ID Q8P8F1_XANCP Unreviewed; 689 AA. AC Q8P8F1; DT 01-OCT-2002, integrated into UniProtKB/TrEMBL. DT 01-OCT-2002, sequence version 1. DT 27-MAR-2024, entry version 125. DE RecName: Full=PAS domain S-box protein {ECO:0008006|Google:ProtNLM}; GN OrderedLocusNames=XCC2291 {ECO:0000313|EMBL:AAM41570.1}; OS Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB OS 528 / LMG 568 / P 25). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=190485 {ECO:0000313|EMBL:AAM41570.1, ECO:0000313|Proteomes:UP000001010}; RN [1] {ECO:0000313|EMBL:AAM41570.1, ECO:0000313|Proteomes:UP000001010} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25 RC {ECO:0000313|Proteomes:UP000001010}; RX PubMed=12024217; DOI=10.1038/417459a; RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R., RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F.Jr., RA Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G., RA Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B., RA Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B., RA Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F., RA Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T., RA Leite R.P.Jr., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A., RA Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J., RA Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M., RA Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A.Jr., Rossi A., RA Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A., RA Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M., RA Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.; RT "Comparison of the genomes of two Xanthomonas pathogens with differing host RT specificities."; RL Nature 417:459-463(2002). RN [2] {ECO:0007829|PDB:4F3H, ECO:0007829|PDB:4F48} RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 437-684 IN COMPLEX WITH CYCLIC RP DIGUANOSINE MONOPHOSPHATE. RX PubMed=22993092; DOI=10.1107/S0907444912030594; RA Chin K.-H., Kou W.-T., Yu Y.-J., Liao Y.-T., Yang M.T., Chou S.-H.; RT "Structural polymorphism of c-di-GMP bound to an EAL domain and in complex RT with a type II PilZ-domain protein."; RL Acta Crystallogr. D 68:1380-1392(2012). 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; AE008922; AAM41570.1; -; Genomic_DNA. DR RefSeq; NP_637646.1; NC_003902.1. DR RefSeq; WP_011037435.1; NC_003902.1. DR PDB; 4F3H; X-ray; 2.50 A; A=437-684. DR PDB; 4F48; X-ray; 3.00 A; A=437-684. DR PDBsum; 4F3H; -. DR PDBsum; 4F48; -. DR AlphaFoldDB; Q8P8F1; -. DR SMR; Q8P8F1; -. DR STRING; 190485.XCC2291; -. DR EnsemblBacteria; AAM41570; AAM41570; XCC2291. DR KEGG; xcc:XCC2291; -. DR PATRIC; fig|190485.4.peg.2441; -. DR eggNOG; COG0745; Bacteria. DR eggNOG; COG2199; Bacteria. DR eggNOG; COG2200; Bacteria. DR HOGENOM; CLU_000445_70_50_6; -. DR OrthoDB; 7052318at2; -. DR Proteomes; UP000001010; Chromosome. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR CDD; cd01948; EAL; 1. DR CDD; cd01949; GGDEF; 1. DR CDD; cd00130; PAS; 1. DR Gene3D; 3.30.70.270; -; 1. DR Gene3D; 3.20.20.450; EAL domain; 1. DR Gene3D; 3.30.450.20; PAS domain; 1. 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; IPR035965; PAS-like_dom_sf. DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase. DR NCBIfam; TIGR00254; GGDEF; 1. DR NCBIfam; TIGR00229; sensory_box; 1. DR PANTHER; PTHR33121; CYCLIC DI-GMP PHOSPHODIESTERASE PDEF; 1. DR PANTHER; PTHR33121:SF82; FIMX; 1. DR Pfam; PF00563; EAL; 1. DR Pfam; PF00990; GGDEF; 1. DR SMART; SM00052; EAL; 1. DR SMART; SM00267; GGDEF; 1. DR SUPFAM; SSF141868; EAL domain-like; 1. DR SUPFAM; SSF55073; Nucleotide cyclase; 1. DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1. DR PROSITE; PS50883; EAL; 1. DR PROSITE; PS50887; GGDEF; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:4F3H, ECO:0007829|PDB:4F48}; KW Nucleotide-binding {ECO:0007829|PDB:4F3H, ECO:0007829|PDB:4F48}; KW Reference proteome {ECO:0000313|Proteomes:UP000001010}. FT DOMAIN 299..431 FT /note="GGDEF" FT /evidence="ECO:0000259|PROSITE:PS50887" FT DOMAIN 442..689 FT /note="EAL" FT /evidence="ECO:0000259|PROSITE:PS50883" FT BINDING 480 FT /ligand="3',3'-c-di-GMP" FT /ligand_id="ChEBI:CHEBI:58805" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:4F3H" FT BINDING 481 FT /ligand="3',3'-c-di-GMP" FT /ligand_id="ChEBI:CHEBI:58805" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4F48" FT BINDING 481 FT /ligand="3',3'-c-di-GMP" FT /ligand_id="ChEBI:CHEBI:58805" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:4F3H" FT BINDING 490 FT /ligand="3',3'-c-di-GMP" FT /ligand_id="ChEBI:CHEBI:58805" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:4F3H" FT BINDING 508 FT /ligand="3',3'-c-di-GMP" FT /ligand_id="ChEBI:CHEBI:58805" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:4F3H" FT BINDING 534 FT /ligand="3',3'-c-di-GMP" FT /ligand_id="ChEBI:CHEBI:58805" FT /ligand_label="2" FT /ligand_note="covalent" FT /evidence="ECO:0007829|PDB:4F3H" FT BINDING 653 FT /ligand="3',3'-c-di-GMP" FT /ligand_id="ChEBI:CHEBI:58805" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:4F3H" FT BINDING 654 FT /ligand="3',3'-c-di-GMP" FT /ligand_id="ChEBI:CHEBI:58805" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:4F3H" SQ SEQUENCE 689 AA; 76026 MW; C62FD2B62C18E793 CRC64; MQKGKDLTLR LMIVDDSVES AEAIVTALRN GGIAVRPSRP QTPEELGSML SGQIDLAVQG QAQQIPMSAL QQQIAGSGKD IPIIQLADRI EENALVEAAA HGVRAIALRH RTEHLLALVR SEWADLQARR GLRRIEAQMR ETERRCDALI ASSRDPIAYV HEGMHIRANE AYLEMFGFES FEDVEGVSLL DMIAAQYVDD FKQLLKALSK GEPPPAQYKV DARRLEGDTF PATMEFATAT YEGEPCIQVV FRRREEFDPE LAREVEDLRQ RDQVTGLLNR PTFMVALEQA VAQAGRSEGQ SGFLLIEPDH YARILPEIGL DSADALIASL AAHLASVLDD SVVAARFGEH SFALLMDGNY ARSHALAELV RDAFAQHVFS VGERSATVTV SIGGVQIGEK IASIGQVLNR GTEAVRTTAE LGGNAVSIFD PAAADRAEEE RIERWVEQLR EALIGDGFLL HYQPVLNLQG EPLELYQAFL RLERNGEMMS PNAFMAIAEE HDLITEIDRW VVARAIRQLG ERQRAGHKTH LLVRIGPNSF SDPQMIDTIR EQLAVYGVPG ERLWLQTPES KVFTHLRNAQ QFLASVSAMG CKVGLEQFGS GLDSFQLLAH FQPAFLKLDR SITGDIASAR ESQEKIREIT SRAQPTGILT VAEFVADAQS MSSFFTAGVD YVQGDFVAPT GPLMNYEFG //