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Database: UniProt
Entry: A0A177QV66_9PROT
LinkDB: A0A177QV66_9PROT
Original site: A0A177QV66_9PROT 
ID   A0A177QV66_9PROT        Unreviewed;       422 AA.
AC   A0A177QV66;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OAI50443.1};
GN   ORFNames=AYO46_10110 {ECO:0000313|EMBL:OAI50443.1};
OS   Betaproteobacteria bacterium SCGC AG-212-J23.
OC   Bacteria; Pseudomonadota; Betaproteobacteria.
OX   NCBI_TaxID=1799662 {ECO:0000313|EMBL:OAI50443.1, ECO:0000313|Proteomes:UP000077532};
RN   [1] {ECO:0000313|Proteomes:UP000077532}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCGC AG-212-J23 {ECO:0000313|Proteomes:UP000077532};
RA   Choi J., Stepanauskas R., Howe A.;
RL   Submitted (FEB-2016) 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   -!- SIMILARITY: Belongs to the protein kinase superfamily. NEK Ser/Thr
CC       protein kinase family. NIMA subfamily. {ECO:0000256|ARBA:ARBA00010886}.
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:OAI50443.1}.
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DR   EMBL; LSTF01000096; OAI50443.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A177QV66; -.
DR   Proteomes; UP000077532; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030553; F:cGMP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00038; CAP_ED; 1.
DR   CDD; cd14014; STKc_PknB_like; 1.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR018490; cNMP-bd_dom_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR43671:SF13; LD04361P; 1.
DR   PANTHER; PTHR43671; SERINE/THREONINE-PROTEIN KINASE NEK; 1.
DR   Pfam; PF00027; cNMP_binding; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00100; cNMP; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF51206; cAMP-binding domain-like; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50042; CNMP_BINDING_3; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; cGMP {ECO:0000256|ARBA:ARBA00022535};
KW   cGMP-binding {ECO:0000256|ARBA:ARBA00022992};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000077532}.
FT   DOMAIN          10..275
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          295..393
FT                   /note="Cyclic nucleotide-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50042"
FT   BINDING         39
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   422 AA;  46027 MW;  30F6BAF2D18F0232 CRC64;
     MDLTLQVGKY EVQKHLGKGA SGTVYLAKDT FTGKEVALKT IEPEVFRDPE FGTVYRSQFL
     NEASLAGKLR HPHIVSILDA VVGEESGHIA MELVMGGDLS KHVISGKLLP IADVLQIAFK
     CCGALEYAAA QGIVHRDIKP ANIMIAQGTE VKIADFGAAF LKKSQVVQTA AMGSPYYMSP
     EQIQGKEVSF HSDMYSLGVV LYELLTGGRP FGGKNIEALM QKIIQEEAAP PSSLRADLPK
     PLDSLVLRAL KKDPKQRYPT WAEFALEITK IGPLVLPAGA ISDSEKYTML KSVPMLSTLA
     DSELWELARA GKWARLAKGK QIVKEKEKGT SFFFLAKGEA KVTKGPRLLN MVSGTEFFGE
     MAWIAGGEAR HATVESHTEV LISEFEPMAL EKMSLGAQLQ LTRALVRNVA DRLALANTRL
     AR
//
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