ID A0A074M323_ERYLO Unreviewed; 338 AA.
AC A0A074M323;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 39.
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 ORFNames=EH31_15930 {ECO:0000313|EMBL:KEO88916.1};
OS Erythrobacter longus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX NCBI_TaxID=1044 {ECO:0000313|EMBL:KEO88916.1, ECO:0000313|Proteomes:UP000027647};
RN [1] {ECO:0000313|EMBL:KEO88916.1, ECO:0000313|Proteomes:UP000027647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6997 {ECO:0000313|EMBL:KEO88916.1,
RC ECO:0000313|Proteomes:UP000027647};
RA Zheng Q.;
RT "A comprehensive comparison of genomes of Erythrobacter spp. strains.";
RL Submitted (APR-2014) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KEO88916.1}.
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DR EMBL; JMIW01000007; KEO88916.1; -; Genomic_DNA.
DR RefSeq; WP_034961769.1; NZ_JMIW01000007.1.
DR AlphaFoldDB; A0A074M323; -.
DR STRING; 1044.EH31_15930; -.
DR eggNOG; COG0430; Bacteria.
DR OrthoDB; 9789235at2; -.
DR Proteomes; UP000027647; Unassembled WGS sequence.
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; 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; 1.
DR SUPFAM; SSF52913; RNA 3'-terminal phosphate cyclase, RPTC, insert domain; 1.
DR PROSITE; PS01287; RTC; 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:UP000027647}.
FT DOMAIN 9..324
FT /note="RNA 3'-terminal phosphate cyclase"
FT /evidence="ECO:0000259|Pfam:PF01137"
FT DOMAIN 180..273
FT /note="RNA 3'-terminal phosphate cyclase insert"
FT /evidence="ECO:0000259|Pfam:PF05189"
FT ACT_SITE 307
FT /note="Tele-AMP-histidine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00200"
FT BINDING 100
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00200"
FT BINDING 282..286
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00200"
SQ SEQUENCE 338 AA; 35782 MW; 453E19A1B7D6F277 CRC64;
MIIIDGSEGE GGGQVLRYSA ALSLLTGEPF TISNIRGERA KPGLMRQHVT SLEAACAIGG
AECSGLTVGA SELTFRPGRV IPGEYHFAVG TAGSTGLVLQ TVLVPLMLAD APSRLVIEGG
THAMAAPPFE FLQKTLLPVL QRMGPKLSIT LERHGFYPRG GGRIVVDIDP APLRPIECVT
RGAFKVGKVE ALVAGIPFDI ADRELKAARK VLADWPDEAF APVQLPAENG PGNALLMVAE
FEHVTEIMSG FGKLGVPAER LAKTAAKRMA GYLASQAFAG PYLQDQLLLP FAMAGRGAFT
TVKLSAHTRT AVDLIERFSG RGFRFAETAD GAHLAEVR
//
