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Database: UniProt
Entry: H0XN98_OTOGA
LinkDB: H0XN98_OTOGA
Original site: H0XN98_OTOGA 
ID   H0XN98_OTOGA            Unreviewed;       362 AA.
AC   H0XN98;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   24-JAN-2024, entry version 63.
DE   RecName: Full=S-adenosylmethionine-dependent nucleotide dehydratase RSAD2 {ECO:0000256|ARBA:ARBA00035038};
DE   AltName: Full=Radical S-adenosyl methionine domain-containing protein 2 {ECO:0000256|ARBA:ARBA00035040};
DE   AltName: Full=Virus inhibitory protein, endoplasmic reticulum-associated, interferon-inducible {ECO:0000256|ARBA:ARBA00035042};
GN   Name=RSAD2 {ECO:0000313|Ensembl:ENSOGAP00000017589.1};
OS   Otolemur garnettii (Small-eared galago) (Garnett's greater bushbaby).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lorisiformes;
OC   Galagidae; Otolemur.
OX   NCBI_TaxID=30611 {ECO:0000313|Ensembl:ENSOGAP00000017589.1, ECO:0000313|Proteomes:UP000005225};
RN   [1] {ECO:0000313|Proteomes:UP000005225}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   The Broad Institute Genome Sequencing Platform;
RA   Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K., Jaffe D.B.,
RA   Gnerre S., MacCallum I., Przybylski D., Ribeiro F.J., Burton J.N.,
RA   Walker B.J., Sharpe T., Hall G.;
RT   "Version 3 of the genome sequence of Otolemur garnettii (Bushbaby).";
RL   Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSOGAP00000017589.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=AH2 + CTP + S-adenosyl-L-methionine = 3'-deoxy-3',4'-
CC         didehydro-CTP + 5'-deoxyadenosine + A + H(+) + H2O + L-methionine;
CC         Xref=Rhea:RHEA:65944, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17319, ChEBI:CHEBI:17499,
CC         ChEBI:CHEBI:37563, ChEBI:CHEBI:57844, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:166821; Evidence={ECO:0000256|ARBA:ARBA00034994};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004397}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004397}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004397}. Lipid droplet
CC       {ECO:0000256|ARBA:ARBA00004502}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004287}. Mitochondrion inner membrane
CC       {ECO:0000256|ARBA:ARBA00004273}. Mitochondrion outer membrane
CC       {ECO:0000256|ARBA:ARBA00004294}.
CC   -!- SIMILARITY: Belongs to the radical SAM superfamily. RSAD2 family.
CC       {ECO:0000256|ARBA:ARBA00035008}.
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DR   EMBL; AAQR03187714; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAQR03187715; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_003803606.1; XM_003803558.2.
DR   AlphaFoldDB; H0XN98; -.
DR   STRING; 30611.ENSOGAP00000017589; -.
DR   Ensembl; ENSOGAT00000031662.1; ENSOGAP00000017589.1; ENSOGAG00000027657.1.
DR   GeneID; 100960257; -.
DR   KEGG; oga:100960257; -.
DR   CTD; 91543; -.
DR   eggNOG; ENOG502QQMH; Eukaryota.
DR   GeneTree; ENSGT00390000013670; -.
DR   HOGENOM; CLU_049058_2_1_1; -.
DR   InParanoid; H0XN98; -.
DR   OMA; QPFRWKC; -.
DR   OrthoDB; 3671494at2759; -.
DR   TreeFam; TF300085; -.
DR   Proteomes; UP000005225; Unassembled WGS sequence.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0001650; C:fibrillar center; IEA:Ensembl.
DR   GO; GO:0005811; C:lipid droplet; IEA:InterPro.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:Ensembl.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043621; F:protein self-association; IEA:Ensembl.
DR   GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0050709; P:negative regulation of protein secretion; IEA:Ensembl.
DR   GO; GO:0045071; P:negative regulation of viral genome replication; IEA:Ensembl.
DR   CDD; cd01335; Radical_SAM; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR006638; Elp3/MiaA/NifB-like_rSAM.
DR   InterPro; IPR026372; RSAD2.
DR   InterPro; IPR007197; rSAM.
DR   NCBIfam; TIGR04278; viperin; 1.
DR   NCBIfam; NF038283; viperin_w_prok; 1.
DR   PANTHER; PTHR21339; RADICAL S-ADENOSYL METHIONINE DOMAIN-CONTAINING PROTEIN 2; 1.
DR   PANTHER; PTHR21339:SF0; RADICAL S-ADENOSYL METHIONINE DOMAIN-CONTAINING PROTEIN 2; 1.
DR   Pfam; PF13353; Fer4_12; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   SFLD; SFLDG01088; antiviral_proteins; 1.
DR   SFLD; SFLDG01067; SPASM/twitch_domain_containing; 1.
DR   SFLD; SFLDF00318; Viperin; 1.
DR   SMART; SM00729; Elp3; 1.
DR   SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR   PROSITE; PS51918; RADICAL_SAM; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW   Antiviral defense {ECO:0000256|ARBA:ARBA00023118};
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Immunity {ECO:0000256|ARBA:ARBA00022859};
KW   Innate immunity {ECO:0000256|ARBA:ARBA00022588};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Lipid droplet {ECO:0000256|ARBA:ARBA00022677};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005225};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..40
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           41..362
FT                   /note="S-adenosylmethionine-dependent nucleotide
FT                   dehydratase RSAD2"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003546187"
FT   DOMAIN          70..290
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
FT   REGION          46..72
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   362 AA;  41430 MW;  1FDE8784973CA1A6 CRC64;
     MWMLEPSAFA GKLLSALRLP LGSLWKSLVP LLCWLRAAFG LPGTERRQQL QVQREPGEPT
     EGEEGDIPAA TTPTSVNYHF TRQCNYKCGF CFHTAKTSFV LPLQEAKRGL LLLKEAGMEK
     INFSGGEPFI HDRGEYLGKL VRFCKEELQL PSVSIVSNGS LIRERWFQSY GEFLDILAIS
     CDSFDESVNV LIGRGQAKKN HVENLQKLRA WCRDYRVAFK INSVINRFNV DEDMNEEIKA
     LNPVRWKVFQ CLLIEGENSG EDALREAGRF VISDEEFEGF LERHKGVSCL VPESNQKMKD
     SYLILDEYMR FLNCRNGRKE PSKSILDVGV EEAIKFSGFD EKMFLKRGGK YVWSKADLKL
     DW
//
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