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Database: UniProt
Entry: V8C9Z1_9HELI
LinkDB: V8C9Z1_9HELI
Original site: V8C9Z1_9HELI 
ID   V8C9Z1_9HELI            Unreviewed;       216 AA.
AC   V8C9Z1;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   RecName: Full=Endoribonuclease YbeY {ECO:0000256|HAMAP-Rule:MF_00009};
DE            EC=3.1.-.- {ECO:0000256|HAMAP-Rule:MF_00009};
GN   Name=ybeY {ECO:0000256|HAMAP-Rule:MF_00009};
GN   ORFNames=HMPREF2086_00983 {ECO:0000313|EMBL:ETD24233.1};
OS   Helicobacter macacae MIT 99-5501.
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=1357400 {ECO:0000313|EMBL:ETD24233.1, ECO:0000313|Proteomes:UP000018731};
RN   [1] {ECO:0000313|EMBL:ETD24233.1, ECO:0000313|Proteomes:UP000018731}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 99-5501 {ECO:0000313|EMBL:ETD24233.1,
RC   ECO:0000313|Proteomes:UP000018731};
RX   PubMed=25212613;
RA   Shen Z., Sheh A., Young S.K., Abouelliel A., Ward D.V., Earl A.M.,
RA   Fox J.G.;
RT   "Draft genome sequences of six enterohepatic helicobacter species isolated
RT   from humans and one from rhesus macaques.";
RL   Genome Announc. 2:e00857-e00814(2014).
CC   -!- FUNCTION: Single strand-specific metallo-endoribonuclease involved in
CC       late-stage 70S ribosome quality control and in maturation of the 3'
CC       terminus of the 16S rRNA. {ECO:0000256|HAMAP-Rule:MF_00009}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00009};
CC       Note=Binds 1 zinc ion. {ECO:0000256|HAMAP-Rule:MF_00009};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00009}.
CC   -!- SIMILARITY: Belongs to the endoribonuclease YbeY family.
CC       {ECO:0000256|ARBA:ARBA00010875, ECO:0000256|HAMAP-Rule:MF_00009}.
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:ETD24233.1}.
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DR   EMBL; AZJI01000004; ETD24233.1; -; Genomic_DNA.
DR   RefSeq; WP_023927707.1; NZ_KI669454.1.
DR   AlphaFoldDB; V8C9Z1; -.
DR   STRING; 1357400.HMPREF2086_00983; -.
DR   PATRIC; fig|1357400.3.peg.1343; -.
DR   eggNOG; COG0319; Bacteria.
DR   HOGENOM; CLU_106710_1_1_7; -.
DR   Proteomes; UP000018731; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0004521; F:RNA endonuclease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.390.30; Metalloproteases ('zincins'), catalytic domain; 1.
DR   HAMAP; MF_00009; Endoribonucl_YbeY; 1.
DR   InterPro; IPR023091; MetalPrtase_cat_dom_sf_prd.
DR   InterPro; IPR002036; YbeY.
DR   InterPro; IPR020549; YbeY_CS.
DR   NCBIfam; TIGR00043; rRNA maturation RNase YbeY; 1.
DR   PANTHER; PTHR46986; ENDORIBONUCLEASE YBEY, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR46986:SF1; ENDORIBONUCLEASE YBEY, CHLOROPLASTIC; 1.
DR   Pfam; PF02130; YbeY; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   PROSITE; PS01306; UPF0054; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00009};
KW   Endonuclease {ECO:0000256|ARBA:ARBA00022759, ECO:0000256|HAMAP-
KW   Rule:MF_00009};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00009};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00009};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_00009};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018731};
KW   Ribosome biogenesis {ECO:0000256|HAMAP-Rule:MF_00009};
KW   rRNA processing {ECO:0000256|HAMAP-Rule:MF_00009};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00009}.
FT   BINDING         171
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00009"
FT   BINDING         175
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00009"
FT   BINDING         181
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00009"
SQ   SEQUENCE   216 AA;  24155 MW;  093899D533E3C8CD CRC64;
     MLEICNHTKS TLPQGIESRL DSTVGVVLES VLDFRLDCAL DSASKSTLDS ASLDSALGYF
     CRDSKNLCEK IHIELVFVSS AKMRKINKEF LAKDYATDVL SFPLIDFPLI DSADSPLVDF
     LLEKLQDLSL DSSEFLPLLL GSIVINLPLA RKNSLKFAHS LDDEIIILFI HAVLHLLGFD
     HERDRGAHRQ KEREIMQKLD LSKSIKSLIS RASSPQ
//
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