ID A0A1F7VFC8_9BACT Unreviewed; 508 AA.
AC A0A1F7VFC8;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 13-SEP-2023, entry version 19.
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=A3H75_02930 {ECO:0000313|EMBL:OGL89240.1};
OS Candidatus Uhrbacteria bacterium RIFCSPLOWO2_02_FULL_51_9.
OC Bacteria; Candidatus Uhrbacteria.
OX NCBI_TaxID=1802410 {ECO:0000313|EMBL:OGL89240.1, ECO:0000313|Proteomes:UP000176678};
RN [1] {ECO:0000313|EMBL:OGL89240.1, ECO:0000313|Proteomes:UP000176678}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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}.
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:OGL89240.1}.
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DR EMBL; MGES01000011; OGL89240.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F7VFC8; -.
DR STRING; 1802410.A3H75_02930; -.
DR Proteomes; UP000176678; 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 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..24
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00335"
FT DOMAIN 325..417
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT COILED 33..128
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 508 AA; 57481 MW; 897B62338CFA19F1 CRC64;
MDTILPILVS GLIMGAGIGI GYIIRKYVAQ ARANSVETRA EALLTEAKNQ QQELIMRAKE
KAIAMLEDGK KEEETRRHEI RALQDRLEKR EGLFDEKLIE FQEKQQRLQE KSTQLDTERA
RVEEIKTAQV TELERVAKLS RDEARELIMQ RVKEELQEDL AVRVMKLERE SSDIFEQKAK
RILSDTIHRI ASSHAAEVTT SIVQLPSEDM KGRIIGKEGR NIKTLERITG CDLIVDDTPE
IITISSFSPI RRQVAKIALE KLIEDGRIQP ARIEAFVEDA KKDLARDMKK TAEEALYELG
ITGLDPKLVM IIGRLKYRYS YGQNNIMHAK EVANLSALLA EELGVDRALA RKAGFLHDIG
KAIDHETEGG HPEIGYRILL KFGLPEEIAY CCIAHHEDKP KTLLGAIVKA ADAISGGRPG
ARRDSYEQYI TRLQDLENIA TGFTGVEKAY AIQAGREVRV FVNPHNIDDY AAYTLAKDIA
RKIEQEMQYP GEIRVSVIRE TRVIEYAK
//
