ID D4CTE0_9FUSO Unreviewed; 521 AA.
AC D4CTE0;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 24-JAN-2024, entry version 62.
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=FUSPEROL_00652 {ECO:0000313|EMBL:EFE87369.1};
OS Fusobacterium periodonticum ATCC 33693.
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Fusobacteriaceae;
OC Fusobacterium.
OX NCBI_TaxID=546275 {ECO:0000313|EMBL:EFE87369.1, ECO:0000313|Proteomes:UP000003748};
RN [1] {ECO:0000313|EMBL:EFE87369.1, ECO:0000313|Proteomes:UP000003748}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33693 {ECO:0000313|EMBL:EFE87369.1,
RC ECO:0000313|Proteomes:UP000003748};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (FEB-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}.
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:EFE87369.1}.
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DR EMBL; ACJY01000038; EFE87369.1; -; Genomic_DNA.
DR RefSeq; WP_005971704.1; NZ_GG665893.1.
DR AlphaFoldDB; D4CTE0; -.
DR STRING; 546275.FUSPEROL_00652; -.
DR GeneID; 78418942; -.
DR eggNOG; COG1418; Bacteria.
DR HOGENOM; CLU_028328_1_0_0; -.
DR OrthoDB; 9803205at2; -.
DR Proteomes; UP000003748; 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 27..154
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 521 AA; 58390 MW; DE4305DABA98D62C CRC64;
MNLLIFLGLA LLALALVFTV FFKKSVIDRQ IEKLNDLEDE VEKAKLKAKE IVEEAEKDAS
SKAKEIELKA KEKAYQIKEE VEKEARNLKN EIAQKEARIV KKEEILDGKI EKAENKSLEL
EKINNELDAK RKEIDELKIK QEEELSRVSE LTKAEAREIL LRKIREELTH DMAITIREFE
TKLDEEKEKI SQKILSTAIG KAAADYVADA TVSVINLPND EMKGRIIGRE GRNIRTIEAL
TGVDVIIDDT PEAVVLSCFD GVKREIARLT IEKLITDGRI HPGKIEEIVN KCKKEIEKEI
VAAGEEALIE LSIPSMHPEI IKTLGRLKYR TSYGQNVLTH SIEVAKIAST MAAEIGANVE
LAKRGGLLHD IGKVLVNEIE TSHAIVGGEF VKKFGEKQEV VNAVMAHHNE VEFETVEAIL
VQAADAVSAS RPGARRETLT AYIKRLENLE EIANSFDGVE SSFAIQAGRE LRIVINPDKV
SDDEATLMSR EVAKKIEDTM QYPGQIKVTI LRETRAVEYA K
//
