ID U4KT42_9MOLU Unreviewed; 518 AA.
AC U4KT42;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, 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 ECO:0000313|EMBL:CCV66034.1};
GN ORFNames=BN85310130 {ECO:0000313|EMBL:CCV66034.1};
OS Paracholeplasma brassicae.
OC Bacteria; Mycoplasmatota; Mollicutes; Acholeplasmatales;
OC Acholeplasmataceae; Paracholeplasma.
OX NCBI_TaxID=61635 {ECO:0000313|EMBL:CCV66034.1, ECO:0000313|Proteomes:UP000032737};
RN [1] {ECO:0000313|EMBL:CCV66034.1, ECO:0000313|Proteomes:UP000032737}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0502 {ECO:0000313|Proteomes:UP000032737};
RX PubMed=24158107; DOI=10.1159/000354322;
RA Kube M., Siewert C., Migdoll A.M., Duduk B., Holz S., Rabus R.,
RA Seemuller E., Mitrovic J., Muller I., Buttner C., Reinhardt R.;
RT "Analysis of the Complete Genomes of Acholeplasma brassicae , A. palmae and
RT A. laidlawii and Their Comparison to the Obligate Parasites from '
RT Candidatus Phytoplasma'.";
RL J. Mol. Microbiol. Biotechnol. 24:19-36(2013).
CC -!- FUNCTION: Endoribonuclease that initiates mRNA decay.
CC {ECO:0000256|HAMAP-Rule:MF_00335}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00335};
CC Single-pass membrane protein {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; FO681348; CCV66034.1; -; Genomic_DNA.
DR RefSeq; WP_030004896.1; NC_022549.1.
DR AlphaFoldDB; U4KT42; -.
DR STRING; 61635.BN85310130; -.
DR KEGG; abra:BN85310130; -.
DR HOGENOM; CLU_028328_1_0_14; -.
DR OrthoDB; 9803205at2; -.
DR Proteomes; UP000032737; Chromosome Acholeplasma brassicae.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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 Cell membrane {ECO:0000256|HAMAP-Rule:MF_00335};
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 Membrane {ECO:0000256|HAMAP-Rule:MF_00335};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_00335};
KW Reference proteome {ECO:0000313|Proteomes:UP000032737};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_00335}; Transmembrane {ECO:0000256|HAMAP-Rule:MF_00335};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00335}.
FT TRANSMEM 6..24
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00335"
FT DOMAIN 334..427
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT COILED 61..144
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 518 AA; 58022 MW; 028A4AC8AD4CE3F8 CRC64;
MTEIIISILL GLIIGVVTGF FIRVKMHEKS LENSRLESKK IVEDGQKEAE KIKKELILEA
RQDIFNQKKE LERDIKERKQ VVIDLETKIM NRDEMLNRRA SNLDKREEHL GLKEIKLDEK
KVELEQLNSK VEDILKKQEE KLIEISGIST EQAQGFIMDR VRNEMSEEIS AYIKEAEEKA
KAESDQKAKG LLTLAIQKYA SETTSERTVS VVTLPTDEMK GRIIGREGRN IRTIEALTGV
DLIIDDTPEA VVLSGFDPIR REIAKRALTS LVEDGRIHPG RIEEVVERAQ AEVDMFIREA
GENAVFETGV GKMHPDLVKL LGRMSFRTSY GQNVLKHSIE TAFLAGKLAA EIGENEVLAK
RAGLLHDIGK AVDHEVEGSH VEIGVSIVSR YNEPKEVIDA IASHHGDKEP QSIIAVLVAA
ADALSAARPG ARSESMDNYI KRLEQLETIS NSITGVERSF AIQAGREIRV IVKPDEVDDL
STFKVAREIK EQIEANLQYP GTIKVTVVRE TRATDIAK
//
