ID A0A0Q7Z4S4_9SPHN Unreviewed; 340 AA.
AC A0A0Q7Z4S4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 43.
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=ASD67_05705 {ECO:0000313|EMBL:KQZ64018.1};
OS Sphingopyxis sp. Root1497.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=1736474 {ECO:0000313|EMBL:KQZ64018.1, ECO:0000313|Proteomes:UP000051141};
RN [1] {ECO:0000313|Proteomes:UP000051141}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1497 {ECO:0000313|Proteomes:UP000051141};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQZ64018.1, ECO:0000313|Proteomes:UP000051141}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1497 {ECO:0000313|EMBL:KQZ64018.1,
RC ECO:0000313|Proteomes:UP000051141};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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}.
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:KQZ64018.1}.
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DR EMBL; LMGF01000003; KQZ64018.1; -; Genomic_DNA.
DR RefSeq; WP_056344593.1; NZ_LMGF01000003.1.
DR AlphaFoldDB; A0A0Q7Z4S4; -.
DR STRING; 1736474.ASD67_05705; -.
DR OrthoDB; 9789235at2; -.
DR Proteomes; UP000051141; 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}.
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 340 AA; 35565 MW; 2382025BBB14F46F CRC64;
MIIIDGSEGE GGGQVLRYAC ALALLTGTPF TIENIRGGRE KPGLMRQHVT AIEAACVIGG
AECTGLAVGS NSLSFRPGRV TPGDYHFAVG TAGSTGLVLQ TILVPLMLAD APSRLVIEGG
THAMAAPPFE FLERTLLPVI NRMGPTVSAR LVRHGFFPRG GGRIEVDIVP APLRPIACLA
RGGLRRVGAT AILAGIPFDV GDRELKTAAK TLADWPEDAF ATRQLPAEQG PGNALILEAA
FEHVTEVMSA FGKIGVPAER LAKTAARRMG GYLACDAFAG PYLQDQLLLP FALAGDGVFS
TVKVSQHTLT AAALVAHFVG RGFRFRSCED GATLVEVVSA
//
