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Database: UniProt/SWISS-PROT
Entry: RTCA_SULIM
LinkDB: RTCA_SULIM
Original site: RTCA_SULIM 
ID   RTCA_SULIM              Reviewed;         337 AA.
AC   C3MU91;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   19-FEB-2014, entry version 33.
DE   RecName: Full=RNA 3'-terminal phosphate cyclase;
DE            Short=RNA cyclase;
DE            Short=RNA-3'-phosphate cyclase;
DE            EC=6.5.1.4;
GN   Name=rtcA; OrderedLocusNames=M1425_0235;
OS   Sulfolobus islandicus (strain M.14.25 / Kamchatka #1).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=427317;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M.14.25 / Kamchatka #1;
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'-
CC       cyclic phosphodiester at the end of RNA. The mechanism of action
CC       of the enzyme occurs in 3 steps: (A) adenylation of the enzyme by
CC       ATP; (B) transfer of adenylate to an RNA-N3'P to produce RNA-
CC       N3'PP5'A; (C) and attack of the adjacent 2'-hydroxyl on the 3'-
CC       phosphorus in the diester linkage to produce the cyclic end
CC       product. The biological role of this enzyme is unknown but it is
CC       likely to function in some aspects of cellular RNA processing (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + RNA 3'-terminal-phosphate = AMP +
CC       diphosphate + RNA terminal-2',3'-cyclic-phosphate.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Potential).
CC   -!- SIMILARITY: Belongs to the RNA 3'-terminal cyclase family. Type 1
CC       subfamily.
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DR   EMBL; CP001400; ACP37125.1; -; Genomic_DNA.
DR   RefSeq; YP_002828423.1; NC_012588.1.
DR   STRING; 427317.M1425_0235; -.
DR   EnsemblBacteria; ACP37125; ACP37125; M1425_0235.
DR   GeneID; 7796476; -.
DR   KEGG; sia:M1425_0235; -.
DR   eggNOG; COG0430; -.
DR   HOGENOM; HOG000015264; -.
DR   KO; K01974; -.
DR   OMA; RRGHYPK; -.
DR   ProtClustDB; PRK04204; -.
DR   BioCyc; SISL427317:GI7C-239-MONOMER; -.
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-HAMAP.
DR   GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR   Gene3D; 3.30.360.20; -; 1.
DR   Gene3D; 3.65.10.20; -; 2.
DR   HAMAP; MF_00200; RTC; 1.
DR   InterPro; IPR013791; RNA3'-term_phos_cycl_insert.
DR   InterPro; IPR023797; RNA3'_phos_cyclase_dom.
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   PANTHER; PTHR11096; PTHR11096; 1.
DR   Pfam; PF01137; RTC; 1.
DR   Pfam; PF05189; RTC_insert; 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; Complete proteome; Cytoplasm; Ligase; Nucleotide-binding.
FT   CHAIN         1    337       RNA 3'-terminal phosphate cyclase.
FT                                /FTId=PRO_1000204095.
FT   NP_BIND     282    285       ATP (By similarity).
FT   ACT_SITE    306    306       Tele-AMP-histidine intermediate (By
FT                                similarity).
FT   BINDING     101    101       ATP (By similarity).
SQ   SEQUENCE   337 AA;  36697 MW;  3415D82D130FB025 CRC64;
     MIEIDGSFGE GGGQILRTSL TLSVITGKPF RIFNIRANRP NPGLQRQHLW AVKAMKMISN
     AETKGDEVGS KELIFVPHEI KGNINIDIDV GTAGSVTLII QTVLPAIINK NVRIRIKGGT
     DVPKSPTIDY IRLVYLEILR KIGIEAKLNL IKRGHYPEGG GEVIIENVNG NPSAFSLLEL
     GKLTIIKGIS HVSSLPAHIA ERQMNSAREL LSKLGVPIEI QTDVRQGEVS KGSGIALAAI
     GEKSIIGADS LGERGKRAEI VGEEAARILI DNLNTKASVD IHMSDMLMIF ASLYGGEYIG
     AELTSHAYTN MEIIKKFLDI KIDVSGKRPF RFKAKIF
//
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