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Protein

Deoxynucleoside triphosphate triphosphohydrolase SAMHD1

Gene

SAMHD1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Host restriction nuclease that blocks early-stage virus replication in dendritic and other myeloid cells. Likewise, suppresses LINE-1 retrotransposon activity. May function by reducing the cellular dNTP levels to levels too low for retroviral reverse transcription to occur. May play a role in mediating proinflammatory responses to TNF-alpha signaling (By similarity).By similarity

Catalytic activityi

dNTP + H2O = Deoxynucleoside + triphosphate.

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Enzyme regulationi

Allosterically stimulated by dGTP which binds in a cleft at the interface of the homodimer and promotes the formation of highly active homotetramers. Each allosteric site binds two molecules of dGTP (dGTP1 and dGTP 2) between adjoining subunits. Not activated by dATP, dCTP and dTTP (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei104 – 1041dGTP 1By similarity
Binding sitei107 – 1071dGTP 2; via amide nitrogen; shared with neighboring subunitBy similarity
Binding sitei137 – 1371SubstrateBy similarity
Binding sitei152 – 1521SubstrateBy similarity
Metal bindingi155 – 1551Zinc; via tele nitrogenBy similarity
Metal bindingi194 – 1941Zinc; via tele nitrogenBy similarity
Metal bindingi195 – 1951ZincBy similarity
Binding sitei198 – 1981SubstrateBy similarity
Active sitei221 – 2211By similarity
Metal bindingi300 – 3001ZincBy similarity
Binding sitei304 – 3041SubstrateBy similarity
Binding sitei308 – 3081SubstrateBy similarity
Binding sitei322 – 3221dGTP 2By similarity
Binding sitei347 – 3471dGTP 2By similarity
Binding sitei355 – 3551SubstrateBy similarity
Binding sitei365 – 3651dGTP 2; shared with neighboring subunitBy similarity
Binding sitei366 – 3661dGTP 2; shared with neighboring subunitBy similarity
Binding sitei440 – 4401dGTP 1; shared with neighboring subunitBy similarity
Binding sitei444 – 4441dGTP 1; shared with neighboring subunitBy similarity
Binding sitei512 – 5121dGTP 2By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi125 – 1339dGTPBy similarity
Nucleotide bindingi125 – 1339dGTP 1By similarity
Nucleotide bindingi341 – 3433dGTP 2By similarity

GO - Molecular functioni

  1. dGTPase activity Source: UniProtKB
  2. dGTP binding Source: UniProtKB
  3. nucleic acid binding Source: UniProtKB
  4. RNA binding Source: UniProtKB
  5. zinc ion binding Source: UniProtKB

GO - Biological processi

  1. dATP catabolic process Source: UniProtKB
  2. defense response to virus Source: UniProtKB
  3. dGTP catabolic process Source: UniProtKB
  4. innate immune response Source: UniProtKB-KW
  5. protein homotetramerization Source: Ensembl
  6. regulation of innate immune response Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Immunity, Innate immunity

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Deoxynucleoside triphosphate triphosphohydrolase SAMHD1 (EC:3.1.5.-)
Short name:
dNTPase
Gene namesi
Name:SAMHD1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Unplaced

Subcellular locationi

Nucleus By similarity

GO - Cellular componenti

  1. nucleus Source: UniProtKB
  2. plasma membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 589589Deoxynucleoside triphosphate triphosphohydrolase SAMHD1PRO_0000361968Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei18 – 181PhosphoserineBy similarity
Modified residuei21 – 211PhosphothreonineBy similarity

Post-translational modificationi

Ubiquitinated and targeted for proteasomal degradation by a DCX (DDB1-CUL4-X-box) E3 ubiquitin ligase with the help of the viral accessory protein Vpx.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ0VCA5.

Expressioni

Gene expression databases

ExpressionAtlasiQ0VCA5. baseline.

Interactioni

Subunit structurei

Homodimer. Homotetramer; in dGTP-bound form (By similarity).By similarity

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000041236.

Structurei

3D structure databases

ProteinModelPortaliQ0VCA5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini45 – 10056SAMAdd
BLAST
Domaini152 – 308157HDAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni298 – 3047Substrate bindingBy similarity
Regioni359 – 3646Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the SAMHD1 family.Curated
Contains 1 HD domain.Curated

Phylogenomic databases

eggNOGiCOG1078.
HOGENOMiHOG000264286.
HOVERGENiHBG054208.
InParanoidiQ0VCA5.

Family and domain databases

Gene3Di1.10.3210.10. 2 hits.
InterProiIPR003607. HD/PDEase_dom.
IPR006674. HD_domain.
IPR013761. SAM/pointed.
[Graphical view]
PfamiPF01966. HD. 1 hit.
[Graphical view]
SMARTiSM00471. HDc. 1 hit.
[Graphical view]
SUPFAMiSSF47769. SSF47769. 1 hit.

Sequencei

Sequence statusi: Complete.

Q0VCA5-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MQSADSQNTP KRPRRDGSPR TPPDSPLADA ETSPSHDLDP DYRTWGPEQV
60 70 80 90 100
WSFLRRCGFS DSELLKRCRE KRMSGSLLPF PEDLGISSHG KKMKLLNCIQ
110 120 130 140 150
DTMKVINDPI HGHIEFHPLL MRIIDTPQFQ RLRYIKQLGG GYYVFPGASH
160 170 180 190 200
NRFEHSLGVG YLAGRLVREL SEKQPELQIS ERDILCVQIA GLCHDLGHGP
210 220 230 240 250
FSHMFDGRFI PLARPEIKWT HEQGSVMMFE HLINSNGLQD VMKYYGLIPE
260 270 280 290 300
EDILFIKEQI TGPPESPIKD ASKWLYKGRP KEKSFLYEIV ANKRNGIDVD
310 320 330 340 350
KWDYFARDCH HLGIQNSFDY KRFLKFARVC EVDNMKHICT REKEVGNLYD
360 370 380 390 400
MFHTRNCLHR RAYQHKVGNI IDTMITDAFL KADDHIEITG SAGRKYHIST
410 420 430 440 450
AIDDMEAFTK LTDNIFLEIL YSTDPNLNDA RMILKKIESR NLYKFVGETQ
460 470 480 490 500
PMIQRIKKEN YEHLPNEVAS AKPSDVELEA ELKAEDLIVD VINMDYGMED
510 520 530 540 550
KNPIDHVRFY CKSDLSKAVM ITRNQVSQFL PETFAEQLIR VYCKKTDEKT
560 570 580
LFAARQHFVH WCLINDFTKP QIKKLPLRKL KKELTTATG
Length:589
Mass (Da):68,239
Last modified:September 5, 2006 - v1
Checksum:i260B7E035B2A6F85
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC120271 mRNA. Translation: AAI20272.1.
RefSeqiNP_001069329.1. NM_001075861.1.
UniGeneiBt.92388.

Genome annotation databases

GeneIDi524683.
KEGGibta:524683.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC120271 mRNA. Translation: AAI20272.1.
RefSeqiNP_001069329.1. NM_001075861.1.
UniGeneiBt.92388.

3D structure databases

ProteinModelPortaliQ0VCA5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000041236.

Proteomic databases

PaxDbiQ0VCA5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi524683.
KEGGibta:524683.

Organism-specific databases

CTDi25939.

Phylogenomic databases

eggNOGiCOG1078.
HOGENOMiHOG000264286.
HOVERGENiHBG054208.
InParanoidiQ0VCA5.

Miscellaneous databases

NextBioi20874017.

Gene expression databases

ExpressionAtlasiQ0VCA5. baseline.

Family and domain databases

Gene3Di1.10.3210.10. 2 hits.
InterProiIPR003607. HD/PDEase_dom.
IPR006674. HD_domain.
IPR013761. SAM/pointed.
[Graphical view]
PfamiPF01966. HD. 1 hit.
[Graphical view]
SMARTiSM00471. HDc. 1 hit.
[Graphical view]
SUPFAMiSSF47769. SSF47769. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. NIH - Mammalian Gene Collection (MGC) project
    Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Fetal medulla.

Entry informationi

Entry nameiSAMH1_BOVIN
AccessioniPrimary (citable) accession number: Q0VCA5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: September 5, 2006
Last modified: January 7, 2015
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Allosteric enzyme, Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.