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
//