ID E3GX28_METFV Unreviewed; 337 AA.
AC E3GX28;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 67.
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 OrderedLocusNames=Mfer_0114 {ECO:0000313|EMBL:ADP76917.1};
OS Methanothermus fervidus (strain ATCC 43054 / DSM 2088 / JCM 10308 / V24 S).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanothermaceae; Methanothermus.
OX NCBI_TaxID=523846 {ECO:0000313|EMBL:ADP76917.1, ECO:0000313|Proteomes:UP000002315};
RN [1] {ECO:0000313|EMBL:ADP76917.1, ECO:0000313|Proteomes:UP000002315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43054 / DSM 2088 / JCM 10308 / V24 S
RC {ECO:0000313|Proteomes:UP000002315};
RX PubMed=21304736;
RA Anderson I., Djao O.D., Misra M., Chertkov O., Nolan M., Lucas S.,
RA Lapidus A., Del Rio T.G., Tice H., Cheng J.F., Tapia R., Han C.,
RA Goodwin L., Pitluck S., Liolios K., Ivanova N., Mavromatis K.,
RA Mikhailova N., Pati A., Brambilla E., Chen A., Palaniappan K., Land M.,
RA Hauser L., Chang Y.J., Jeffries C.D., Sikorski J., Spring S., Rohde M.,
RA Eichinger K., Huber H., Wirth R., Goker M., Detter J.C., Woyke T.,
RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P.,
RA Kyrpides N.C.;
RT "Complete genome sequence of Methanothermus fervidus type strain (V24S).";
RL Stand. Genomic Sci. 3:315-324(2010).
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}.
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DR EMBL; CP002278; ADP76917.1; -; Genomic_DNA.
DR RefSeq; WP_013413195.1; NC_014658.1.
DR AlphaFoldDB; E3GX28; -.
DR STRING; 523846.Mfer_0114; -.
DR GeneID; 9961825; -.
DR KEGG; mfv:Mfer_0114; -.
DR HOGENOM; CLU_027882_0_0_2; -.
DR OrthoDB; 7994at2157; -.
DR Proteomes; UP000002315; 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 CDD; cd00874; RNA_Cyclase_Class_II; 1.
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 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:UP000002315}.
FT DOMAIN 8..325
FT /note="RNA 3'-terminal phosphate cyclase"
FT /evidence="ECO:0000259|Pfam:PF01137"
FT DOMAIN 183..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 337 AA; 36250 MW; 4DA5EA1700A254CD CRC64;
MIKIDGSYGE GGGALVRVAT ALSALTKKTI RIDNIRANRP RKGLSHQHLN AIEAVSKLCN
AEVDGLKLGS TTIIFSPKEL EGGSLNVNIG TAGSIGLVLQ ALMIPAAFSE SKTKITITGG
TDVKWAPPID YISNVTLPIL KKMGYKGKIS LLRRGYYPKG GGKVIAEIKP IKKLKPLKLI
ESEIESIEGI SYASNLPKHV ADRQAKSAYN ILKKTGLDID IDVRHDNESL SPGSGIVLWA
KGNTRIGSSS LGERGKRAEI VGKEAAKELL NFLNSGAPLD KYMGDQIIPY ISLTENSKVR
TAEFTLHAHT NVYVVKKILG KELKIENGLG KITTIST
//
