ID B5B850_PANTR Unreviewed; 365 AA.
AC B5B850;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=2'-5' oligoadenylate synthase {ECO:0000256|ARBA:ARBA00012577};
DE EC=2.7.7.84 {ECO:0000256|ARBA:ARBA00012577};
GN Name=oas1 {ECO:0000313|EMBL:CAQ57746.1};
OS Pan troglodytes troglodytes.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=37011 {ECO:0000313|EMBL:CAQ57746.1};
RN [1] {ECO:0000313|EMBL:CAQ57746.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Lee {ECO:0000313|EMBL:CAQ57746.1};
RA Ferguson W.G.;
RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CAQ57746.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Lee {ECO:0000313|EMBL:CAQ57746.1};
RX PubMed=22104212; DOI=10.1093/molbev/msr247;
RA Ferguson W., Dvora S., Fikes R.W., Stone A.C., Boissinot S.;
RT "Long-Term Balancing Selection at the Antiviral Gene OAS1 in Central
RT African Chimpanzees.";
RL Mol. Biol. Evol. 29:1093-1103(2012).
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; FM163425; CAQ57746.1; -; Genomic_DNA.
DR AlphaFoldDB; B5B850; -.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0001730; F:2'-5'-oligoadenylate synthetase activity; ISS:UniProtKB.
DR GO; GO:0035457; P:cellular response to interferon-alpha; ISS:UniProtKB.
DR GO; GO:0051607; P:defense response to virus; ISS:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0045071; P:negative regulation of viral genome replication; ISS:UniProtKB.
DR GO; GO:0060700; P:regulation of ribonuclease activity; ISS:UniProtKB.
DR CDD; cd05400; NT_2-5OAS_ClassI-CCAase; 1.
DR Gene3D; 1.10.1410.20; 2'-5'-oligoadenylate synthetase 1, domain 2; 1.
DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
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:SF13; 2'-5'-OLIGOADENYLATE SYNTHASE 1; 1.
DR PANTHER; PTHR11258; 2-5 OLIGOADENYLATE SYNTHETASE; 1.
DR Pfam; PF01909; NTP_transf_2; 1.
DR Pfam; PF10421; OAS1_C; 1.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR SUPFAM; SSF81631; PAP/OAS1 substrate-binding domain; 1.
DR PROSITE; PS00832; 25A_SYNTH_1; 1.
DR PROSITE; PS00833; 25A_SYNTH_2; 1.
DR PROSITE; PS50152; 25A_SYNTH_3; 1.
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 38..111
FT /note="Polymerase nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF01909"
FT DOMAIN 165..346
FT /note="2'-5'-oligoadenylate synthetase 1"
FT /evidence="ECO:0000259|Pfam:PF10421"
SQ SEQUENCE 365 AA; 41906 MW; B943690F270057BE CRC64;
MMDLRNTPAK SLDKFIEDYL LPDTCFRMQI NHAIDIICGF LKERCFRGSS YPVCVSKVVK
GGSSGKGTTL RGRSDADLVV FLSPLTTFQD QLNRRGEFIQ EIRRQLEACQ REERAFSVKF
EVQAPRRDNP RALSFVLSSL QLGEGVEFDV LPAFDALGQL TGGYKPDPQI YVKLIEECTY
LQKEGEFSTC FTELQRDFLK ERPTKLKSLI RLVKHWYQNC KKKLGKLPPQ YALELLTVYA
WERGSMKTHF NTAQGFRTVL ELVINYQQLC IYWTKYYDFK NPIIEKYLSR QLEKPRPVIL
DPADPTGNLG GGDPKGWRQL AQEAEAWLNY PCFKNWDGSP VSSWILLVRP PASSLPFIPA
PLHEA
//