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Database: UniProt
Entry: A0A1X9Z0X9_9SPHI
LinkDB: A0A1X9Z0X9_9SPHI
Original site: A0A1X9Z0X9_9SPHI 
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
//
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