ID A0A1V3QW05_9BACT Unreviewed; 521 AA.
AC A0A1V3QW05;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Ribonuclease Y {ECO:0000256|HAMAP-Rule:MF_00335};
DE Short=RNase Y {ECO:0000256|HAMAP-Rule:MF_00335};
DE EC=3.1.-.- {ECO:0000256|HAMAP-Rule:MF_00335};
GN Name=rny {ECO:0000256|HAMAP-Rule:MF_00335};
GN ORFNames=B0E43_22055 {ECO:0000313|EMBL:OOG68762.1};
OS Algoriphagus sp. A40.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Algoriphagus.
OX NCBI_TaxID=1945863 {ECO:0000313|EMBL:OOG68762.1, ECO:0000313|Proteomes:UP000188460};
RN [1] {ECO:0000313|EMBL:OOG68762.1, ECO:0000313|Proteomes:UP000188460}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A40 {ECO:0000313|EMBL:OOG68762.1,
RC ECO:0000313|Proteomes:UP000188460};
RA Lycus P., Bothun K.L., Bergaust L., Shapleigh J.P., Bakken L.R.,
RA Frostegard A.;
RT "Phenotypic and genotypic richness of denitrifiers revealed by a novel
RT isolation strategy.";
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Endoribonuclease that initiates mRNA decay.
CC {ECO:0000256|HAMAP-Rule:MF_00335}.
CC -!- SIMILARITY: Belongs to the RNase Y family. {ECO:0000256|HAMAP-
CC Rule:MF_00335}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OOG68762.1}.
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DR EMBL; MUNY01000082; OOG68762.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V3QW05; -.
DR STRING; 1945863.B0E43_22055; -.
DR OrthoDB; 9803205at2; -.
DR Proteomes; UP000188460; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004521; F:RNA endonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006402; P:mRNA catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd00077; HDc; 1.
DR CDD; cd22431; KH-I_RNaseY; 1.
DR Gene3D; 1.10.3210.10; Hypothetical protein af1432; 1.
DR Gene3D; 3.30.1370.10; K Homology domain, type 1; 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 NCBIfam; TIGR00277; HDIG; 1.
DR NCBIfam; TIGR03319; RNase_Y; 1.
DR PANTHER; PTHR12826; RIBONUCLEASE Y; 1.
DR PANTHER; PTHR12826:SF15; RIBONUCLEASE Y; 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; Eukaryotic type KH-domain (KH-domain type I); 1.
DR SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR PROSITE; PS51831; HD; 1.
DR PROSITE; PS50084; KH_TYPE_1; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759, ECO:0000256|HAMAP-
KW Rule:MF_00335};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00335};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_00335};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_00335}.
FT DOMAIN 337..430
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT COILED 85..137
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 521 AA; 58287 MW; 186F07F3C6342B85 CRC64;
MADVLFIILA ALAGLGGGAA LAGFFIKNKN AKLEGEAKEK VKSMLREAEL TAETIKKDRI
LEAKEKFLKM KAEFDEDTNN KKNIILTNET KVKQLQQQVA KEQEAVKRRE AELDSKKENL
TAQLHSVQVK KEELDRITNQ RIADLEKIAG LTREEAKEQI VSMLTEEAQT KASSHIKDIL
DEAKLTATKQ AKKIVLDTIQ RTATEHAVEN CVSVFNIESD DIKGKIIGRE GRNIRALEAA
TGVEIVVDDT PEAIIISGFD PVRREIARLS LHRLVQDGRI HPARIEEVVA KTEKNIEEEI
VEIGERTCID LGIHGLHPEL IRLVGRMRFR SSYGQNLLQH SREVAKLAAT MAAEMGLNAK
LAKRAGLLHD IGKVWPEEQE LPHAVLGMEL AKRYKEHPEI CNAIGAHHDE IEMTSMISPI
VQASDAISGS RPGARREIMD SYVKRLKELE ELALAFDGVN KCFAMQAGRE LRILVDADNV
DDQKAGKLSF DISQKIEKEM QYPGQIKVTV IREMRAVNYA R
//