ID   Q47QZ5_THEFY            Unreviewed;       833 AA.
AC   Q47QZ5;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   27-MAR-2024, entry version 118.
DE   SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:AAZ55122.1};
GN   OrderedLocusNames=Tfu_1084 {ECO:0000313|EMBL:AAZ55122.1};
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Nocardiopsaceae; Thermobifida.
OX   NCBI_TaxID=269800 {ECO:0000313|EMBL:AAZ55122.1};
RN   [1] {ECO:0000313|EMBL:AAZ55122.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=YX {ECO:0000313|EMBL:AAZ55122.1};
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};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000088; AAZ55122.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q47QZ5; -.
DR   STRING; 269800.Tfu_1084; -.
DR   KEGG; tfu:Tfu_1084; -.
DR   eggNOG; COG0515; Bacteria.
DR   HOGENOM; CLU_340629_0_0_11; -.
DR   OrthoDB; 5492697at2; -.
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   GO; GO:0010506; P:regulation of autophagy; IEA:InterPro.
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; IPR008271; Ser/Thr_kinase_AS.
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; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:AAZ55122.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:AAZ55122.1};
KW   Transferase {ECO:0000313|EMBL:AAZ55122.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        758..780
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        800..830
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          95..342
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
SQ   SEQUENCE   833 AA;  93495 MW;  6310124762EC6B3E CRC64;
     MTVPQPSDPE SPTRKIEAVE PTVQLTPSEP GVTRKLTALL RPGATRRLPA AEPRTAVLTR
     PVRRRGRLGR LAWRVLEGPA SEVEYRIPAE LRERYTVQEY VGAGGEAVVY RAVPVGRDGP
     PIALKLYRSG HDINRDLLDR ISALGTVSPH IPVLHGYGYA RAPWGEEIAW EAQEYFALGS
     LRTLIDQAPL PDDQARAVIA ALSDCLGYWQ QSLNYNHTDV KPENLLIRSL DPPVFALTDF
     GGAVRATMSQ IYGGQAITEA YAAPEVIEGR REAPAAWWSL GVIAHELVTG QRPPRSGNWL
     TARSTAVDLS AVADERWRLL IRGLLTPDPK TRWGDAQVRQ WLRGERPSVA RPRKHRPITF
     EGVAHEDPPS LAFDLMDRFD KGAVWLQRRH QEVETWLSRE VHDLTFDPAP LKQLRTRPER
     AHVAISALAA QYVPGLPPRY RGHQITAEGV LELARGESTQ QAVLREAIEW GAVQSAARHW
     CTHPRCRSHE TRRCQLLELV HHEVPLIMRQ VRATVDGLAQ TPDFTPPEEH DWDAAWARAA
     ELVLDPEAAA RYRRLLLTRS WLPGRYGDAA RARWWTEQRT TALRGDRTAR STRAALVTAV
     LLLPSAVQAG AAQRARAATE SRERRQQRWE RFTSSVESRW SATRARLARQ WEKRRTGPFE
     WHTPEAREER RRRREARRME RGMARLQRAM AAGRCRRFAR PAALAGLLDG CGLWLWESQG
     GLFTDQEWVV TAFGWAEAIR DNSLVTLAAQ LCSSLLELLP GGIGLVWWFP VLLGVLLFAL
     GRTAANQHRS ARTRLVAYRL AVVASVLVVV RALAHGLFFL FMGVLIPAAL LAG
//