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RTCA_SULIN
ID   RTCA_SULIN              Reviewed;         337 AA.
AC   C3NMT8;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   03-AUG-2022, entry version 72.
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=YN1551_2842;
OS   Sulfolobus islandicus (strain Y.N.15.51 / Yellowstone #2).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=419942;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y.N.15.51 / Yellowstone #2;
RX   PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA   Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT   "Biogeography of the Sulfolobus islandicus pan-genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
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}.
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DR   EMBL; CP001404; ACP49745.1; -; Genomic_DNA.
DR   RefSeq; WP_012718117.1; NC_012623.1.
DR   AlphaFoldDB; C3NMT8; -.
DR   SMR; C3NMT8; -.
DR   EnsemblBacteria; ACP49745; ACP49745; YN1551_2842.
DR   GeneID; 7808835; -.
DR   KEGG; sin:YN1551_2842; -.
DR   HOGENOM; CLU_027882_0_0_2; -.
DR   OMA; PKPGLSH; -.
DR   Proteomes; UP000006818; 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; SSF55205; SSF55205; 1.
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..337
FT                   /note="RNA 3'-terminal phosphate cyclase"
FT                   /id="PRO_1000204096"
FT   ACT_SITE        306
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         282..285
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00200"
SQ   SEQUENCE   337 AA;  36717 MW;  DF26E860FBC754E1 CRC64;
     MIEIDGSFGE GGGQILRTSL TLSIITGKPF RIFNIRANRP NPGLQRQHLW AVKAMKMISN
     AETKGDEVGS KELIFVPHEI KGNTNIDMDV GTAGSVTLII QTVLPAIINK NVRIRIKGGT
     DVPKSPTIDY IRLVYLEILR KIGIEAKLNL IKRGHYPEGG GEVIIENVNG NPSAFSLLEL
     GKLTIIKGIS HVSSLPAHIA ERQMNSAREI LSKLGVPIEI ETDVRQGEVS KGSGIALAAI
     GEKSIIGADS LGERGKRAEI VGEEAARILI NNLNTKASVD IHMSDMLMIF ASLYGGEYIG
     AELTSHAYTN MEIIKKFLDI KIDVSGKRPF RFKAKIF
 
 
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