ID L7UFT6_MYXSD Unreviewed; 338 AA.
AC L7UFT6;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 58.
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 OrderedLocusNames=MYSTI_05472 {ECO:0000313|EMBL:AGC46750.1};
OS Myxococcus stipitatus (strain DSM 14675 / JCM 12634 / Mx s8).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Myxococcaceae; Myxococcus.
OX NCBI_TaxID=1278073 {ECO:0000313|EMBL:AGC46750.1, ECO:0000313|Proteomes:UP000011131};
RN [1] {ECO:0000313|EMBL:AGC46750.1, ECO:0000313|Proteomes:UP000011131}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14675 / JCM 12634 / Mx s8
RC {ECO:0000313|Proteomes:UP000011131};
RX PubMed=23516218; DOI=10.1128/genomeA.00100-13;
RA Huntley S., Kneip S., Treuner-Lange A., Sogaard-Andersen L.;
RT "Complete genome sequence of Myxococcus stipitatus strain DSM 14675, a
RT fruiting myxobacterium.";
RL Genome Announc. 1:E0010013-E0010013(2013).
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; CP004025; AGC46750.1; -; Genomic_DNA.
DR RefSeq; WP_015351006.1; NC_020126.1.
DR AlphaFoldDB; L7UFT6; -.
DR STRING; 1278073.MYSTI_05472; -.
DR KEGG; msd:MYSTI_05472; -.
DR PATRIC; fig|1278073.3.peg.5547; -.
DR eggNOG; COG0430; Bacteria.
DR HOGENOM; CLU_027882_0_0_7; -.
DR OrthoDB; 9789235at2; -.
DR Proteomes; UP000011131; 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}.
FT DOMAIN 9..324
FT /note="RNA 3'-terminal phosphate cyclase"
FT /evidence="ECO:0000259|Pfam:PF01137"
FT DOMAIN 179..272
FT /note="RNA 3'-terminal phosphate cyclase insert"
FT /evidence="ECO:0000259|Pfam:PF05189"
FT ACT_SITE 306
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 281..285
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00200"
SQ SEQUENCE 338 AA; 36484 MW; 8A6C92D1642C85F6 CRC64;
MLRIDGSKGE GGGQVLRTSL ALSLVTGTPF TMTNIRAGRA KPGLLRQHLT AVKAAESVGA
AEVSGAELGS RELTFRPRTI AAGNYHFAVG TAGSATLVFQ TVLPALLHAA EPSTLVLEGG
THNPAAPPFD FLTRAYLPLL NKMGPEVSAT LERPGFFPAG GGKFRVDLQP RALKPLSLLE
RGRVLRREVK AVVAMIPFDV AKREMETAGA LLKWRPDELR VEELKRTACP GNVLVAEVES
EHVTEVFTGF GERGKRAEVV AEEVASEVKR YLDAEVPVGE HLCDQLLLLF ALAKGGTFRT
VPLDGHAVTQ IETMSHFLEV KVDVREVSRE VREVVVRG
//
