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Database: UniProt
Entry: B6RC76_PANPA
LinkDB: B6RC76_PANPA
Original site: B6RC76_PANPA 
ID   B6RC76_PANPA            Unreviewed;      1087 AA.
AC   B6RC76;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=2'-5' oligoadenylate synthase {ECO:0000256|ARBA:ARBA00012577};
DE            EC=2.7.7.84 {ECO:0000256|ARBA:ARBA00012577};
GN   Name=OAS3 {ECO:0000313|EMBL:ACJ13113.1};
OS   Pan paniscus (Pygmy chimpanzee) (Bonobo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9597 {ECO:0000313|EMBL:ACJ13113.1};
RN   [1] {ECO:0000313|EMBL:ACJ13113.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Coriell NG05253 {ECO:0000313|EMBL:ACJ13113.1};
RC   TISSUE=Skin {ECO:0000313|EMBL:ACJ13113.1};
RA   Magness C.L., Steiger K.V., Scherer C.A., Fellin P.C., Olson A.N.,
RA   Guillaudeux T., Miner D.G., Rosenberg G., Berthier A.M., Carithers R.L.,
RA   Green P., Growe G.H., Hagan H., Hough E., Justesen J., Katze M.G.,
RA   Mathisen T.L., Myers R.M., Shuhart M.C., Iadonato S.P.;
RT   "Human immune diversity and evidence of balancing natural selection in
RT   oligoadenylate synthetases.";
RL   Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3 ATP = 5'-triphosphoadenylyl-(2'->5')-adenylyl-(2'->5')-
CC         adenosine + 2 diphosphate; Xref=Rhea:RHEA:34407, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:67143; EC=2.7.7.84;
CC         Evidence={ECO:0000256|ARBA:ARBA00001112};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the 2-5A synthase family.
CC       {ECO:0000256|ARBA:ARBA00009526}.
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DR   EMBL; EF364080; ACJ13113.1; -; Genomic_DNA.
DR   AlphaFoldDB; B6RC76; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0001730; F:2'-5'-oligoadenylate synthetase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   CDD; cd05400; NT_2-5OAS_ClassI-CCAase; 3.
DR   Gene3D; 1.10.1410.20; 2'-5'-oligoadenylate synthetase 1, domain 2; 3.
DR   Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 3.
DR   InterPro; IPR018952; 2-5-oligoAdlate_synth_1_dom2/C.
DR   InterPro; IPR006117; 2-5OAS_C_CS.
DR   InterPro; IPR043518; 2-5OAS_N_CS.
DR   InterPro; IPR006116; NT_2-5OAS_ClassI-CCAase.
DR   InterPro; IPR043519; NT_sf.
DR   InterPro; IPR002934; Polymerase_NTP_transf_dom.
DR   PANTHER; PTHR11258:SF4; 2'-5'-OLIGOADENYLATE SYNTHASE 3; 1.
DR   PANTHER; PTHR11258; 2-5 OLIGOADENYLATE SYNTHETASE; 1.
DR   Pfam; PF01909; NTP_transf_2; 1.
DR   Pfam; PF10421; OAS1_C; 3.
DR   SUPFAM; SSF81301; Nucleotidyltransferase; 3.
DR   SUPFAM; SSF81631; PAP/OAS1 substrate-binding domain; 3.
DR   PROSITE; PS00832; 25A_SYNTH_1; 3.
DR   PROSITE; PS00833; 25A_SYNTH_2; 2.
DR   PROSITE; PS50152; 25A_SYNTH_3; 3.
PE   3: Inferred from homology;
KW   Antiviral defense {ECO:0000256|ARBA:ARBA00023118};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Immunity {ECO:0000256|ARBA:ARBA00022859};
KW   Innate immunity {ECO:0000256|ARBA:ARBA00022588}.
FT   DOMAIN          161..341
FT                   /note="2'-5'-oligoadenylate synthetase 1"
FT                   /evidence="ECO:0000259|Pfam:PF10421"
FT   DOMAIN          560..744
FT                   /note="2'-5'-oligoadenylate synthetase 1"
FT                   /evidence="ECO:0000259|Pfam:PF10421"
FT   DOMAIN          780..870
FT                   /note="Polymerase nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF01909"
FT   DOMAIN          904..1085
FT                   /note="2'-5'-oligoadenylate synthetase 1"
FT                   /evidence="ECO:0000259|Pfam:PF10421"
FT   REGION          362..393
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1087 AA;  121033 MW;  0F24DA381AF9DCF8 CRC64;
     MDLYSTPAAA LDRFVARRLQ PRKEFVEKAR RALGALAAAL RERGGRLGAA APRVLKTVKG
     GSSGRGTALK GGCDSELVIF LDCFKSYVDQ RARRAEILSE MRASLESWWQ NPVPGLRLTF
     PEQSVPGALQ FRLTSVDLED WMDVSLVPAF NVLGQAGSGV KPKPQVYSTL LNSGCQGGEH
     AACFTELRRN FVNIRPAKLK NLILLVKHWY HQVCLQGLWK ETLPPVYALE LLTIFAWEQG
     CKKDAFSLAE GLRTVLGLIQ QHQHLCVFWT VNYGFEDPAV GQFLQRQLKR PRPVILDPAD
     PTWDLGNGAA WHWDLLAQEA ASCYDHPCFL RGMGDPVQSW KGPGLPCAGC SGLGHPIQLD
     PNQKTPENSK SLSAVYPRAG SKPPSCPAPG PTGAASIVPS VPGMALDLSQ IPTKELDRFI
     QDHLKPSPQF QEQVKKAIDI ILRCLRENCV HKASRVSKGG SFGRGTDLRD GCDVELIIFL
     NCFTDYKDQG PRRAEILDEM RAQLESWWQD QVPGLSLQFP EQNVPEALQF QLVSTALKSW
     MDVSLLPAFD AVGQLSSGTK PNPQVYSRLL TSGCQEGEHK ACFAELRRNF MNIRPVKLKN
     LILLVKHWYH QVAAQNKGKR PAPASLPPAY ALELLTIFAW EQGCGQDCFN MAQGFRTVLG
     LVQQHQQLCV YWTVNYSTED PAMRMHLLGQ LGKPRPLVLD PADPTWNVGH GSWELLAREA
     AALGMQACFL SRDGTSVQPW DVMPALLYQT PAGDLDKFIS EFLQPNRQFL AQVNKAIDTI
     CSFLKENCFR NSPIKVIKVV KGGSSAKGTA LRGRSDADLV VFLSCFSQFT EQGNKRAEII
     SEIRAQLEAC QQERQFEVKF EVSKWENPRV LSFSLTSQTM LDQSVDFDVL PAFDALGQLV
     SGSRPSSQVY VDLIHSYSNA GEYSTCFTEL QRDFIISRPT KLKSLIRLVK HWYQQCTKIS
     KGRGSLPPQH GLELLTVYAW EQGGKDSQFN MAEGFRTVLE LVTQYRQLCI YWTINYNAKD
     KTVGDFLKQQ LQKPRPIILD PADPTGNLGH NARWDLLAKE AAACTSALCC MGRNGIPIQP
     WPVKAAV
//
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