ID Q4JAT2_SULAC Unreviewed; 185 AA. AC Q4JAT2; DT 02-AUG-2005, integrated into UniProtKB/TrEMBL. DT 02-AUG-2005, sequence version 1. DT 27-MAR-2024, entry version 76. DE SubName: Full=Conserved Archaeal protein {ECO:0000313|EMBL:AAY80097.1}; GN OrderedLocusNames=Saci_0718 {ECO:0000313|EMBL:AAY80097.1}; OS Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC OS 15157 / NCIMB 11770). OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae; OC Sulfolobus. OX NCBI_TaxID=330779 {ECO:0000313|EMBL:AAY80097.1, ECO:0000313|Proteomes:UP000001018}; RN [1] {ECO:0000313|EMBL:AAY80097.1, ECO:0000313|Proteomes:UP000001018} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770 RC {ECO:0000313|Proteomes:UP000001018}; RX PubMed=15995215; DOI=10.1128/JB.187.14.4992-4999.2005; RA Chen L., Brugger K., Skovgaard M., Redder P., She Q., Torarinsson E., RA Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.; RT "The genome of Sulfolobus acidocaldarius, a model organism of the RT Crenarchaeota."; RL J. Bacteriol. 187:4992-4999(2005). RN [2] {ECO:0007829|PDB:7NS8, ECO:0007829|PDB:7NS9} RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 2-185 IN COMPLEX WITH ATP; CA(2+) RP AND MG(2+). RX PubMed=34029589; DOI=10.1016/j.jbc.2021.100820; RA Vogt M.S., Ngouoko Nguepbeu R.R., Mohr M.K.F., Albers S.V., Essen L.O., RA Banerjee A.; RT "The archaeal triphosphate tunnel metalloenzyme SaTTM defines structural RT determinants for the diverse activities in the CYTH protein family."; RL J. Biol. Chem. 297:100820-100820(2021). 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; CP000077; AAY80097.1; -; Genomic_DNA. DR RefSeq; WP_011277599.1; NZ_CP046615.1. DR PDB; 7NS8; X-ray; 2.30 A; A=2-185. DR PDB; 7NS9; X-ray; 1.75 A; A=2-185. DR PDB; 7NSA; X-ray; 1.95 A; A=2-185. DR PDB; 7NSD; X-ray; 2.19 A; A=2-185. DR PDB; 7NSF; X-ray; 2.00 A; A=2-185. DR PDB; 7OA2; X-ray; 2.70 A; A=2-185. DR AlphaFoldDB; Q4JAT2; -. DR SMR; Q4JAT2; -. DR STRING; 330779.Saci_0718; -. DR GeneID; 78441060; -. DR KEGG; sai:Saci_0718; -. DR PATRIC; fig|330779.12.peg.685; -. DR eggNOG; arCOG01723; Archaea. DR HOGENOM; CLU_105244_2_0_2; -. DR Proteomes; UP000001018; Chromosome. DR CDD; cd07890; CYTH-like_AC_IV-like; 1. DR Gene3D; 2.40.320.10; Hypothetical Protein Pfu-838710-001; 1. DR InterPro; IPR008173; Adenylyl_cyclase_CyaB. DR InterPro; IPR033469; CYTH-like_dom_sf. DR InterPro; IPR023577; CYTH_domain. DR NCBIfam; TIGR00318; cyaB; 1. DR PANTHER; PTHR21028:SF2; CYTH DOMAIN-CONTAINING PROTEIN; 1. DR PANTHER; PTHR21028; SI:CH211-156B7.4; 1. DR Pfam; PF01928; CYTH; 1. DR SMART; SM01118; CYTH; 1. DR SUPFAM; SSF55154; CYTH-like phosphatases; 1. DR PROSITE; PS51707; CYTH; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:7NS8, ECO:0007829|PDB:7NS9}; KW ATP-binding {ECO:0007829|PDB:7NSD}; KW Calcium {ECO:0007829|PDB:7NS9, ECO:0007829|PDB:7NSA}; KW Metal-binding {ECO:0007829|PDB:7NS9, ECO:0007829|PDB:7NSA}; KW Nucleotide-binding {ECO:0007829|PDB:7NSD}; KW Reference proteome {ECO:0000313|Proteomes:UP000001018}. FT DOMAIN 3..174 FT /note="CYTH" FT /evidence="ECO:0000259|PROSITE:PS51707" FT BINDING 5 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:7NS9, ECO:0007829|PDB:7NSD" FT BINDING 7 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:7NSA" FT BINDING 7 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:7NS9, ECO:0007829|PDB:7NSD" FT BINDING 7 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0007829|PDB:7NSF" FT BINDING 9 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0007829|PDB:7NSD" FT BINDING 56 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0007829|PDB:7NSD" FT BINDING 58 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0007829|PDB:7NSD" FT BINDING 69 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0007829|PDB:7NSD" FT BINDING 78 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0007829|PDB:7NSD" FT BINDING 80 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0007829|PDB:7NSD" FT BINDING 110 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0007829|PDB:7NSD" FT BINDING 112 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0007829|PDB:7NSD" FT BINDING 135 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:7NSA" FT BINDING 135 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:7NS9, ECO:0007829|PDB:7NSD" FT BINDING 135 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0007829|PDB:7NSF" FT BINDING 137 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:7NS9, ECO:0007829|PDB:7NSD" FT BINDING 168 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0007829|PDB:7NSD" SQ SEQUENCE 185 AA; 22174 MW; E485390885A709ED CRC64; MSYIEREIKL RVISPSLEEI EERIRNNYTF INEEHQIDIY YNNPIRDFRK SDEALRLRNT NGKVILTYKG PKQSKETKTR EEIEVEVSDL HKMDLILRKL GFIRSFQVEK IRKNYKYADF IISLDSIKEL GEFIEIEGIN KTEKELISFV DEFVKKHQIQ YEKTIKSYLE LLVEHAKKTN NSNTH //