ID A4TCY8_MYCGI Unreviewed; 388 AA. AC A4TCY8; DT 15-MAY-2007, integrated into UniProtKB/TrEMBL. DT 15-MAY-2007, sequence version 1. DT 27-MAR-2024, entry version 95. DE SubName: Full=Putative PAS/PAC sensor protein {ECO:0000313|EMBL:ABP46329.1}; GN OrderedLocusNames=Mflv_3857 {ECO:0000313|EMBL:ABP46329.1}; OS Mycolicibacterium gilvum (strain PYR-GCK) (Mycobacterium gilvum (strain OS PYR-GCK)). OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae; OC Mycolicibacterium. OX NCBI_TaxID=350054 {ECO:0000313|EMBL:ABP46329.1}; RN [1] {ECO:0000313|EMBL:ABP46329.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PYR-GCK {ECO:0000313|EMBL:ABP46329.1}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Mikhailova N., Miller C., Richardson P.; RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ABP46329.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PYR-GCK {ECO:0000313|EMBL:ABP46329.1}; RX PubMed=23469141; RA Badejo A.C., Badejo A.O., Shin K.H., Chai Y.G.; RT "A Gene Expression Study of the Activities of Aromatic Ring-Cleavage RT Dioxygenases in Mycobacterium gilvum PYR-GCK to Changes in Salinity and pH RT during Pyrene Degradation."; RL PLoS ONE 8:E58066-E58066(2013). CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000656; ABP46329.1; -; Genomic_DNA. DR AlphaFoldDB; A4TCY8; -. DR STRING; 350054.Mflv_3857; -. DR KEGG; mgi:Mflv_3857; -. DR eggNOG; COG2208; Bacteria. DR HOGENOM; CLU_672301_0_0_11; -. DR OrthoDB; 5241041at2; -. DR CDD; cd00130; PAS; 1. DR Gene3D; 3.30.450.20; PAS domain; 1. DR Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1. DR InterPro; IPR000014; PAS. DR InterPro; IPR000700; PAS-assoc_C. DR InterPro; IPR035965; PAS-like_dom_sf. DR InterPro; IPR013656; PAS_4. DR InterPro; IPR036457; PPM-type-like_dom_sf. DR InterPro; IPR001932; PPM-type_phosphatase-like_dom. DR NCBIfam; TIGR00229; sensory_box; 1. DR PANTHER; PTHR43156:SF2; MULTIDOMAIN REGULATORY PROTEIN RV1364C; 1. DR PANTHER; PTHR43156; STAGE II SPORULATION PROTEIN E-RELATED; 1. DR Pfam; PF08448; PAS_4; 1. DR Pfam; PF07228; SpoIIE; 1. DR SMART; SM00091; PAS; 1. DR SMART; SM00331; PP2C_SIG; 1. DR SUPFAM; SSF81606; PP2C-like; 1. DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1. DR PROSITE; PS50113; PAC; 1. DR PROSITE; PS50112; PAS; 1. PE 4: Predicted; FT DOMAIN 11..53 FT /note="PAS" FT /evidence="ECO:0000259|PROSITE:PS50112" FT DOMAIN 81..133 FT /note="PAC" FT /evidence="ECO:0000259|PROSITE:PS50113" SQ SEQUENCE 388 AA; 41675 MW; A92C7211FFEE1764 CRC64; MTDDPRPTGG LDDFFDSAPC GLLLTSPDGR IIRANETFSR WVGYRSEHLT GRQFPDLLAA GSRIHYETHF VSMLHMNGSL DGVAADLLTA DGTRLAGFVT ANVERDAAGA VVALRIAIQD ASERRSYERE LLETRRRADR ERERAQVLAA TLQRSLIPPT LSPPRGLTAA AHYHNASRDD VGGDFYDLFP MAEDRWGMFL GDVSGKGAGA AAVTSLTRYT LRAAAVNDRD PVAVLHTLDA VLSHEFHGDD PRFCTVIFGV ITAAPDGFDV QLATGGHPPA LLLPVDGPAR YVATPGGQAV GLIRNPRFVS TSVHLGPGDT LVMYTDGLTE AKTGRTRRFD DDDALLEFAG RHTPTDAGAF VEAVRVLLAS FGDGLEDDAA VIALSVPR //