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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//