ID A0A1X9Z0X9_9SPHI Unreviewed; 523 AA.
AC A0A1X9Z0X9;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
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=CA265_02770 {ECO:0000313|EMBL:ARS38661.1};
OS Sphingobacteriaceae bacterium GW460-11-11-14-LB5.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae.
OX NCBI_TaxID=1986952 {ECO:0000313|EMBL:ARS38661.1, ECO:0000313|Proteomes:UP000194429};
RN [1] {ECO:0000313|Proteomes:UP000194429}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Ray J., Price M., Deutschbauer A.;
RL Submitted (MAY-2017) 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; CP021237; ARS38661.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X9Z0X9; -.
DR KEGG; sbx:CA265_02770; -.
DR OrthoDB; 9803205at2; -.
DR Proteomes; UP000194429; 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; 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 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:UP000194429};
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..28
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00335"
FT DOMAIN 339..432
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT REGION 76..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 523 AA; 58786 MW; CA422FF81A434A75 CRC64;
MEIVEILGYV FAVIAGIAIG VVVGRFLLRN LLKQQEVAAQ NKVKKILKDA ENNAEILKKN
KLLEAKEKFL QMKAEHEQEV NAKNNNINQR ENTMKQKEQS VNQRMENFNK KEQELDKHKS
NLEKQTELAV KKQEEVEVLK NQHLKQLETI AGLSAEEAKE QLVENLKQEA RTQAMMQVKD
IVDEAKLTAS KEAKKVVIQT IQRTATEAAI ENSVSIFHIE SDEIKGRVIG REGRNIRALE
AATGIEIIVD DTPEAIILSG FDPVRREIAR LALHRLVTDG RIHPARIEEI VAKTKKQIED
EIVEIGERTV IDLGIHGLHP ELIRMVGRMR YRSSYGQNLL HHSREVANFC ATMAAELGLN
AKMAKRAGLL HDIGKVPDDN PELPHAILGM QLAEKYKEHP EICNAIGAHH DEIEMTSMIS
PIVQACDAIS GARPGARREV VESYIKRLKD LEELALSYPG VEKTFAIQAG RELRVIVESE
RITDAQAELL AADISTRIQT EMTYPGQIKV TVIRETRSVA FAK
//