ID C0KIC5_TASV2 Unreviewed; 261 AA.
AC C0KIC5;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 08-NOV-2023, entry version 47.
DE RecName: Full=Non-structural polyprotein 1AB {ECO:0000256|ARBA:ARBA00019743};
DE Flags: Fragment;
OS Turkey astrovirus 2 (TAstV-2).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Stellavirales; Astroviridae; Avastrovirus; Avastrovirus 3.
OX NCBI_TaxID=246343 {ECO:0000313|EMBL:ACM90312.1};
OH NCBI_TaxID=9103; Meleagris gallopavo (Wild turkey).
RN [1] {ECO:0000313|EMBL:ACM90312.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=TK/MN/B1016/08 {ECO:0000313|EMBL:ACM90312.1};
RA Jindal N., Patnayak D.P., Chander Y., Ziegler A.F., Goyal S.M.;
RT "Detection and molecular characterization of enteric viruses in breeder
RT turkeys.";
RL Avian Pathol. 39:53-61(2010).
CC -!- FUNCTION: Contains the viral protease participating in the cleavage of
CC the polyprotein into functional products. It contains also the
CC activities necessary for replication of genomic RNA, as well as
CC transcription of subgenomic mRNA. {ECO:0000256|ARBA:ARBA00029407}.
CC -!- SUBCELLULAR LOCATION: Host membrane {ECO:0000256|ARBA:ARBA00004301};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004301}.
CC -!- SIMILARITY: Belongs to the astroviridae polyprotein 1AB family.
CC {ECO:0000256|ARBA:ARBA00005873}.
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DR EMBL; FJ605163; ACM90312.1; -; Genomic_RNA.
DR GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003968; F:RNA-dependent RNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR CDD; cd23172; ps-ssRNAv_Astroviridae_RdRp; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR001205; RNA-dir_pol_C.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR Pfam; PF00680; RdRP_1; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PE 3: Inferred from homology;
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Ribosomal frameshifting {ECO:0000256|ARBA:ARBA00022758};
KW RNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022484};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Viral RNA replication {ECO:0000256|ARBA:ARBA00022953}.
FT DOMAIN 24..158
FT /note="RdRp catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50507"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ACM90312.1"
FT NON_TER 261
FT /evidence="ECO:0000313|EMBL:ACM90312.1"
SQ SEQUENCE 261 AA; 30461 MW; EF763FBAFABB8A87 CRC64;
QVGWTPFFGG LDRRVRRLCG DGDRYFVEMD WTRYDGTIPK SLFWRIRQIR FFFLHDSHKT
PKMRRLYNWY VKNLLEKIIL LPTGEVCQVK KGNPSGQYST TVDNNMINVW LTTFEVSYLF
FKQRGRLPTE KELQENCSMI CYGDDRLLSI RKGFVEYEPD TVIEMYKSIF GMWVKRSNIK
IQDTPEGLSF CGLTIVKSSA GAYVGVPNVN KILSTLENPV RRLPDVESLW GKLVSLRILC
ENAPSNVKHF LDEQISNVEE F
//