RTCA_MACFA
ID RTCA_MACFA Reviewed; 366 AA.
AC Q4R3J0;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=RNA 3'-terminal phosphate cyclase;
DE Short=RNA cyclase;
DE Short=RNA-3'-phosphate cyclase;
DE EC=6.5.1.4 {ECO:0000250|UniProtKB:O00442};
DE AltName: Full=RNA terminal phosphate cyclase domain-containing protein 1;
GN Name=RTCA; Synonyms=RTCD1; ORFNames=QtsA-16663;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250|UniProtKB:O00442}.
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:0000250|UniProtKB:O00442};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:O00442}.
CC -!- SIMILARITY: Belongs to the RNA 3'-terminal cyclase family. Type 1
CC subfamily. {ECO:0000305}.
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DR EMBL; AB179276; BAE02327.1; -; mRNA.
DR RefSeq; NP_001270084.1; NM_001283155.1.
DR AlphaFoldDB; Q4R3J0; -.
DR SMR; Q4R3J0; -.
DR STRING; 9541.XP_005542650.1; -.
DR Ensembl; ENSMFAT00000026242; ENSMFAP00000007548; ENSMFAG00000034132.
DR GeneID; 101925644; -.
DR CTD; 8634; -.
DR VEuPathDB; HostDB:ENSMFAG00000034132; -.
DR eggNOG; KOG3980; Eukaryota.
DR GeneTree; ENSGT00530000063404; -.
DR OMA; PKPGLSH; -.
DR OrthoDB; 1151685at2759; -.
DR Proteomes; UP000233100; Chromosome 1.
DR Bgee; ENSMFAG00000034132; Expressed in skeletal muscle tissue and 13 other tissues.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003963; F:RNA-3'-phosphate cyclase activity; ISS:UniProtKB.
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; SSF52913; SSF52913; 1.
DR SUPFAM; SSF55205; SSF55205; 2.
DR TIGRFAMs; TIGR03399; RNA_3prim_cycl; 1.
DR PROSITE; PS01287; RTC; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Ligase; Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..366
FT /note="RNA 3'-terminal phosphate cyclase"
FT /id="PRO_0000288838"
FT ACT_SITE 320
FT /note="Tele-AMP-histidine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 104
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 294..298
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 366 AA; 39410 MW; C8EF307D6C46A8D7 CRC64;
MAGPRVEVDG SIMEGGGQIL RVSTALSCLL GLPLRVQKIR AGRSTPGLRP QHLSGLEMIR
DLCDGRLEGA EIGSTEITFT PEKIKGGIHT ADTKTAGSVC LLMQVSMPCV LFAASPSELH
LKGGTNAEMA PQIDYTVMVF KPIVEKFGFR FNCDIKTRGY YPKGGGEVIV RMSPVKQLNP
INLTDRGCVT KIYGRAFVAG VLPFKVAKDM AAAAVRCIRK EIRDLYVNIQ PVQEPKDQAF
GNGNGIIIIA ETSTGCLFAG SSLGKRGVNA DKVGIEAAEM LLANLRHGGT VDEYLQDQLI
VFMALANGVS RIKTGPVTLH TQTAIHFAEQ IAKAKFIVKK SEDEEDASKD TYIIECQGIG
MTNPNL
