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THPR_THET8
ID   THPR_THET8              Reviewed;         198 AA.
AC   Q5SHB1; Q84CU4;
DT   04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=RNA 2',3'-cyclic phosphodiesterase {ECO:0000255|HAMAP-Rule:MF_01940};
DE            Short=RNA 2',3'-CPDase {ECO:0000255|HAMAP-Rule:MF_01940};
DE            EC=3.1.4.58 {ECO:0000255|HAMAP-Rule:MF_01940};
GN   OrderedLocusNames=TTHA1819 {ECO:0000312|EMBL:BAD71642.1};
OS   Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=300852;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS),
RP   AND ACTIVE SITES.
RC   STRAIN=ATCC 27634 / DSM 579 / HB8;
RX   PubMed=12798681; DOI=10.1016/s0022-2836(03)00448-0;
RA   Kato M., Shirouzu M., Terada T., Yamaguchi H., Murayama K., Sakai H.,
RA   Kuramitsu S., Yokoyama S.;
RT   "Crystal structure of the 2'-5' RNA ligase from Thermus thermophilus HB8.";
RL   J. Mol. Biol. 329:903-911(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27634 / DSM 579 / HB8;
RA   Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA   Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT   "Complete genome sequence of Thermus thermophilus HB8.";
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Hydrolyzes RNA 2',3'-cyclic phosphodiester to an RNA 2'-
CC       phosphomonoester. {ECO:0000255|HAMAP-Rule:MF_01940}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + H2O = a 3'-
CC         end 2'-phospho-ribonucleotide-RNA + H(+); Xref=Rhea:RHEA:11828,
CC         Rhea:RHEA-COMP:10464, Rhea:RHEA-COMP:17353, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:83064, ChEBI:CHEBI:173113;
CC         EC=3.1.4.58; Evidence={ECO:0000255|HAMAP-Rule:MF_01940};
CC   -!- SIMILARITY: Belongs to the 2H phosphoesterase superfamily. ThpR family.
CC       {ECO:0000255|HAMAP-Rule:MF_01940}.
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DR   EMBL; AB107665; BAC67697.1; -; Genomic_DNA.
DR   EMBL; AP008226; BAD71642.1; -; Genomic_DNA.
DR   RefSeq; WP_011173843.1; NC_006461.1.
DR   RefSeq; YP_145085.1; NC_006461.1.
DR   PDB; 1IUH; X-ray; 2.50 A; A=1-198.
DR   PDBsum; 1IUH; -.
DR   AlphaFoldDB; Q5SHB1; -.
DR   SMR; Q5SHB1; -.
DR   STRING; 300852.55773201; -.
DR   EnsemblBacteria; BAD71642; BAD71642; BAD71642.
DR   GeneID; 3168502; -.
DR   KEGG; ttj:TTHA1819; -.
DR   PATRIC; fig|300852.9.peg.1790; -.
DR   eggNOG; COG1514; Bacteria.
DR   HOGENOM; CLU_081251_0_1_0; -.
DR   OMA; HITLRFL; -.
DR   PhylomeDB; Q5SHB1; -.
DR   Proteomes; UP000000532; Chromosome.
DR   GO; GO:0004113; F:2',3'-cyclic-nucleotide 3'-phosphodiesterase activity; IEA:InterPro.
DR   GO; GO:0008664; F:2'-5'-RNA ligase activity; IEA:InterPro.
DR   HAMAP; MF_01940; RNA_CPDase; 1.
DR   InterPro; IPR009097; Cyclic_Pdiesterase.
DR   InterPro; IPR014051; Phosphoesterase_HXTX.
DR   InterPro; IPR004175; RNA_CPDase.
DR   PANTHER; PTHR35561; PTHR35561; 1.
DR   Pfam; PF02834; LigT_PEase; 2.
DR   SUPFAM; SSF55144; SSF55144; 1.
DR   TIGRFAMs; TIGR02258; 2_5_ligase; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Hydrolase; Reference proteome.
FT   CHAIN           1..198
FT                   /note="RNA 2',3'-cyclic phosphodiesterase"
FT                   /id="PRO_0000431802"
FT   MOTIF           39..42
FT                   /note="HXTX 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01940,
FT                   ECO:0000305|PubMed:12798681"
FT   MOTIF           130..133
FT                   /note="HXTX 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01940,
FT                   ECO:0000305|PubMed:12798681"
FT   ACT_SITE        39
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01940,
FT                   ECO:0000305|PubMed:12798681"
FT   ACT_SITE        130
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01940,
FT                   ECO:0000305|PubMed:12798681"
FT   STRAND          2..8
FT                   /evidence="ECO:0007829|PDB:1IUH"
FT   HELIX           11..21
FT                   /evidence="ECO:0007829|PDB:1IUH"
FT   HELIX           22..24
FT                   /evidence="ECO:0007829|PDB:1IUH"
FT   STRAND          30..32
FT                   /evidence="ECO:0007829|PDB:1IUH"
FT   HELIX           35..37
FT                   /evidence="ECO:0007829|PDB:1IUH"
FT   STRAND          39..47
FT                   /evidence="ECO:0007829|PDB:1IUH"
FT   HELIX           50..52
FT                   /evidence="ECO:0007829|PDB:1IUH"
FT   HELIX           53..66
FT                   /evidence="ECO:0007829|PDB:1IUH"
FT   STRAND          70..85
FT                   /evidence="ECO:0007829|PDB:1IUH"
FT   STRAND          87..94
FT                   /evidence="ECO:0007829|PDB:1IUH"
FT   HELIX           96..113
FT                   /evidence="ECO:0007829|PDB:1IUH"
FT   HELIX           114..119
FT                   /evidence="ECO:0007829|PDB:1IUH"
FT   TURN            121..124
FT                   /evidence="ECO:0007829|PDB:1IUH"
FT   STRAND          130..138
FT                   /evidence="ECO:0007829|PDB:1IUH"
FT   STRAND          150..154
FT                   /evidence="ECO:0007829|PDB:1IUH"
FT   STRAND          156..164
FT                   /evidence="ECO:0007829|PDB:1IUH"
FT   STRAND          166..178
FT                   /evidence="ECO:0007829|PDB:1IUH"
SQ   SEQUENCE   198 AA;  22411 MW;  D85B66890413350E CRC64;
     MRLFYAVFLP EEVRAALVEA QTKVRPFRGW KPVPPHQLHL TLLFLGERPE EELPDYLALG
     HRLARLEAPF RARLRGTGYF PNEGTPRVWF AKAEAEGFLR LAEGLRAGVE ELLGEEAVRI
     PGWDKPFKPH ITLARRKAPA PRVPPVLFGL EWPVEGFALV RSELKPKGPV YTVLEKFSLR
     GEHGREQAQG PGERPEGD
 
 
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