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 01-MAY-2013, entry version 31.
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: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; RNA3'_cycl/enolpyr_transf_A/B; 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
//
