RTCA_PYRHO
ID RTCA_PYRHO Reviewed; 341 AA.
AC O59198;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=RNA 3'-terminal phosphate cyclase;
DE Short=RNA cyclase;
DE Short=RNA-3'-phosphate cyclase;
DE EC=6.5.1.4;
GN Name=rtcA; OrderedLocusNames=PH1529; ORFNames=PHCV028;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
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 (By similarity). {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the RNA 3'-terminal cyclase family. Type 1
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA30639.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BA000001; BAA30639.1; ALT_INIT; Genomic_DNA.
DR PIR; G71029; G71029.
DR RefSeq; WP_048053416.1; NC_000961.1.
DR PDB; 4O89; X-ray; 1.90 A; A/B=1-341.
DR PDB; 4O8J; X-ray; 2.04 A; A/B=1-341.
DR PDBsum; 4O89; -.
DR PDBsum; 4O8J; -.
DR AlphaFoldDB; O59198; -.
DR SMR; O59198; -.
DR STRING; 70601.3257956; -.
DR EnsemblBacteria; BAA30639; BAA30639; BAA30639.
DR GeneID; 1443845; -.
DR KEGG; pho:PH1529; -.
DR eggNOG; arCOG04125; Archaea.
DR OMA; PKPGLSH; -.
DR OrthoDB; 52581at2157; -.
DR BRENDA; 6.5.1.4; 5244.
DR Proteomes; UP000000752; 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; 3.30.360.20; -; 1.
DR Gene3D; 3.65.10.20; -; 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 PANTHER; PTHR11096; PTHR11096; 1.
DR PANTHER; PTHR11096:SF0; PTHR11096:SF0; 1.
DR Pfam; PF01137; RTC; 1.
DR Pfam; PF05189; RTC_insert; 1.
DR PIRSF; PIRSF005378; RNA3'_term_phos_cycl_euk; 1.
DR SUPFAM; SSF55205; SSF55205; 1.
DR TIGRFAMs; TIGR03399; RNA_3prim_cycl; 1.
DR PROSITE; PS01287; RTC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Ligase; Nucleotide-binding.
FT CHAIN 1..341
FT /note="RNA 3'-terminal phosphate cyclase"
FT /id="PRO_0000156433"
FT ACT_SITE 307
FT /note="Tele-AMP-histidine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 100
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 283..287
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT STRAND 2..5
FT /evidence="ECO:0007829|PDB:4O89"
FT HELIX 13..26
FT /evidence="ECO:0007829|PDB:4O89"
FT STRAND 30..34
FT /evidence="ECO:0007829|PDB:4O89"
FT STRAND 38..41
FT /evidence="ECO:0007829|PDB:4O89"
FT HELIX 46..59
FT /evidence="ECO:0007829|PDB:4O89"
FT STRAND 62..65
FT /evidence="ECO:0007829|PDB:4O89"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:4O89"
FT STRAND 85..88
FT /evidence="ECO:0007829|PDB:4O89"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:4O8J"
FT HELIX 95..106
FT /evidence="ECO:0007829|PDB:4O89"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:4O89"
FT STRAND 113..122
FT /evidence="ECO:0007829|PDB:4O89"
FT HELIX 129..134
FT /evidence="ECO:0007829|PDB:4O89"
FT HELIX 136..141
FT /evidence="ECO:0007829|PDB:4O89"
FT TURN 142..144
FT /evidence="ECO:0007829|PDB:4O89"
FT STRAND 147..153
FT /evidence="ECO:0007829|PDB:4O89"
FT TURN 157..159
FT /evidence="ECO:0007829|PDB:4O89"
FT STRAND 162..168
FT /evidence="ECO:0007829|PDB:4O89"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:4O89"
FT STRAND 185..197
FT /evidence="ECO:0007829|PDB:4O89"
FT HELIX 199..213
FT /evidence="ECO:0007829|PDB:4O89"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:4O89"
FT STRAND 220..227
FT /evidence="ECO:0007829|PDB:4O89"
FT STRAND 233..244
FT /evidence="ECO:0007829|PDB:4O89"
FT STRAND 246..252
FT /evidence="ECO:0007829|PDB:4O89"
FT HELIX 259..274
FT /evidence="ECO:0007829|PDB:4O89"
FT STRAND 278..280
FT /evidence="ECO:0007829|PDB:4O89"
FT HELIX 282..287
FT /evidence="ECO:0007829|PDB:4O89"
FT HELIX 289..295
FT /evidence="ECO:0007829|PDB:4O89"
FT STRAND 297..302
FT /evidence="ECO:0007829|PDB:4O89"
FT HELIX 306..319
FT /evidence="ECO:0007829|PDB:4O89"
FT STRAND 323..327
FT /evidence="ECO:0007829|PDB:4O89"
FT STRAND 333..339
FT /evidence="ECO:0007829|PDB:4O89"
SQ SEQUENCE 341 AA; 37167 MW; 1E24A4F6BF9FAC29 CRC64;
MITIDGSYGE GGGQILRTSV ALSTITGEPV RIVNIRANRP NPGLRPQHLH AILALKHLAN
AEVKGAHVGS RELVFIPKKL EAKEISIDIG TAGSITLVLQ ALLPAMVFAR EKVKFRITGG
TDVSWSPPVD YLSNVTLFAL EKIGIHGEIR VIRRGHYPKG GGIVEGYVEP WNEKRELVAK
EYSRIIKIEG ISHATNLPSH VAERQARAAK DELLQLKVPI EIRTEISRSI GPGSGIVVWA
ETDCLRLGGD ALGKKGKPAE IVGKEAAQEL LDQLKPGHCV DKFLGDQLIP FLAFSGGVIW
VSEITNHLKT NIWVVESFLG RIFDVDGNVG EPGKIRVIRR V
