ID A0A166YMB2_9GAMM Unreviewed; 1371 AA.
AC A0A166YMB2;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN ORFNames=N475_00110 {ECO:0000313|EMBL:KZN43015.1};
OS Pseudoalteromonas luteoviolacea DSM 6061.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=1365250 {ECO:0000313|EMBL:KZN43015.1, ECO:0000313|Proteomes:UP000076643};
RN [1] {ECO:0000313|EMBL:KZN43015.1, ECO:0000313|Proteomes:UP000076643}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6061 {ECO:0000313|EMBL:KZN43015.1,
RC ECO:0000313|Proteomes:UP000076643};
RA Vynne N.G., Mansson M., Gram L.;
RT "Comparative Genomic and Metabolomic Analysis of Twelve Strains of
RT Pseudoalteromonas luteoviolacea.";
RL Submitted (JUL-2013) 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:KZN43015.1}.
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DR EMBL; AUYB01000081; KZN43015.1; -; Genomic_DNA.
DR PATRIC; fig|1365250.3.peg.873; -.
DR Proteomes; UP000076643; 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; 3.30.70.1230; Nucleotide cyclase; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR041664; AAA_16.
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 InterPro; IPR011990; TPR-like_helical_dom_sf.
DR NCBIfam; TIGR03903; TOMM_kin_cyc; 1.
DR PANTHER; PTHR16305:SF28; ADENYLATE CYCLASE 10; 1.
DR PANTHER; PTHR16305; TESTICULAR SOLUBLE ADENYLYL CYCLASE; 1.
DR Pfam; PF13191; AAA_16; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF81901; HCP-like; 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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000076643}.
FT DOMAIN 34..303
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 63
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1371 AA; 155186 MW; A7693FDDD4EE4EE8 CRC64;
MPQTDIYLEK LITIMSLTQF SDSYIYDSFE SSHYELLNKV GEGGFGKVFK AKQKSTGQFV
AIKFLAIEPH CEEQKKQRYI ERFKRETSLS SQLQHPNIVR LLDQGQINDD LLYGVFEFVE
GHSLREHLLL EGPFSAPEAT DIMSQVLDAL IHAHSKGIVH RDIKPANIML SKTGAKLHAK
ILDFGIGTLT HDSRQADFRT LTLTQETLGT PSYSAPEQLR GEPATTKTDL YVWGLVYLEC
ITGAPAMNGT SVASIYHKQL SDAHIPMPSA LLGHPLSGLL RRVLNKNAIE RVITGEEAFN
ELKSINVSNL VGKISLSSSS QVAEDETIVM RNDHDTVIAP LGYTSLTERK QITVLALRFS
TSFTDAREHD LEVIDTLFKS QRNYCLDIAI RFGAFHVGSV ADVSLFYFGH PTASDNDTRL
CARSALEITS EISKRNALMK DAHGAQLNVH IGIHTGVFVT YANSTPEGHV ANAAMTLART
AREKQVLCSS EARAILDPYS EFEGYVELKL GQSYRPEPVY ELKGERQVEA FGFMRGTRNN
HELIGREEEL NQVKAQINKE VPSEKHTHIF GEAGIGKSRL LQEIRVHAPK HQHLIAQCLP
EHQNNALYPI LTLIHNLFNT HKLSAEAVTE EFHKLLDKYF NGDLPNDAIP ILLVWLNIDL
GKNYQPSMLP ADIQKQILFS CLQALLVSQI HSLNDNKLFV FEDIHWSDST TLEFINYFEH
SLSTQHFIIS TSRNDIPTSL SRNKIKPIEL NKLDEKATEQ FILKLFDQRP VAQNVLDVLI
ARTDGIPLFI EELVAMLINK QLVDINEHPI DFISPERLDQ VPSSLRESLQ QKLDGLNHAK
ETAQLAATIG REFEYELLVA SSTLSENQIQ NDLNELIKND LIIKQRRVNR ESYIFKHALV
RDAGYESMSR QVAEEVHGKL ANTLESLFME RVENNPHEIA HHFANSKCFD KAINYILRSA
TKHLDFSASS DCIEECQLAI QWSEPLEDKL KQKYTLNANI LITLALMNKD GWAGESVSDY
ANQCLKSVDS LYFNSDLSGF IESDENIESD IIELLVQIYY SVILHNIVAG NRGTLKGFEG
KTLQNTVYEL EKIVEKYPHV ECAAHAILGY YYYTKGDFAK GRVLLESVIN CYDESLHRNH
GVLFGFDSKA WSAATLGLLY WLIDEEQLAI EHANMAIDFA EQLGHMPSLC IGLMYKSILY
QYMVQPHVVF DTASELVSKA KLHSLPAHET YGAIVYQWAL AQTKQLSEQE KENVLNNALQ
PVLGLKAMGC FHAVAFFESL LADIEISQNK LQEAHARLAY CEDLCHEIGE HYYQPMLPYR
RSQLELIMGQ KEQSIESLER SMKWSQKTGM KRVTQMCNKQ IKLFKNRKKE Q
//
