ID Q9YNB1_9POTY Unreviewed; 1420 AA.
AC Q9YNB1;
DT 01-MAY-1999, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2002, sequence version 2.
DT 27-MAR-2024, entry version 113.
DE SubName: Full=Polyprotein {ECO:0000313|EMBL:CAA76842.3};
DE Flags: Fragment;
OS Sugarcane streak mosaic virus.
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Patatavirales; Potyviridae; Poacevirus.
OX NCBI_TaxID=53954 {ECO:0000313|EMBL:CAA76842.3};
RN [1] {ECO:0000313|EMBL:CAA76842.3}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Andhra Pradesh {ECO:0000313|EMBL:CAA76842.3};
RX PubMed=10226614; DOI=10.1007/s007050050519;
RA Hema M., Joseph J., Gopinath K., Sreenivasulu P., Savithri H.S.;
RT "Molecular characterization and interviral relationships of a flexuous
RT filamentous virus causing mosaic disease of sugarcane (Saccharum
RT officinarum L.) in India.";
RL Arch. Virol. 144:479-490(1999).
RN [2] {ECO:0000313|EMBL:CAA76842.3}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Andhra Pradesh {ECO:0000313|EMBL:CAA76842.3};
RA Hema M.;
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Has RNA-binding and proteolytic activities.
CC {ECO:0000256|ARBA:ARBA00029399}.
CC -!- FUNCTION: Indispensable for virus replication.
CC {ECO:0000256|ARBA:ARBA00034080}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolyzes glutaminyl bonds, and activity is further
CC restricted by preferences for the amino acids in P6 - P1' that vary
CC with the species of potyvirus, e.g. Glu-Xaa-Xaa-Tyr-Xaa-Gln-|-(Ser or
CC Gly) for the enzyme from tobacco etch virus. The natural substrate is
CC the viral polyprotein, but other proteins and oligopeptides
CC containing the appropriate consensus sequence are also cleaved.;
CC EC=3.4.22.44; Evidence={ECO:0000256|ARBA:ARBA00000785};
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000256|ARBA:ARBA00004328}.
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DR EMBL; Y17738; CAA76842.3; -; mRNA.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:InterPro.
DR GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
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:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR CDD; cd23175; ps-ssRNAv_Potyviridae_RdRp; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001592; Poty_coat.
DR InterPro; IPR001730; Potyv_NIa-pro_dom.
DR InterPro; IPR013648; PP_Potyviridae.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR001205; RNA-dir_pol_C.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR Pfam; PF00863; Peptidase_C4; 1.
DR Pfam; PF00767; Poty_coat; 1.
DR Pfam; PF08440; Poty_PP; 1.
DR Pfam; PF00680; RdRP_1; 1.
DR PRINTS; PR00966; NIAPOTYPTASE.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS51436; POTYVIRUS_NIA_PRO; 1.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PE 2: Evidence at transcript level;
KW Capsid protein {ECO:0000313|EMBL:CAA76842.3};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW RNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022484};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Viral RNA replication {ECO:0000256|ARBA:ARBA00022953};
KW Virion {ECO:0000256|ARBA:ARBA00022844}.
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 399..616
FT /note="Peptidase C4"
FT /evidence="ECO:0000259|PROSITE:PS51436"
FT DOMAIN 874..994
FT /note="RdRp catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50507"
FT REGION 1136..1174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CAA76842.3"
SQ SEQUENCE 1420 AA; 160422 MW; 4B8B456258D87275 CRC64;
QLPIPFYSND FAVPFYIALG HITAEAIKPR SFTVRLPVPN VKKAVLRLST SEAQVDRTIG
ILQVRLQQIR ERLGQIQHTT SWTAGLRLTN LFNTVLHKST SQSEKSLQAS LILGNRTLII
TWRLLALRKM IRSSRKLLAN NPMLSECLIY HGGQEAFLEQ YLFPTFKHPI KAYLVAIACL
TVGVGCLGYY YLKRRETLIM HAGKKRRTHA REDRYKRTGL MGQDEASYHW VGSEKDIIDD
WGAAYARKNA GKKKPSDWDD GKQQWDSREG TYTNVFKTLY DLDPTKFKYV VAEAPGYRFK
KKLNRQEKKR LSETIIEGIR SQMASEGIYD YPEVTQATLY LFGDPGQPAK KVILTPHNPL
AVSQGSGNPV GFPSNRGELR QTGAAMEMTE EERQRALANE TIVMHAQARI DISHVEKNVG
LISDGSYTSQ CFITQSWCVA PYHLASYFKQ TNNTLTITTT SGHYTLPRPL VHKILNHDLV
IFKMPGDFPP MKKISCLRKP NLDDEVVLIT TKRTPSGLRT TFSSSFYISE HHSGMMQYAL
KSVPGFCGGP IMSIKDGQII GFHSAARVVN MQDKGSTFTC VNDEVLEVLQ SESSQALIPW
LFNEEMVQWK GVNSNLDPRN FPIAKTHTEL IFHGAEIQHG TDKYFGDNLT IQGRINQSFN
NRHVIKGSDT YFDEFVMHVR PAPDRVDAHL PSDLSVEAFF KDFLKYATPV ELGRVDLGCL
ASAVDKVINH LEDQGFVAHE FQVETNFYTL LNSMNLDTAM GALYQTKKRD VLVPATHEEL
STWFTDSLTN LYNGKFGIWK ASLKAELRPV EKVQQHKTRV FTAAPFDVSF GAKAFVDGFN
NKFYERQAGS HWTVGINKFN CGWDELARRF NHDWKFIDAD GSRYDSSLTP LLFNCVLHIR
EHFMDLDSDE KRCLRNLYTQ LVWTPVSTIT GQIVKKCKGG PSGQPSTVVD NTLMLMIAVE
YSKLRTKIAD SELNYTCNGD DLLLNASLDT CTKIRESFTE TMKDLGLTYE FDVEVDNIGQ
VEYMSHKWLN ACGMLIPKLS RERIMSILRW NRSFDLESQA NKINAAWIES FGYADIMDFV
HEYANWWSKH TGKEGFLMDI DKVTALYLTD EVRIDPVPTD LLVSSRVETL VFHATVDGQG
TQPPQNQSSS PATTSSISST TTSQVDSQTT GNLSNTVSQT MRSLYVPPLV KSLKTEAKAK
QMMRYTPPQA LISSSAASIR QFNDWANTAA EGYGKTIQQF TDELLPFWIY WCVVNGATEE
NKTKPKWTKA VLNLDGADGT EITVDENGPQ VEFEMGPMYR NAKPGIRAIM RHFGELAYKW
VQFSVRSGKP IIPHNAVEAG LTTPEFYPCC IDFVMVNILS PAEIDVRNQV INARTPRMGR
PLFRHALRAG GDEDTDLRRE DDAHYGRTQI GGAQFGRAQH
//
