.1.
DR AlphaFoldDB; A0A0D2BWB9; -.
DR STRING; 569365.A0A0D2BWB9; -.
DR GeneID; 27350157; -.
DR VEuPathDB; FungiDB:PV07_10963; -.
DR HOGENOM; CLU_009707_0_0_1; -.
DR OrthoDB; 928649at2759; -.
DR Proteomes; UP000054466; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd14052; PTKc_Wee1_fungi; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR11042; EUKARYOTIC TRANSLATION INITIATION FACTOR 2-ALPHA KINASE EIF2-ALPHA KINASE -RELATED; 1.
DR PANTHER; PTHR11042:SF185; WEE1-LIKE PROTEIN KINASE; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000054466};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 695..1041
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 348..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 448..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 526..661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..167
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..375
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..394
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..425
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 553..569
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..611
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1075 AA; 118688 MW; D5700A743D513C89 CRC64;
MMATYSPHRE EHSPKSAFSR FDPHSAIREI RRSLSRSPSK GSEFRQQSLR SPGPGNLPFS
PSPLSPSRNA TSENFLHLGG MSSHPNRGSS ASRFPRPPLR RTNQSHGVSR LRTSPRSPTK
RVLTDSSDSG NSSPMPLRKR SSAEAERELA LKSLTAGDEK ENDKSTSEPL SWKSVHTRQE
KRRSGGMLIS AVAPLSPMKR SDGPRSDETP GCESPSAKRR SLHGPGLDFS IFESDTLDSG
MFGDKRAQDD NDWFVSNSFL SSSRFSTIPK RSSSLRKSTI QQRQIDRSTN LKFYNVTEAD
KSWLDFTPAA NPKKEMRMSL DNNMNAFPRD SPFPTQGNLL SASIHPMTVS QNGSSYQPRH
PLSRTMTQSS SQPDEQDDSP THEPMHRPSR PRSHDFSKSL PVGSSRPVPS SDENEFSSQA
SFATPGNYKA AKPLPAAFMS TGLISKKNRN VEDPNAGLPK AHMPDTPCKK QPAIFQNEQK
FAPAKGAVNR ISRQSFGVPP SPLEVSHGPS KVSAFPFSKS VGIFGPRPSR HNLLREGSFA
SIDPEDKGTG RAPLSRANSQ STDSDYPPTP TKHLTDPHDR SSVSPSPHQS ALSTNRAVAP
SAHVTRLSSI SPRIEKTDRG SPHTPLDSFF PPDPSGLTIS GRAERPPTRQ NNMAPIIPAT
PTGPREYFTN FSNRPSLNLA SLDATNIDSS LTSRFDKVDL IGSGEFSQVY RVSQPPETSP
FHKIYSVSTS RPSSRSSVPE KIWAVKRSRY PYAGARDRQR KIHEVDVLKA LGHSDHIVTF
VDSWEENGHL YIQTEFCEEG TLDVFLAQVG LKARLDDFRI WKILLELGMG LKHIHDSGFI
HLDLKPANVL ITFEGVLKIA DFGMATRWPA KAGIEGEGDR EYIGPEILMG RYDKPADIFA
LGLIMLETAG NVELPDNGVS WQKLRNGDMS DVPSLTWSSG TSGILRDSSG NPVSRENSFE
FRQDSDHHDV EVMDGDDFEA TVARPHQKTP PFERSGELVN PPQFMVDPSH EQALDRVVRW
MISPDPNDRP LAGEVLNTEG VRWAETRRRA GATVFEGNWG PADEVLAEDA EMIDV
//
