SPM_005380

Uniprot: A0A037UJL0
Description: ribonuclease J
EC number: 3.1.-.-
Annotation score: 2 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 102 102 Zinc 1; via tele nitrogen; catalytic. {ECO:0000256|HAMAP-Rule:MF_01491}.; METAL 104 104 Zinc 1; via pros nitrogen; catalytic. {ECO:0000256|HAMAP-Rule:MF_01491}.; METAL 106 106 Zinc 2; catalytic. {ECO:0000256|HAMAP-Rule:MF_01491}.; METAL 107 107 Zinc 2; via tele nitrogen; catalytic. {ECO:0000256|HAMAP-Rule:MF_01491}.; METAL 171 171 Zinc 1; via tele nitrogen; catalytic. {ECO:0000256|HAMAP-Rule:MF_01491}.; METAL 193 193 Zinc 1; catalytic. {ECO:0000256|HAMAP-Rule:MF_01491}.; METAL 193 193 Zinc 2; catalytic. {ECO:0000256|HAMAP-Rule:MF_01491}.; METAL 420 420 Zinc 2; via tele nitrogen; catalytic. {ECO:0000256|HAMAP-Rule:MF_01491}.
Nucleotide binding:
Site:
Gene names (primary): rnj
Gene names (synonym):
Mass: 65,303
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 49 244 Lactamase_B. {ECO:0000259|SMART:SM00849}.
Motif:
Region: REGION 394 398 Substrate binding. {ECO:0000256|HAMAP-Rule:MF_01491, ECO:0000256|PIRSR:PIRSR004803-2}.
EMBL: AGBZ02000004
ProteinModelPortal: A0A037UJL0
MEROPS:
EnsemblBacteria KO: KAI92169
UniPathway:
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

140633-142394(-)

>nucleotide sequence
TTATTTTTTATTTAAAATTACTGGAATAATTAATGGATTACGACGTTTATAACGGTAAAT
GAAAGGAGATAATGATTGCTTGATAGCATTTTTTAGAGCCCCAAAAGTTGGCTTTTGAGT
TTTTAAAACTTCATTAACTGCTTCGGTTGCTAAGCGAATTGATTCATTAATAATATTTCC
AGATTCTTTAACATAGAAACTTCCTCTTGAAATAATCCGTGGTGGAGTTAGCAATTGGTT
ATTTTGTGAATCAATTGAAATAACAACAGCAATTAAACCATCTTTTGATAAGATTTCACG
GTCACGAACAACAGCTGTTGTTTGACCTGATAAATCTTTGCCATCAACATAGACAGCTTC
AGCTTCAATTCGTTTTCCAATTGCTGCTGTTCCATTTAATAATTCAATTTGATCACCATT
AGCACAAATAAAGACATTATCTTTTGGCACATTGACACTAATTGCTGTTTCACCATGTTG
ACGAAGCATACGATAGTCACCATGCATTGGCATAAAGTATTTTGGCTTCAATAGGGTAAA
TAATAATTTTTGTTCTTCTTGCGAAGCATGACCAGAAGTATGAATTTGATTTAGAGGACT
ATTTTCTTGTACAATAGCACCGGCACGAACTAGTTTATTAATAACTCGTTCAACATCAGC
TTGATTACCAGGAATTGGTGATGATGAAAAAATAACAGTATCACCAGGAATAATAGAAAT
ATGTTGATGTTGGTTATTTGCAATTCGTGATAATGCAGCCATTGGTTCACCTTGACTTCC
AGTACAAATAATTAATATTTCATTATCTTTATAGTTTTTAGCATCATTAGCTTTAATAAA
TGCCTTATCGGAAATTTTTAAATGTCCCATTTGACGAATAATTTTAATAATTCGATCTAA
GCTTCGACCAAAAACTAAAATTTTTCGTCCATATTTATTTGCAATTTCAACAATATGTTG
AATTCGATGGACATTTGAAGCAAAAGTTGAAATTAAAATTCGCCCTTTAGCTTTAACAAA
TAATTCACTAATATTTTTAATAATTTTTGTTTCAGTTTGAGTATAACCTTCAACTTCAGC
ATTAGTACTATCAGCCATTAATAACATAACACCTTCTTGCCCCATATTTGCCATTCGTTC
AATATCAGCACGATGTCCTAGTGGCGTTCAGTCAAATTTATAATCACCTGTTGAAACAAC
TTTTCCATTTGGAGTAACTACTGAAATTCCAAAAGCATCAGGAATACTATGATTAACAGC
AAAAAAGTTAATTTTAAAGTTTTTCGTTTTAATCACACTCATATTATCAACTTCTTTAAC
AATTGTGGTTTGTTCCAATTTTGCTTCTTTTAGCCGATCACGAATTAAAGCAGCTGCTAA
TCGTGGTGCATAAATAATTGGAATATTAACTTCACGTAATAAATAGGGAATTCCACCAAT
ATGGTCTTCGTGCCCATGCGTAATAAATAACGCTTTTATTTTTCGTTGATTTTCTTTTAA
ATAATTATAATTCGGAATAACAGCATCAACTCCAAGCATTGTTGAACTTGGGAATTTAAC
TCCTGCATCAAGCATAATTAACTCTTCATCATGCTCAATACAATATGTATTTTTTCCAAC
TTCTTCTAATCCGCCTAAAGCAAAGACTTTTGTTGGAATTTTATTTTTAACAACATTTTG
TGTTGGTTGTTTTGTTACTATACTAGTTGGTTTTGTAACTATTGTTTTGTTTTTACTTGT
TTCTTTCTTTTCTTCATTCAT

>protein sequence
MNEEKKETSKNKTIVTKPTSIVTKQPTQNVVKNKIPTKVFALGGLEEVGKNTYCIEHDEE
LIMLDAGVKFPSSTMLGVDAVIPNYNYLKENQRKIKALFITHGHEDHIGGIPYLLREVNI
PIIYAPRLAAALIRDRLKEAKLEQTTIVKEVDNMSVIKTKNFKINFFAVNHSIPDAFGIS
VVTPNGKVVSTGDYKFDWTPLGHRADIERMANMGQEGVMLLMADSTNAEVEGYTQTETKI
IKNISELFVKAKGRILISTFASNVHRIQHIVEIANKYGRKILVFGRSLDRIIKIIRQMGH
LKISDKAFIKANDAKNYKDNEILIICTGSQGEPMAALSRIANNQHQHISIIPGDTVIFSS
SPIPGNQADVERVINKLVRAGAIVQENSPLNQIHTSGHASQEEQKLLFTLLKPKYFMPMH
GDYRMLRQHGETAISVNVPKDNVFICANGDQIELLNGTAAIGKRIEAEAVYVDGKDLSGQ
TTAVVRDREILSKDGLIAVVISIDSQNNQLLTPPRIISRGSFYVKESGNIINESIRLATE
AVNEVLKTQKPTFGALKNAIKQSLSPFIYRYKRRNPLIIPVILNKK