ID A0A1F5ARN5_9BACT Unreviewed; 1406 AA.
AC A0A1F5ARN5;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OGD21052.1};
GN ORFNames=A2W03_10250 {ECO:0000313|EMBL:OGD21052.1};
OS Candidatus Aminicenantes bacterium RBG_16_63_16.
OC Bacteria; Candidatus Aminicenantes.
OX NCBI_TaxID=1797273 {ECO:0000313|EMBL:OGD21052.1, ECO:0000313|Proteomes:UP000178699};
RN [1] {ECO:0000313|EMBL:OGD21052.1, ECO:0000313|Proteomes:UP000178699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGD21052.1}.
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DR EMBL; MEYB01000050; OGD21052.1; -; Genomic_DNA.
DR Proteomes; UP000178699; Unassembled WGS sequence.
DR GO; GO:0004016; F:adenylate cyclase activity; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0009190; P:cyclic nucleotide biosynthetic process; IEA:InterPro.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR CDD; cd07302; CHD; 1.
DR CDD; cd14014; STKc_PknB_like; 1.
DR Gene3D; 3.30.70.1230; Nucleotide cyclase; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR001054; A/G_cyclase.
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; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR16305:SF28; ADENYLATE CYCLASE 10; 1.
DR PANTHER; PTHR16305; TESTICULAR SOLUBLE ADENYLYL CYCLASE; 1.
DR Pfam; PF13191; AAA_16; 1.
DR Pfam; PF00211; Guanylate_cyc; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00044; CYCc; 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 SUPFAM; SSF48452; TPR-like; 2.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 1..247
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 278..406
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
SQ SEQUENCE 1406 AA; 159303 MW; C4123870D20ED118 CRC64;
MGVVYKAEDI KLGRMVAIKL LPAELTDDLE ARERFVHEAR TASALDHPNI CSIYEIDETV
EGQIFIAMAF YSGRALQNKI KQSPPSIKET IDIVMQVARG LSKAHSKGIV HRDIKPANVM
IGEDGLVKIV DFGLAKLARG TPLTRTSEIM GTLAYMSPEQ AGGESVDQRT DIWSLGVMFY
ELLTGQQPFQ GDNEPSMLHA IIHKTPRPPR DLKDDIPEEA EWIVLNCLQK QPERRPQSAD
RLISDLTKLK ISLEKEKEDL ATKKRLAAGR ETERRQATIL SGEILGYSEV LESLETEEAA
LVIDRCFTML DSVIRKYESR IDEITGGRFM ASFGIPLALE DAPKKAINAA IELRNSLEAF
NTSENLRIPL QVRIGINSGT VVAGVDASGK VYSVIGEEVR LAAQLRDISL KNNITVGPLT
YRYAKDNFEF VALESVSLEG RTEPITVFKL LSAKERVYRA RLGVERMIYS DMVGRENELD
KLKLHVLKAI NGEGSIVNLV GEAGLGKSRL IEELNRSDEL KKVTLLRGRA LSIGANLSFH
PVMDILKSWA QIKEEDPPAV SAQKLEKVIR SVSPEGVSEI FPFMATLMGI KLTGKHAERI
KGIEGDALEK LILKNIRDLI AKASLIKPLV FVLEDIHWAD STSVDLFESL FRLAESKSIL
FINVVRPNYE TSERILRTIR NRYPAFSTEI HLEPLDDSQC EALIGNLLNV KALPGRIKEL
IARRAEGNPF FIEEVARSFI DDGVVEIENG RFRVTEKIDS VIIPETINDL VMARFDKLGE
QTKSLLRSAS VIGRNFFYKI LTDVAKSVED IDDKLEHLKE VQLIKERRRM NELEYMFKHA
LAWDAVYNSI LLKKRKQLHL DVARSIESVF CERLQEFYGM LALHYSRGEN LEKSEEYLTK
AGEEALKTAA SNEALSYFQE ALSLYLKKHG AAGDPGKIAH LEKSIALALY NKGRYAESLI
YFDNVLDYLG VKRPKNKLLS TINLLLNLSN VLLNLYLPRK KKTMMPTAKD NEIADLMYKR
GEVLSSLDRT RFFMDSIGLI RRLNKLDLTG IENGTTHYAA SSALFSVSGV SFRISKKILD
YSSRFIDKKD KKSIFRITVY QLLLDCLAGN WEKNPEYDQS LIDDMLKLGD MFLPRIQLSW
SGLIRLEQGK FDDANVLAEK LTEIGADYEH DGAISGKYSL KTLLLLKKRQ LDDALDEANQ
GIEVQKSMHK THLLLEMLAL KSNILIIQRE MDGAAKTLAE AKELLVRERH ITPFYMGHFL
LSQFLSDLFL FEESIESNEV SKISRLRKKT YQSGRAARKN ALNYAANKTE VFRCLGVYYW
LAGKQKKAIR WWRKSVTIGR GLQALPELAR SYMEIGKRLM EKQSQFSEID GRNNKWYLKE
AEKIFKKLNL EWDIQELSKL MILEED
//
