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Database: UniProt
Entry: A0A0S7DMI0_9EURO
LinkDB: A0A0S7DMI0_9EURO
Original site: A0A0S7DMI0_9EURO 
ID   A0A0S7DMI0_9EURO        Unreviewed;       637 AA.
AC   A0A0S7DMI0;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KAF4174672.1};
GN   ORFNames=ALT_000776 {ECO:0000313|EMBL:GIM38393.1}, CNMCM8060_008403
GN   {ECO:0000313|EMBL:KAF4174672.1};
OS   Aspergillus lentulus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=293939 {ECO:0000313|EMBL:KAF4174672.1, ECO:0000313|Proteomes:UP000713487};
RN   [1] {ECO:0000313|EMBL:GIM38393.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=IFM 54703 {ECO:0000313|EMBL:GIM38393.1};
RA   Kusuya Y., Sakai K., Kamei K., Takahashi H., Yaguchi T.;
RT   "Draft Genome sequence of the pathogenic filamentous fungus Aspergillus
RT   lentulus IFM 54703T.";
RL   Genome Announc. 4:e01568-15(2016).
RN   [2] {ECO:0000313|EMBL:KAF4174672.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CNM-CM8060 {ECO:0000313|EMBL:KAF4174672.1};
RA   dos Santos R.A.C., Steenwyk J.L., Rivero-Menendez O., Mead M.E.,
RA   Silva L.P., Bastos R.W., Alastruey-Izquierdo A., Goldman G.H., Rokas A.;
RT   "Genomic and phenotypic heterogeneity of clinical isolates of the human
RT   pathogens Aspergillus fumigatus, Aspergillus lentulus and Aspergillus
RT   fumigatiaffinis.";
RL   bioRxiv 0:0-0(2020).
RN   [3] {ECO:0000313|EMBL:KAF4174672.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CNM-CM8060 {ECO:0000313|EMBL:KAF4174672.1};
RA   Santos R.A.C., Steenwyk J.L., Rivero-Menendez O., Mead M.E., Silva L.P.,
RA   Bastos R.W., Alastruey-Izquierdo A., Goldman G.H., Rokas A.;
RL   Submitted (APR-2020) to the EMBL/GenBank/DDBJ databases.
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:KAF4174672.1}.
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DR   EMBL; BCLY01000008; GIM38393.1; -; Genomic_DNA.
DR   EMBL; JAAAPS010000072; KAF4174672.1; -; Genomic_DNA.
DR   STRING; 293939.A0A0S7DMI0; -.
DR   VEuPathDB; FungiDB:TMP_alenIFM54703_4081; -.
DR   OrthoDB; 10768at2759; -.
DR   Proteomes; UP000713487; 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   CDD; cd11651; YPK1_N_like; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR000961; AGC-kinase_C.
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; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR   PANTHER; PTHR24351:SF243; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00433; Pkinase_C; 1.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 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   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          294..551
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          552..623
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51285"
FT   REGION          22..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          104..140
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        104..139
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         327
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   637 AA;  70897 MW;  10786BFFBB4EEA12 CRC64;
     MSWKLTKKLK ETHLAPLTNT FTRSSSTSTI KGESGEETPI VSQTPSISST NSNGINASES
     LVSPPVDPVK PGILIVTLHE GRGFALSPHF QQVFTSHFQN NNYSSSVRPS SSSSHSTHGQ
     TASFAQSGRP QSTSGGINAA PTIHGRYSTK YLPYALLDFE KNQVFVDAVS GTPENPLWAG
     DNTAFKFDVS RKTELNVQLY LRNPSARPGA GRSEDIFLGA VRVLPRFEEA QPYVDDPKLS
     KKDNQKAAAA HANNERHLGQ LGAEWLDLQF GTGSIKIGVS FVENKQRSLK LEDFDLLKVV
     GKGSFGKVMQ VMKKDTGRIY ALKTIRKAHI ISRSEVTHTL AERSVLAQIN NPFIVPLKFS
     FQSPEKLYLV LAFVNGGELF HHLQREQRFD INRARFYTAE LLCALECLHG FKVIYRDLKP
     ENILLDYTGH IALCDFGLCK LDMKDEDRTN TFCGTPEYLA PELLLGNGYT KTVDWWTLGV
     LLYEMLTGLP PFYDENTNDM YRKILQEPLT FPSSDIVPPA ARDLLTRLLD RDPQRRLGAN
     GAAEIKSHHF FANIDWRKLL QRKYEPSFRP NVMGASDTTN FDTEFTSEAP QDSYVDGPVL
     SQTMQQQFAG WSYNRPVAGL GDAGGSVKDP SFGSIPE
//
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