ID A0A0F7FG59_9CREN Unreviewed; 352 AA.
AC A0A0F7FG59;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 37.
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|HAMAP-Rule:MF_00200};
GN Name=rtcA {ECO:0000256|HAMAP-Rule:MF_00200};
GN ORFNames=MA03_00435 {ECO:0000313|EMBL:AKG38060.1};
OS Infirmifilum uzonense.
OC Archaea; Thermoproteota; Thermoprotei; Thermofilales; Thermofilaceae;
OC Infirmifilum.
OX NCBI_TaxID=1550241 {ECO:0000313|EMBL:AKG38060.1, ECO:0000313|Proteomes:UP000067434};
RN [1] {ECO:0000313|EMBL:AKG38060.1, ECO:0000313|Proteomes:UP000067434}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1807-2 {ECO:0000313|EMBL:AKG38060.1,
RC ECO:0000313|Proteomes:UP000067434};
RX PubMed=26664700; DOI=10.1186/s40793-015-0105-y;
RA Toshchakov S.V., Korzhenkov A.A., Samarov N.I., Mazunin I.O., Mozhey O.I.,
RA Shmyr I.S., Derbikova K.S., Taranov E.A., Dominova I.N.,
RA Bonch-Osmolovskaya E.A., Patrushev M.V., Podosokorskaya O.A.,
RA Kublanov I.V.;
RT "Complete genome sequence of and proposal of Thermofilum uzonense sp. nov.
RT a novel hyperthermophilic crenarchaeon and emended description of the genus
RT Thermofilum.";
RL Stand. Genomic Sci. 10:122-122(2015).
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|HAMAP-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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00200}.
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DR EMBL; CP009961; AKG38060.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F7FG59; -.
DR STRING; 1550241.MA03_00435; -.
DR KEGG; thf:MA03_00435; -.
DR PATRIC; fig|1550241.5.peg.87; -.
DR HOGENOM; CLU_027882_0_0_2; -.
DR Proteomes; UP000067434; 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; 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|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00200}; 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:UP000067434}.
FT DOMAIN 10..332
FT /note="RNA 3'-terminal phosphate cyclase"
FT /evidence="ECO:0000259|Pfam:PF01137"
FT DOMAIN 191..279
FT /note="RNA 3'-terminal phosphate cyclase insert"
FT /evidence="ECO:0000259|Pfam:PF05189"
FT ACT_SITE 314
FT /note="Tele-AMP-histidine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00200"
FT BINDING 103
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00200"
SQ SEQUENCE 352 AA; 37865 MW; 1E49B1B121B94B90 CRC64;
MMIEIDGSFG EGGGQLLRYS VALAALTGEP LRIYNIRAKR DNPGLRPQHL AAVKFIADLV
RAEVEGLRVG STEIIFKPTL KQLPSGTYSV DIGTAGSVTL FLQATLPVLI AASGSLSMQV
KGGTSVRWSP PYHYFENILL RLFSKIGVKA SSRLIRHGFY PEGGGIVAVK TEPSYPLKSI
KLTGGPRATP VEGISYSANL PCNIAKRQAV SATQLLSQRG YQVSQIRLDC ETPAIGKGTG
IVLWSFVGDG IVGGDSIGEK GKPAEVVGRE AAENILKSLE AQVPVDPHAA DNLVIYLSLA
EGESMFYTSQ LTLHLETALE LCKNILGAHY KIDEEENKFK ITVRGIGFTP KR
//
