ID   Q47SS5_THEFY            Unreviewed;       464 AA.
AC   Q47SS5;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   27-MAR-2024, entry version 124.
DE   SubName: Full=Tyrosine protein kinase:Serine/threonine protein kinase {ECO:0000313|EMBL:AAZ54492.1};
GN   OrderedLocusNames=Tfu_0454 {ECO:0000313|EMBL:AAZ54492.1};
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Nocardiopsaceae; Thermobifida.
OX   NCBI_TaxID=269800 {ECO:0000313|EMBL:AAZ54492.1};
RN   [1] {ECO:0000313|EMBL:AAZ54492.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=YX {ECO:0000313|EMBL:AAZ54492.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Di Bartolo G., Chain P., Schmutz J.,
RA   Larimer F., Land M., Lykidis A., Richardson P.;
RT   "Complete sequence of Thermobifida fusca YX.";
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP000088; AAZ54492.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q47SS5; -.
DR   STRING; 269800.Tfu_0454; -.
DR   KEGG; tfu:Tfu_0454; -.
DR   eggNOG; COG0515; Bacteria.
DR   HOGENOM; CLU_000288_63_44_11; -.
DR   OrthoDB; 5241055at2; -.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   GO; GO:0010506; P:regulation of autophagy; IEA:InterPro.
DR   CDD; cd14014; STKc_PknB_like; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR045269; Atg1-like.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   PANTHER; PTHR24348:SF22; NON-SPECIFIC SERINE_THREONINE PROTEIN KINASE; 1.
DR   PANTHER; PTHR24348; SERINE/THREONINE-PROTEIN KINASE UNC-51-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.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Kinase {ECO:0000313|EMBL:AAZ54492.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:AAZ54492.1};
KW   Transferase {ECO:0000313|EMBL:AAZ54492.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        282..300
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          10..265
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         39
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   464 AA;  51023 MW;  F0B3B5CA453D373B CRC64;
     MAQPERFGRY RVLRRLGSGS FATVWLGHDD LLDTPVAIKV LAENWAHNLD IHQRFVEEAR
     ILRQADSEWL VRVHDIGTLP DDRPYFVMTY ADRGSVADRI AQGPLPLDEA LRLLTEIGQG
     VTVLHRHGTI HRDIKPSNVL LQSSPVGERV LVADLGFAKS IDGASGFTAS AGTPGYMSPE
     QSVVGGDIDV RADVYSLGAV AYELVTGKRP PSPPVRVPPS RLRPGVPPAL DELIMSALSP
     NRSDRPPDAA TFTSRIREIR MSPDLELATP WWQRYRATWT RLVALVATAV AVLGVAPAAS
     ASPHLPMMEI YDASGELHVR VPTPWLRQMQ LNGWSPRELG LPGGHEPGLL VATDLDAWSD
     ARQSVSGLFA GLFVSDGQSP DLDRLISSGL CSGQPQRQRF TNAHWDGELW QWVDCSPDSS
     EGDVFTAAVL QHRGQERTLY LEIRQTEHQP QTVAEILDGL RLIS
//