MRNCL_FUSNN
ID MRNCL_FUSNN Reviewed; 129 AA.
AC Q8RIL0;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Mini-ribonuclease 3-like protein;
GN Name=mrnCL; OrderedLocusNames=FN1578;
OS Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / DSM 15643 /
OS BCRC 10681 / CIP 101130 / JCM 8532 / KCTC 2640 / LMG 13131 / VPI 4355).
OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; Fusobacterium.
OX NCBI_TaxID=190304;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25586 / DSM 15643 / BCRC 10681 / CIP 101130 / JCM 8532 / KCTC
RC 2640 / LMG 13131 / VPI 4355;
RX PubMed=11889109; DOI=10.1128/jb.184.7.2005-2018.2002;
RA Kapatral V., Anderson I., Ivanova N., Reznik G., Los T., Lykidis A.,
RA Bhattacharyya A., Bartman A., Gardner W., Grechkin G., Zhu L., Vasieva O.,
RA Chu L., Kogan Y., Chaga O., Goltsman E., Bernal A., Larsen N., D'Souza M.,
RA Walunas T., Pusch G., Haselkorn R., Fonstein M., Kyrpides N.C.,
RA Overbeek R.;
RT "Genome sequence and analysis of the oral bacterium Fusobacterium nucleatum
RT strain ATCC 25586.";
RL J. Bacteriol. 184:2005-2018(2002).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS).
RC STRAIN=ATCC 25586 / DSM 15643 / BCRC 10681 / CIP 101130 / JCM 8532 / KCTC
RC 2640 / LMG 13131 / VPI 4355;
RA Forouhar F., Su M., Jayaraman S., Conover K., Janjua H., Xiao R.,
RA Acton T.B., Montelione G.T., Tong L., Hunt J.F.;
RT "Crystal structure of the hypothetical protein (FN1578) from Fusobacterium
RT nucleatum, NESG target NR1.";
RL Submitted (APR-2006) to the PDB data bank.
CC -!- FUNCTION: Might be a ribonuclease involved in RNA processing.
CC -!- SIMILARITY: Belongs to the MrnC RNase family. {ECO:0000305}.
CC -!- CAUTION: Strongly resembles the MrnC Mini-3 enzyme, but is missing a
CC highly conserved, possibly catalytically important site at position 72.
CC {ECO:0000305}.
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DR EMBL; AE009951; AAL93693.1; -; Genomic_DNA.
DR RefSeq; NP_602394.1; NC_003454.1.
DR PDB; 2GSL; X-ray; 2.60 A; A/B/C/D/E/F=1-129.
DR PDBsum; 2GSL; -.
DR AlphaFoldDB; Q8RIL0; -.
DR SMR; Q8RIL0; -.
DR STRING; 190304.FN1578; -.
DR EnsemblBacteria; AAL93693; AAL93693; FN1578.
DR KEGG; fnu:FN1578; -.
DR PATRIC; fig|190304.8.peg.70; -.
DR eggNOG; COG1939; Bacteria.
DR HOGENOM; CLU_091169_2_1_0; -.
DR InParanoid; Q8RIL0; -.
DR OMA; MEYREAT; -.
DR BioCyc; FNUC190304:G1FZS-82-MON; -.
DR EvolutionaryTrace; Q8RIL0; -.
DR Proteomes; UP000002521; Chromosome.
DR GO; GO:0004525; F:ribonuclease III activity; IEA:InterPro.
DR GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR Gene3D; 1.10.1520.10; -; 1.
DR InterPro; IPR008226; Mini3_fam.
DR InterPro; IPR000999; RNase_III_dom.
DR InterPro; IPR036389; RNase_III_sf.
DR Pfam; PF00636; Ribonuclease_3; 1.
DR PIRSF; PIRSF005520; UCP005520; 1.
DR SUPFAM; SSF69065; SSF69065; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Endonuclease; Hydrolase; Nuclease; Reference proteome.
FT CHAIN 1..129
FT /note="Mini-ribonuclease 3-like protein"
FT /id="PRO_0000415998"
FT ACT_SITE 23
FT /evidence="ECO:0000255"
FT TURN 9..11
FT /evidence="ECO:0007829|PDB:2GSL"
FT HELIX 15..34
FT /evidence="ECO:0007829|PDB:2GSL"
FT HELIX 41..52
FT /evidence="ECO:0007829|PDB:2GSL"
FT HELIX 54..64
FT /evidence="ECO:0007829|PDB:2GSL"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:2GSL"
FT HELIX 70..80
FT /evidence="ECO:0007829|PDB:2GSL"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:2GSL"
FT HELIX 93..111
FT /evidence="ECO:0007829|PDB:2GSL"
FT HELIX 115..127
FT /evidence="ECO:0007829|PDB:2GSL"
SQ SEQUENCE 129 AA; 15028 MW; E760C81975B7D3E3 CRC64;
MDNVDFSKDI RDYSGLELAF LGDAIWELEI RKYYLQFGYN IPTLNKYVKA KVNAKYQSLI
YKKIINDLDE EFKVIGKRAK NSNIKTFPRS CTVMEYKEAT ALEAIIGAMY LLKKEEEIKK
IINIVIKGE
