RNY_CLOTE
ID RNY_CLOTE Reviewed; 523 AA.
AC Q895I4;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 112.
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=CTC_01290;
OS Clostridium tetani (strain Massachusetts / E88).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=212717;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Massachusetts / E88;
RX PubMed=12552129; DOI=10.1073/pnas.0335853100;
RA Brueggemann H., Baeumer S., Fricke W.F., Wiezer A., Liesegang H.,
RA Decker I., Herzberg C., Martinez-Arias R., Merkl R., Henne A.,
RA Gottschalk G.;
RT "The genome sequence of Clostridium tetani, the causative agent of tetanus
RT disease.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(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; AE015927; AAO35856.1; -; Genomic_DNA.
DR RefSeq; WP_011099518.1; NC_004557.1.
DR AlphaFoldDB; Q895I4; -.
DR SMR; Q895I4; -.
DR STRING; 212717.CTC_01290; -.
DR PRIDE; Q895I4; -.
DR EnsemblBacteria; AAO35856; AAO35856; CTC_01290.
DR KEGG; ctc:CTC_01290; -.
DR HOGENOM; CLU_028328_1_0_9; -.
DR OMA; PHAILGM; -.
DR Proteomes; UP000001412; 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..523
FT /note="Ribonuclease Y"
FT /id="PRO_0000344856"
FT TRANSMEM 28..48
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00335"
FT DOMAIN 227..312
FT /note="KH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00335"
FT DOMAIN 353..446
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
SQ SEQUENCE 523 AA; 59445 MW; FF5C77A7E35E5484 CRC64;
MTLSKLLYLS AIDYLNTKSK GGAHLNLTYY IVATIIIAVI AVYVDYYIRK NVSAAKISNA
EEKGRNIIED AKREAESKKK EAILEAKEEM HRLRNDFEKE SKDRRNEIQR LERRIIQREE
ALDKKGDMLE KKEESLNKKH QELENKKSNI ENLYEKQREE LERLAGLTSD QAKEMLLEEV
RKEIKHETAM LIKEVETKAK EEADKKAREI TTYAIQRCAA DHVAETTVYV VNLPNDEMKG
RIIGREGRNI RTLETLTGVD LIIDDTPEAV ILSAFDPVRR EVARIALEKL IMDGRIHPAR
IEEMVEKAKK EVENNIREEG EQATFETSVH GLHSELIKLL GRLKYRTSYG QNVLKHSIEV
SYLAGLMASE LGMDPTLAKR AGLLHDIGKA VDHEVEGPHA IIGAEVAKRY HESSIVVNAI
AAHHGDEEFE SIEAILVQAA DAISAARPGA RRETLEAYIK RLEKLEEIAN SYEGVEKSYA
IQAGRELRII VKPEVVDDAG SYEMARNMAK TIENELEYLV KLR