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Database: UniProt
Entry: K9ZKN9_ANACC
LinkDB: K9ZKN9_ANACC
Original site: K9ZKN9_ANACC 
ID   K9ZKN9_ANACC            Unreviewed;       554 AA.
AC   K9ZKN9;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   SubName: Full=Response regulator receiver protein {ECO:0000313|EMBL:AFZ59756.1};
DE            EC=1.8.1.9 {ECO:0000313|EMBL:AFZ59756.1};
GN   OrderedLocusNames=Anacy_4396 {ECO:0000313|EMBL:AFZ59756.1};
OS   Anabaena cylindrica (strain ATCC 27899 / PCC 7122).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Anabaena.
OX   NCBI_TaxID=272123 {ECO:0000313|EMBL:AFZ59756.1, ECO:0000313|Proteomes:UP000010474};
RN   [1] {ECO:0000313|Proteomes:UP000010474}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27899 / PCC 7122 {ECO:0000313|Proteomes:UP000010474};
RX   PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA   Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA   Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA   Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA   Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT   "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT   genome sequencing.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
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DR   EMBL; CP003659; AFZ59756.1; -; Genomic_DNA.
DR   RefSeq; WP_015216372.1; NZ_AP018166.1.
DR   AlphaFoldDB; K9ZKN9; -.
DR   STRING; 272123.Anacy_4396; -.
DR   KEGG; acy:Anacy_4396; -.
DR   PATRIC; fig|272123.3.peg.4789; -.
DR   eggNOG; COG0492; Bacteria.
DR   eggNOG; COG3437; Bacteria.
DR   HOGENOM; CLU_031864_5_8_3; -.
DR   OrthoDB; 109585at2; -.
DR   Proteomes; UP000010474; Chromosome.
DR   GO; GO:0004791; F:thioredoxin-disulfide reductase (NADP) activity; IEA:UniProtKB-EC.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   PANTHER; PTHR48105:SF5; BLR1248 PROTEIN; 1.
DR   PANTHER; PTHR48105; THIOREDOXIN REDUCTASE 1-RELATED-RELATED; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00469; PNDRDTASEII.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:AFZ59756.1};
KW   Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010474}.
FT   DOMAIN          5..128
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         62
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   554 AA;  61030 MW;  7D5F88598A01B83B CRC64;
     MNKPMILTVD DDPQVLQAIA RDLRREYGDR FRILRADSGA QALEAIKELK LRNETVALFL
     ADQRMPQMTG IEFLQEAITI FPEAKRALLT AYADTDAAIA AINKTNINYY LTKPWDPPEE
     RLYPILNDLL DDWLASYHPP FEGIRVVGNR WSPDSHNIKD FLARNHVPYQ WLDIERDQEA
     QDLLNYSGEN KLSLPLVILG NGERLVKPSN IQIAEKVGLQ TQAKQPFYDL AIIGGGPAGL
     AAAVYGASEG LRTVMIEREA PGGQAGTSSR IENYLGFPVG LSGADLARRG VTQAKRFGVE
     ILTPQEVIGI RINDSYRYAL LKDGSEIACH ALMLAMGVSW RRLNVPGIEK LTGRGVYYGA
     AMTEAMECSN EQVYIIGGAN SAGQAAMHFS KFAKQVHMLV RADNLAKGMS QYLVDQIGAT
     ENIIVQLNSS VIEAKGEDSL EALTILNNVT DEQETVAANS LFIFIGAVPH TDWLEGIVER
     DERGFILTGP DLFKDGKRPK GWYADRDPYL LETSIPGIFA VGDVHHGSVK RVASGVGEGS
     ICVSFIHQYL AKVL
//
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