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Database: UniProt
Entry: A0A1I2SMN2_9BACT
LinkDB: A0A1I2SMN2_9BACT
Original site: A0A1I2SMN2_9BACT 
ID   A0A1I2SMN2_9BACT        Unreviewed;       511 AA.
AC   A0A1I2SMN2;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
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   ORFNames=SAMN05216383_11953 {ECO:0000313|EMBL:SFG54038.1};
OS   Prevotella sp. KH2C16.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=1855325 {ECO:0000313|EMBL:SFG54038.1, ECO:0000313|Proteomes:UP000198560};
RN   [1] {ECO:0000313|Proteomes:UP000198560}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KH2C16 {ECO:0000313|Proteomes:UP000198560};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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; FOOW01000019; SFG54038.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I2SMN2; -.
DR   STRING; 1855325.SAMN05216383_11953; -.
DR   OrthoDB; 9803205at2; -.
DR   Proteomes; UP000198560; Unassembled WGS sequence.
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; 1.10.3210.10; Hypothetical protein af1432; 1.
DR   Gene3D; 3.30.1370.10; K Homology domain, type 1; 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; 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   Coiled coil {ECO:0000256|SAM:Coils};
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:UP000198560};
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..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00335"
FT   DOMAIN          327..420
FT                   /note="HD"
FT                   /evidence="ECO:0000259|PROSITE:PS51831"
FT   COILED          47..144
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   511 AA;  57314 MW;  18E340325FF1CF16 CRC64;
     MTTILIVAAI ALVIGIAAGY LIFRYVIKGK YKGIVEAANK EADVIKEKKL LEVKEKFLNK
     KSELEKEVQV RNQKIQQNEN RLKQREISLN QRQEELGRKK MEIDQQQQRV DSEKKHLQAK
     QVDLEKMQEQ ERMKLEELSG LSAEEAKSRL IESLKDQAKL DAASYVNEIV ADAKLDANRQ
     AKKIVIQTIQ RVATETAIEN SVSVFHIDND EIKGRIIGRE GRNIRALEAA TGVEIVVDDT
     PEAIVISAFD PVRREVCRLA LHQLVADGRI HPARIEEVVA KVKKQLDNEI IETGKRTTID
     LGIHGLHPEL IRIVGKMKYR SSYGQNLLQH ARETANLCAI MASELGLNPK KAKRAGLLHD
     IGKVPDEESE LPHALYGAKI AEKYKEKPDI CNAIGAHHDE VEMQTLLAPI VQVCDAISGA
     RPGARREVVE AYIKRLNDLE SIAMSYPGVT KTYAIQAGRE LRVIVGADKM NDEESVKLSD
     EIATKIQNEM TYPGQVKITV IRETRSVAYA K
//
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