RTCA_PYRIL
ID RTCA_PYRIL Reviewed; 348 AA.
AC A1RSJ7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=RNA 3'-terminal phosphate cyclase {ECO:0000255|HAMAP-Rule:MF_00200};
DE Short=RNA cyclase {ECO:0000255|HAMAP-Rule:MF_00200};
DE Short=RNA-3'-phosphate cyclase {ECO:0000255|HAMAP-Rule:MF_00200};
DE EC=6.5.1.4 {ECO:0000255|HAMAP-Rule:MF_00200};
GN Name=rtcA {ECO:0000255|HAMAP-Rule:MF_00200}; OrderedLocusNames=Pisl_0753;
OS Pyrobaculum islandicum (strain DSM 4184 / JCM 9189 / GEO3).
OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=384616;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4184 / JCM 9189 / GEO3;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Meincke L., Brettin T.,
RA Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Lowe T., Richardson P.;
RT "Complete sequence of Pyrobaculum islandicum DSM 4184.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the conversion of 3'-phosphate to a 2',3'-cyclic
CC phosphodiester at the end of RNA. The mechanism of action of the enzyme
CC occurs in 3 steps: (A) adenylation of the enzyme by ATP; (B) transfer
CC of adenylate to an RNA-N3'P to produce RNA-N3'PP5'A; (C) and attack of
CC the adjacent 2'-hydroxyl on the 3'-phosphorus in the diester linkage to
CC produce the cyclic end product. The biological role of this enzyme is
CC unknown but it is likely to function in some aspects of cellular RNA
CC processing. {ECO:0000255|HAMAP-Rule:MF_00200}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 3'-end 3'-phospho-ribonucleotide-RNA + ATP = a 3'-end 2',3'-
CC cyclophospho-ribonucleotide-RNA + AMP + diphosphate;
CC Xref=Rhea:RHEA:23976, Rhea:RHEA-COMP:10463, Rhea:RHEA-COMP:10464,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:83062,
CC ChEBI:CHEBI:83064, ChEBI:CHEBI:456215; EC=6.5.1.4;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00200};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00200}.
CC -!- SIMILARITY: Belongs to the RNA 3'-terminal cyclase family. Type 1
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00200}.
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; CP000504; ABL87929.1; -; Genomic_DNA.
DR RefSeq; WP_011762505.1; NC_008701.1.
DR AlphaFoldDB; A1RSJ7; -.
DR SMR; A1RSJ7; -.
DR STRING; 384616.Pisl_0753; -.
DR EnsemblBacteria; ABL87929; ABL87929; Pisl_0753.
DR GeneID; 4618208; -.
DR KEGG; pis:Pisl_0753; -.
DR eggNOG; arCOG04125; Archaea.
DR HOGENOM; CLU_027882_0_0_2; -.
DR OMA; PKPGLSH; -.
DR OrthoDB; 52581at2157; -.
DR Proteomes; UP000002595; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003963; F:RNA-3'-phosphate cyclase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR Gene3D; 3.30.360.20; -; 1.
DR Gene3D; 3.65.10.20; -; 1.
DR HAMAP; MF_00200; RTC; 1.
DR InterPro; IPR013791; RNA3'-term_phos_cycl_insert.
DR InterPro; IPR023797; RNA3'_phos_cyclase_dom.
DR InterPro; IPR037136; RNA3'_phos_cyclase_dom_sf.
DR InterPro; IPR000228; RNA3'_term_phos_cyc.
DR InterPro; IPR017770; RNA3'_term_phos_cyc_type_1.
DR InterPro; IPR020719; RNA3'_term_phos_cycl-like_CS.
DR InterPro; IPR013792; RNA3'P_cycl/enolpyr_Trfase_a/b.
DR InterPro; IPR036553; RPTC_insert.
DR PANTHER; PTHR11096; PTHR11096; 1.
DR PANTHER; PTHR11096:SF0; PTHR11096:SF0; 1.
DR Pfam; PF01137; RTC; 1.
DR Pfam; PF05189; RTC_insert; 1.
DR PIRSF; PIRSF005378; RNA3'_term_phos_cycl_euk; 1.
DR SUPFAM; SSF52913; SSF52913; 1.
DR SUPFAM; SSF55205; SSF55205; 2.
DR TIGRFAMs; TIGR03399; RNA_3prim_cycl; 1.
DR PROSITE; PS01287; RTC; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Ligase; Nucleotide-binding.
FT CHAIN 1..348
FT /note="RNA 3'-terminal phosphate cyclase"
FT /id="PRO_1000012115"
FT ACT_SITE 312
FT /note="Tele-AMP-histidine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00200"
FT BINDING 101
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00200"
FT BINDING 286..289
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00200"
SQ SEQUENCE 348 AA; 37233 MW; 4A4891FF6D440D5E CRC64;
MIVKIDGSYG EGGGQILRTS IALSALLGKP VEIINIRAKR TNPGLQPQHL TGVSAAALLT
DADIEGAAKG STRLYFKPKT LKCGTFNIDI GTAGSISLVI QTLAPILLYA PCPTKLVITG
GTDVAWAPPI DYMRYVFVKV LSLFGAKIAI ELVRRGHYPR GGGRVIVYVE PIKKLRAVHY
VEFGRLVKIS GISHAVNLPT HVAERQAKAA KETLAKLGYV AEVEVETRSD GLGPGSGIVL
WAESDIGNVV GGDALGERGK PAEEVGREAA ERLAAVLKTG VSLDPHMADM AVVYMALAEG
RSKMSTSEAT LHLQTNMYIV EQFLPVKFKL EKTGARYIIE VDGIGYSR
