ACL_RS01545
  | Uniprot: A9NF01
Description: ribonuclease J EC number: 3.1.-.- Annotation score: 3 out of 5 Miscellaneous [CC]: Protein existence: Inferred from homology Catalytic activity: Cofactor: COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-Rule:MF_01491}; ; Note=Binds up to 2 Zn(2+) ions per subunit. It is not clear if Zn(2+) or Mg(2+) is physiologically important. {ECO:0000256|HAMAP-Rule:MF_01491} Enzyme regulation: Function [CC]: FUNCTION: An RNase that has 5'-3' exonuclease and possibly endonuclease activity. Involved in maturation of rRNA and in some organisms also mRNA maturation and/or decay. {ECO:0000256|HAMAP-Rule:MF_01491}. Pathway: Active site: Binding site: Calcium binding: DNA binding: Metal binding: METAL 77 77 Zinc 1; via tele nitrogen; catalytic. {ECO:0000256|HAMAP-Rule:MF_01491}.; METAL 79 79 Zinc 1; via pros nitrogen; catalytic. {ECO:0000256|HAMAP-Rule:MF_01491}.; METAL 81 81 Zinc 2; catalytic. {ECO:0000256|HAMAP-Rule:MF_01491}.; METAL 82 82 Zinc 2; via tele nitrogen; catalytic. {ECO:0000256|HAMAP-Rule:MF_01491}.; METAL 146 146 Zinc 1; via tele nitrogen; catalytic. {ECO:0000256|HAMAP-Rule:MF_01491}.; METAL 168 168 Zinc 1; catalytic. {ECO:0000256|HAMAP-Rule:MF_01491}.; METAL 168 168 Zinc 2; catalytic. {ECO:0000256|HAMAP-Rule:MF_01491}.; METAL 395 395 Zinc 2; via tele nitrogen; catalytic. {ECO:0000256|HAMAP-Rule:MF_01491}. Nucleotide binding: Site: Gene names (primary): rnj Gene names (synonym): Mass: 62,330 Subunit structure [CC]: SUBUNIT: Homodimer, may be a subunit of the RNA degradosome. {ECO:0000256|HAMAP-Rule:MF_01491}. Gene ontology (GO): cytoplasm [GO:0005737]; 5'-3' exoribonuclease activity [GO:0004534]; endoribonuclease activity [GO:0004521]; RNA binding [GO:0003723]; zinc ion binding [GO:0008270]; rRNA processing [GO:0006364] Gene ontology IDs: GO:0003723; GO:0004521; GO:0004534; GO:0005737; GO:0006364; GO:0008270 Chain: Signal peptide: Domain [CC]: Sequence similarities: SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. RNA-metabolizing metallo-beta-lactamase-like family. Bacterial RNase J subfamily. {ECO:0000256|HAMAP-Rule:MF_01491}. Protein families: Metallo-beta-lactamase superfamily, RNA-metabolizing metallo-beta-lactamase-like family, Bacterial RNase J subfamily Coiled coil: Domain [FT]: DOMAIN 24 219 Lactamase_B. {ECO:0000259|SMART:SM00849}. Motif: Region: REGION 369 373 Substrate binding. {ECO:0000256|HAMAP-Rule:MF_01491, ECO:0000256|PIRSR:PIRSR004803-2}. EMBL: CP000896 ProteinModelPortal: A9NF01 MEROPS: EnsemblBacteria KO: ABX80931 UniPathway: K12574 CDD: Gene3D: HAMAP: 3.60.15.10 InterPro: MF_01491 PANTHER: IPR001279;IPR011108;IPR004613;IPR030854;IPR001587 PIRSF: PTHR11203:SF22 PRINTS: PIRSF004803 PROSITE: Pfam: PS01292 ProDom: PF00753;PF07521 SMART: SUPFAM: SM00849 TIGRFAMs: SSF56281 |
318871-320554(-) >nucleotide sequence GTCACTTAATTGATCAATGATCATTTGTTTTAAGTTGAGTTCATTATAACTCTTCTTTGG TAATTCTCTTAAAGTAATATGTTTAACCATGCTAGCTAAACTTGAAGTTAATTCTTCATT ACCCTTCATATAAATGAAACCACGTGAGATTACAGTTGGCTCATTGATTAATGTTTTAGT TTCTAAGTCAATAGATAGGATTACTGAGAATAAACCTTCTTCAGATAATATCTTTCGTTC TCTTAAGACATTAGAACCGATATTACCAATACCTGTACCATCAATATAAATATCTCCGGC TTGGACTTTACCTGCATAACGAATGCTTTCTTTATTAAGTGCTGCAACATCACCATTATC CATAATTAATATATTATTTGGATCAACACCACACTCAACTGCTAATTGTTTATGACGTTT GAGCATTCGATGTTCACCGTGCATTGGTATAAAGTGTTTAGGTTTTACGAGTGTTAACAT AAGTTTTAAGTCTGGTCCACTACCATGACCTGATGTATGTGTATCTGTAATAGGTCCATG GGTAATGACGTTTACATCATTTCTGAACAAGAGGTTAATGGTTTTATTAATTGGATCTTG ATTACCAGGAATTGGAGAAGAAGAAAAAATTACAGTATCACCTTTAACAGTTTTAATTTG TCTGTGTGAGCCATTAGCAATTCTTGATAAAGCTGCTAAAGGTTCACCTTGAGAACCTGT AACTAATATACATGTTTCCTCTAAGGTATATTTTTTTAATTCCTCAGGTCCAACAATTGT ACCCTTTTTAGGTTTAATATAACCAGATTGTTGTCCGGCTTCAATGGTTCTTTCCATGGA ACGGCCAAATACCGCGATTTTACGACCGGTTAATTCGGCAGCTTCAATGATTTGTTGAAT TCTATAAAGGTTAGATGCGAAGGTTGCGATAATAATTCTACCAGGGATTCTAGTAAAGAG TTCATTAATAGAACGTCCTACTTTAGATTCAGATTGAATTAAACCGTCTTGTTCAGCATT TGTAGAGTCTGATACTAAAAGAAGTGTACCTTCTTGGCCTAAATTTGCTAATTTTTCATA TTCTGCATGTGGTCCTACTGGTGTGTAGTCGATTTTAAAATCACCTGTATGAAATAATGG TCCCTCAGGCGTTCTAAACACAATACCAAACATATCTGGAATAGAGTGGTTTAATCTAAT AAAGGATACAACCACATCTTTAAAGTTATAGGTATAGTAGGATTTATATTCTTCAATTTT AGGTGCACGTAAATCTTTATGTTCACCTAATTTATATTCAATTAAATCAACAGCAATACC AGAAGCATAGATTCTTGGAATCTTTACTTGACGTAATAAATAAGGTATACCACCAATATG ATCCTCATGACCATGCGTTATGAATAAACCTACAATACGGTCCTCATTTTCTTTTAAATA AGTATAATCTGGAATCACATAATCAATACCTAGTAGATCATCATCGGGAAAAAGGATCCC TGCGTCCACTACAAAAATTTGATTATTTATTTCATATACATAGGTATTTTTACCTACTTC ACCTAATCCACCTAGCGCAAAAACTCCGATTTCGCCGGTTTTCAACAACGTGTTTTTTGA CAT >protein sequence TYLKENEDRIVGLFITHGHEDHIGGIPYLLRQVKIPRIYASGIAVDLIEYKLGEHKDLRA PKIEEYKSYYTYNFKDVVVSFIRLNHSIPDMFGIVFRTPEGPLFHTGDFKIDYTPVGPHA EYEKLANLGQEGTLLLVSDSTNAEQDGLIQSESKVGRSINELFTRIPGRIIIATFASNLY RIQQIIEAAELTGRKIAVFGRSMERTIEAGQQSGYIKPKKGTIVGPEELKKYTLEETCIL VTGSQGEPLAALSRIANGSHRQIKTVKGDTVIFSSSPIPGNQDPINKTINLLFRNDVNVI THGPITDTHTSGHGSGPDLKLMLTLVKPKHFIPMHGEHRMLKRHKQLAVECGVDPNNILI MDNGDVAALNKESIRYAGKVQAGDIYIDGTGIGNIGSNVLRERKILSEEGLFSVILSIDL ETKTLINEPTVISRGFIYMKGNEELTSSLASMVKHITLRELPKKSYNELNLKQMIIDQLS DKIYDITLRKPMILPIIMNI |
© Fisunov Lab of Proteomics, 2016.