RNY_MYCMY
ID RNY_MYCMY Reviewed; 422 AA.
AC Q01444;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 25-MAY-2022, entry version 84.
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};
DE Flags: Fragment;
GN Name=rny {ECO:0000255|HAMAP-Rule:MF_00335};
OS Mycoplasma mycoides.
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=2102;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1280809; DOI=10.1093/nar/20.21.5763;
RA Samuelsson T.B.;
RT "A Mycoplasma protein homologous to mammalian SRP54 recognizes a highly
RT conserved domain of SRP RNA.";
RL Nucleic Acids Res. 20:5763-5770(1992).
CC -!- FUNCTION: Endoribonuclease that initiates mRNA decay.
CC {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; M91593; AAA25440.1; -; Genomic_DNA.
DR PIR; S35480; S35480.
DR AlphaFoldDB; Q01444; -.
DR SMR; Q01444; -.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006402; P:mRNA catabolic process; IEA:InterPro.
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.
PE 3: Inferred from homology;
KW Endonuclease; Hydrolase; Nuclease; RNA-binding.
FT CHAIN <1..422
FT /note="Ribonuclease Y"
FT /id="PRO_0000163781"
FT DOMAIN 112..172
FT /note="KH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00335"
FT DOMAIN 238..331
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT NON_TER 1
SQ SEQUENCE 422 AA; 47328 MW; D64F4FAD873C0969 CRC64;
DLRANDLKRS QEIVESKSQR LDAGILDLEK RKFLVDQKEE YLIKLLEDVS GLTKYQAKEL
LIKQIKNKSE KELISILKNA ELQAHSKAKI ISNNILILAM ERIKVELTSQ RTTNIVKLPS
DDLKGRIIGK DGRNMKTFEQ IGGVDIVVDE TPNVVVVSSF NPIRREIATR TLEQLIIDGR
IQPVKIENEL KKQEQELEYI IQETGLNTIK ELNINDIDIE LVKLIGKLKF RTSYGQNVLA
HSIEVAKLSG AIASELGLDV EKAIRAGLLH DIGKAIDFEK QGSHVVLGAE IARKYNEDPI
IINSIESHHE DKEKSSEIAA IVAIADSISA SRPGARYNAI DEFILRMHEI EKIGNSIPGV
AKTYALQSGR QIRLIVDPLV ASDLDLALIL EKMKEQIKNK VIIPGEITIT VIREKKETDI
LK