ID A0A2U3WN15_ODORO Unreviewed; 399 AA.
AC A0A2U3WN15;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
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|RefSeq:XP_004410437.1};
OS Odobenus rosmarus divergens (Pacific walrus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Pinnipedia; Odobenidae;
OC Odobenus.
OX NCBI_TaxID=9708 {ECO:0000313|Proteomes:UP000245340, ECO:0000313|RefSeq:XP_004410437.1};
RN [1] {ECO:0000313|RefSeq:XP_004410437.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 RefSeq; XP_004410437.1; XM_004410380.1.
DR AlphaFoldDB; A0A2U3WN15; -.
DR STRING; 9708.A0A2U3WN15; -.
DR GeneID; 101373749; -.
DR KEGG; oro:101373749; -.
DR CTD; 4938; -.
DR InParanoid; A0A2U3WN15; -.
DR OrthoDB; 4638494at2759; -.
DR Proteomes; UP000245340; Unplaced.
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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000245340}.
FT DOMAIN 43..116
FT /note="Polymerase nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF01909"
FT DOMAIN 164..347
FT /note="2'-5'-oligoadenylate synthetase 1"
FT /evidence="ECO:0000259|Pfam:PF10421"
SQ SEQUENCE 399 AA; 45934 MW; 780EB0A78AE3575B CRC64;
MWELEETPAR FLDKFIENYL LPDTHFRRQI KEAVHIISTF LKERCFQGAA HPVRVSKVVK
GGSSGKGTSL RGRSDADLVV FLSNLRSFEE QLHKRGQFIW EIKRQLEACQ IEETFEVQFE
LGSLQPEKPR ALSFLLQNRS LGEGVEFDVL PAFDVLGQWT NNGRPNSQVY LKLIQECQDL
GKEGEFSTCF TELQRDFLRQ RPTKVKSLIR LVKHWYQKCK NKLGKPLPQQ YALELLTVYA
WEKGSKQTEF STAQGFQTVL KLVLNYQQLC IYWTKYYDFE NPIIGRYLER QLAKSRPVIL
DPADPTGNVA AGDLHGWWRL ADEARAWLSY PCFKKGDGSP VGSWDMPLAE GNEDNWVTCE
HRMYQSQDYG WCPLSAGSLS TGMTPPTAQK EDDWVCAIL
//
