ID A0A142X080_9PLAN Unreviewed; 353 AA.
AC A0A142X080;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=RNA 3'-terminal phosphate cyclase {ECO:0000256|ARBA:ARBA00021428, ECO:0000256|HAMAP-Rule:MF_00200};
DE Short=RNA cyclase {ECO:0000256|HAMAP-Rule:MF_00200};
DE Short=RNA-3'-phosphate cyclase {ECO:0000256|HAMAP-Rule:MF_00200};
DE EC=6.5.1.4 {ECO:0000256|ARBA:ARBA00012725, ECO:0000256|HAMAP-Rule:MF_00200};
GN Name=rtcA {ECO:0000256|HAMAP-Rule:MF_00200,
GN ECO:0000313|EMBL:AMV20315.1};
GN ORFNames=VT03_20625 {ECO:0000313|EMBL:AMV20315.1};
OS Planctomyces sp. SH-PL14.
OC Bacteria; Planctomycetota; Planctomycetia; Planctomycetales;
OC Planctomycetaceae; Planctomyces.
OX NCBI_TaxID=1632864 {ECO:0000313|EMBL:AMV20315.1, ECO:0000313|Proteomes:UP000076318};
RN [1] {ECO:0000313|EMBL:AMV20315.1, ECO:0000313|Proteomes:UP000076318}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SH-PL14 {ECO:0000313|EMBL:AMV20315.1,
RC ECO:0000313|Proteomes:UP000076318};
RA van der Voort M., Raaijmakers J.M.;
RT "Genome minning of novel planctomycete species.";
RL Submitted (APR-2015) 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. {ECO:0000256|HAMAP-Rule:MF_00200}.
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:0000256|ARBA:ARBA00024481, ECO:0000256|HAMAP-
CC Rule:MF_00200};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00200}.
CC -!- SIMILARITY: Belongs to the RNA 3'-terminal cyclase family. Type 1
CC subfamily. {ECO:0000256|ARBA:ARBA00009206, ECO:0000256|HAMAP-
CC Rule:MF_00200}.
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DR EMBL; CP011270; AMV20315.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A142X080; -.
DR STRING; 1632864.VT03_20625; -.
DR KEGG; pls:VT03_20625; -.
DR PATRIC; fig|1632864.3.peg.4734; -.
DR Proteomes; UP000076318; Chromosome.
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-UniRule.
DR GO; GO:0006396; P:RNA processing; IEA:InterPro.
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; 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; 1.
DR SUPFAM; SSF52913; RNA 3'-terminal phosphate cyclase, RPTC, insert domain; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00200};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00200};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00200};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00200}; Reference proteome {ECO:0000313|Proteomes:UP000076318}.
FT DOMAIN 13..338
FT /note="RNA 3'-terminal phosphate cyclase"
FT /evidence="ECO:0000259|Pfam:PF01137"
FT DOMAIN 184..276
FT /note="RNA 3'-terminal phosphate cyclase insert"
FT /evidence="ECO:0000259|Pfam:PF05189"
FT ACT_SITE 320
FT /note="Tele-AMP-histidine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00200"
FT BINDING 104
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00200"
FT BINDING 285..289
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00200"
SQ SEQUENCE 353 AA; 37942 MW; 6DBAE2F2ED204243 CRC64;
MGAELVTIDG SQGEGGGQIL RSTLALSLVT RRPVRIENIR AGRPKPGLMR QHLTAVQAAA
RIGSAEVTGA EIGSKALTFV PQTVTPGRYT FSVGTAGSAT LVLQTVLPAL MIADGPSQLT
LEGGTHNQWA PTFEFLKHAY LPIVSRMGPK VTAALERHGF HPAGGGRFQV EIEPVPRLKP
LDLLERGELK NRSASAVVAN LPGHIGDREV TTILDRLNWP PTNSLVEVVP AHGPGNVVFA
TLEYEHVTEV FTGFGRVGAS AEHVANEVVR DVRNYLRSET PVGHYLADQI LLPQGLCAYQ
SRLDGEPGRS SFATGPLTRH GITHIEILRK LLDLQITVED RPDRALHVVT VGP
//
