RNY_RHOBA
ID RNY_RHOBA Reviewed; 522 AA.
AC Q7UNE3;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 25-MAY-2022, entry version 103.
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=RB7627;
OS Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC Bacteria; Planctomycetes; Planctomycetia; Pirellulales; Pirellulaceae;
OC Rhodopirellula.
OX NCBI_TaxID=243090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10527 / NCIMB 13988 / SH1;
RX PubMed=12835416; DOI=10.1073/pnas.1431443100;
RA Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W.,
RA Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R.,
RA Reinhardt R.;
RT "Complete genome sequence of the marine planctomycete Pirellula sp. strain
RT 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003).
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}.
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DR EMBL; BX294146; CAD75476.1; -; Genomic_DNA.
DR RefSeq; NP_867929.1; NC_005027.1.
DR RefSeq; WP_007325643.1; NC_005027.1.
DR AlphaFoldDB; Q7UNE3; -.
DR STRING; 243090.RB7627; -.
DR EnsemblBacteria; CAD75476; CAD75476; RB7627.
DR KEGG; rba:RB7627; -.
DR PATRIC; fig|243090.15.peg.3686; -.
DR eggNOG; COG1418; Bacteria.
DR HOGENOM; CLU_028328_1_0_0; -.
DR InParanoid; Q7UNE3; -.
DR OMA; PHAILGM; -.
DR OrthoDB; 1012190at2; -.
DR Proteomes; UP000001025; 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..522
FT /note="Ribonuclease Y"
FT /id="PRO_0000226298"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00335"
FT DOMAIN 212..272
FT /note="KH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00335"
FT DOMAIN 338..431
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
SQ SEQUENCE 522 AA; 58223 MW; F0B6B06F4092E16D CRC64;
MNPQLASTIL YCLFFFFLGI AAVLAFIQRQ AVKRRERLDA EAEAVLESAR REAETRGNQI
IVDAREKALA IKAEADREVA AMRETEQIRD RKLDAREDQL ASGQESLRKA QRGLESSQTR
LAAQMRNLTE QRAELDRLVQ ESQRALEKVS GMTQEEAAEK LMQSLRQDLE HEIGSTVLKH
QRELGRRVDA QAREMLLTAM QRYASVHTAD TTTSTVGVPT DDMKGRIIGR EGRNIRAFEK
ATGVDLIIDD TPGVVVVSGF DPVRREVARM SLEKLIADGR IHPSKIEETV EQAGKEIQAF
ILQKGQEAAG EVNVSGLHDR VIEMLGRLHF RTSYSQNVLR HSVEVAFLAG MMAEMIGLDG
DLARRCGLLH DIGKAADHEL EGGHPKIGAD LLRRSKENDE VVHAAKGHHD EIVTEFPYTM
LVATADACSA SRPGARRESL ERYVKRMEEL ESIAQRFDGV QQAYAISAGR ELRVMVGSQQ
VSDERAAAIC RDIASTFEKE LTYPGEIKVT VVREARFTNT AK