GenomeNet

Database: UniProt
Entry: Q5J0M4_HORSE
LinkDB: Q5J0M4_HORSE
Original site: Q5J0M4_HORSE 
ID   Q5J0M4_HORSE            Unreviewed;      1084 AA.
AC   Q5J0M4;
DT   15-FEB-2005, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2005, sequence version 1.
DT   24-JAN-2024, entry version 68.
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:AAT72304.1};
OS   Equus caballus (Horse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX   NCBI_TaxID=9796 {ECO:0000313|EMBL:AAT72304.1};
RN   [1] {ECO:0000313|EMBL:AAT72304.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=16093721; DOI=10.1159/000085670;
RA   Perelygin A.A., Lear T.L., Zharkikh A.A., Brinton M.A.;
RT   "Structure of equine 2'-5'oligoadenylate synthetase (OAS) gene family and
RT   FISH mapping of OAS genes to ECA8p15-->p14 and BTA17q24-->q25.";
RL   Cytogenet. Genome Res. 111:51-56(2005).
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; AY569128; AAT72304.1; -; mRNA.
DR   RefSeq; NP_001075226.1; NM_001081757.1.
DR   AlphaFoldDB; Q5J0M4; -.
DR   GeneID; 791225; -.
DR   KEGG; ecb:791225; -.
DR   CTD; 4940; -.
DR   OrthoDB; 4638494at2759; -.
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   2: Evidence at transcript level;
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..342
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..867
FT                   /note="Polymerase nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF01909"
FT   DOMAIN          901..1082
FT                   /note="2'-5'-oligoadenylate synthetase 1"
FT                   /evidence="ECO:0000259|Pfam:PF10421"
FT   REGION          340..408
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1084 AA;  120742 MW;  A39D7284372AC2FF CRC64;
     MDVYRTPAAE LDGLVARSLQ PPAEFVGAAR RALGNLSAAL RERGGRPGAA AQPWRVLKIG
     GSSGRGTALR GGCDSELVIF LDCFKSYEDQ GAHRAEILNE MRALLESSWQ DTVLGLSLEF
     PEQNTPGVLQ LRLASTDLEN WMDVSLVPAF DALGQLRTGA KPEPRVYSSL LDSGSRGGEH
     AACFAELRRN FVNARPTKLK NLILLVKHWY RQVCPQEASR ELLPPAYALE LLTIFAWERG
     CGKDAFSLAQ GLRTVLGLVQ DYRHLCVFWT LNYSFEDPAL RQFLRRQLER PRPVILDPAD
     PTWDVGNGAA WRWDLLAKEA ESCCDHPCFL QAARGPVQPW EGPDLPRAGC PGLDHRIQQD
     PAQRTPEDSG VLTGVHPSTR KRQPWSPAPG PSSAASIAPR PPQEVSDLSR IPAPELDRFI
     QDHLMPSSQF QKQVSKAIDV ILRGLRENCV HKPSRASKGG SFGRGTDLRG GCDAELVIFL
     NCFKDYKDQG ARRGQILEEI RAQLESWWQD RVPSLSLKFP EQSAPGALQL QLASAALESR
     VDVSLLPAFD AIGQLRAGAK PEPGVYSSLL DSGSRGGEHA ACFAELRRNF VNTRPTKLKN
     LILLVKHWYR QVAAQNKGAQ RAGASLPPAY ALELLTIFAW EQGCGEDRFS MAQGLRTVLG
     LVQQHRQLCV YWTVNYSFED PALRTHLLGQ LRNPRPLVLD PADPTWNVGQ GSWELLAQEA
     AALGTQPCLM SREGTPVQPW DVMPALLCQT PASDLDKFIT EFLQPNRHFL EQVNKAVDTI
     CSFLRDNCFR NSPIKVLKGG SSAKGTALRG RSDADLVVFL SCFSQFTEQG NRRAEIISEI
     RAQLEACQQE REFEVKFEIS KWENPRVLSF SLTSQTMLDQ SVDFDVLPAF DALGQLVPDS
     RPRPQVYVDL IHSYSNAGEY SPCFTELQRN FISSRPTKLK SLIRLVKHWY QQCNKMPKGR
     GSLPPQHGLE LLTVYAWEQG GCDCQFSMAE GFRTVLELVR QYRQLCVYWT VNYDNENETV
     RDFLKLQLQK PRPIILDPAD PTGNLGPNAR WDLLAKEAVA CMSAPCCMGR DGSPIQPWPV
     KAAV
//
DBGET integrated database retrieval system