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Database: UniProt
Entry: C7N5C4_SLAHD
LinkDB: C7N5C4_SLAHD
Original site: C7N5C4_SLAHD 
ID   C7N5C4_SLAHD            Unreviewed;       513 AA.
AC   C7N5C4;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   27-MAR-2024, entry version 83.
DE   RecName: Full=Ribonuclease Y {ECO:0000256|HAMAP-Rule:MF_00335};
DE            Short=RNase Y {ECO:0000256|HAMAP-Rule:MF_00335};
DE            EC=3.1.-.- {ECO:0000256|HAMAP-Rule:MF_00335};
GN   Name=rny {ECO:0000256|HAMAP-Rule:MF_00335};
GN   OrderedLocusNames=Shel_10740 {ECO:0000313|EMBL:ACV22109.1};
OS   Slackia heliotrinireducens (strain ATCC 29202 / DSM 20476 / NCTC 11029 /
OS   RHS 1) (Peptococcus heliotrinreducens).
OC   Bacteria; Actinomycetota; Coriobacteriia; Eggerthellales; Eggerthellaceae;
OC   Slackia.
OX   NCBI_TaxID=471855 {ECO:0000313|EMBL:ACV22109.1, ECO:0000313|Proteomes:UP000002026};
RN   [1] {ECO:0000313|EMBL:ACV22109.1, ECO:0000313|Proteomes:UP000002026}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29202 / DSM 20476 / NCTC 11029 / RHS 1
RC   {ECO:0000313|Proteomes:UP000002026};
RX   PubMed=21304663; DOI=10.4056/sigs.37633;
RA   Pukall R., Lapidus A., Nolan M., Copeland A., Glavina Del Rio T., Lucas S.,
RA   Chen F., Tice H., Cheng J.F., Chertkov O., Bruce D., Goodwin L., Kuske C.,
RA   Brettin T., Detter J.C., Han C., Pitluck S., Pati A., Mavrommatis K.,
RA   Ivanova N., Ovchinnikova G., Chen A., Palaniappan K., Schneider S.,
RA   Rohde M., Chain P., D'haeseleer P., Goker M., Bristow J., Eisen J.A.,
RA   Markowitz V., Kyrpides N.C., Klenk H.P., Hugenholtz P.;
RT   "Complete genome sequence of Slackia heliotrinireducens type strain (RHS
RT   1).";
RL   Stand. Genomic Sci. 1:234-241(2009).
CC   -!- FUNCTION: Endoribonuclease that initiates mRNA decay.
CC       {ECO:0000256|HAMAP-Rule:MF_00335}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00335};
CC       Single-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_00335}.
CC   -!- SIMILARITY: Belongs to the RNase Y family. {ECO:0000256|HAMAP-
CC       Rule:MF_00335}.
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DR   EMBL; CP001684; ACV22109.1; -; Genomic_DNA.
DR   RefSeq; WP_012798212.1; NC_013165.1.
DR   AlphaFoldDB; C7N5C4; -.
DR   STRING; 471855.Shel_10740; -.
DR   KEGG; shi:Shel_10740; -.
DR   eggNOG; COG1418; Bacteria.
DR   HOGENOM; CLU_028328_1_0_11; -.
DR   Proteomes; UP000002026; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004521; F:RNA endonuclease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006402; P:mRNA catabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00077; HDc; 1.
DR   CDD; cd22431; KH-I_RNaseY; 1.
DR   Gene3D; 3.30.300.20; -; 1.
DR   Gene3D; 1.10.3210.10; Hypothetical protein af1432; 1.
DR   HAMAP; MF_00335; RNase_Y; 1.
DR   InterPro; IPR003607; HD/PDEase_dom.
DR   InterPro; IPR006674; HD_domain.
DR   InterPro; IPR006675; HDIG_dom.
DR   InterPro; IPR004087; KH_dom.
DR   InterPro; IPR015946; KH_dom-like_a/b.
DR   InterPro; IPR004088; KH_dom_type_1.
DR   InterPro; IPR036612; KH_dom_type_1_sf.
DR   InterPro; IPR017705; Ribonuclease_Y.
DR   InterPro; IPR022711; RNase_Y_N.
DR   NCBIfam; TIGR00277; HDIG; 1.
DR   NCBIfam; TIGR03319; RNase_Y; 1.
DR   PANTHER; PTHR12826; RIBONUCLEASE Y; 1.
DR   PANTHER; PTHR12826:SF15; RIBONUCLEASE Y; 1.
DR   Pfam; PF01966; HD; 1.
DR   Pfam; PF00013; KH_1; 1.
DR   Pfam; PF12072; RNase_Y_N; 1.
DR   SMART; SM00471; HDc; 1.
DR   SMART; SM00322; KH; 1.
DR   SUPFAM; SSF54791; Eukaryotic type KH-domain (KH-domain type I); 1.
DR   SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR   PROSITE; PS51831; HD; 1.
DR   PROSITE; PS50084; KH_TYPE_1; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_00335};
KW   Endonuclease {ECO:0000256|ARBA:ARBA00022759, ECO:0000256|HAMAP-
KW   Rule:MF_00335};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00335};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_00335};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_00335};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002026};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_00335}; Transmembrane {ECO:0000256|HAMAP-Rule:MF_00335};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00335}.
FT   TRANSMEM        6..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00335"
FT   DOMAIN          329..422
FT                   /note="HD"
FT                   /evidence="ECO:0000259|PROSITE:PS51831"
FT   REGION          95..123
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   513 AA;  57273 MW;  AB5950AF1605F0DD CRC64;
     MDYVIVILVL IVGIAAGVAI GLIVSRNMAN SSTRRAADEA KRLIDDAERQ ADTLRREAVV
     EAKDEVLKMK QEAQAENKER MREVRAAENR INQREESLDR RVESLDAREH QLSSMQGQVE
     RRERDVAKAM EEVNVRLEEV AGMSPQEAKE ELLDSLRDEV THESAAIIRD AEQRTKAEAD
     RNAREILSLA IQRVAADHTA ETTVKTIHIP SDDLKGRIIG REGRNIRSFE QLTGVNLLID
     DTPECVTISC FDPVRREIGR ITMENLIADG RIHPARIEEM FSKAERLVNQ QVQEAGEQAT
     FDCGIHDLHP ELVRTLGRLR YRTSYGQSVL NHSLEVAYLC GVMASELGLD PAPAKRAGLL
     HDIGKAIDHE VEGPHALIGG DLARRFGERP EIVHAIEAHH NDIETNSVID VLVQAADAVS
     AARPGARKES LESYIKRLEK FEEIANAHPG VERTYAMQAG REIRVMVAPE QVDEAASVVL
     AHDIAKQIED EMQYPGQVKV VVIRESRAID YAK
//
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