ID A0A0S2K7L1_9GAMM Unreviewed; 1285 AA.
AC A0A0S2K7L1;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Serine/threonine protein kinase {ECO:0000313|EMBL:ALO44380.1};
GN ORFNames=PP2015_3912 {ECO:0000313|EMBL:ALO44380.1};
OS Pseudoalteromonas phenolica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=161398 {ECO:0000313|EMBL:ALO44380.1, ECO:0000313|Proteomes:UP000061457};
RN [1] {ECO:0000313|EMBL:ALO44380.1, ECO:0000313|Proteomes:UP000061457}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 12086 {ECO:0000313|EMBL:ALO44380.1,
RC ECO:0000313|Proteomes:UP000061457};
RA Zhang Y., Guo Z.;
RL Submitted (NOV-2015) 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; CP013188; ALO44380.1; -; Genomic_DNA.
DR RefSeq; WP_058032239.1; NZ_CP013188.1.
DR STRING; 161398.PP2015_3912; -.
DR KEGG; pphe:PP2015_3912; -.
DR PATRIC; fig|161398.10.peg.4004; -.
DR OrthoDB; 9801841at2; -.
DR Proteomes; UP000061457; Chromosome II.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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 CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 3.30.70.1230; Nucleotide cyclase; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR041664; AAA_16.
DR InterPro; IPR045269; Atg1-like.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR023889; TOMM_kin_cyc.
DR NCBIfam; TIGR03903; TOMM_kin_cyc; 1.
DR PANTHER; PTHR24348:SF22; NON-SPECIFIC SERINE_THREONINE PROTEIN KINASE; 1.
DR PANTHER; PTHR24348; SERINE/THREONINE-PROTEIN KINASE UNC-51-RELATED; 1.
DR Pfam; PF13191; AAA_16; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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}; Kinase {ECO:0000313|EMBL:ALO44380.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000061457};
KW Serine/threonine-protein kinase {ECO:0000313|EMBL:ALO44380.1};
KW Transferase {ECO:0000313|EMBL:ALO44380.1}.
FT DOMAIN 20..290
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 49
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1285 AA; 144922 MW; A4DCD0D0CFE22325 CRC64;
MSLSQFSDQL IHEQFSSDQY QLLHKIGEGG FGKVFKAIQV NTGQHVAIKF LAIEPHCEEQ
QKQRYIERFK RETALSSQLQ HPNIVRLLDK GQINDDLLYG VFEYIEGQSL REHLIQEGAL
NAVDAKEVML QVLDALVHAH QNGIVHRDIK PANIMLTKTG AKTHAKILDF GIGTLTQDSR
QADFNTLTLT QETLGTPSYS APEQLRGEPA TEKTDLYVWG LVFLECLTGL PAITGSSIAA
VYHKQLSDMQ VSIPSSLLGH PIAALLRRVL IKNATDRVIT GDALYQEVAL VNMSNLVGVL
ADLRVQQQAD DDTMIMRDDG PAGASMQNFT AHIERKQITV LAMRLSSKVL TDKELDLDIV
DTLFRSQRNH CIDIATRYGA THVGNLADSV LFYFGYPIAS DNDTRLCART ILDAISDIAK
RNALTQEAHG VQINVHAGIH AGVFTTYATA MPEGHIANTA MALAREAGER QILCSEESRA
ILEPYSEFEY FGEKLLSSNL SKKRIFSLKG ERRVEAFGFM RGTRNSHELV GRSNELEQSL
SIFNHESTES RFTHIHGEAG IGKSRLLQEI RSSASKYQHL VAQCLPEHQN NALYPILTLV
RYLYNTSNLT TSNAIETFTA IITAHDKTLD CEQVLPILLI WLNIELSDEL TASTLAPDAQ
KAYLFKALTA LLMSQSFTIN ANKLYIVEDI HWADITTIEF IQHFAKQLHN GDVLISTSRQ
KVPTQLQDLT LLEVGLKKLT QQATEDFIVK LFDDQAVSQN VLDVLVNRTD GIPLFIEELI
DMLKQKKLVS VINDAINFTS PDKLDQVPTS LRESLQQKLD SLIHAKETAQ LAATIGREFE
YELLVAASSL SENQIQNDLN ELVAKDLIVH QRSVDHDSYI FKHALVRDAA YESTNTASKE
KNHNKIASIL VTKPKLEALL IAYHYKHAQK FLLSSTYGFK AAEHTYEGSL YKEAFNITNE
YFQIAKKIND ETESIKWQLR LNSYNISSLM LGFGYGDVRI FEKAKQNEVL LRQSNESIDL
STEEYQRLHH QLIWSQISYH NNKNERYKAI TLAEEALTDN THKATYLHRL LTQSMLANNY
VFDAQLEKAE QSLSECFALL DELNHEEIRN GLKTYGLLPN CLPYYFNGIF QAVTGQSTQS
IKSVEKALQI AQKFNHLPSY LMGLNYSAII SYIINDTTLA KKTIERARQE FKTDSHLYLV
FIPTDALNAC LNQDTDMLKG ICEKIEKTGQ VHSLSFYKAM YIDTLIESKQ IDRALNQLSE
LTSWCETQNE KIMLNKLKEL KNGIC
//
