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Database: UniProt
Entry: A0A2V1ECF7_9PLEO
LinkDB: A0A2V1ECF7_9PLEO
Original site: A0A2V1ECF7_9PLEO 
ID   A0A2V1ECF7_9PLEO        Unreviewed;      1207 AA.
AC   A0A2V1ECF7;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN   ORFNames=DM02DRAFT_156040 {ECO:0000313|EMBL:PVI08213.1};
OS   Periconia macrospinosa.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Massarineae; Periconiaceae; Periconia.
OX   NCBI_TaxID=97972 {ECO:0000313|EMBL:PVI08213.1, ECO:0000313|Proteomes:UP000244855};
RN   [1] {ECO:0000313|EMBL:PVI08213.1, ECO:0000313|Proteomes:UP000244855}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSE2036 {ECO:0000313|EMBL:PVI08213.1,
RC   ECO:0000313|Proteomes:UP000244855};
RX   PubMed=29679020; DOI=10.1038/s41598-018-24686-4;
RA   Knapp D.G., Nemeth J.B., Barry K., Hainaut M., Henrissat B., Johnson J.,
RA   Kuo A., Lim J.H.P., Lipzen A., Nolan M., Ohm R.A., Tamas L.,
RA   Grigoriev I.V., Spatafora J.W., Nagy L.G., Kovacs G.M.;
RT   "Comparative genomics provides insights into the lifestyle and reveals
RT   functional heterogeneity of dark septate endophytic fungi.";
RL   Sci. Rep. 8:6321-6321(2018).
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DR   EMBL; KZ805301; PVI08213.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2V1ECF7; -.
DR   STRING; 97972.A0A2V1ECF7; -.
DR   Proteomes; UP000244855; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
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; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR48012:SF10; SERINE_THREONINE-PROTEIN KINASE KIC1; 1.
DR   PANTHER; PTHR48012; STERILE20-LIKE KINASE, ISOFORM B-RELATED; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 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};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000244855}.
FT   DOMAIN          202..474
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          767..793
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          847..895
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          952..1002
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1082..1105
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1182..1207
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        853..869
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1086..1105
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1183..1200
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         231
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1207 AA;  135743 MW;  37CB224958E20B68 CRC64;
     MDEPRPVPAL VYGSVIRLKR AKTSLSDVET VDSDLRTRGP TLSIGALPRQ DVAARKRPRR
     GFSLNKLTTS LGLQKPTRQR IDKASISRPI VDCQSVVPVS PSSLQLGHIS PTSHTSHFLH
     ATTSPTGRLS QRIPPFTEQP PATNLCRSFN NTAQKLGKMD PSRLSLQPPA TGTKLRARQQ
     AQEMQNLVIE RARRSGEDPP PYEFFELIGR GSFGRVFKGA DRKTGDTVAI KILDIDSSDY
     IERSQDQLST TLKEISILQQ LRDSKARPYV NVIMEALPVH NELWIISEYA SGGSVSTLMK
     PTINQGLEEK FIIPIARELA WALKYTHEIG ILHRDLKCAN ILILEDGRVQ LCDFGVSGIV
     EARQAEPSKR FSVHGTPHWL APELIPPLIN NEFETELPYG AEVDIWAYAC TVYEMATGKP
     PNATTAAINL PNAPLPTLEG DRYSEDLKDF VDFLFVRDPE NRPTTDQILE HPYLVNSTKM
     YPTVMLVKLL EDYTQWERGG GARASLFDPR AGAMAPDPLA PEDDDDDDWT FSTSEEFETR
     LSRAFPEQFG IPNQNQDGEA NDSVHGQDRF ANLMEIWKQE RIARGKEGLE RLFNPNADPY
     QWDNNGRPPS DLVLRDYHPG APNRETVIDL DFAAPVASDG PSIDLGDVPH VRASRRYLRD
     SQLEMDDSDT FDMDAMMKRA TQEWKFPSSE DQDLTVKRST QDWKFPLNEE IARRATKDWK
     FPMTEESLKR ATRDMKLPVN EEALKRATKD WKFPMSEEAL KRATQDWKFP PMPEQPNRQT
     KDFQFPPPAK NRGTREWTFS AAIAEANYNQ RNSRRETRDW KFPTAVPAEQ PINRKTRDFV
     FPMSETVEDE ADQGRQIQSS PTLESNFRPS LRHAATEPAS SFDDYPRVDS TPNSPLRSSM
     IDLDMAMVDD YRPPSAGSAS TTIRTALSEQ LHDNPFNLED QVHLSENNNR ASYHTKSQSE
     PNHAIPGLLT PQTFDEQGQP TNVDSHHQNM HARGVSSVSQ MQAQLKPPTT NNAITQHRPY
     QRSQAQIWDG WSHSAAYNTG SDESPPASVV TDISVDDEDI DEAWDALEKQ TIFRNRYQIP
     GTHHQTTASR DDDVHYPDAD NGDYEDPARH IRVSLGPNGK PLVEFPIPRG PDPEALLGIN
     GIGDGSAKLQ DALWKSAAEI RDGVRACRDL MKAMRLVEGA DEDESNNLNN GNSTDISATV
     RLSRVDR
//
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