ID   RTCA_BOVIN              Reviewed;         366 AA.
AC   Q2HJ88;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 104.
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;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Uterus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (FEB-2006) 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; BC113251; AAI13252.1; -; mRNA.
DR   RefSeq; NP_001039520.1; NM_001046055.1.
DR   AlphaFoldDB; Q2HJ88; -.
DR   SMR; Q2HJ88; -.
DR   STRING; 9913.ENSBTAP00000008293; -.
DR   PaxDb; Q2HJ88; -.
DR   PRIDE; Q2HJ88; -.
DR   Ensembl; ENSBTAT00000008293; ENSBTAP00000008293; ENSBTAG00000006321.
DR   GeneID; 510469; -.
DR   KEGG; bta:510469; -.
DR   CTD; 8634; -.
DR   VEuPathDB; HostDB:ENSBTAG00000006321; -.
DR   VGNC; VGNC:34193; RTCA.
DR   eggNOG; KOG3980; Eukaryota.
DR   GeneTree; ENSGT00530000063404; -.
DR   HOGENOM; CLU_027882_0_1_1; -.
DR   InParanoid; Q2HJ88; -.
DR   OMA; PKPGLSH; -.
DR   OrthoDB; 1151685at2759; -.
DR   TreeFam; TF300831; -.
DR   Proteomes; UP000009136; Chromosome 3.
DR   Bgee; ENSBTAG00000006321; Expressed in semen and 106 other tissues.
DR   GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
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_0000288837"
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;  39252 MW;  417C040DBA122145 CRC64;
     MAGPRVEVDG GIMEGGGQIL RVSTALSCLL GLPLRVQKIR AGRSTPGLRP QHLSGLEMIR
     DLCDGQLEGA EIGSTEITFT PEKIKGGVHT ADTKTAGSVC LLMQVSMPCV LFAACPSELR
     LKGGTNAEMA PQIDYTAMVF KPIVEKFGFT FNCDIKMRGY YPKGGGEVIV RMSPVKQLSP
     INLTDRGCVT KIYGRAFVAG VLPFKVAKDM AAAAVRCIRK EIRDLYVNIQ PVQEPKDQAF
     GNGNGIIIIA ETSTGCLFAG SSLGKRGVNA DKVGIEAAEM LLANLRHGGA VDEYLQDQLI
     IFMALASGIS RIKTGPVTLH TQTAIHFAEQ LAKAKFTVKK SEDEEDASKD TYIIECQGIG
     MTNPNL