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Database: UniProt
Entry: Q8TU70_METAC
LinkDB: Q8TU70_METAC
Original site: Q8TU70_METAC 
ID   Q8TU70_METAC            Unreviewed;      1274 AA.
AC   Q8TU70;
DT   01-JUN-2002, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2002, sequence version 1.
DT   27-MAR-2024, entry version 117.
DE   SubName: Full=Signal-transducing histidine kinase {ECO:0000313|EMBL:AAM03656.1};
GN   OrderedLocusNames=MA_0203 {ECO:0000313|EMBL:AAM03656.1};
OS   Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS   C2A).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=188937 {ECO:0000313|EMBL:AAM03656.1, ECO:0000313|Proteomes:UP000002487};
RN   [1] {ECO:0000313|EMBL:AAM03656.1, ECO:0000313|Proteomes:UP000002487}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A
RC   {ECO:0000313|Proteomes:UP000002487};
RX   PubMed=11932238; DOI=10.1101/gr.223902;
RA   Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA   Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA   Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA   McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA   Cann I., Graham D.E., Grahame D.A., Guss A., Hedderich R., Ingram-Smith C.,
RA   Kuettner C.H., Krzycki J.A., Leigh J.A., Li W., Liu J., Mukhopadhyay B.,
RA   Reeve J.N., Smith K., Springer T.A., Umayam L.A., White O., White R.H.,
RA   de Macario E.C., Ferry J.G., Jarrell K.F., Jing H., Macario A.J.L.,
RA   Paulsen I., Pritchett M., Sowers K.R., Swanson R.V., Zinder S.H.,
RA   Lander E., Metcalf W.W., Birren B.;
RT   "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT   physiological diversity.";
RL   Genome Res. 12:532-542(2002).
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DR   EMBL; AE010299; AAM03656.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8TU70; -.
DR   STRING; 188937.MA_0203; -.
DR   EnsemblBacteria; AAM03656; AAM03656; MA_0203.
DR   KEGG; mac:MA_0203; -.
DR   HOGENOM; CLU_000445_114_57_2; -.
DR   InParanoid; Q8TU70; -.
DR   PhylomeDB; Q8TU70; -.
DR   Proteomes; UP000002487; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd00130; PAS; 5.
DR   Gene3D; 2.10.70.100; -; 1.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 5.
DR   InterPro; IPR003018; GAF.
DR   InterPro; IPR029016; GAF-like_dom_sf.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR025847; MEDS_domain.
DR   InterPro; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013656; PAS_4.
DR   InterPro; IPR013767; PAS_fold.
DR   InterPro; IPR013655; PAS_fold_3.
DR   InterPro; IPR011495; Sig_transdc_His_kin_sub2_dim/P.
DR   NCBIfam; TIGR00229; sensory_box; 5.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   PANTHER; PTHR43065:SF23; SENSOR HISTIDINE KINASE PDTAS-RELATED; 1.
DR   Pfam; PF13185; GAF_2; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF07568; HisKA_2; 1.
DR   Pfam; PF14417; MEDS; 1.
DR   Pfam; PF00989; PAS; 1.
DR   Pfam; PF08447; PAS_3; 1.
DR   Pfam; PF08448; PAS_4; 2.
DR   Pfam; PF13426; PAS_9; 1.
DR   SMART; SM00065; GAF; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00086; PAC; 5.
DR   SMART; SM00091; PAS; 5.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF55781; GAF domain-like; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 5.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 5.
DR   PROSITE; PS50112; PAS; 5.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:AAM03656.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002487};
KW   Transferase {ECO:0000313|EMBL:AAM03656.1}.
FT   DOMAIN          217..287
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          276..339
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          521..567
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          595..646
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          700..744
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          746..798
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          795..864
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          868..920
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          921..991
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          993..1045
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          1053..1271
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   COILED          497..531
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          634..682
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          904..931
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1274 AA;  144136 MW;  1E1D0856818AA589 CRC64;
     MYHQNWRKYG MRKYLRNSGI DIVGNVSFGT HFCQFYQTKE DLMDMLVPYF KAGLESNEFC
     MWVTSQPLEV EKAKKALRKS VPDLDIYLEK GQIEIIPCTC WYLNEGIFDS RRILNGYVEK
     LDQALANGYD GLRLSESTFW GGKKDWNNFV NYEKEIDRVI GNYHMLALST CPLDRCSATE
     IIEVVSSHQF SLIKKEGKWE REDNFGRKKA EEAAVRDAGD WEQTFDAIPD LIAILDTEYQ
     IVRANRAMAV KLGVTPEECI GQTCYRIIHG KSKPPSSCPH RQLLKDGAEH TAEVYEDCLG
     GYSIVSVSPL YDSKGKLTGS IHVARDINER KQEEHRIHRY NRILGEINRI FSNVVQAKTE
     KELGNACLSV ALEMTGSQIG FIGELGIDGI LHDIAISESG LDQCLMYDKT GHRYRPGVLV
     VHGLYGSVVN SGKSFFTNDP PSHFDSIGVP NGHPPLTSFL GVPLVQDGKT IGVLTVANRE
     GGYSCEQQED LEAIAPAVTQ ALQRKKAEQE RKRAEEALIR RENEFRTLAE NSPDMIARFD
     RQNHHTYVNP AAAEVYDLSQ EEIIGKTHSE LGRNLKHVTF WEKHNEKVFT TGNSETMEFH
     YTSSQGKECH FNTRIVPEFV NGKVTSVLAI SRDITDIKEA EAKLKETLDN LENLVKERTA
     QLEKAYNLLK ENEKGLAEAQ RMAHLGNWDW NLVTGEIHCS DELYRIFGLN PREFSTICSE
     ALSYVHPDDR DHVNDAIKKA LDGKPCSIDF RIISTDGAER IVHAQGEVVC DEKNTPVRIK
     GIVQDITERK RAEEKIQILA NAVESSDDAI ITKSLDGIIT SWNKGAEKVY GYSAEEVLGK
     PISILEPSFF GGETKKLTEM VKQGERVHHH ETMRLRKDGT RISVSMALSP VFDIHGNLTA
     ISAITRDITE SKRAEDKLRE SEEKYRNIVE TANEGVLIID DNAMITYANK KMTDMSGYRL
     EEGIGRSIWD FISEGSKAIA KLNLKRRRQG ANGSYELKLI RGDGSPLWVL INAKSLFDKD
     GKFAGSLSML TDVTERKEAE ETLANLEIAR KKEIHHRIKN NLQVISSLLD LQAEKFNSRE
     DIKDSEVLEA FRESQDRVIS MALIHEELYK GGEFDTLDFS SYIEELTENL FLTYRLGNTD
     ISLNMDLEEN IFFDMDTAVP LGMIINELVS NSFKYAFQGR NRGEIRIKFR REENGKYINS
     GVKSKNGGCK SNNFTLTVSD NGVGIPENFD IEDLDSLGFQ LITSLVDQLD GKLELKRNNG
     TEFTVRFTVR DKNE
//
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