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Ribonuclease H2 subunit A (RNase H2 subunit A) (EC 3.1.26.4) (Aicardi-Goutieres syndrome 4 protein) (AGS4) (RNase H(35)) (Ribonuclease HI large subunit) (RNase HI large subunit) (Ribonuclease HI subunit A)

 RNH2A_HUMAN             Reviewed;         299 AA.
O75792; B2RCY1; Q96F11;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
15-MAY-2002, sequence version 2.
05-DEC-2018, entry version 166.
RecName: Full=Ribonuclease H2 subunit A;
Short=RNase H2 subunit A;
EC=3.1.26.4;
AltName: Full=Aicardi-Goutieres syndrome 4 protein;
Short=AGS4;
AltName: Full=RNase H(35);
AltName: Full=Ribonuclease HI large subunit;
Short=RNase HI large subunit;
AltName: Full=Ribonuclease HI subunit A;
Name=RNASEH2A; Synonyms=RNASEHI, RNHIA;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9789007; DOI=10.1073/pnas.95.22.12872;
Frank P., Braunshofer-Reiter C., Wintersberger U., Grimm R.,
Buesen W.;
"Cloning of the cDNA encoding the large subunit of human RNase HI, a
homologue of the prokaryotic RNase HII.";
Proc. Natl. Acad. Sci. U.S.A. 95:12872-12877(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Thalamus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-204 AND THR-216, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[7]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[8]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-277, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[10]
X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS), SUBUNIT, FUNCTION, CATALYTIC
ACTIVITY, COFACTOR, AND MUTAGENESIS OF ASP-67; LYS-69; ASN-112;
TYR-210 AND THR-240.
PubMed=21177858; DOI=10.1074/jbc.M110.181974;
Figiel M., Chon H., Cerritelli S.M., Cybulska M., Crouch R.J.,
Nowotny M.;
"The structural and biochemical characterization of human RNase H2
complex reveals the molecular basis for substrate recognition and
Aicardi-Goutieres syndrome defects.";
J. Biol. Chem. 286:10540-10550(2011).
[11]
VARIANT AGS4 SER-37, CHARACTERIZATION OF VARIANT AGS4 SER-37,
FUNCTION, AND INTERACTION WITH RNASEH2B AND RNASEH2C.
PubMed=16845400; DOI=10.1038/ng1842;
Crow Y.J., Leitch A., Hayward B.E., Garner A., Parmar R., Griffith E.,
Ali M., Semple C., Aicardi J., Babul-Hirji R., Baumann C., Baxter P.,
Bertini E., Chandler K.E., Chitayat D., Cau D., Dery C., Fazzi E.,
Goizet C., King M.D., Klepper J., Lacombe D., Lanzi G., Lyall H.,
Martinez-Frias M.L., Mathieu M., McKeown C., Monier A., Oade Y.,
Quarrell O.W., Rittey C.D., Rogers R.C., Sanchis A.,
Stephenson J.B.P., Tacke U., Till M., Tolmie J.L., Tomlin P., Voit T.,
Weschke B., Woods C.G., Lebon P., Bonthron D.T., Ponting C.P.,
Jackson A.P.;
"Mutations in genes encoding ribonuclease H2 subunits cause Aicardi-
Goutieres syndrome and mimic congenital viral brain infection.";
Nat. Genet. 38:910-916(2006).
[12]
VARIANTS AGS4 SER-37; TRP-108; TRP-186; LEU-230; GLN-235; MET-240 AND
HIS-291, AND VARIANTS ASP-99; SER-202; GLU-205 AND GLY-260.
PubMed=17846997; DOI=10.1086/521373;
Rice G., Patrick T., Parmar R., Taylor C.F., Aeby A., Aicardi J.,
Artuch R., Montalto S.A., Bacino C.A., Barroso B., Baxter P.,
Benko W.S., Bergmann C., Bertini E., Biancheri R., Blair E.M.,
Blau N., Bonthron D.T., Briggs T., Brueton L.A., Brunner H.G.,
Burke C.J., Carr I.M., Carvalho D.R., Chandler K.E., Christen H.J.,
Corry P.C., Cowan F.M., Cox H., D'Arrigo S., Dean J., De Laet C.,
De Praeter C., Dery C., Ferrie C.D., Flintoff K., Frints S.G.,
Garcia-Cazorla A., Gener B., Goizet C., Goutieres F., Green A.J.,
Guet A., Hamel B.C., Hayward B.E., Heiberg A., Hennekam R.C.,
Husson M., Jackson A.P., Jayatunga R., Jiang Y.H., Kant S.G., Kao A.,
King M.D., Kingston H.M., Klepper J., van der Knaap M.S.,
Kornberg A.J., Kotzot D., Kratzer W., Lacombe D., Lagae L.,
Landrieu P.G., Lanzi G., Leitch A., Lim M.J., Livingston J.H.,
Lourenco C.M., Lyall E.G., Lynch S.A., Lyons M.J., Marom D.,
McClure J.P., McWilliam R., Melancon S.B., Mewasingh L.D.,
Moutard M.L., Nischal K.K., Ostergaard J.R., Prendiville J.,
Rasmussen M., Rogers R.C., Roland D., Rosser E.M., Rostasy K.,
Roubertie A., Sanchis A., Schiffmann R., Scholl-Burgi S., Seal S.,
Shalev S.A., Corcoles C.S., Sinha G.P., Soler D., Spiegel R.,
Stephenson J.B., Tacke U., Tan T.Y., Till M., Tolmie J.L., Tomlin P.,
Vagnarelli F., Valente E.M., Van Coster R.N., Van der Aa N.,
Vanderver A., Vles J.S., Voit T., Wassmer E., Weschke B.,
Whiteford M.L., Willemsen M.A., Zankl A., Zuberi S.M., Orcesi S.,
Fazzi E., Lebon P., Crow Y.J.;
"Clinical and molecular phenotype of Aicardi-Goutieres syndrome.";
Am. J. Hum. Genet. 81:713-725(2007).
[13]
VARIANTS AGS4 2-TYR-PRO-3 AND TRP-186.
PubMed=20131292; DOI=10.1002/art.27367;
Ramantani G., Kohlhase J., Hertzberg C., Innes A.M., Engel K.,
Hunger S., Borozdin W., Mah J.K., Ungerath K., Walkenhorst H.,
Richardt H.H., Buckard J., Bevot A., Siegel C., von Stuelpnagel C.,
Ikonomidou C., Thomas K., Proud V., Niemann F., Wieczorek D.,
Haeusler M., Niggemann P., Baltaci V., Conrad K., Lebon P.,
Lee-Kirsch M.A.;
"Expanding the phenotypic spectrum of lupus erythematosus in Aicardi-
Goutieres syndrome.";
Arthritis Rheum. 62:1469-1477(2010).
-!- FUNCTION: Catalytic subunit of RNase HII, an endonuclease that
specifically degrades the RNA of RNA:DNA hybrids. Participates in
DNA replication, possibly by mediating the removal of lagging-
strand Okazaki fragment RNA primers during DNA replication.
Mediates the excision of single ribonucleotides from DNA:RNA
duplexes. {ECO:0000269|PubMed:16845400,
ECO:0000269|PubMed:21177858}.
-!- CATALYTIC ACTIVITY:
Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.;
EC=3.1.26.4; Evidence={ECO:0000269|PubMed:21177858};
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Note=Manganese or magnesium. Binds 1 divalent metal ion per
monomer in the absence of substrate. May bind a second metal ion
after substrate binding. {ECO:0000250};
-!- SUBUNIT: The RNase H2 complex is a heterotrimer composed of the
catalytic subunit RNASEH2A and the non-catalytic subunits RNASEH2B
and RNASEH2C. {ECO:0000269|PubMed:21177858}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
-!- DISEASE: Aicardi-Goutieres syndrome 4 (AGS4) [MIM:610333]: A form
of Aicardi-Goutieres syndrome, a genetically heterogeneous disease
characterized by cerebral atrophy, leukoencephalopathy,
intracranial calcifications, chronic cerebrospinal fluid (CSF)
lymphocytosis, increased CSF alpha-interferon, and negative
serologic investigations for common prenatal infection. Clinical
features as thrombocytopenia, hepatosplenomegaly and elevated
hepatic transaminases along with intermittent fever may
erroneously suggest an infective process. Severe neurological
dysfunctions manifest in infancy as progressive microcephaly,
spasticity, dystonic posturing and profound psychomotor
retardation. Death often occurs in early childhood.
{ECO:0000269|PubMed:16845400, ECO:0000269|PubMed:17846997,
ECO:0000269|PubMed:20131292}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the RNase HII family. Eukaryotic subfamily.
{ECO:0000305}.
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EMBL; Z97029; CAB09725.1; -; mRNA.
EMBL; AK315327; BAG37728.1; -; mRNA.
EMBL; CH471106; EAW84313.1; -; Genomic_DNA.
EMBL; BC011748; AAH11748.1; -; mRNA.
CCDS; CCDS12282.1; -.
RefSeq; NP_006388.2; NM_006397.2.
UniGene; Hs.532851; -.
PDB; 3P56; X-ray; 4.06 A; A/D=1-299.
PDB; 3PUF; X-ray; 3.10 A; A/D/G/J/M/P=1-299.
PDBsum; 3P56; -.
PDBsum; 3PUF; -.
ProteinModelPortal; O75792; -.
SMR; O75792; -.
BioGrid; 115789; 47.
IntAct; O75792; 27.
STRING; 9606.ENSP00000221486; -.
iPTMnet; O75792; -.
PhosphoSitePlus; O75792; -.
BioMuta; RNASEH2A; -.
EPD; O75792; -.
MaxQB; O75792; -.
PaxDb; O75792; -.
PeptideAtlas; O75792; -.
PRIDE; O75792; -.
ProteomicsDB; 50197; -.
DNASU; 10535; -.
Ensembl; ENST00000221486; ENSP00000221486; ENSG00000104889.
GeneID; 10535; -.
KEGG; hsa:10535; -.
UCSC; uc002mvg.2; human.
CTD; 10535; -.
DisGeNET; 10535; -.
EuPathDB; HostDB:ENSG00000104889.4; -.
GeneCards; RNASEH2A; -.
GeneReviews; RNASEH2A; -.
HGNC; HGNC:18518; RNASEH2A.
HPA; HPA042692; -.
MalaCards; RNASEH2A; -.
MIM; 606034; gene.
MIM; 610333; phenotype.
neXtProt; NX_O75792; -.
OpenTargets; ENSG00000104889; -.
Orphanet; 51; Aicardi-Goutieres syndrome.
PharmGKB; PA38565; -.
eggNOG; KOG2299; Eukaryota.
eggNOG; COG0164; LUCA.
GeneTree; ENSGT00390000010768; -.
HOGENOM; HOG000100290; -.
HOVERGEN; HBG023585; -.
InParanoid; O75792; -.
KO; K10743; -.
OMA; REECRFF; -.
OrthoDB; EOG091G0E06; -.
PhylomeDB; O75792; -.
TreeFam; TF314302; -.
BioCyc; MetaCyc:HS02645-MONOMER; -.
EvolutionaryTrace; O75792; -.
GeneWiki; RNASEH2A; -.
GenomeRNAi; 10535; -.
PRO; PR:O75792; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000104889; Expressed in 164 organ(s), highest expression level in endometrium epithelium.
CleanEx; HS_RNASEH2A; -.
Genevisible; O75792; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0032299; C:ribonuclease H2 complex; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004540; F:ribonuclease activity; TAS:ProtInc.
GO; GO:0003723; F:RNA binding; IEA:InterPro.
GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IDA:UniProtKB.
GO; GO:0006260; P:DNA replication; TAS:UniProtKB.
GO; GO:0043137; P:DNA replication, removal of RNA primer; IBA:GO_Central.
GO; GO:0006298; P:mismatch repair; IDA:MGI.
GO; GO:0006401; P:RNA catabolic process; IDA:UniProtKB.
Gene3D; 1.10.10.460; -; 1.
Gene3D; 3.30.420.10; -; 1.
InterPro; IPR004649; RNase_H2_suA.
InterPro; IPR001352; RNase_HII/HIII.
InterPro; IPR024567; RNase_HII/HIII_dom.
InterPro; IPR023160; RNase_HII_hlx-loop-hlx_cap_dom.
InterPro; IPR012337; RNaseH-like_sf.
InterPro; IPR036397; RNaseH_sf.
PANTHER; PTHR10954; PTHR10954; 1.
Pfam; PF01351; RNase_HII; 1.
SUPFAM; SSF53098; SSF53098; 1.
TIGRFAMs; TIGR00729; TIGR00729; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Aicardi-Goutieres syndrome;
Complete proteome; Disease mutation; Endonuclease; Hydrolase;
Metal-binding; Nuclease; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome.
CHAIN 1 299 Ribonuclease H2 subunit A.
/FTId=PRO_0000111710.
METAL 34 34 Divalent metal cation. {ECO:0000250}.
METAL 35 35 Divalent metal cation. {ECO:0000250}.
METAL 141 141 Divalent metal cation. {ECO:0000250}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378}.
MOD_RES 204 204 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 216 216 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 257 257 Phosphoserine.
{ECO:0000250|UniProtKB:Q9CWY8}.
MOD_RES 277 277 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VARIANT 2 3 DL -> YP (in AGS4).
/FTId=VAR_070623.
VARIANT 37 37 G -> S (in AGS4; strongly impairs enzyme
activity but not interaction with
RNASEH2B and RNASEH2C; dbSNP:rs76857106).
{ECO:0000269|PubMed:16845400,
ECO:0000269|PubMed:17846997}.
/FTId=VAR_027377.
VARIANT 99 99 N -> D. {ECO:0000269|PubMed:17846997}.
/FTId=VAR_070624.
VARIANT 108 108 R -> W (in AGS4; dbSNP:rs76436818).
{ECO:0000269|PubMed:17846997}.
/FTId=VAR_070625.
VARIANT 186 186 R -> W (in AGS4; dbSNP:rs77103971).
{ECO:0000269|PubMed:17846997,
ECO:0000269|PubMed:20131292}.
/FTId=VAR_070626.
VARIANT 202 202 L -> S (in dbSNP:rs7247284).
{ECO:0000269|PubMed:17846997}.
/FTId=VAR_024617.
VARIANT 205 205 D -> E (in dbSNP:rs62619782).
{ECO:0000269|PubMed:17846997}.
/FTId=VAR_070627.
VARIANT 230 230 F -> L (in AGS4; dbSNP:rs79767407).
{ECO:0000269|PubMed:17846997}.
/FTId=VAR_070628.
VARIANT 235 235 R -> Q (in AGS4; dbSNP:rs75718910).
{ECO:0000269|PubMed:17846997}.
/FTId=VAR_070629.
VARIANT 240 240 T -> M (in AGS4; dbSNP:rs79843600).
{ECO:0000269|PubMed:17846997}.
/FTId=VAR_070630.
VARIANT 258 258 A -> G (in dbSNP:rs15389).
/FTId=VAR_027378.
VARIANT 260 260 E -> G (in dbSNP:rs770898096).
{ECO:0000269|PubMed:17846997}.
/FTId=VAR_070631.
VARIANT 291 291 R -> H (in AGS4; dbSNP:rs75037667).
{ECO:0000269|PubMed:17846997}.
/FTId=VAR_070632.
MUTAGEN 67 67 D->A: Loss of enzyme activity.
{ECO:0000269|PubMed:21177858}.
MUTAGEN 69 69 K->A: Strongly reduced enzyme activity.
{ECO:0000269|PubMed:21177858}.
MUTAGEN 112 112 N->A: Reduced enzyme activity.
{ECO:0000269|PubMed:21177858}.
MUTAGEN 210 210 Y->A: Strongly reduced enzyme activity.
{ECO:0000269|PubMed:21177858}.
MUTAGEN 210 210 Y->F: Loss of enzyme activity.
{ECO:0000269|PubMed:21177858}.
MUTAGEN 240 240 T->A: Strongly reduced enzyme activity.
{ECO:0000269|PubMed:21177858}.
CONFLICT 152 152 R -> Q (in Ref. 1; CAB09725).
{ECO:0000305}.
HELIX 4 7 {ECO:0000244|PDB:3PUF}.
STRAND 15 17 {ECO:0000244|PDB:3PUF}.
HELIX 23 26 {ECO:0000244|PDB:3PUF}.
STRAND 29 36 {ECO:0000244|PDB:3PUF}.
STRAND 41 43 {ECO:0000244|PDB:3PUF}.
STRAND 45 54 {ECO:0000244|PDB:3PUF}.
HELIX 57 62 {ECO:0000244|PDB:3PUF}.
HELIX 73 84 {ECO:0000244|PDB:3PUF}.
STRAND 86 88 {ECO:0000244|PDB:3PUF}.
STRAND 90 96 {ECO:0000244|PDB:3PUF}.
HELIX 98 105 {ECO:0000244|PDB:3PUF}.
STRAND 107 109 {ECO:0000244|PDB:3PUF}.
HELIX 113 130 {ECO:0000244|PDB:3PUF}.
STRAND 135 144 {ECO:0000244|PDB:3PUF}.
HELIX 146 156 {ECO:0000244|PDB:3PUF}.
STRAND 160 166 {ECO:0000244|PDB:3PUF}.
HELIX 168 171 {ECO:0000244|PDB:3PUF}.
HELIX 173 191 {ECO:0000244|PDB:3PUF}.
HELIX 214 222 {ECO:0000244|PDB:3PUF}.
TURN 226 228 {ECO:0000244|PDB:3PUF}.
HELIX 239 248 {ECO:0000244|PDB:3PUF}.
HELIX 286 290 {ECO:0000244|PDB:3PUF}.
STRAND 293 295 {ECO:0000244|PDB:3PUF}.
SEQUENCE 299 AA; 33395 MW; 34992FE85130157B CRC64;
MDLSELERDN TGRCRLSSPV PAVCRKEPCV LGVDEAGRGP VLGPMVYAIC YCPLPRLADL
EALKVADSKT LLESERERLF AKMEDTDFVG WALDVLSPNL ISTSMLGRVK YNLNSLSHDT
ATGLIQYALD QGVNVTQVFV DTVGMPETYQ ARLQQSFPGI EVTVKAKADA LYPVVSAASI
CAKVARDQAV KKWQFVEKLQ DLDTDYGSGY PNDPKTKAWL KEHVEPVFGF PQFVRFSWRT
AQTILEKEAE DVIWEDSASE NQEGLRKITS YFLNEGSQAR PRSSHRYFLE RGLESATSL


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