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
//