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Database: UniProt
Entry: A0A418V594_9DEIO
LinkDB: A0A418V594_9DEIO
Original site: A0A418V594_9DEIO 
ID   A0A418V594_9DEIO        Unreviewed;       778 AA.
AC   A0A418V594;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   ORFNames=D3875_06560 {ECO:0000313|EMBL:RJF71283.1};
OS   Deinococcus cavernae.
OC   Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=2320857 {ECO:0000313|EMBL:RJF71283.1, ECO:0000313|Proteomes:UP000286287};
RN   [1] {ECO:0000313|EMBL:RJF71283.1, ECO:0000313|Proteomes:UP000286287}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K2S05-167 {ECO:0000313|EMBL:RJF71283.1,
RC   ECO:0000313|Proteomes:UP000286287};
RA   Zhu H.;
RL   Submitted (SEP-2018) 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   -!- 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:RJF71283.1}.
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DR   EMBL; QYUJ01000014; RJF71283.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A418V594; -.
DR   OrthoDB; 9788659at2; -.
DR   Proteomes; UP000286287; 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-EC.
DR   CDD; cd14014; STKc_PknB_like; 1.
DR   Gene3D; 3.10.450.50; -; 1.
DR   Gene3D; 1.10.101.10; PGBD-like superfamily/PGBD; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR032710; NTF2-like_dom_sf.
DR   InterPro; IPR002477; Peptidoglycan-bd-like.
DR   InterPro; IPR036365; PGBD-like_sf.
DR   InterPro; IPR036366; PGBDSf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1.
DR   PANTHER; PTHR43289:SF37; SERINE_THREONINE-PROTEIN KINASE A; 1.
DR   Pfam; PF01471; PG_binding_1; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   PRINTS; PR01217; PRICHEXTENSN.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF54427; NTF2-like; 1.
DR   SUPFAM; SSF47090; PGBD-like; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 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};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000286287}.
FT   DOMAIN          15..287
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          331..419
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        337..412
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         44
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   778 AA;  82762 MW;  E37D58509723EE12 CRC64;
     MSALAAGSVL QGGRYRIDGV LGQGGFGITY AATQTVLNAP VAIKELFPSG TLRQGQTVFP
     PATFGLQEWA QAKRDFTTEA QLLAQFQHPD IVRVLDLFED SGTAYMVMER LAGETLQQRL
     ERRGALDPQD VQGLAERVAR ALGVVHSAGL LHRDLKPDNI FLEASGRVVL IDFGSARGFV
     VGQTVRHTRL VTPGYAPMEQ YGSEARFGPY TDIYALGATL HHALTGKMPP SAPDLMTGTP
     LPALPANTPA GLQDALQAAL SPRVTDRPQS AQEFLTLLSG PPSAPAVPAP APQLPTPLAP
     PAQKRGFSAW PLALVALAGA GGFALLRGHD RSSPPAAATP AEPPVVPEAS TPPADPAIPP
     APTAAPPTTA PPTTAPPTTA PPTTPPAPAP EAAPPEPAPP EAELPAPAEA EPTPDVPAIS
     DGQVREFVDE YLRLGGQDDL NASMNLYAEQ VEYFDQGTQS RAALMDDKRA YFRRWPRRSY
     QRTTDIALHG SGDVRQVRFD YRYTVSNDTR ELSGTAYTVL DLVGDGEHLV ITAERGAIHP
     ETKVERDLAP ENADELSAAA EALTNTLKPT LTEGNSGPAV SRLQTLLQAQ GAEVGVDGFF
     GPETTDAVKG FQQSRGLEAD GVVGPDTWAA LEAQADTTQA ATTPAEAPTF AQWFFTTCQD
     AQTGASHTGL TLGALQFCSL VIETVPNGAR PVSASFSYEL EYLEDGEARK KTIGARSRWP
     ADGEPAVNFE EQGNNLVFSL PLTVREREGR QYTSINVIGD IVFDNGRTKR VYEKLPIQ
//
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