ID A0A229TKA8_9PSEU Unreviewed; 786 AA.
AC A0A229TKA8;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Histidine kinase {ECO:0000313|EMBL:OXM71608.1};
GN ORFNames=CF165_00675 {ECO:0000313|EMBL:OXM71608.1};
OS Amycolatopsis vastitatis.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=1905142 {ECO:0000313|EMBL:OXM71608.1, ECO:0000313|Proteomes:UP000215199};
RN [1] {ECO:0000313|Proteomes:UP000215199}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H5 {ECO:0000313|Proteomes:UP000215199};
RA Adamek M., Alanjary M., Sales-Ortells H., Goodfellow M., Bull A.T.,
RA Kalinowski J., Ziemert N.;
RT "Comparative genome mining reveals phylogenetic distribution patterns of
RT secondary metabolites in Amycolatopsis.";
RL Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
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:OXM71608.1}.
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DR EMBL; NMUL01000001; OXM71608.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A229TKA8; -.
DR OrthoDB; 23692at2; -.
DR Proteomes; UP000215199; Unassembled WGS sequence.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd01948; EAL; 1.
DR CDD; cd01949; GGDEF; 1.
DR CDD; cd00130; PAS; 3.
DR Gene3D; 3.30.70.270; -; 1.
DR Gene3D; 3.20.20.450; EAL domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 3.
DR InterPro; IPR001633; EAL_dom.
DR InterPro; IPR035919; EAL_sf.
DR InterPro; IPR000160; GGDEF_dom.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR NCBIfam; TIGR00254; GGDEF; 1.
DR NCBIfam; TIGR00229; sensory_box; 3.
DR PANTHER; PTHR44757:SF11; DIGUANYLATE CYCLASE DGCE-RELATED; 1.
DR PANTHER; PTHR44757; DIGUANYLATE CYCLASE DGCP; 1.
DR Pfam; PF00563; EAL; 1.
DR Pfam; PF00990; GGDEF; 1.
DR Pfam; PF13188; PAS_8; 1.
DR Pfam; PF13426; PAS_9; 2.
DR SMART; SM00052; EAL; 1.
DR SMART; SM00267; GGDEF; 1.
DR SMART; SM00091; PAS; 3.
DR SUPFAM; SSF141868; EAL domain-like; 1.
DR SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR PROSITE; PS50883; EAL; 1.
DR PROSITE; PS50887; GGDEF; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 2.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:OXM71608.1};
KW Transferase {ECO:0000313|EMBL:OXM71608.1}.
FT DOMAIN 140..178
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 238..282
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 316..368
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 394..528
FT /note="GGDEF"
FT /evidence="ECO:0000259|PROSITE:PS50887"
FT DOMAIN 537..786
FT /note="EAL"
FT /evidence="ECO:0000259|PROSITE:PS50883"
SQ SEQUENCE 786 AA; 84314 MW; 52CADE1D2449F607 CRC64;
MEADAVAASG PAEPSADPAE LVELSPDAIC VHRNGVLTYA NLAALDTFAA RSADEVVGRR
FIDFVAEESQ STWVEELAKL TKPGAATKPV EALMCRLDGS KFAVETVSVR LHDHLAYQVV
MRDITAKKAA ADALHYQAAL VSHVSDALIA TTGEGVVTSW NPAAEAVYGW TAAEAVGRCA
SELVGAPLDL PAIRRGGGVA EAVHRRRDGA PLAVRVSAAE MNDGYVLVCA DETARRRAEQ
NYRTVVASLD EGVLVMGASG LIEAANPAAC RILGVAEADL IGVPCHTLVL FTESGQWIPP
DEMPSVQTRR TGVTHNGLVV RLRRPDGRDV WVSLTSRLLN PDDPAATAVV TSFTDITETR
AISARLAHDA THDPLTRLGN RTLVLGRLDA RDRGAVTVLF LDLDKFKVIN DSLGHSVGDQ
VLRIVGERLR RSSGRDDLVG RLGGDEFVVV TGEVTDPGEV RALAEHLRAA LAEPIGVLGR
QLHLDASIGV VLVGRDDRRS AEDLLRDADV AMYQAKTLGR GRHHFFDVGL RERMQRRLRM
EQDLRDAVSS DQLWPAYQPV VDLRTGEMVA VEALLRWTHP RHGAISPAEF IPLAEESDLI
NVIGKEMLRA TTRELASRRS GQGLDLTLKV NLSARQLDDP HLVPAVEDAL ANTGLPAAAL
CLEVTESALM RDQAAAAEVL ASLRSLGVLL AIDDFGTGYS SLAQLRSLTL DTLKIDRSFI
TGIAESRDAA AIVTSIIAMA HAVDLTVIAE GVESAEQLEL LRTLGCDQAQ GYHLGRPVPA
AELFGQ
//
