GenomeNet

Database: UniProt
Entry: Q8TZC9
LinkDB: Q8TZC9
Original site: Q8TZC9 
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   19-FEB-2014, entry version 67.
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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
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: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; 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; 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
//
DBGET integrated database retrieval system