RNY_CAMC5
ID RNY_CAMC5 Reviewed; 517 AA.
AC A7GY23;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 88.
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=Ccur92_08110;
GN ORFNames=CCV52592_1398;
OS Campylobacter curvus (strain 525.92).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=360105;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=525.92;
RA Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G.,
RA Mandrell R.E., Lastovica A.J., Nelson K.E.;
RT "Genome sequence of Campylobacter curvus 525.92 isolated from human
RT feces.";
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=EAU00478.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000767; EAU00478.2; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_034966560.1; NC_009715.2.
DR AlphaFoldDB; A7GY23; -.
DR STRING; 360105.CCV52592_1398; -.
DR PRIDE; A7GY23; -.
DR EnsemblBacteria; EAU00478; EAU00478; CCV52592_1398.
DR KEGG; ccv:CCV52592_1398; -.
DR HOGENOM; CLU_028328_1_0_7; -.
DR OrthoDB; 1012190at2; -.
DR Proteomes; UP000006380; 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; 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; PF12072; RNase_Y_N; 1.
DR SMART; SM00471; HDc; 1.
DR SUPFAM; SSF54791; SSF54791; 1.
DR TIGRFAMs; TIGR00277; HDIG; 1.
DR TIGRFAMs; TIGR03319; RNase_Y; 1.
DR PROSITE; PS51831; HD; 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_0000344833"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00335"
FT DOMAIN 207..273
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; 57797 MW; E9891F7D552A9B1B CRC64;
MIEVLIGLGA GVAGVGAGYL YAKKINDANY NIFLEQAKAK AKAIEYEAEL TLKNSKISVQ
EAEFEAKKRY DDKTTKLQKE YSQKFDELNK KEQILLNEQE LLNENKELFE KDRNEAKLTY
EEGLNLKATY QSKVQEALKV LEHAAGLTED EAREVVLKKV EEKSRADIAH IVRKHEEEAK
REAKKRVNYI LAQATSRFAG EFAAERLINV VNIKNDELKG RIIGKEGRNI KTLEMVLGVD
IIIDDTPHAI ILSSFNLYRR AIATRVIELL VEDGRIQPAR IEDLHKKVTE EFEQSIQEEG
ENIVIDLGLS KIHPEITKLI GKLKFRASYG QNALAHSLEV AHLAGIIAAE TGGDEKLAKR
AGLLHDIGKA LTHEFEGSHV DLGAEICKRY KEHPVVINAI YAHHGHEEAT SIESAAVCAA
DCLSAARPGA RREVLESFLK RVEEVENIAK SKDGIKQAYA INAGREIRVI ANAKLINDDE
AVLVAKEIAK EIEEKVQYPG EIKVSVIRET RAVDYAK