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Database: UniProt
Entry: A0A0V7ZV23_9CYAN
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Original site: A0A0V7ZV23_9CYAN 
ID   A0A0V7ZV23_9CYAN        Unreviewed;      1841 AA.
AC   A0A0V7ZV23;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=BC008_32160 {ECO:0000313|EMBL:KST68038.1}, BC008_32965
GN   {ECO:0000313|EMBL:KST68337.1};
OS   Mastigocoleus testarum BC008.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Hapalosiphonaceae;
OC   Mastigocoleus.
OX   NCBI_TaxID=371196 {ECO:0000313|EMBL:KST68038.1, ECO:0000313|Proteomes:UP000053372};
RN   [1] {ECO:0000313|EMBL:KST68038.1, ECO:0000313|Proteomes:UP000053372}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BC008 {ECO:0000313|EMBL:KST68038.1,
RC   ECO:0000313|Proteomes:UP000053372};
RA   Guida B.S., Garcia-Pichel F.;
RT   "Draft Genome of the Euendolithic (true boring) Cyanobacterium
RT   Mastigocoleus testarum strain BC008.";
RL   Genome Announc. 0:0-0(2015).
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
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:KST68038.1}.
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DR   EMBL; LMTZ01000083; KST68038.1; -; Genomic_DNA.
DR   EMBL; LMTZ01000066; KST68337.1; -; Genomic_DNA.
DR   RefSeq; WP_027842674.1; NZ_LMTZ01000083.1.
DR   OrthoDB; 517727at2; -.
DR   Proteomes; UP000053372; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd14014; STKc_PknB_like; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR041664; AAA_16.
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; IPR003661; HisK_dim/P.
DR   InterPro; IPR036097; HisK_dim/P_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   PANTHER; PTHR43642; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE G; 1.
DR   PANTHER; PTHR43642:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE G; 1.
DR   Pfam; PF13191; AAA_16; 1.
DR   Pfam; PF01590; GAF; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00065; GAF; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF55781; GAF domain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053372}.
FT   DOMAIN          13..273
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          1587..1838
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   COILED          1541..1578
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1841 AA;  209860 MW;  CB95B73180A88BE1 CRC64;
     MNIVCRSPII PGYQIREQLY AGSRTKVYRA LREQDSLAVV IKLLNSEYPS FNELLQFRNQ
     YAIAKNLDIP GVIHPLSLET FGNGYILVME DKGEISLDEY IKTHRLSLVE FLSLGIQLAD
     ILHNLYQNKV IHKDIKPANI LIDPETKQIQ LIDFSIASLL TKKTQEIKSP NLLEGTLAYI
     SPEQTGRMNR GIDYRSDFYS LGITLFEMLA GQLPFISDDP MDLVHCHIAQ QAFRISDIKS
     EIPEVISEVI SKLMAKNAED RYQSALGLKH DLETCLYQLK DSGEIRYFEI GQRDVCDHFL
     IPEKLYGREV EVQELLDAFK RVTNGSSEIM LVAGFSGVGK TAVVNEVHKP MTHQRGYFIQ
     GKFNQFNRNI PFSAFVQALR DLMGQLLSES DSQRLRWCTQ ILEAVGENGQ VLIEVIPELE
     ALIGKQPPVS ELSGAAAHNR FNLLFQNFIA VFAKADHPLV IFLDDLQWSD AASMESIKIL
     MSNSHLLLLG AYRDNEVSSV HPLMALLEKF KQAEVVINTI TLQSLSFDDT SRLVADILNC
     STPCTDKSVS ARSRPLTEFI FRKTQGNPFF TTQLLKALYQ NGNIKFNRDD HYWEWDLTQI
     DALFLTDDVV EFIAALLQKL SPETQKVLKL AACIGNHFDL ETLSIVYKKS YYQTARNLWE
     SLQEGLVIPQ GEIYKFFSDD FFTFEFDTEK YVNQERSGKI FYKFLHDRVQ QAVYTLIEDN
     QKKSVHLNIG RLLLSNLQCK SQEERLFEIV DHLNLGHELI TEERDIIELI KLNIHAGEKA
     KKSTAYVAFR DYLRIAQEYI GKSGWDDNYE LSFNIHRLLA EAEQLNGNFQ ESENLILLSL
     EKAQKKLEKA DLYNLFIIQY TMMGQGIMAV DIGRKSLHLF KINLPSTENI EKSLHNSFQN
     VTSKIRDISF QSWLELPEST VPQQRICLQL LNSLLVPSYI SQQEKLHFWL GTKIVELSYQ
     YGTVPASAYG FIVYGMFLGT ALANYKLGYD FGLLGLKLSR KYNKLDDITQ ACYIFGNNVY
     AWNQPLQGSE KIFDEGIQAG LASGNFLFLG YILIYKLLNP FYQGKNLEEI ISNLPECLLF
     VQKNNHQVGE DSILALDMII MNLLGHTSSL ESFDIDGCSE QKYLEKCQNN QSTYALCHYY
     ILKSMLLYLY DRVTESLYYS EETKKIIAVL AAKYQVAVHI FYYSLNIISL YSKASKSQQE
     KYWHKLSENQ EKMKLWAMNC PENFQHKFLL LEAEIARVTG KKIKAVNLYD HAIGKAKENK
     YLQEEALANE LAAKFYLSWG KDKIAAVYMQ GACYCYSRWG AKAKVDHLEQ QYPYLLATIL
     KTNNLNIKNS ANITSTSIEN VIRTSSSQNL SLDFPSVMKA AQAISQEIEL EKLLTTLMET
     AIANAGAQSG HLILCQDDNQ WFVVIQADNK PKQVSTFQEQ VQGEQIQHLE IPLKRYQKIP
     QSLIDLVRCT QKTAVFENLS SVVQFAGDHY IVTHKPKSVL CIPIIRQKKL IGILYLENNL
     TLGAFTLDRI EILQLLTSQA AISIENARLY QKTENYSQIL KSEVKRKTRA LNQKAQDLEQ
     ALRTLQRTQA QLIQNEKMSS LGQLVAGIAH EINNPISFIE GNLSYTKSYI EEMISLLGLY
     QQEYPQPSSV IKGKCEEIDL DFLFEDVTKI IKSMESGSNR IKQIVLSLRN FSRLDESAIK
     AVDIHSGIES TLLILQNRLQ GSENQREIKI IKEYCHNLPK ITCYPSELNQ VFLNIINNAI
     DAIRDNTQRG ENPEIGIRTK AIDEKWVSIG IANTDSTIPV NIQERIFEPF FTTKAVGRGT
     GLGLFVSYSI VQKHGGIVNV YSKPDEGTEF EIILPLQCAQ I
//
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