RNY_CAMHC
ID RNY_CAMHC Reviewed; 517 AA.
AC A7I2Y9;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 2.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=Ribonuclease Y {ECO:0000255|HAMAP-Rule:MF_00335};
DE Short=RNase Y {ECO:0000255|HAMAP-Rule:MF_00335};
DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_00335};
GN Name=rny {ECO:0000255|HAMAP-Rule:MF_00335}; OrderedLocusNames=CHAB381_1330;
OS Campylobacter hominis (strain ATCC BAA-381 / LMG 19568 / NCTC 13146 /
OS CH001A).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=360107;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-381 / LMG 19568 / NCTC 13146 / CH001A;
RA Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G.,
RA Mandrell R.E., Nelson K.E.;
RT "Complete genome sequence of Campylobacter hominis ATCC BAA-381, a
RT commensal isolated from the human gastrointestinal tract.";
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Endoribonuclease that initiates mRNA decay.
CC {ECO:0000255|HAMAP-Rule:MF_00335}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00335};
CC Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00335}.
CC -!- SIMILARITY: Belongs to the RNase Y family. {ECO:0000255|HAMAP-
CC Rule:MF_00335}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABS51127.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000776; ABS51127.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041570508.1; NC_009714.1.
DR AlphaFoldDB; A7I2Y9; -.
DR SMR; A7I2Y9; -.
DR STRING; 360107.CHAB381_1330; -.
DR EnsemblBacteria; ABS51127; ABS51127; CHAB381_1330.
DR KEGG; cha:CHAB381_1330; -.
DR eggNOG; COG1418; Bacteria.
DR HOGENOM; CLU_028328_1_0_7; -.
DR OrthoDB; 1012190at2; -.
DR Proteomes; UP000002407; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004521; F:endoribonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006402; P:mRNA catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd00077; HDc; 1.
DR Gene3D; 3.30.1370.10; -; 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 PANTHER; PTHR12826:SF15; PTHR12826:SF15; 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; SSF54791; 1.
DR TIGRFAMs; TIGR00277; HDIG; 1.
DR TIGRFAMs; TIGR03319; RNase_Y; 1.
DR PROSITE; PS51831; HD; 1.
DR PROSITE; PS50084; KH_TYPE_1; 1.
PE 3: Inferred from homology;
KW Cell membrane; Endonuclease; Hydrolase; Membrane; Nuclease;
KW Reference proteome; RNA-binding; Transmembrane; Transmembrane helix.
FT CHAIN 1..517
FT /note="Ribonuclease Y"
FT /id="PRO_0000344835"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00335"
FT DOMAIN 207..271
FT /note="KH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00335"
FT DOMAIN 333..426
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
SQ SEQUENCE 517 AA; 57653 MW; 0442DB5EEBF1F9CB CRC64;
MIEFLIGLIA AVVGILVGYL IARKINNANY EIFLEQAKAK AKAIEFEAEG ILRNSKISVQ
EAEFEAKKAY EDKALKLQKD YNAKFDEISK KEQTVLTEQE ILKDSREELE KEKKSAQTIY
DEGTSLKKTY ETKVEESLKL LERVAGLTED EAKSEILQKV EEKSRAEIAH IVRKYEEEAK
KEAKRNANYI LAQATTRYAG EYAAERLINV VNIKNDDLKG RIIGKDGRNI KTLEMISGVD
VIIDDTPNAI ILSSHNLYRR AIAVRTVELL VEDGRIQPAR IEDVYKKVSE EFEAGIQEEG
ENIVMDLGLT KIHPEIVKLI GKLKFRASYG QNALIHSLEV AHLAGIIAAE TGGDENLARR
AGILHDIGKA LTHEFEGSHV DLGAEICKRY KENPVVINAI YAHHGHEEPT SVESAAVCTA
DVLSAARPGA RREVLEAFLK RVSEIENIAT SKEGVKQAYA INAGREIRVI ANAKLVNDDE
AVLLAKEIAE EIQAKVQYPG EIKVNIIRET RAVDYAK