YHAM_BACAH
ID YHAM_BACAH Reviewed; 314 AA.
AC A0RAN0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=3'-5' exoribonuclease YhaM {ECO:0000255|HAMAP-Rule:MF_01427};
DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_01427};
GN Name=yhaM {ECO:0000255|HAMAP-Rule:MF_01427}; OrderedLocusNames=BALH_0905;
OS Bacillus thuringiensis (strain Al Hakam).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=412694;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Al Hakam;
RX PubMed=17337577; DOI=10.1128/jb.00241-07;
RA Challacombe J.F., Altherr M.R., Xie G., Bhotika S.S., Brown N., Bruce D.,
RA Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C.,
RA Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A.,
RA Green L.D., Han C.S., Hill K.K., Hitchcock P., Jackson P.J., Keim P.,
RA Kewalramani A.R., Longmire J., Lucas S., Malfatti S., Martinez D.,
RA McMurry K., Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C.,
RA Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P.,
RA Robinson D.L., Saunders E., Tapia R., Tesmer J.G., Thayer N.,
RA Thompson L.S., Tice H., Ticknor L.O., Wills P.L., Gilna P., Brettin T.S.;
RT "The complete genome sequence of Bacillus thuringiensis Al Hakam.";
RL J. Bacteriol. 189:3680-3681(2007).
CC -!- FUNCTION: Shows a 3'-5' exoribonuclease activity. {ECO:0000255|HAMAP-
CC Rule:MF_01427}.
CC -!- SIMILARITY: Belongs to the YhaM family. {ECO:0000255|HAMAP-
CC Rule:MF_01427}.
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DR EMBL; CP000485; ABK84273.1; -; Genomic_DNA.
DR RefSeq; WP_000726638.1; NC_008600.1.
DR AlphaFoldDB; A0RAN0; -.
DR SMR; A0RAN0; -.
DR EnsemblBacteria; ABK84273; ABK84273; BALH_0905.
DR GeneID; 59157295; -.
DR GeneID; 64200342; -.
DR GeneID; 67505723; -.
DR KEGG; btl:BALH_0905; -.
DR HOGENOM; CLU_056349_2_0_9; -.
DR OMA; NLVGHLV; -.
DR Proteomes; UP000000761; Chromosome.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR CDD; cd00077; HDc; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR HAMAP; MF_01427; 3_5_Exoribonuc_YhaM; 1.
DR InterPro; IPR020873; 3'-5'_exoribonuclease_YhaM.
DR InterPro; IPR003607; HD/PDEase_dom.
DR InterPro; IPR006674; HD_domain.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004365; NA-bd_OB_tRNA.
DR Pfam; PF01966; HD; 1.
DR Pfam; PF01336; tRNA_anti-codon; 1.
DR SMART; SM00471; HDc; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR PROSITE; PS51831; HD; 1.
PE 3: Inferred from homology;
KW Exonuclease; Hydrolase; Nuclease.
FT CHAIN 1..314
FT /note="3'-5' exoribonuclease YhaM"
FT /id="PRO_1000024348"
FT DOMAIN 163..279
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
SQ SEQUENCE 314 AA; 35514 MW; 57EEFAC9CF7B0FE8 CRC64;
MKKKIAEYEV GEQVDIFLLI KTATKGIASN GKPFLTVILQ DPSGDIEAKL WDVSPEVEKQ
YVAETIVKVA GDILNYKGRI QLRVKQIRVA NENEVTDISD FVEKAPVKKE DMVEKITQYI
FEMRNPNIQR LTRHLLNKHQ NEFLDYPAAT KNHHEFVSGL AYHVVSMLDL AKAISNLYPS
LDKDLLYAGV ILHDLGKVIE LSGPISTTYT LEGNLLGHIS IMVNEIGKAA DELQIDAEEV
LILQHIVLSH HGKAEWGSPK PPLVKEAEIL HYIDNLDAKM NMMDRALGRT KPGEYTERVF
ALDNRSFYKP SFHN