ID   RTCA_PONAB              Reviewed;         366 AA.
AC   Q5R7P3;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   08-NOV-2023, entry version 87.
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   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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 (By similarity). The mechanism of
CC       action of the enzyme occurs in 3 steps: (A) adenylation of the enzyme
CC       by 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 product (By
CC       similarity). Likely functions in some aspects of cellular RNA
CC       processing (By similarity). Function plays an important role in
CC       regulating axon regeneration by inhibiting central nervous system (CNS)
CC       axon regeneration following optic nerve injury (By similarity).
CC       {ECO:0000250|UniProtKB:O00442, ECO:0000250|UniProtKB:Q9D7H3}.
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   -!- 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; CR860069; CAH92217.1; -; mRNA.
DR   RefSeq; NP_001126296.1; NM_001132824.1.
DR   AlphaFoldDB; Q5R7P3; -.
DR   SMR; Q5R7P3; -.
DR   STRING; 9601.ENSPPYP00000001293; -.
DR   GeneID; 100173273; -.
DR   KEGG; pon:100173273; -.
DR   CTD; 8634; -.
DR   eggNOG; KOG3980; Eukaryota.
DR   InParanoid; Q5R7P3; -.
DR   OrthoDB; 315241at2759; -.
DR   Proteomes; UP000001595; Unplaced.
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   CDD; cd00874; RNA_Cyclase_Class_II; 1.
DR   Gene3D; 3.65.10.20; RNA 3'-terminal phosphate cyclase domain; 1.
DR   Gene3D; 3.30.360.20; RNA 3'-terminal phosphate cyclase, insert domain; 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   NCBIfam; TIGR03399; RNA_3prim_cycl; 1.
DR   PANTHER; PTHR11096; RNA 3' TERMINAL PHOSPHATE CYCLASE; 1.
DR   PANTHER; PTHR11096:SF0; RNA 3'-TERMINAL PHOSPHATE CYCLASE; 1.
DR   Pfam; PF01137; RTC; 1.
DR   Pfam; PF05189; RTC_insert; 1.
DR   PIRSF; PIRSF005378; RNA3'_term_phos_cycl_euk; 1.
DR   SUPFAM; SSF55205; EPT/RTPC-like; 2.
DR   SUPFAM; SSF52913; RNA 3'-terminal phosphate cyclase, RPTC, insert domain; 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_0000288839"
FT   ACT_SITE        320
FT                   /note="Tele-AMP-histidine intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P46849"
FT   BINDING         104
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P46849"
FT   BINDING         131
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P46849"
FT   BINDING         294
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P46849"
FT   BINDING         297
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P46849"
FT   BINDING         298
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P46849"
FT   BINDING         320
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P46849"
SQ   SEQUENCE   366 AA;  39140 MW;  B8DD96AF8EB43420 CRC64;
     MAGPRVEVDG SIMEGGGQIL RVSTALSCLL GLPLRVQKIR AGRSTPGLRP QHLSGLEMIR
     DLCDGQLEGA EIGSTEITFT PEKIKGGIHT ADTKTAGSVC LLMQVSMPCV LFAASPSKLH
     LKGGTNAEMA PQIDYTVMVF KPIVEKFGFV FNCDIKTRGY YPKGGGEVIV RMSPVKQLDP
     VNLTDRGCVT KIYGRAFVTG VLPFKVAKDM AAAAARCIRK EIRDSYVNIQ PVQEPKDQAF
     GNGNGIIIIA ETSTGCLFAG SSLGKRGVNA DKVGIGAAEM LLANLRHGGT VDEYLQDQLI
     VFMALANGVS RIKTGPVTLH TQTAIHFAEQ IAKAKFIVKK SEDEEDAAKG TYIIECQGIG
     MTNPNL
//