ID   Q47TL3_THEFY            Unreviewed;       569 AA.
AC   Q47TL3;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   27-MAR-2024, entry version 113.
DE   SubName: Full=Tyrosine protein kinase:Serine/threonine protein kinase {ECO:0000313|EMBL:AAZ54201.1};
GN   OrderedLocusNames=Tfu_0163 {ECO:0000313|EMBL:AAZ54201.1};
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Nocardiopsaceae; Thermobifida.
OX   NCBI_TaxID=269800 {ECO:0000313|EMBL:AAZ54201.1};
RN   [1] {ECO:0000313|EMBL:AAZ54201.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=YX {ECO:0000313|EMBL:AAZ54201.1};
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.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001433};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
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DR   EMBL; CP000088; AAZ54201.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q47TL3; -.
DR   STRING; 269800.Tfu_0163; -.
DR   KEGG; tfu:Tfu_0163; -.
DR   eggNOG; COG0515; Bacteria.
DR   HOGENOM; CLU_000288_135_1_11; -.
DR   OrthoDB; 3915799at2; -.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd14014; STKc_PknB_like; 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; PTHR43671:SF13; LD04361P; 1.
DR   PANTHER; PTHR43671; SERINE/THREONINE-PROTEIN KINASE NEK; 1.
DR   Pfam; PF00069; Pkinase; 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   Kinase {ECO:0000313|EMBL:AAZ54201.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:AAZ54201.1};
KW   Transferase {ECO:0000313|EMBL:AAZ54201.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        407..428
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          16..269
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          304..402
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          439..569
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        353..381
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        467..481
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   569 AA;  58735 MW;  F5F4CFF20F7DC3E7 CRC64;
     MTSPLRPEDP TRVGDYDLVA RIGKGGQGVV YLGKAPDGTR VAVKVMETSW ASNSRARSRF
     AKEIEAASKV APFCTAALLD SDINADPPYI VSEYIEGPSL RDAVLRDGPR TGAALDRLAI
     STATALVAIH QAGVIHRDFK PANVLLGPDG PRVIDFGIAR HSEATVTATD SIVGTPAYMA
     PEQVEGRELT PAVDIFAWAG VMVFAATGQS PFHDETLPAI INRVLHQPPR LDGVDERLRP
     LLEACLAKEP ERRPTAVQVL GVLVGHDPAT LPQVPVEEVL ENGYTAALNE QTQIAATAAL
     PIPIGDQAPE PAPTAVMPAA EDTPAPESRT PVSGLAALAA NRPADEAPAS SPPSGPLRTT
     SGLAALVNTG ENKQPTASSP GEGPPRRSAG PGHQPLPPRS TRERKTVLSW LVAAGILIIV
     LAGGWFLIDT FLLSPNGQSP EATPVDGTRR DTPAQDGIDD SVPSPSAIDP DTPTSSDTGY
     PGGELYPSLP YDDMSQTDPM EEPHLNPTIP GEGPWHSPPA GEEAPGQPHG GGAEEGGSEG
     GEQPGTGGPG GSGEGGAGVG RVAVSPAAP
//