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RNY_BACLD
ID   RNY_BACLD               Reviewed;         519 AA.
AC   Q65JF1; Q62UV6;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 117.
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};
GN   OrderedLocusNames=BLi01919, BL03655;
OS   Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 /
OS   NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=279010;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC   / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX   PubMed=15383718; DOI=10.1159/000079829;
RA   Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P.,
RA   Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.;
RT   "The complete genome sequence of Bacillus licheniformis DSM13, an organism
RT   with great industrial potential.";
RL   J. Mol. Microbiol. Biotechnol. 7:204-211(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC   / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX   PubMed=15461803; DOI=10.1186/gb-2004-5-10-r77;
RA   Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J.,
RA   Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B.,
RA   Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A.,
RA   Bolotin A., Lapidus A., Galleron N., Ehrlich S.D., Berka R.M.;
RT   "Complete genome sequence of the industrial bacterium Bacillus
RT   licheniformis and comparisons with closely related Bacillus species.";
RL   Genome Biol. 5:R77.1-R77.12(2004).
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; CP000002; AAU23453.1; -; Genomic_DNA.
DR   EMBL; AE017333; AAU40813.1; -; Genomic_DNA.
DR   RefSeq; WP_003181928.1; NC_006322.1.
DR   AlphaFoldDB; Q65JF1; -.
DR   STRING; 279010.BL03655; -.
DR   EnsemblBacteria; AAU23453; AAU23453; BL03655.
DR   GeneID; 66216071; -.
DR   KEGG; bld:BLi01919; -.
DR   KEGG; bli:BL03655; -.
DR   eggNOG; COG1418; Bacteria.
DR   HOGENOM; CLU_028328_1_0_9; -.
DR   OMA; PHAILGM; -.
DR   OrthoDB; 1012190at2; -.
DR   BioCyc; BLIC279010:BLI_RS09490-MON; -.
DR   Proteomes; UP000000606; 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..519
FT                   /note="Ribonuclease Y"
FT                   /id="PRO_0000344819"
FT   TRANSMEM        3..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00335"
FT   DOMAIN          209..272
FT                   /note="KH"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00335"
FT   DOMAIN          335..428
FT                   /note="HD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
SQ   SEQUENCE   519 AA;  58852 MW;  B6BA1173B8522B03 CRC64;
     MSPLAILISI LLSLFCLVVG YYVRKIIAEA KISGARNAAE QILGDAKRDA EALKKEALLE
     AKDEIHTLRI EAEQEVRERR NELQKQENRL LQKEENLDRK DESLDKREAM LEKKDHSLNE
     RQQHIEEMES KVDEMIRMQQ SELERISSLT RDEAKQIILE RVENELSHDI AIMMKESENR
     AKEEADKKAK NILSLALQRC AADHVAETTV SVVNLPNDEM KGRIIGREGR NIRTLETLTG
     IDLIIDDTPE AVILSGFDPI RRETARIALD KLVQDGRIHP ARIEEMVEKS RREVDDYIRE
     MGEQTTFEVG VHGLHPDLIK ILGRLKFRTS YGQNVLKHSM EVAFLTGLMA SELGEDVTLA
     KRAGLLHDIG KAIDHEVEGS HVEIGVELAT KYKEHPVVIN SIASHHGDQE PTSIIAVLVA
     AADALSAARP GARSETLENY IRRLEKLEEI SESYEGVEKS FAIQAGREVR IMVKPDSIND
     LEAHRLARDI RKRIEDELDY PGHIKVTVIR ETRAVEYAK
 
 
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