ID Q08YT6_STIAD Unreviewed; 1401 AA.
AC Q08YT6;
DT 31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2006, sequence version 1.
DT 24-JAN-2024, entry version 88.
DE SubName: Full=Putative adenylate cyclase {ECO:0000313|EMBL:EAU65617.1};
GN ORFNames=STIAU_6477 {ECO:0000313|EMBL:EAU65617.1};
OS Stigmatella aurantiaca (strain DW4/3-1).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Archangiaceae; Stigmatella.
OX NCBI_TaxID=378806 {ECO:0000313|EMBL:EAU65617.1, ECO:0000313|Proteomes:UP000032702};
RN [1] {ECO:0000313|EMBL:EAU65617.1, ECO:0000313|Proteomes:UP000032702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DW4/3-1 {ECO:0000313|EMBL:EAU65617.1,
RC ECO:0000313|Proteomes:UP000032702};
RA Nierman W.C.;
RL Submitted (APR-2006) 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:EAU65617.1}.
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DR EMBL; AAMD01000076; EAU65617.1; -; Genomic_DNA.
DR PATRIC; fig|378806.16.peg.4684; -.
DR Proteomes; UP000032702; Unassembled WGS sequence.
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; 1.25.40.10; Tetratricopeptide repeat domain; 1.
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 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; 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; 1.
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.
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}.
FT DOMAIN 105..380
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 394..528
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 51..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 134
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1401 AA; 155304 MW; B5A42C497CE412D4 CRC64;
MRRRQRACGR AGALHHSPAQ EGSFRGRLPG TCPGDGRPLT SHRAPCRTVC QGTPEGDEMR
QDGMESDEAS EELDDVFLRH VAQVSVPLRT PMRGESLGGQ DGRRFEIREQ LGGGSMGLVF
RARDQELQRV VALKFLHLRD RGSEEPMSAL LRQEAKAIAQ LDHENIVRIF DVAEWIGEPW
EPKVPFLIME CLEGEPLSAL LSRELPPLRR CIDIMRGMAA GLAHAHEHHI VHRDLKPGNV
FITRSGQVKL LDFGLAYLTD AVSPAAPHLP AAGTPAYMAP EQWLGQAQDA RTDIWAAGIV
LFEMLTGELP CSEMSLVGLK EWALSPAPVA SVRERRPELP EDVEQLLATM LAKAPEQRLA
SAAELGERLR QLEAGLTPWS GEMASLGPQR RQVTLVACWL SDLAGLAEHL DAEDFSDLEG
AFHQACSEIL AQHGGSITTC MGDEVLACFG YPQAREDDSE KAARAGLHLV THLGAVIQQK
LPYLPRRKLT VKVGLHTDTV VLDNLLPGLQ GRTAALQGEA PKMAFWLARQ AAPESVCLSH
TAWHLVRDAF RTEPMGVHSF QGLSGEVKGA IYRLVREKRT TRSRFERAHE SGGLTPWVGR
EAELRRLLGY WEQAQQGSGA FVLVQGEAGI GKSRLLQELR ERISLEGGSR LHVQCWAQFS
SSALRPIIEL LLSVLKLDPE GNPQSNLRKL QGRMGAVGLP IEHVRMLAAF LSLPVAELPP
HMRVAPERQK EKTFEALVTL LLRMTEDRPV FAVVEDLHWA DPSTLELLGA LLGHVGNARL
CVFLSARPDF KPAWAENPRV HPVPLERLSP QQTAELIRLS TIGKALPDET VEQLVAKTDG
VPLFAEEMTR MVVEQAPAGT AAGPPSTIPI TLSGLLLARL DMLPRQQKTL AQLCAVVGRG
FSHSLLTALS GRSPVNLQRD LTGLLQAGLL QQEEVASEAR YRFRHALIQD AAYHSLLRRT
RREYHRRIAQ TLAIQAPELA ETQPELLAHH YTEAGENERA IRLWTKAGEQ ASLRSANVEA
LRHLGQALRL LGTLPDTRAR SEQELQLRVA FGMPLMQLRS LRSREMEQNY SRVMELLHQV
GDAMPRLSIS TWGTYAYAFG RAKFHVAQEL AELTVGQGER QHSRELLALG HRMIATNHFT
WGNMSTALEH VDAALEFSDF DLAQHRELAV RQWVNPRVAA LAYGSVVLSA VGRDALARRY
GDEAVTLAEK IGHPHTLGFG LTYVALGCQL RKEPGCAQQW VERCIAISSE HHFRLWLGWS
VFIKSWLLAE QGRVQEGLTL MQANLARWRN AGIRAGMPLF LGMFAELHLK LGQFTQGMAA
VTHALGWAET LEERSYEAEL RRLEGELHRA LGNESAATES FSQARAVARL QGSAGFGRRA
EESLNRQFRE LGWDRGHAHP R
//
