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Database: UniProt
Entry: D7UUL7_LISGR
LinkDB: D7UUL7_LISGR
Original site: D7UUL7_LISGR 
ID   D7UUL7_LISGR            Unreviewed;       211 AA.
AC   D7UUL7;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   24-JAN-2024, entry version 46.
DE   RecName: Full=Ribonuclease M5 {ECO:0000256|HAMAP-Rule:MF_01469};
DE            EC=3.1.26.8 {ECO:0000256|HAMAP-Rule:MF_01469};
DE   AltName: Full=RNase M5 {ECO:0000256|HAMAP-Rule:MF_01469};
DE   AltName: Full=Ribosomal RNA terminal maturase M5 {ECO:0000256|HAMAP-Rule:MF_01469};
GN   Name=rnmV {ECO:0000256|HAMAP-Rule:MF_01469,
GN   ECO:0000313|EMBL:EFI84943.1};
GN   ORFNames=HMPREF0556_10142 {ECO:0000313|EMBL:EFI84943.1};
OS   Listeria grayi DSM 20601.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=525367 {ECO:0000313|EMBL:EFI84943.1, ECO:0000313|Proteomes:UP000010119};
RN   [1] {ECO:0000313|EMBL:EFI84943.1, ECO:0000313|Proteomes:UP000010119}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20601 {ECO:0000313|EMBL:EFI84943.1,
RC   ECO:0000313|Proteomes:UP000010119};
RA   Muzny D., Qin X., Buhay C., Dugan-Rocha S., Ding Y., Chen G., Hawes A.,
RA   Holder M., Jhangiani S., Johnson A., Khan Z., Li Z., Liu W., Liu X.,
RA   Perez L., Shen H., Wang Q., Watt J., Xi L., Xin Y., Zhou J., Deng J.,
RA   Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L., Villasana D., Johnson A.,
RA   Liu J., Liyanage D., Lorensuhewa L., Robinson T., Song A., Song B.-B.,
RA   Dinh H., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M.,
RA   Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N.,
RA   Okwuonu G., Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W.,
RA   Jakkamsetti A., Pham P., Ruth R., San Lucas F., Warren J., Zhang J.,
RA   Zhao Z., Zhou C., Zhu D., Lee S., Bess C., Blankenburg K., Forbes L.,
RA   Fu Q., Gubbala S., Hirani K., Jayaseelan J.C., Lara F., Munidasa M.,
RA   Palculict T., Patil S., Pu L.-L., Saada N., Tang L., Weissenberger G.,
RA   Zhu Y., Hemphill L., Shang Y., Youmans B., Ayvaz T., Ross M.,
RA   Santibanez J., Aqrawi P., Gross S., Joshi V., Fowler G., Nazareth L.,
RA   Reid J., Worley K., Petrosino J., Highlander S., Gibbs R.;
RL   Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Required for correct processing of both the 5' and 3' ends of
CC       5S rRNA precursor. Cleaves both sides of a double-stranded region
CC       yielding mature 5S rRNA in one step. {ECO:0000256|HAMAP-Rule:MF_01469}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage of RNA, removing 21 and 42
CC         nucleotides, respectively, from the 5'- and 3'-termini of a 5S-rRNA
CC         precursor.; EC=3.1.26.8; Evidence={ECO:0000256|HAMAP-Rule:MF_01469};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01469}.
CC   -!- SIMILARITY: Belongs to the ribonuclease M5 family. {ECO:0000256|HAMAP-
CC       Rule:MF_01469}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EFI84943.1}.
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DR   EMBL; ACCR02000002; EFI84943.1; -; Genomic_DNA.
DR   AlphaFoldDB; D7UUL7; -.
DR   STRING; 525367.HMPREF0556_10142; -.
DR   eggNOG; COG1658; Bacteria.
DR   HOGENOM; CLU_109405_0_0_9; -.
DR   Proteomes; UP000010119; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0043822; F:ribonuclease M5 activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-UniRule.
DR   CDD; cd01027; TOPRIM_RNase_M5_like; 1.
DR   Gene3D; 3.40.1360.10; -; 1.
DR   HAMAP; MF_01469; RNase_M5; 1.
DR   InterPro; IPR004466; RNase_M5.
DR   InterPro; IPR025156; RNase_M5_C.
DR   InterPro; IPR006171; TOPRIM_domain.
DR   InterPro; IPR034141; TOPRIM_RNase_M5-like.
DR   NCBIfam; TIGR00334; 5S_RNA_mat_M5; 1.
DR   PANTHER; PTHR39156; RIBONUCLEASE M5; 1.
DR   PANTHER; PTHR39156:SF1; RIBONUCLEASE M5; 1.
DR   Pfam; PF13331; DUF4093; 1.
DR   Pfam; PF01751; Toprim; 1.
DR   SMART; SM00493; TOPRIM; 1.
DR   SUPFAM; SSF110455; Toprim domain; 1.
DR   PROSITE; PS50880; TOPRIM; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01469};
KW   Endonuclease {ECO:0000256|ARBA:ARBA00022759, ECO:0000256|HAMAP-
KW   Rule:MF_01469};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01469};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_01469};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010119};
KW   Ribosome biogenesis {ECO:0000256|ARBA:ARBA00022517, ECO:0000256|HAMAP-
KW   Rule:MF_01469};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_01469};
KW   rRNA processing {ECO:0000256|ARBA:ARBA00022552, ECO:0000256|HAMAP-
KW   Rule:MF_01469};
KW   rRNA-binding {ECO:0000256|ARBA:ARBA00022730, ECO:0000256|HAMAP-
KW   Rule:MF_01469}.
FT   DOMAIN          26..109
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
SQ   SEQUENCE   211 AA;  23650 MW;  420C6E0BB64DADDA CRC64;
     MPKLWYDKSQ MRSREGTDMD QKPMIQEFIV VEGRDDTTAI HRAVLADTIE TNGSALNEKT
     IERIRLAAET RGVIVFTDPD FPGEKIRKQI DAEVPGCKHA FLSKIEARPK NGRGIGVEHA
     TPESIRKALA HFHQTAESQT AHTTLISKEL LIKMHLLGGT GSKARRARLG DILRIGYTNG
     KQLQARLNMF GIDESKLQEA YEQMKQEAGN E
//
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