ID G2FIK9_9GAMM Unreviewed; 792 AA.
AC G2FIK9;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Serine/threonine-protein kinase {ECO:0000313|EMBL:EGW53399.1};
DE EC=2.7.11.1 {ECO:0000313|EMBL:EGW53399.1};
GN ORFNames=TevJSym_bd00350 {ECO:0000313|EMBL:EGW53399.1};
OS endosymbiont of Tevnia jerichonana (vent Tica).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; sulfur-oxidizing symbionts.
OX NCBI_TaxID=1049564 {ECO:0000313|EMBL:EGW53399.1, ECO:0000313|Proteomes:UP000005167};
RN [1] {ECO:0000313|EMBL:EGW53399.1, ECO:0000313|Proteomes:UP000005167}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Gardebrecht A., Markert S., Felbeck H., Thuermer A., Albrecht D.,
RA Wollherr A., Kabisch J., Lehmann R., Daniel R., Liesegang H., Hecker M.,
RA Sievert S.M., Schweder T.;
RT "The endosymbionts of the deep-sea tubeworms Riftia pachyptila and Tevnia
RT jerichonana share an identical physiology as revealed by proteogenomic
RT analyses.";
RL ISME J. 0:0-0(2011).
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 -!- 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:EGW53399.1}.
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DR EMBL; AFZB01000030; EGW53399.1; -; Genomic_DNA.
DR RefSeq; WP_006475511.1; NZ_AFZB01000030.1.
DR AlphaFoldDB; G2FIK9; -.
DR eggNOG; COG0515; Bacteria.
DR eggNOG; COG1639; Bacteria.
DR Proteomes; UP000005167; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 1.10.3210.10; Hypothetical protein af1432; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR013976; HDOD.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR44167; OVARIAN-SPECIFIC SERINE/THREONINE-PROTEIN KINASE LOK-RELATED; 1.
DR PANTHER; PTHR44167:SF8; OVARIAN-SPECIFIC SERINE_THREONINE-PROTEIN KINASE LOK; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF08668; HDOD; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51833; HDOD; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:EGW53399.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005167};
KW Transferase {ECO:0000313|EMBL:EGW53399.1}.
FT DOMAIN 9..259
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 289..484
FT /note="HDOD"
FT /evidence="ECO:0000259|PROSITE:PS51833"
SQ SEQUENCE 792 AA; 88000 MW; 62BBC99E81B970EA CRC64;
MTLNQIGRFK VGKKLGAGAQ GTVYLCFDTQ LQRRVAIKLL DRSVKESAQC GEARAMSRLQ
HPNIVSIYEA GEQRGLPFMV FEYVEGELLS DQIRSARLEL PLALNIFRGI LQGMAEAHRA
GIVHRDLKPG NIIINPDGVA KIMDFGIARL LSEGRERDRS RIGTPRYLAP EYISRGEVGA
PADVFALGLI LDEMLTGMPV FSGSSQQIVL DSILKARVQP PSRFNEAVDE RLDRFVLKAL
EKDPDARYAD AGDMLKAFEA LKGEPAEEVD GAHGTVEFLL RRMRRKSDFP VLSQSVRRIN
AMSQVRGKDA GQMASVIVKD FALTNKILKV VNSAYYGRFS GKIGTVSRAV VVLGIQAIRS
LAASLIFFEH LGDKQQAERL REQVSAAMFS AVFASQLARQ QGENDTEGFF LAAMLRDLGR
ILVAFYLPDE SREVERLQQL ESLQPIQAQH QVLGVSFETV GIEIARQWNF PDLLTDAMKH
WKEDRPPTSE TERRRMLAAF AGDATRLMAE QGIGDSQAVS RLLERYRKGL GFDRKTFLHL
SHNAMDEFKA YAKVLNSDIS QGFVSKIVSG SGKPPVTEPV GDAQPGGGAT LPDGLTETRI
LNGSNEQEEV EQAVTAESLI TPQESETLLM DGLQEVTSLM VADCEISELF NVVLETMYRS
MGFRRVVLAL YNRQSGEVMG RSGFGDDLEP FIKAFRFPMK YSVDVFHGAL KNAVDVYIAN
TAEQKMQQDI PQWYKQISNA GSFLLFPLVL NGRPLGLIYA DHPQPDALEI DKKKLNLLKA
LRNQILLALR SQ
//
