ID E3FU28_STIAD Unreviewed; 1325 AA.
AC E3FU28;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=Conserved uncharacterized protein {ECO:0000313|EMBL:ADO72168.1};
GN OrderedLocusNames=STAUR_4388 {ECO:0000313|EMBL:ADO72168.1};
OS Stigmatella aurantiaca (strain DW4/3-1).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Archangiaceae; Stigmatella.
OX NCBI_TaxID=378806 {ECO:0000313|EMBL:ADO72168.1, ECO:0000313|Proteomes:UP000001351};
RN [1] {ECO:0000313|EMBL:ADO72168.1, ECO:0000313|Proteomes:UP000001351}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DW4/3-1 {ECO:0000313|EMBL:ADO72168.1,
RC ECO:0000313|Proteomes:UP000001351};
RX PubMed=21037205; DOI=10.1093/molbev/msq292;
RA Huntley S., Hamann N., Wegener-Feldbrugge S., Treuner-Lange A., Kube M.,
RA Reinhardt R., Klages S., Muller R., Ronning C.M., Nierman W.C.,
RA Sogaard-Andersen L.;
RT "Comparative genomic analysis of fruiting body formation in Myxococcales.";
RL Mol. Biol. Evol. 28:1083-1097(2011).
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; CP002271; ADO72168.1; -; Genomic_DNA.
DR STRING; 378806.STAUR_4388; -.
DR KEGG; sur:STAUR_4388; -.
DR eggNOG; COG0457; Bacteria.
DR eggNOG; COG0515; Bacteria.
DR eggNOG; COG2114; Bacteria.
DR eggNOG; COG3899; Bacteria.
DR HOGENOM; CLU_004435_3_2_7; -.
DR Proteomes; UP000001351; Chromosome.
DR GO; GO:0004016; F:adenylate cyclase activity; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
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 SMART; SM00028; TPR; 4.
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; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50005; TPR; 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}; TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339}.
FT DOMAIN 50..322
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 339..445
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT REPEAT 1268..1301
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT BINDING 79
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1325 AA; 147383 MW; 37E7E9540B68B1BB CRC64;
MLAAEVEMPG GSDDDSDFDD ALIREVARAP PPLPLPGVGE HLGGKTGQRF EILAPLGVGS
MGRVFRAWDL ELQRVVALKF IPPHEALGEA PLRTLLREAR AIAQLDHENI VRVFDMSEWS
GQVWEPRVPF LIMECLQGES LSSLLERERL PLGRALEIMV GIAAGLAHAH EHQVIHRDLK
PSNVFINQRG TAKLLDFGLA HLLSSGPSAL PHLPSAGTPV YMAPEQWQGE AQDERTDIWA
AGAVFYEMLT GEPPYPHSTS LEDLRAQVAS AEPVPSVRGR NPELPQEVEQ LLATALAKEP
ARRFPTAQEF GEELQELAHR FGHRPAVHRP SAPERRQVTL VSCALCGLAS GPKRLDEDDL
GELEEAFLQC CEEILQRHGG TLAMSLGDEV LACFGYPVAR EEDTERAVRA GLELVQEVPR
VLHRQMAALP LGTLAVKAGL HTGKVALRAH PRESPGALLV IHGEALKAAP WVASQAEPGV
LLVSQSTWAL VRGAFEARPV GSRMFESPSG VRPLGLYRVL QERPSEFRFD RVLAAGGLTP
LVGREPELRR LLTYWEGAQR GHGALVLVSG EAGIGKSRLI QELHAHMTLE EAAHFQCQCW
PQFSASAFHP LIEMLRRRLP EFPLPGLTAE HEYLLSALLE VSAAGAPPRP PPSLDRWKER
TLQALLSLLL RTARERPVLA IIEDVHWADP STLEFLGLVL ENMERERLLV VLSERPDFRP
AWPPRPWLHR MEVERLPAKL TARMVREAAR GRALPEETVQ QLALKTDGIP LFVEEMTHMV
LERAPDGEAP VSGEGAAIPG TLHELLLARL DLLPSRQRTL AQVCAVVGRG IPLALPAAVL
RRDEAGVRRD LEGLVAAGLL QPQAVGWEAG YQFRHMLLQD AALHALPRST RREYHRRIAE
VLEERFPDMV AFQPEVLAHH HTEAGEYALA IRSWYRAGQR ASLRSAHPEA VSHFQRALKL
LKSLPDADQR ASEELELLIA LGTPLAQIQG YRSPSVERIY ARARELFQQV GEDLPRLELS
YWGPFAYYFS RAEYPLAHEL AERLVDLGRR QHHQELLALG HRMMASILFI WGQIPAAQEH
ILQALENSRF ELAQHQQLAE KHWVNPRVMA LAFGAMVLSV MGRDAEAQRF SHEALQLSRS
IGHPHTTASA LTYITVACHL RRDVEGALRW ADEAIAIASE HGFPAWQLWC TLVRIWALSE
RGEAREGLTL MREGISRWSR LGIRAGLYQH NLGLLAEMHL KLGQPREALE LLPSALHRPE
TAEHFYEAEL IRLRGEALRA LGREEEALAC FRQALQIARS QEAHAFEQRA LEALGAHSEE
ASPAS
//
