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Deoxynucleoside triphosphate triphosphohydrolase SAMHD1 (dNTPase) (EC 3.1.5.-) (Interferon-gamma-inducible protein Mg11) (SAM domain and HD domain-containing protein 1)

 SAMH1_MOUSE             Reviewed;         658 AA.
Q60710; E9Q0K6; F8WJE0; Q3U5X2; Q543A4; Q91VK8;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
18-JUL-2018, sequence version 3.
12-SEP-2018, entry version 151.
RecName: Full=Deoxynucleoside triphosphate triphosphohydrolase SAMHD1 {ECO:0000305};
Short=dNTPase {ECO:0000305};
EC=3.1.5.- {ECO:0000269|PubMed:29379009};
AltName: Full=Interferon-gamma-inducible protein Mg11 {ECO:0000303|PubMed:7884320};
AltName: Full=SAM domain and HD domain-containing protein 1 {ECO:0000305};
Short=mSAMHD1 {ECO:0000303|PubMed:29379009};
Name=Samhd1 {ECO:0000312|MGI:MGI:1927468};
Synonyms=Mg11 {ECO:0000303|PubMed:7884320};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] OF 16-658 (ISOFORM 1).
TISSUE=Macrophage;
PubMed=7884320;
Lafuse W.P., Brown D., Castle L., Zwilling B.S.;
"Cloning and characterization of a novel cDNA that is IFN-gamma-
induced in mouse peritoneal macrophages and encodes a putative GTP-
binding protein.";
J. Leukoc. Biol. 57:477-483(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 22-658 (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Bone marrow, and Ovary;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 12-658 (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Brain, and Mammary gland;
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 SER-49; THR-52 AND THR-634,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-634, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
"Large scale localization of protein phosphorylation by use of
electron capture dissociation mass spectrometry.";
Mol. Cell. Proteomics 8:904-912(2009).
[7]
INDUCTION.
PubMed=19525956; DOI=10.1038/ng.373;
Rice G.I., Bond J., Asipu A., Brunette R.L., Manfield I.W., Carr I.M.,
Fuller J.C., Jackson R.M., Lamb T., Briggs T.A., Ali M., Gornall H.,
Couthard L.R., Aeby A., Attard-Montalto S.P., Bertini E., Bodemer C.,
Brockmann K., Brueton L.A., Corry P.C., Desguerre I., Fazzi E.,
Cazorla A.G., Gener B., Hamel B.C.J., Heiberg A., Hunter M.,
van der Knaap M.S., Kumar R., Lagae L., Landrieu P.G., Lourenco C.M.,
Marom D., McDermott M.F., van der Merwe W., Orcesi S.,
Prendiville J.S., Rasmussen M., Shalev S.A., Soler D.M., Shinawi M.,
Spiegel R., Tan T.Y., Vanderver A., Wakeling E.L., Wassmer E.,
Whittaker E., Lebon P., Stetson D.B., Bonthron D.T., Crow Y.J.;
"Mutations involved in Aicardi-Goutieres syndrome implicate SAMHD1 as
regulator of the innate immune response.";
Nat. Genet. 41:829-832(2009).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49; THR-52; SER-55;
THR-56 AND THR-634, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[9]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=23972988; DOI=10.1016/j.celrep.2013.07.037;
Behrendt R., Schumann T., Gerbaulet A., Nguyen L.A., Schubert N.,
Alexopoulou D., Berka U., Lienenklaus S., Peschke K., Gibbert K.,
Wittmann S., Lindemann D., Weiss S., Dahl A., Naumann R., Dittmer U.,
Kim B., Mueller W., Gramberg T., Roers A.;
"Mouse SAMHD1 has antiretroviral activity and suppresses a spontaneous
cell-intrinsic antiviral response.";
Cell Rep. 4:689-696(2013).
[10]
FUNCTION, DISRUPTION PHENOTYPE, AND ALTERNATIVE SPLICING (ISOFORMS 1
AND 2).
PubMed=23872947; DOI=10.1038/emboj.2013.163;
Rehwinkel J., Maelfait J., Bridgeman A., Rigby R., Hayward B.,
Liberatore R.A., Bieniasz P.D., Towers G.J., Moita L.F., Crow Y.J.,
Bonthron D.T., Reis e Sousa C.;
"SAMHD1-dependent retroviral control and escape in mice.";
EMBO J. 32:2454-2462(2013).
[11]
FUNCTION, PHOSPHORYLATION AT THR-634, AND MUTAGENESIS OF THR-634.
PubMed=26667483; DOI=10.1186/s12977-015-0229-6;
Wittmann S., Behrendt R., Eissmann K., Volkmann B., Thomas D.,
Ebert T., Cribier A., Benkirane M., Hornung V., Bouzas N.F.,
Gramberg T.;
"Phosphorylation of murine SAMHD1 regulates its antiretroviral
activity.";
Retrovirology 12:103-103(2015).
[12]
FUNCTION.
PubMed=29669924; DOI=10.1073/pnas.1719771115;
Thientosapol E.S., Bosnjak D., Durack T., Stevanovski I.,
van Geldermalsen M., Holst J., Jahan Z., Shepard C., Weninger W.,
Kim B., Brink R., Jolly C.J.;
"SAMHD1 enhances immunoglobulin hypermutation by promoting
transversion mutation.";
Proc. Natl. Acad. Sci. U.S.A. 115:4921-4926(2018).
[13] {ECO:0000244|PDB:6BRG, ECO:0000244|PDB:6BRH, ECO:0000244|PDB:6BRK}
X-RAY CRYSTALLOGRAPHY (3.40 ANGSTROMS) IN COMPLEX WITH MAGNESIUM AND
DGTP, FUNCTION, CATALYTIC ACTIVITY, DOMAIN, ACTIVITY REGULATION, AND
MUTAGENESIS OF PHE-109; PHE-112 AND ARG-143.
PubMed=29379009; DOI=10.1038/s41467-017-02783-8;
Buzovetsky O., Tang C., Knecht K.M., Antonucci J.M., Wu L., Ji X.,
Xiong Y.;
"The SAM domain of mouse SAMHD1 is critical for its activation and
regulation.";
Nat. Commun. 9:411-411(2018).
-!- FUNCTION: Isoform 1: Protein that acts both as a host restriction
factor involved in defense response to virus and as a regulator of
DNA end resection at stalled replication forks (By similarity).
Has deoxynucleoside triphosphate (dNTPase) activity, which is
required to restrict infection by viruses: dNTPase activity
reduces cellular dNTP levels to levels too low for retroviral
reverse transcription to occur, blocking early-stage virus
replication in dendritic and other myeloid cells (PubMed:23972988,
PubMed:23872947, PubMed:26667483, PubMed:29379009). Likewise,
suppresses LINE-1 retrotransposon activity (PubMed:26667483). In
addition to virus restriction, dNTPase activity acts as a
regulator of DNA precursor pools by regulating dNTP pools (By
similarity). Phosphorylation at Thr-634 acts as a switch to
control dNTPase-dependent and -independent functions: it inhibits
dNTPase activity and ability to restrict infection by viruses,
while it promotes DNA end resection at stalled replication forks
(By similarity). Functions during S phase at stalled DNA
replication forks to promote the resection of gapped or reversed
forks: acts by stimulating the exonuclease activity of MRE11,
activating the ATR-CHK1 pathway and allowing the forks to restart
replication (By similarity). Its ability to promote degradation of
nascent DNA at stalled replication forks is required to prevent
induction of type I interferons, thereby preventing chronic
inflammation (By similarity). Ability to promote DNA end resection
at stalled replication forks is independent of dNTPase activity
(By similarity). Enhances immunoglobulin hypermutation in B-
lymphocytes by promoting transversion mutation (PubMed:29669924).
{ECO:0000250|UniProtKB:Q9Y3Z3, ECO:0000269|PubMed:23872947,
ECO:0000269|PubMed:23972988, ECO:0000269|PubMed:26667483,
ECO:0000269|PubMed:29379009, ECO:0000269|PubMed:29669924}.
-!- CATALYTIC ACTIVITY: dNTP + H(2)O = Deoxynucleoside + triphosphate.
{ECO:0000269|PubMed:29379009}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000250|UniProtKB:Q9Y3Z3};
Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q9Y3Z3};
-!- ACTIVITY REGULATION: Allosterically activated and regulated via
the combined actions of GTP and dNTPs (dATP, dGTP, dTTP and dCTP):
Allosteric site 1 binds GTP, while allosteric site 2 binds dNTP.
Allosteric activation promotes the formation of highly active
homotetramers. Isoform 1: Phosphorylation at Thr-634 impairs
homotetramerization, thereby inhibiting dNTPase activity, leading
to reduced ability to restrict infection by viruses.
{ECO:0000305|PubMed:29379009}.
-!- SUBUNIT: Homodimer; in absence of GTP and dNTP (By similarity).
Homotetramer; in GTP- and dNTP-bound form (PubMed:29379009).
Interacts with MRE11; leading to stimulate the exonuclease
activity of MRE11 (By similarity). Interacts with RBBP8/CtIP (By
similarity). {ECO:0000250|UniProtKB:Q9Y3Z3,
ECO:0000269|PubMed:29379009}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9Y3Z3}.
Chromosome {ECO:0000250|UniProtKB:Q9Y3Z3}. Note=Localizes to sites
of DNA double-strand breaks in response to DNA damage.
{ECO:0000250|UniProtKB:Q9Y3Z3}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q60710-1; Sequence=Displayed;
Name=2;
IsoId=Q60710-2; Sequence=VSP_059661;
-!- INDUCTION: By interferon alpha, beta and gamma (IFN-alpha, IFN-
beta and IFN-gamma). {ECO:0000269|PubMed:19525956}.
-!- DOMAIN: In mouse, the SAM domain is required for deoxynucleoside
triphosphate (dNTPase) activity and ability to restrict infection
by viruses. It acts by capping allosteric sites.
{ECO:0000269|PubMed:29379009}.
-!- PTM: Isoform 1: Phosphorylation at Thr-634 by CDK1 acts as a
switch to control deoxynucleoside triphosphate (dNTPase)-dependent
and -independent functions (PubMed:26667483) (By similarity).
Phosphorylation at Thr-634 takes place in cycling cells: it
reduces the stability of the homotetramer, impairing the dNTPase
activity and subsequent ability to restrict infection by viruses
(Probable). It also inhibits ability to suppress LINE-1
retrotransposon activity (PubMed:26667483). In contrast,
phosphorylation at Thr-634 promotes DNA end resection at stalled
replication forks in response to DNA damage (By similarity).
{ECO:0000250|UniProtKB:Q9Y3Z3, ECO:0000269|PubMed:26667483,
ECO:0000305|PubMed:26667483}.
-!- PTM: Isoform 2: Not phosphorylated by CDK1 at the C-terminus.
{ECO:0000305}.
-!- DISRUPTION PHENOTYPE: Mice are viable and fertile but show
increased cellular dNTP concentrations and impaired ability to
restrict retroviral replication in lymphocytes, macrophages and
dendritic cells (PubMed:23972988). Mice also diplay interferon
(IFN)-beta-dependent transcriptional up-regulation of type I IFN-
inducible genes in various cell types indicative of spontaneous
IFN production (PubMed:23972988, PubMed:23872947).
{ECO:0000269|PubMed:23872947, ECO:0000269|PubMed:23972988}.
-!- SIMILARITY: Belongs to the SAMHD1 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA66219.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAA66219.1; Type=Frameshift; Positions=607; Evidence={ECO:0000305};
Sequence=AAH12721.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAH67198.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAC35801.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAE30313.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAE31954.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; U15635; AAA66219.1; ALT_SEQ; mRNA.
EMBL; AK054490; BAC35801.1; ALT_INIT; mRNA.
EMBL; AK151335; BAE30313.1; ALT_INIT; mRNA.
EMBL; AK153390; BAE31954.1; ALT_INIT; mRNA.
EMBL; AL669828; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC012721; AAH12721.1; ALT_INIT; mRNA.
EMBL; BC067198; AAH67198.1; ALT_INIT; mRNA.
PIR; I49127; I49127.
RefSeq; NP_001132992.1; NM_001139520.1.
RefSeq; NP_061339.3; NM_018851.3.
UniGene; Mm.248478; -.
UniGene; Mm.468781; -.
PDB; 6BRG; X-ray; 3.50 A; A/B/C/D=1-658.
PDB; 6BRH; X-ray; 3.40 A; A/B=1-658.
PDB; 6BRK; X-ray; 3.50 A; A=1-658.
PDBsum; 6BRG; -.
PDBsum; 6BRH; -.
PDBsum; 6BRK; -.
ProteinModelPortal; Q60710; -.
SMR; Q60710; -.
BioGrid; 207791; 11.
IntAct; Q60710; 3.
MINT; Q60710; -.
STRING; 10090.ENSMUSP00000059717; -.
CarbonylDB; Q60710; -.
iPTMnet; Q60710; -.
PhosphoSitePlus; Q60710; -.
SwissPalm; Q60710; -.
EPD; Q60710; -.
MaxQB; Q60710; -.
PaxDb; Q60710; -.
PeptideAtlas; Q60710; -.
PRIDE; Q60710; -.
DNASU; 56045; -.
Ensembl; ENSMUST00000057725; ENSMUSP00000059717; ENSMUSG00000027639. [Q60710-1]
Ensembl; ENSMUST00000088523; ENSMUSP00000085880; ENSMUSG00000027639. [Q60710-2]
GeneID; 56045; -.
KEGG; mmu:56045; -.
CTD; 25939; -.
MGI; MGI:1927468; Samhd1.
eggNOG; KOG2681; Eukaryota.
eggNOG; COG1078; LUCA.
GeneTree; ENSGT00390000013867; -.
HOGENOM; HOG000264286; -.
HOVERGEN; HBG054208; -.
InParanoid; Q60710; -.
KO; K22544; -.
OMA; EVKWTHE; -.
OrthoDB; EOG091G060J; -.
PhylomeDB; Q60710; -.
TreeFam; TF316113; -.
Reactome; R-MMU-8956319; Nucleobase catabolism.
ChiTaRS; Samhd1; mouse.
PMAP-CutDB; Q60710; -.
PRO; PR:Q60710; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000027639; Expressed in 267 organ(s), highest expression level in decidua.
CleanEx; MM_SAMHD1; -.
ExpressionAtlas; F8WJE0; baseline and differential.
GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0032567; F:dGTP binding; ISS:UniProtKB.
GO; GO:0008832; F:dGTPase activity; ISS:UniProtKB.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0003676; F:nucleic acid binding; ISS:UniProtKB.
GO; GO:0004540; F:ribonuclease activity; ISS:UniProtKB.
GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
GO; GO:0016793; F:triphosphoric monoester hydrolase activity; ISO:MGI.
GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
GO; GO:0046061; P:dATP catabolic process; ISS:UniProtKB.
GO; GO:0051607; P:defense response to virus; ISS:UniProtKB.
GO; GO:0006203; P:dGTP catabolic process; ISS:UniProtKB.
GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0051289; P:protein homotetramerization; ISO:MGI.
GO; GO:0045088; P:regulation of innate immune response; ISS:UniProtKB.
CDD; cd00077; HDc; 1.
InterPro; IPR003607; HD/PDEase_dom.
InterPro; IPR006674; HD_domain.
InterPro; IPR001660; SAM.
InterPro; IPR013761; SAM/pointed_sf.
Pfam; PF01966; HD; 1.
Pfam; PF07647; SAM_2; 1.
SMART; SM00471; HDc; 1.
SMART; SM00454; SAM; 1.
SUPFAM; SSF47769; SSF47769; 1.
PROSITE; PS51831; HD; 1.
PROSITE; PS50105; SAM_DOMAIN; 1.
1: Evidence at protein level;
3D-structure; Allosteric enzyme; Alternative splicing;
Antiviral defense; Chromosome; Complete proteome; DNA damage;
DNA repair; DNA replication; GTP-binding; Hydrolase; Immunity;
Innate immunity; Isopeptide bond; Metal-binding; Nucleotide-binding;
Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation; Zinc.
CHAIN 1 658 Deoxynucleoside triphosphate
triphosphohydrolase SAMHD1.
/FTId=PRO_0000153733.
DOMAIN 77 142 SAM. {ECO:0000255|PROSITE-
ProRule:PRU00184}.
DOMAIN 196 348 HD. {ECO:0000255|PROSITE-
ProRule:PRU01175}.
NP_BIND 169 177 GTP. {ECO:0000244|PDB:6BRH,
ECO:0000305|PubMed:29379009}.
NP_BIND 395 397 dNTP. {ECO:0000250|UniProtKB:Q9Y3Z3}.
REGION 341 347 Substrate binding.
{ECO:0000250|UniProtKB:Q9Y3Z3}.
REGION 413 418 Substrate binding.
{ECO:0000250|UniProtKB:Q9Y3Z3}.
ACT_SITE 265 265 {ECO:0000250|UniProtKB:Q9Y3Z3}.
METAL 199 199 Zinc; via tele nitrogen.
{ECO:0000244|PDB:6BRH,
ECO:0000305|PubMed:29379009}.
METAL 238 238 Zinc; via tele nitrogen.
{ECO:0000244|PDB:6BRH,
ECO:0000305|PubMed:29379009}.
METAL 239 239 Zinc. {ECO:0000244|PDB:6BRH,
ECO:0000305|PubMed:29379009}.
METAL 343 343 Zinc. {ECO:0000244|PDB:6BRH,
ECO:0000305|PubMed:29379009}.
BINDING 148 148 GTP. {ECO:0000244|PDB:6BRH,
ECO:0000305|PubMed:29379009}.
BINDING 151 151 dNTP; via amide nitrogen; shared with
neighboring subunit.
{ECO:0000250|UniProtKB:Q9Y3Z3}.
BINDING 181 181 Substrate.
{ECO:0000250|UniProtKB:Q9Y3Z3}.
BINDING 196 196 Substrate.
{ECO:0000250|UniProtKB:Q9Y3Z3}.
BINDING 242 242 Substrate.
{ECO:0000250|UniProtKB:Q9Y3Z3}.
BINDING 347 347 Substrate.
{ECO:0000250|UniProtKB:Q9Y3Z3}.
BINDING 351 351 Substrate.
{ECO:0000250|UniProtKB:Q9Y3Z3}.
BINDING 365 365 dNTP. {ECO:0000250|UniProtKB:Q9Y3Z3}.
BINDING 401 401 dNTP. {ECO:0000250|UniProtKB:Q9Y3Z3}.
BINDING 409 409 Substrate.
{ECO:0000250|UniProtKB:Q9Y3Z3}.
BINDING 419 419 dNTP; shared with neighboring subunit.
{ECO:0000250|UniProtKB:Q9Y3Z3}.
BINDING 420 420 dNTP; shared with neighboring subunit.
{ECO:0000244|PDB:6BRH,
ECO:0000305|PubMed:29379009}.
BINDING 494 494 GTP; shared with neighboring subunit.
{ECO:0000244|PDB:6BRH,
ECO:0000305|PubMed:29379009}.
BINDING 498 498 GTP; shared with neighboring subunit.
{ECO:0000250|UniProtKB:Q9Y3Z3}.
BINDING 565 565 dNTP. {ECO:0000250|UniProtKB:Q9Y3Z3}.
MOD_RES 49 49 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 52 52 Phosphothreonine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 55 55 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 56 56 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 64 64 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Y3Z3}.
MOD_RES 125 125 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Y3Z3}.
MOD_RES 634 634 Phosphothreonine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:19131326,
ECO:0000244|PubMed:21183079,
ECO:0000269|PubMed:26667483}.
CROSSLNK 509 509 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q9Y3Z3}.
VAR_SEQ 625 658 DGDIIAPLITPLKWNNKTSSCLQEVSKVKTCLKF -> QCG
AGEMAEDPDSIPSTQQPHAAHNQL (in isoform 2).
/FTId=VSP_059661.
MUTAGEN 109 109 F->L: In LCH mutant; abolishes formation
of the tetramer and deoxynucleoside
triphosphate (dNTPase) activity; when
associated with C-112 and H-143.
{ECO:0000269|PubMed:29379009}.
MUTAGEN 112 112 F->C: In LCH mutant; abolishes formation
of the tetramer and deoxynucleoside
triphosphate (dNTPase) activity; when
associated with L-109 and H-143.
{ECO:0000269|PubMed:29379009}.
MUTAGEN 143 143 R->H: In LCH mutant; abolishes formation
of the tetramer and deoxynucleoside
triphosphate (dNTPase) activity; when
associated with L-109 and C-112.
{ECO:0000269|PubMed:29379009}.
MUTAGEN 634 634 T->A,V: Increased ability to restrict
LINE-1 retrotransposon activity.
{ECO:0000269|PubMed:26667483}.
MUTAGEN 634 634 T->E: Mimicks phosphorylation state,
reduced ability to restrict LINE-1
retrotransposon activity.
{ECO:0000269|PubMed:26667483}.
CONFLICT 371 371 R -> L (in Ref. 2; BAE31954/BAE30313).
{ECO:0000305}.
HELIX 48 57 {ECO:0000244|PDB:6BRH}.
HELIX 63 71 {ECO:0000244|PDB:6BRH}.
HELIX 76 81 {ECO:0000244|PDB:6BRH}.
HELIX 84 90 {ECO:0000244|PDB:6BRH}.
HELIX 97 107 {ECO:0000244|PDB:6BRH}.
HELIX 113 115 {ECO:0000244|PDB:6BRG}.
STRAND 117 121 {ECO:0000244|PDB:6BRH}.
TURN 122 124 {ECO:0000244|PDB:6BRH}.
STRAND 125 129 {ECO:0000244|PDB:6BRH}.
HELIX 131 137 {ECO:0000244|PDB:6BRH}.
HELIX 140 143 {ECO:0000244|PDB:6BRH}.
HELIX 144 147 {ECO:0000244|PDB:6BRH}.
HELIX 152 156 {ECO:0000244|PDB:6BRH}.
HELIX 165 186 {ECO:0000244|PDB:6BRH}.
HELIX 188 190 {ECO:0000244|PDB:6BRH}.
HELIX 194 205 {ECO:0000244|PDB:6BRH}.
TURN 206 210 {ECO:0000244|PDB:6BRH}.
HELIX 216 220 {ECO:0000244|PDB:6BRH}.
HELIX 222 226 {ECO:0000244|PDB:6BRH}.
STRAND 228 230 {ECO:0000244|PDB:6BRK}.
HELIX 234 248 {ECO:0000244|PDB:6BRH}.
HELIX 251 257 {ECO:0000244|PDB:6BRH}.
HELIX 262 274 {ECO:0000244|PDB:6BRH}.
STRAND 289 291 {ECO:0000244|PDB:6BRH}.
HELIX 293 300 {ECO:0000244|PDB:6BRH}.
TURN 305 308 {ECO:0000244|PDB:6BRH}.
HELIX 311 324 {ECO:0000244|PDB:6BRH}.
HELIX 332 337 {ECO:0000244|PDB:6BRH}.
STRAND 339 347 {ECO:0000244|PDB:6BRH}.
STRAND 355 363 {ECO:0000244|PDB:6BRH}.
HELIX 365 367 {ECO:0000244|PDB:6BRH}.
HELIX 368 384 {ECO:0000244|PDB:6BRH}.
TURN 385 387 {ECO:0000244|PDB:6BRH}.
HELIX 389 405 {ECO:0000244|PDB:6BRH}.
TURN 406 408 {ECO:0000244|PDB:6BRH}.
HELIX 414 416 {ECO:0000244|PDB:6BRH}.
TURN 421 423 {ECO:0000244|PDB:6BRH}.
HELIX 424 426 {ECO:0000244|PDB:6BRH}.
HELIX 428 431 {ECO:0000244|PDB:6BRH}.
HELIX 438 444 {ECO:0000244|PDB:6BRH}.
HELIX 448 450 {ECO:0000244|PDB:6BRH}.
HELIX 451 461 {ECO:0000244|PDB:6BRH}.
STRAND 467 472 {ECO:0000244|PDB:6BRH}.
STRAND 474 477 {ECO:0000244|PDB:6BRH}.
HELIX 483 486 {ECO:0000244|PDB:6BRH}.
HELIX 487 493 {ECO:0000244|PDB:6BRH}.
HELIX 506 508 {ECO:0000244|PDB:6BRH}.
STRAND 509 515 {ECO:0000244|PDB:6BRH}.
STRAND 559 566 {ECO:0000244|PDB:6BRH}.
HELIX 570 586 {ECO:0000244|PDB:6BRH}.
SEQUENCE 658 AA; 75893 MW; 8ED07CE9EB6239D6 CRC64;
MDSLLGCGVS AAAREPVPRY LTSQPRVSEV AMQSAPLEQP AKRPRCDGSP RTPPSTPPAT
ANLSADDDFQ NTDLRTWEPE DVCSFLENRG FREKKVLDIF RDNKIAGSFL PFLDEDRLED
LGVSSLEERK KMIECIQQLS QSRIDLMKVF NDPIHGHIEF HPLLIRIIDT PQFQRLRYIK
QLGGGYYVFP GASHNRFEHS LGVGYLAGCL VRALAEKQPE LQISERDILC VQIAGLCHDL
GHGPFSHMFD GRFIPRARPE KKWKHEQGSI EMFEHLVNSN ELKLVMKNYG LVPEEDITFI
KEQIMGPPIT PVKDSLWPYK GRPATKSFLY EIVSNKRNGI DVDKWDYFAR DCHHLGIQNN
FDYKRFIKFA RICEVEYKVK EDKTYIRKVK HICSREKEVG NLYDMFHTRN CLHRRAYQHK
ISNLIDIMIT DAFLKADPYV EITGTAGKKF RISTAIDDME AFTKLTDNIF LEVLHSTDPQ
LSEAQSILRN IECRNLYKYL GETQPKREKI RKEEYERLPQ EVAKAKPEKA PDVELKAEDF
IVDVINVDYG MEDKNPIDRV HFYCKSNSKQ AVRINKEQVS QLLPEKFAEQ LIRVYCKKKD
GKSLDAAGKH FVQWCALRDF TKPQDGDIIA PLITPLKWNN KTSSCLQEVS KVKTCLKF


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