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RDRP_GLVWB
ID   RDRP_GLVWB              Reviewed;        1907 AA.
AC   Q67653;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-FEB-2011, sequence version 2.
DT   29-SEP-2021, entry version 55.
DE   RecName: Full=Probable RNA-directed RNA polymerase;
DE            EC=2.7.7.48;
DE   AltName: Full=Gag-Pol protein;
GN   Name=gag-pol;
OS   Giardia lamblia virus (isolate Wang) (GLV).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Chrymotiviricetes;
OC   Ghabrivirales; Totiviridae; Giardiavirus.
OX   NCBI_TaxID=649893;
OH   NCBI_TaxID=5741; Giardia intestinalis (Giardia lamblia).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=8378334; DOI=10.1073/pnas.90.18.8595;
RA   Wang A.L., Yang H.M., Shen K.A., Wang C.C.;
RT   "Giardiavirus double-stranded RNA genome encodes a capsid polypeptide and a
RT   gag-pol-like fusion protein by a translation frameshift.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:8595-8599(1993).
CC   -!- FUNCTION: RNA-dependent RNA polymerase which replicates the viral
CC       genome. Catalyzes the transcription of fully conservative plus-strand
CC       genomic RNAs that are extruded from the virion into the cytoplasm where
CC       they function as mRNAs for translation of viral proteins and also as
CC       substrates for encapsidation to form new virions. Once encapsidated,
CC       the positive strand is converted to dsRNA by the RNA-directed RNA
CC       polymerase. Displays ssRNA-binding activity (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC         RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC         COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC         EC=2.7.7.48;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Ribosomal frameshifting; Named isoforms=2;
CC       Name=RNA-directed RNA polymerase; Synonyms=Pol protein;
CC         IsoId=Q67653-1; Sequence=Displayed;
CC       Name=Major capsid protein; Synonyms=Gag protein;
CC         IsoId=Q67652-1; Sequence=External;
CC   -!- MISCELLANEOUS: One molecule or two of Gag capsid protein is replaced in
CC       the virion by Gag-Pol because the fusion protein is essential for RNA
CC       encapsidation and replication.
CC   -!- MISCELLANEOUS: [Isoform RNA-directed RNA polymerase]: Produced by -1
CC       ribosomal frameshifting.
CC   -!- SIMILARITY: Belongs to the totiviridae RNA-directed RNA polymerase
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB01579.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; L13218; AAB01579.1; ALT_SEQ; Genomic_RNA.
DR   PIR; C47521; C47521.
DR   Proteomes; UP000000350; Genome.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR001795; RNA-dir_pol_luteovirus.
DR   Pfam; PF02123; RdRP_4; 1.
DR   SUPFAM; SSF56672; SSF56672; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW   Ribosomal frameshifting; RNA-binding; RNA-directed RNA polymerase;
KW   Transferase; Viral RNA replication.
FT   CHAIN           1..1907
FT                   /note="Probable RNA-directed RNA polymerase"
FT                   /id="PRO_0000404511"
FT   REGION          42..61
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1907 AA;  214248 MW;  E1BB38CD8ECE1132 CRC64;
     MVWGTGYGNP SPLNPYGFAS LHRGGLNPLI LAPENITFDT LNTHNDHEET HGESPEVPKA
     SIAPAGRQNV PVLQQNQENE DNHALGGSED AKDEREIRFS AIKTLYNYYS EGPSTPIMPH
     LVNRLRGLDA LAKIDATLTK VDMNAAYIFA LRPTFPYSYG YKQRFSNRRL TTSALCYART
     GLSSFLTVDK TYTSNSPLKG GSRGWPIFNV DVSSHVAEPH MRTLSPIGLE VFNLATSQFS
     KTLLTASSKV FTQSLYTADI LSIFGEVFLP HVMQPVSNYT PILVRALLAL IHILGPGSGN
     CSLSSSIFES SIPQFLTVSH STNMSNRTRY CLHTRSAYKD MFRNGIPPQS TLPPTLAPEG
     SSARVLIPEA LVTSPMFPWL LILVSSGPQF FLYSKDASIN TVDIGSRGRI TSPIPDVAKL
     DLHRLWNLFR FDGYRYIDVV IVGADRDYVW PYQNGVYVHG GKGPNGTGNY GNADVHDGIG
     TIFSSFNNNV NVQTSDLMLG LLTLWNHITT TYATEEEVTM AIKIAAAFAL VYPVQPIVYS
     GCPKAFQRHT SYYQPSSENC YATDTAEVKS VWDTVELSVQ VNNAMVLGMT LPFGQPTLSS
     AQWYNNIDKA EISMFKVGNL PLQNLDYLSL DMMEFYAPTT GQLYDIRSDN LILSAHRTVN
     LGIGYTALAD FFAYLASVPA QSFYHDRMVT SPISKQTYSV YERFIERFID DFVGWDRCDL
     FNLDTLLGAK HIAGVASSPI PWHCSLQRCP LPIIMHYTGL TFGQEHITVR DVAGVEGLQQ
     IVMRDFQGRI VVERLGTAAP SRIAVKLDWS RLSAWYSDTT CAIPLIRSCD GDRQLRGNMG
     SYTGKTRTGF VYTYFSPNFL SSFNVSEPIF NTSINLTPPY DDTSQAVIQN LSMPQMLSFD
     PYYESTFYVV SADNEWIPTS GPAWKVPYLE NVVKRSGRRL LAELRIASNN GSGDRTFLTT
     CKTRKGRHFT YFSAALGGKI LEFVCAPLSS ISLQGGQTIY APIQLQDVIP VRKEDPVPGS
     IYAVFKFFSE PKAWEARALK SYKVRFQDLP SHIVISELKE RAARSYIGSR GYVDTGFKAL
     DIYIDILSQM ELPKYIHEFL ILLRGKVCEV SRLYKKEQVF VILLTVFSEL TAIVRHRGNK
     STGSMGRMWT LLSDFETLLG KVSYKNPSII EEQVVPWLTS DPIPRTPDFY STYFKTAVQF
     MHRTFVPVTL RSAPPLTFHE YCGRPELWGT TGSGYIGYGK RSFNKWSIYG AYPTEEIYRL
     ALYGDNPPLK PLEKPELTKV RAVISASLQS YILMSYLEYI MADTIVDKAF TTTLMNDRQL
     ENLERHMMTM TGGVRVPVDQ SNFDRQPDLV QIGIWQQLLF HLASASAPYR ARDSVSLVIS
     RLASTTTFPN LKVRMSDGDK RVLHGLPSGW KWTALLGALI NVTQLLTMAE LSNTLASLRS
     TVVQGDDIAL SMTDREQATQ LVDTYARQGF EVNPKKFWIS PDRDEFLRRV ATPGIVAGYP
     ARMMIKLLYQ LTEPEEPSHY ISMLPKLAKV PNVVQEHVKP RSDVPWSETV EELDWREALA
     ILRHRPARTS ELVTQWLQLI GRFTAAHPDK RALTLLYRWF VRDLTHATKI KKRNLLVLLQ
     QPGFWGGYSQ SLVGLLRTTH LADMIVSELD IGLPGPRATS SRFGTSPTSL APHYLTLIVP
     SSVHVQSQKE LDLWGLCRSS KYAKHYSNIF RYYKLTLPTL VLWAQRLGDK HVTDFIRSVT
     LGSEIPKYDP HARLFTSNGV SVGMLIRIRV RHFTHRVLRR ETPKCIPVIV GLYREQTLSV
     PESVRLSEPD KILLSLQRAS GYSLNLVKKI LQITRKPVDH PVDARFSQAF PNNWSDLART
     AGTFLLTVPA EVSGDNADLV PERLGFNHSS WLHAIFRSRK FLLCVVA
 
 
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