(data stored in ACNUC10043 zone)

HOGENOM: MEKAN1_1_PE1

ID   MEKAN1_1_PE1                         STANDARD;      PRT;   352 AA.
AC   MEKAN1_1_PE1; Q8TZC9;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=RNA 3'-terminal phosphate cyclase; Short=RNA cyclase;
DE   Short=RNA-3'-phosphate cyclase; EC=6.5.1 4; (MEKAN1_1.PE1).
GN   Name=rtcA; OrderedLocusNames=MK0001;
OS   METHANOPYRUS KANDLERI AV19.
OC   Archaea; Euryarchaeota; Methanopyri; Methanopyrales; Methanopyraceae;
OC   Methanopyrus.
OX   NCBI_TaxID=190192;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS MEKAN1_1.PE1.
CC       Methanopyrus kandleri AV19, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:RTCA_METKA
CC   -!- FUNCTION: Catalyzes the conversion of 3'-phosphate to a 2',3'-
CC       cyclic phosphodiester at the end of RNA. The mechanism of action
CC       of the enzyme occurs in 3 steps: (A) adenylation of the enzyme by
CC       ATP; (B) transfer of adenylate to an RNA-N3'P to produce RNA-
CC       N3'PP5'A; (C) and attack of the adjacent 2'-hydroxyl on the 3'-
CC       phosphorus in the diester linkage to produce the cyclic end
CC       product. The biological role of this enzyme is unknown but it is
CC       likely to function in some aspects of cellular RNA processing (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + RNA 3'-terminal-phosphate = AMP +
CC       diphosphate + RNA terminal-2',3'-cyclic-phosphate.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Potential).
CC   -!- SIMILARITY: Belongs to the RNA 3'-terminal cyclase family. Type 1
CC       subfamily.
CC   -!- GENE_FAMILY: HOG000015264 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; Q8TZC9; -.
DR   EMBL; AE009439; AAM01218.1; -; Genomic_DNA.
DR   RefSeq; NP_613288.1; NC_003551.1.
DR   ProteinModelPortal; Q8TZC9; -.
DR   GeneID; 1477327; -.
DR   GenomeReviews; AE009439_GR; MK0001.
DR   KEGG; mka:MK0001; -.
DR   NMPDR; fig|190192.1.peg.1; -.
DR   OMA; GGTDVAW; -.
DR   ProtClustDB; PRK04204; -.
DR   BioCyc; MKAN190192:MK0001-MON; -.
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:EC.
DR   GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR   HAMAP; MF_00200; RTC; 1; -.
DR   InterPro; IPR013791; RNA3'-term_phos_cycl_insert.
DR   InterPro; IPR023797; RNA3'_phos_cyclase_dom.
DR   InterPro; IPR020719; RNA3'_term_phos_cycl-like_CS.
DR   InterPro; IPR013796; RNA3'_term_phos_cycl_insert.
DR   InterPro; IPR020723; RNA3'_term_phos_cycl_prd.
DR   InterPro; IPR017770; RNA3'_term_phos_cycl_sub.
DR   InterPro; IPR000228; RNA3'_term_phos_cyclase.
DR   InterPro; IPR013792; RNA3'P_cycl/enolpyr_Trfase_a/b.
DR   Gene3D; G3DSA:3.65.10.20; RNA3'_term_phos_cycl; 2.
DR   PANTHER; PTHR11096; RNA3'_term_phos_cycl; 1.
DR   Pfam; PF01137; RTC; 1.
DR   Pfam; PF05189; RTC_insert; 1.
DR   SUPFAM; SSF52913; RNA3'-term_phos_cycl_insert; 1.
DR   SUPFAM; SSF55205; RNA3'_cycl/enolpyr_transf_A/B; 2.
DR   TIGRFAMs; TIGR03399; RNA_3prim_cycl; 1.
DR   PROSITE; PS01287; RTC; 1.
DR   HOGENOMDNA; MEKAN1_1.PE1; -.
KW   ATP-binding; Complete proteome; Cytoplasm; Ligase; Nucleotide-binding;
KW   Reference proteome.
SQ   SEQUENCE   352 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSLIEIDGSY GEGGGQILRT AVGMSALTGE PVRIYNIRAN RPRPGLSHQH LHAVKAVAEI
     CDAECEGLEI GSTEIVFEPG KVKGGEYEVD IGTAGSVTLL LQAVKLAAIA ADGPVEMEVR
     GGTDVKWSPP VDYEINVNAH YLDRLGYRYE LEVLRRGHYP RGGGIVRARM EPPKRLKPLE
     AVKFGELESV RGISHCVRLP PHVAERQAKA ASEIIERELG IRPEIEIETY PKGRDPHLGP
     GSGIVLWAED DQGNRIGADA LGEKGKPAEV VGREAAEQLV QRLRTGMALD EHMGDQILPF
     LAIADGESVF GVTGVDPHLP TNAWVVEKFL PVSVEIRGKE GEPATVEVRP EG
//

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