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Database: UniProt
Entry: U5DMY7_9CHRO
LinkDB: U5DMY7_9CHRO
Original site: U5DMY7_9CHRO 
ID   U5DMY7_9CHRO            Unreviewed;      1198 AA.
AC   U5DMY7;
DT   11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   SubName: Full=PAS domain S-box {ECO:0000313|EMBL:ERN41979.1};
GN   ORFNames=KR51_00013100 {ECO:0000313|EMBL:ERN41979.1};
OS   Rubidibacter lacunae KORDI 51-2.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Chroococcales; Aphanothecaceae; Rubidibacter.
OX   NCBI_TaxID=582515 {ECO:0000313|EMBL:ERN41979.1, ECO:0000313|Proteomes:UP000016960};
RN   [1] {ECO:0000313|EMBL:ERN41979.1, ECO:0000313|Proteomes:UP000016960}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KORDI 51-2 {ECO:0000313|EMBL:ERN41979.1,
RC   ECO:0000313|Proteomes:UP000016960};
RA   Choi D.H., Noh J.H., Kwon K.-K., Lee J.-H., Ryu J.-Y.;
RT   "Draft genome sequence of Rubidibacter lacunae KORDI 51-2.";
RL   Submitted (MAY-2013) 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:ERN41979.1}.
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DR   EMBL; ASSJ01000035; ERN41979.1; -; Genomic_DNA.
DR   RefSeq; WP_022605834.1; NZ_ASSJ01000035.1.
DR   AlphaFoldDB; U5DMY7; -.
DR   STRING; 582515.KR51_00013100; -.
DR   eggNOG; COG2202; Bacteria.
DR   eggNOG; COG2203; Bacteria.
DR   eggNOG; COG2205; Bacteria.
DR   eggNOG; COG3920; Bacteria.
DR   InParanoid; U5DMY7; -.
DR   OrthoDB; 415062at2; -.
DR   Proteomes; UP000016960; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd00130; PAS; 5.
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; 6.
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; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
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; 6.
DR   PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF01590; GAF; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF07568; HisKA_2; 1.
DR   Pfam; PF00989; PAS; 2.
DR   Pfam; PF08447; PAS_3; 1.
DR   Pfam; PF13426; PAS_9; 3.
DR   SMART; SM00065; GAF; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00086; PAC; 5.
DR   SMART; SM00091; PAS; 6.
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); 6.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 2.
DR   PROSITE; PS50112; PAS; 5.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000016960}.
FT   DOMAIN          89..159
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          332..402
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          406..458
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          452..499
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          571..644
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          645..697
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          867..904
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          999..1193
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   1198 AA;  134174 MW;  179068B70ACB45B1 CRC64;
     MNYQHLLDRI AAVARRIPNS PHLRSLQTAD SEGTIDPETL RTQLDLDRRR RRLLADELQA
     LVEELPASLG ERSSGHSDRD RVEQKLLHEK NLSDTIVDSL PGAFFILAED NHLLRWNRQL
     ERACGYTSED IERLDPMVLF APSERSRLRA HIEAAFACGE ASTEATLVGK DGNKSTWFIS
     GRCLDLDGQR CLLGVATDIT QRQRAEVERQ KLAALVENST DFIGIADLDG RIEFLNPAGC
     RLVDAEAASG TIADYLGPNL AKCFDREVLP VVRDRGQWNG ETVLRGRGDR QIPVSINAFL
     IRDCTTGNPL KIATIARDIS TSKRVEAELQ ASDEKCRSVV DGLKEVIFQT DAAGCWTFLN
     PAWTELTGFD TERNLGRPIA EFVHPDEQTR HRQHFAPLLA AKKDTCRYEI RFHTCSGGDC
     WLELAARARR NANGAIVGTT GTLNDITERK QAEDRLRAVI DTVPGFVSWV GRDGRYLGVN
     QRMAQTLNLT PEDLVGQELG FLKTSPSYAN FMRDFLASSR QTASQTIATQ TNGTARTYLI
     AAQKYRQGSA AVSVGIDITE RKQAELALRE SEEKFRQLAE NIEQVFWMTD LSRQEAIYVS
     PAYEQTWGRS LETAYCSPQD WLLYVHPHDR DRVAAALPLQ LYGEYDIEYR LQRPNGEVRW
     IHDRAFPVRD GNGHIYRLAG IAQDITESKR AKEALERRER YLTALVGVQR RLLAAGTNRN
     LYSEAISILG LVSAASRIHV YENTCDENGC WRAHERAAWH APDVPPNARP ELDYSTLSDD
     WRSRLLAGEI RQGIVAELPA GERHFFSAED ALAFLVLPLF VNGNFFGSIV FDNCREAREW
     QPLEVGLLSS AAAAIALAKE RQLAQEQLQR QLTAIETTTD GIFIVNAADE LQYVNPAYVQ
     MLGYDNTHDL LGTHWCDYYP SEDSDPIATK LRPELLTAGK WSGEIDALHR SGRTFVQELS
     VTATATGEAI GVCRDISDRK LAECELKASL EEKELLLKEV HHRVKNNLQV ISSIFSLQSQ
     AIADPQALAL LEDSQNRIGS MALIHEKLYQ SARLANIDFS DYIRDLTEHL IASYNANPAW
     IETDTHIDDV RLTLDSAIPC GLLINELVSN ALKHAFPDGR RGRIAIEFRT LEDGNLRLRV
     EDNGVGLPEG LDSNETNSLG LSLIASLAEQ LRGRLQVTNT TGACFEVVFP QPQERRRF
//
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