ID RTCA_METKA Reviewed; 352 AA.
AC Q8TZC9;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 01-MAY-2013, entry version 65.
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=MK0001;
OS Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC
OS 100938).
OC Archaea; Euryarchaeota; Methanopyri; Methanopyrales; Methanopyraceae;
OC Methanopyrus.
OX NCBI_TaxID=190192;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
RX PubMed=11930014; DOI=10.1073/pnas.032671499;
RA Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N.,
RA Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L.,
RA Natale D.A., Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O.,
RA Malykh A.G., Koonin E.V., Kozyavkin S.A.;
RT "The complete genome of hyperthermophile Methanopyrus kandleri AV19
RT and monophyly of archaeal methanogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002).
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; AE009439; AAM01218.1; -; Genomic_DNA.
DR RefSeq; NP_613288.1; NC_003551.1.
DR ProteinModelPortal; Q8TZC9; -.
DR STRING; 190192.MK0001; -.
DR EnsemblBacteria; AAM01218; AAM01218; MK0001.
DR GeneID; 1477327; -.
DR KEGG; mka:MK0001; -.
DR eggNOG; COG0430; -.
DR HOGENOM; HOG000015264; -.
DR KO; K01974; -.
DR OMA; RRGHYPK; -.
DR ProtClustDB; PRK04204; -.
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; SSF52913; RNA3'-term_phos_cycl_insert; 1.
DR SUPFAM; SSF55205; RNA3'_cycl/enolpyr_transf_A/B; 2.
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;
KW Reference proteome.
FT CHAIN 1 352 RNA 3'-terminal phosphate cyclase.
FT /FTId=PRO_0000156427.
FT NP_BIND 292 296 ATP (By similarity).
FT ACT_SITE 318 318 Tele-AMP-histidine intermediate (By
FT similarity).
FT BINDING 102 102 ATP (By similarity).
SQ SEQUENCE 352 AA; 38092 MW; 9E0952828B031E5A CRC64;
MSLIEIDGSY GEGGGQILRT AVGMSALTGE PVRIYNIRAN RPRPGLSHQH LHAVKAVAEI
CDAECEGLEI GSTEIVFEPG KVKGGEYEVD IGTAGSVTLL LQAVKLAAIA ADGPVEMEVR
GGTDVKWSPP VDYEINVNAH YLDRLGYRYE LEVLRRGHYP RGGGIVRARM EPPKRLKPLE
AVKFGELESV RGISHCVRLP PHVAERQAKA ASEIIERELG IRPEIEIETY PKGRDPHLGP
GSGIVLWAED DQGNRIGADA LGEKGKPAEV VGREAAEQLV QRLRTGMALD EHMGDQILPF
LAIADGESVF GVTGVDPHLP TNAWVVEKFL PVSVEIRGKE GEPATVEVRP EG
//
