ID F4MNP1_9FLAO Unreviewed; 521 AA.
AC F4MNP1;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 13-SEP-2023, entry version 49.
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=S18_841_0014 {ECO:0000313|EMBL:CBL88314.1};
OS uncultured Dokdonia sp.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Dokdonia; environmental samples.
OX NCBI_TaxID=575653 {ECO:0000313|EMBL:CBL88314.1};
RN [1] {ECO:0000313|EMBL:CBL88314.1}
RP NUCLEOTIDE SEQUENCE.
RA Genoscope - CEA;
RL Submitted (MAY-2010) 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}.
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DR EMBL; FQ032835; CBL88314.1; -; Genomic_DNA.
DR AlphaFoldDB; F4MNP1; -.
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 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 REGION 81..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 521 AA; 58171 MW; 802CC611EDB7BFC6 CRC64;
MEHNALLFIV GVIALALGFL IAKMLERNNA SQIIKRAKKS AQGILKEAKS EGESIKKDKI
LQAKEKFIEL KAEHEKVILG RDKKMNEAEK RTRDKESQVS GELSRNKKLN QSLEDRIKDY
DKRLEYVDKK KAEAEKMHQS TVQQLEVISG LSAEEAKSQL VTTLKDQAKA DAMKHVQTSI
EEAKMTAEQE AKKIIINTIQ RIGTEEAVEN CVSVFNLESD DVKGRIIGRE GRNIRAIEAA
TGVEIIVDDT PEAIILSCFD SVRREVARLS LHKLVTDGRI HPARIEEVVQ KTTRQIEQEI
VEVGKRTVID LGIHGLHPEL IKAVGRMKYR SSYGQNLLQH SREVAKLCSV MAAELGVNAK
LARRAGLLHD IGKVPDTETE TPHAILGMQW AEKYGEKPDV CNAIGAHHDE IEMTSLLSPI
VQVCDAISGA RPGARRQVLD SYIQRLKDLE EIAFGFQGVK KAYAIQAGRE LRVIVESEKV
NDDKASSLSF EISQKIQTDM TYPGQVKVTV IRETRAVNIA K
//
