ID Q72GF3_THET2 Unreviewed; 517 AA. AC Q72GF3; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 27-MAR-2024, entry version 132. DE SubName: Full=Heat resistant RNA dependent ATPase {ECO:0000313|EMBL:AAS82237.1}; GN OrderedLocusNames=TT_C1895 {ECO:0000313|EMBL:AAS82237.1}; OS Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27). OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus. OX NCBI_TaxID=262724 {ECO:0000313|EMBL:AAS82237.1, ECO:0000313|Proteomes:UP000000592}; RN [1] {ECO:0000313|EMBL:AAS82237.1, ECO:0000313|Proteomes:UP000000592} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27 RC {ECO:0000313|Proteomes:UP000000592}; RX PubMed=15064768; DOI=10.1038/nbt956; RA Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H., RA Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C., RA Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P., RA Overbeek R., Kramer W., Merkl R., Gottschalk G., Fritz H.-J.; RT "The genome sequence of the extreme thermophile Thermus thermophilus."; RL Nat. Biotechnol. 22:547-553(2004). RN [2] {ECO:0007829|PDB:3EAQ, ECO:0007829|PDB:3EAR} RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 215-426. RX PubMed=19050012; DOI=10.1093/nar/gkn947; RA Klostermeier D., Rudolph M.G.; RT "A novel dimerization motif in the C-terminal domain of the Thermus RT thermophilus DEAD box helicase Hera confers substantial flexibility."; RL Nucleic Acids Res. 37:421-430(2009). RN [3] {ECO:0007829|PDB:3I31, ECO:0007829|PDB:3I32} RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 431-517 IN COMPLEX WITH ZINC. RX PubMed=19710183; DOI=10.1261/rna.1820009; RA Rudolph M.G., Klostermeier D.; RT "The Thermus thermophilus DEAD box helicase Hera contains a modified RNA RT recognition motif domain loosely connected to the helicase core."; RL RNA 15:1993-2001(2009). RN [4] {ECO:0007829|PDB:3MWJ, ECO:0007829|PDB:3MWK} RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 8-214. RX PubMed=21391900; DOI=10.1515/BC.2011.034; RA Strohmeier J., Hertel I., Diederichsen U., Rudolph M.G., Klostermeier D.; RT "Changing nucleotide specificity of the DEAD-box helicase Hera abrogates RT communication between the Q-motif and the P-loop."; RL Biol. Chem. 392:357-369(2011). RN [5] {ECO:0007829|PDB:4KBF, ECO:0007829|PDB:4KBG} RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 8-372 IN COMPLEX WITH AMP. RX PubMed=23765433; DOI=10.1002/bip.22316; RA Klostermeier D.; RT "Rearranging RNA structures at 75C? Toward the molecular mechanism and RT physiological function of the Thermus thermophilus DEAD-box helicase RT Hera."; RL Biopolymers 99:1137-1146(2013). RN [6] {ECO:0007829|PDB:4I67, ECO:0007829|PDB:4I68} RP X-RAY CRYSTALLOGRAPHY (1.63 ANGSTROMS) OF 431-517 IN COMPLEX WITH ZINC. RX PubMed=23625962; DOI=10.1093/nar/gkt323; RA Steimer L., Wurm J.P., Linden M.H., Rudolph M.G., Wohnert J., RA Klostermeier D.; RT "Recognition of two distinct elements in the RNA substrate by the RNA- RT binding domain of the T. thermophilus DEAD box helicase Hera."; RL Nucleic Acids Res. 41:6259-6272(2013). RN [7] {ECO:0007829|PDB:5MAO} RP X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 431-498. RA Rudolph M.G., Klostermeier D.; RT "Crystal Structure of HERA CTD."; RL Submitted (NOV-2016) to the PDB data bank. CC -!- SIMILARITY: Belongs to the DEAD box helicase family. CC {ECO:0000256|RuleBase:RU000492}. 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; AE017221; AAS82237.1; -; Genomic_DNA. DR PDB; 3EAQ; X-ray; 2.30 A; A/B=215-426. DR PDB; 3EAR; X-ray; 2.30 A; A/B=215-426. DR PDB; 3EAS; X-ray; 2.80 A; A/B=215-426. DR PDB; 3I31; X-ray; 1.80 A; A=431-517. DR PDB; 3I32; X-ray; 2.80 A; A=218-517. DR PDB; 3MWJ; X-ray; 1.40 A; A/B=8-214. DR PDB; 3MWK; X-ray; 1.45 A; A/B=8-214. DR PDB; 3MWL; X-ray; 1.60 A; A/B=8-214. DR PDB; 3NBF; X-ray; 1.90 A; A/B/C/D=8-214. DR PDB; 3NEJ; X-ray; 2.57 A; A/B=8-214. DR PDB; 4I67; X-ray; 2.33 A; A=431-517. DR PDB; 4I68; X-ray; 1.63 A; A=431-517. DR PDB; 4I69; X-ray; 1.79 A; A/B/C=431-517. DR PDB; 4KBF; X-ray; 1.90 A; A/B=8-372. DR PDB; 4KBG; X-ray; 2.54 A; A/B=8-372. DR PDB; 5MAO; X-ray; 1.35 A; A/B=431-498. DR PDBsum; 3EAQ; -. DR PDBsum; 3EAR; -. DR PDBsum; 3EAS; -. DR PDBsum; 3I31; -. DR PDBsum; 3I32; -. DR PDBsum; 3MWJ; -. DR PDBsum; 3MWK; -. DR PDBsum; 3MWL; -. DR PDBsum; 3NBF; -. DR PDBsum; 3NEJ; -. DR PDBsum; 4I67; -. DR PDBsum; 4I68; -. DR PDBsum; 4I69; -. DR PDBsum; 4KBF; -. DR PDBsum; 4KBG; -. DR PDBsum; 5MAO; -. DR AlphaFoldDB; Q72GF3; -. DR SMR; Q72GF3; -. DR KEGG; tth:TT_C1895; -. DR eggNOG; COG0513; Bacteria. DR HOGENOM; CLU_003041_21_0_0; -. DR OrthoDB; 9805696at2; -. DR EvolutionaryTrace; Q72GF3; -. DR Proteomes; UP000000592; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0003724; F:RNA helicase activity; IEA:InterPro. DR CDD; cd00268; DEADc; 1. DR CDD; cd12938; GUCT_Hera; 1. DR CDD; cd18787; SF2_C_DEAD; 1. DR Gene3D; 3.30.70.1800; -; 1. DR Gene3D; 6.10.250.710; -; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2. DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR048768; Hera-like_DD. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS. DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif. DR PANTHER; PTHR47959:SF13; ATP-DEPENDENT RNA HELICASE RHLE; 1. DR PANTHER; PTHR47959; ATP-DEPENDENT RNA HELICASE RHLE-RELATED; 1. DR Pfam; PF00270; DEAD; 1. DR Pfam; PF00271; Helicase_C; 1. DR Pfam; PF21591; Hera_DD; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS00039; DEAD_ATP_HELICASE; 1. DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1. DR PROSITE; PS51194; HELICASE_CTER; 1. DR PROSITE; PS51195; Q_MOTIF; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:3EAQ, ECO:0007829|PDB:3EAR}; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU000492}; KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU000492}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000492}; KW Metal-binding {ECO:0007829|PDB:3I31, ECO:0007829|PDB:4I68}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, KW ECO:0000256|RuleBase:RU000492}; KW Zinc {ECO:0007829|PDB:3I31, ECO:0007829|PDB:4I68}. FT DOMAIN 8..36 FT /note="DEAD-box RNA helicase Q" FT /evidence="ECO:0000259|PROSITE:PS51195" FT DOMAIN 39..210 FT /note="Helicase ATP-binding" FT /evidence="ECO:0000259|PROSITE:PS51192" FT DOMAIN 235..380 FT /note="Helicase C-terminal" FT /evidence="ECO:0000259|PROSITE:PS51194" FT MOTIF 8..36 FT /note="Q motif" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552" FT BINDING 30 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0007829|PDB:4KBF" FT BINDING 35 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0007829|PDB:4KBF" FT BINDING 56 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0007829|PDB:4KBF" FT BINDING 57 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0007829|PDB:4KBF" FT BINDING 58 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0007829|PDB:4KBF" FT BINDING 59 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0007829|PDB:4KBF" FT BINDING 432 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4I68" FT BINDING 439 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:4I68" FT BINDING 475 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0007829|PDB:3I31" FT BINDING 506 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT /evidence="ECO:0007829|PDB:4I68" SQ SEQUENCE 517 AA; 56738 MW; 83B1412150CEF34A CRC64; MGPERQSMEF KDFPLKPEIL EALHGRGLTT PTPIQAAALP LALEGKDLIG QARTGTGKTL AFALPIAERL APSQERGRKP RALVLTPTRE LALQVASELT AVAPHLKVVA VYGGTGYGKQ KEALLRGADA VVATPGRALD YLRQGVLDLS RVEVAVLDEA DEMLSMGFEE EVEALLSATP PSRQTLLFSA TLPSWAKRLA ERYMKNPVLI NVIKDEPVTY EEEAVPAPVR GRLEVLSDLL YVASPDRAMV FTRTKAETEE IAQGLLRLGH PAQALHGDLS QGERERVLGA FRQGEVRVLV ATDVAARGLD IPQVDLVVHY RLPDRAEAYQ HRSGRTGRAG RGGRVVLLYG PRERRDVEAL ERAVGRRFKR VNPPTPEEVL EAKWRHLLAR LARVPEKDYR LYQDFAGRLF AEGRVEVVAA LLALLLGGAP AERSLLTGEE GWRTYKATGP RLSLPRLVAL LKGQGLEVGK VAEAEGGFYV DLRPEARPEV AGLRLEPARR VEGLLEIPSR TRRPARA //