RNAAM_HAEIN
ID RNAAM_HAEIN Reviewed; 274 AA.
AC P44176;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=5'-3' exoribonuclease {ECO:0000250|UniProtKB:P77766};
DE EC=3.1.13.- {ECO:0000250|UniProtKB:P77766};
DE AltName: Full=3',5'-nucleotide bisphosphate phosphatase {ECO:0000250|UniProtKB:P77766};
DE EC=3.1.3.97 {ECO:0000250|UniProtKB:P77766};
DE AltName: Full=RNase AM {ECO:0000250|UniProtKB:P77766};
GN OrderedLocusNames=HI_1400 {ECO:0000312|EMBL:AAC23046.1};
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
CC -!- FUNCTION: Efficiently catalyzes the hydrolysis of the 3'-phosphate from
CC 3',5'-bis-phosphonucleotides as well as the successive hydrolysis of
CC 5'-phosphomononucleotides from the 5'-end of short pieces of RNA and
CC DNA, with no specificity toward the identity of the nucleotide base. Is
CC more efficient at hydrolyzing RNA oligonucleotides than DNA
CC oligonucleotides. This enzyme can also hydrolyze annealed DNA duplexes,
CC albeit at a catalytic efficiency lower than that of the corresponding
CC single-stranded oligonucleotides. {ECO:0000250|UniProtKB:P77766}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 3',5'-bisphosphate + H2O = a ribonucleoside
CC 5'-phosphate + phosphate; Xref=Rhea:RHEA:43532, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58043, ChEBI:CHEBI:83402; EC=3.1.3.97;
CC Evidence={ECO:0000250|UniProtKB:P77766};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P77766};
CC -!- SIMILARITY: Belongs to the PHP family. TrpH/YciV subfamily.
CC {ECO:0000305}.
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DR EMBL; L42023; AAC23046.1; -; Genomic_DNA.
DR PIR; F64027; F64027.
DR RefSeq; NP_439553.1; NC_000907.1.
DR RefSeq; WP_005693963.1; NC_000907.1.
DR AlphaFoldDB; P44176; -.
DR SMR; P44176; -.
DR STRING; 71421.HI_1400; -.
DR PRIDE; P44176; -.
DR EnsemblBacteria; AAC23046; AAC23046; HI_1400.
DR KEGG; hin:HI_1400; -.
DR PATRIC; fig|71421.8.peg.1460; -.
DR eggNOG; COG0613; Bacteria.
DR HOGENOM; CLU_067347_0_0_6; -.
DR OMA; CTWGGAT; -.
DR PhylomeDB; P44176; -.
DR BioCyc; HINF71421:G1GJ1-1427-MON; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0097657; F:3',5'-nucleotide bisphosphate phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0035312; F:5'-3' exodeoxyribonuclease activity; IBA:GO_Central.
DR GO; GO:0004534; F:5'-3' exoribonuclease activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR InterPro; IPR004013; PHP_dom.
DR InterPro; IPR003141; Pol/His_phosphatase_N.
DR InterPro; IPR016195; Pol/histidinol_Pase-like.
DR Pfam; PF02811; PHP; 1.
DR SMART; SM00481; POLIIIAc; 1.
DR SUPFAM; SSF89550; SSF89550; 1.
PE 3: Inferred from homology;
KW Exonuclease; Hydrolase; Manganese; Metal-binding; Nuclease;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..274
FT /note="5'-3' exoribonuclease"
FT /id="PRO_0000065639"
FT BINDING 8
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7NXD4"
FT BINDING 10
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7NXD4"
FT BINDING 15
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q7NXD4"
FT BINDING 40
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q7NXD4"
FT BINDING 65
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7NXD4"
FT BINDING 65
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q7NXD4"
FT BINDING 76
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q7NXD4"
FT BINDING 190
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q7NXD4"
FT BINDING 247
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7NXD4"
FT BINDING 249
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q7NXD4"
SQ SEQUENCE 274 AA; 30116 MW; F7ED7B0BDFB850D3 CRC64;
MTKKYDLHCH STASDGVLSP TELVHRAYAQ GVNVLALCDH DTIAGIDEAE IAAKEVGIEL
ITGVEISTNW EGRGIHIVGL NFDKTHPKMT ALLQSQKALR EKRAVEIGDK LEKAGIPNAY
DGAKALADGE VTRAHYARYL VQIGKVSNDG QAFKRYLGQG KSAFVKAEWA DIPTAIETIH
AAGGIAIIAH PLRYNMTGKW VRKLIVDFKA WGGDGMEMAD CGQTKDQRQM LARWAKEFDL
QGSVGSDFHF PCGWIELGKN LDLVDSVIPV WEKF
