ID A0A1F4XTS5_9BACT Unreviewed; 509 AA.
AC A0A1F4XTS5;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 13-SEP-2023, 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=A3F55_01270 {ECO:0000313|EMBL:OGC84998.1};
OS Candidatus Adlerbacteria bacterium RIFCSPHIGHO2_12_FULL_53_18.
OC Bacteria; Candidatus Adlerbacteria.
OX NCBI_TaxID=1797242 {ECO:0000313|EMBL:OGC84998.1, ECO:0000313|Proteomes:UP000178091};
RN [1] {ECO:0000313|EMBL:OGC84998.1, ECO:0000313|Proteomes:UP000178091}
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:OGC84998.1}.
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DR EMBL; MEWW01000006; OGC84998.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F4XTS5; -.
DR Proteomes; UP000178091; 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..28
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00335"
FT DOMAIN 325..418
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT COILED 59..93
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 509 AA; 56589 MW; CE514965EDE684AE CRC64;
MSITYALILM GLAGLAGIAI GYIFRWLYGL SQKGSIEVEI KQILLNAREE AKKITATAEE
EGKKILVEAE GELKEQEDKV TRAEERVFKR EEALERKQGE LDRELEGVKG RIEEVKAIKE
RADTLLAERT SELAKVAGLT KDEAKETLYK ELERESGEDL MMRLAKLERD GMERLERRAR
EILTTAIHRL GNSVASDTMA TAITIPNDDL KGKIIGKEGR NIKAFERATG VEVIIDDTPG
NIVLSSYDPL RRAVARVALE NLIIDGRIQP AKIEETVEKA KAEVNKIIKE KAEAAAFETG
VLNLDPRLLM ILGRLHFRTS YGQSVLQHSI EMAHIAGMIA EELGANPAIA RAGALLHDIG
KALDHEVQGT HVEIGRRILQ KFNVSEEVIK AMQAHHEEYP YETTESVIVQ VADAISGGRP
GARRDSVENY LKRLADIEAI ANSFAGVEKS YAISAGREVR VFVKPEEMSD LAARDLARNI
ALRIESDLKY PGEIKISVIR ETRAIEFAR
//
