ID H9CW63_MDMV Unreviewed; 3022 AA.
AC H9CW63;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 12-AUG-2020, sequence version 2.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107};
DE Flags: Precursor;
OS Maize dwarf mosaic virus (MDMV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Patatavirales; Potyviridae; Potyvirus.
OX NCBI_TaxID=12203 {ECO:0000313|EMBL:AFC17879.1};
OH NCBI_TaxID=4560; Sorghum halepense (Johnson grass) (Holcus halepensis).
OH NCBI_TaxID=4577; Zea mays (Maize).
RN [1] {ECO:0000313|EMBL:AFC17879.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=OH-2 {ECO:0000313|EMBL:AFC17879.1};
RX PubMed=22342423; DOI=10.1016/j.virusres.2012.02.004;
RA Stewart L.R., Bouchard R., Redinbaugh M.G., Meulia T.;
RT "Complete sequence and development of a full-length infectious clone of an
RT Ohio isolate of Maize dwarf mosaic virus (MDMV).";
RL Virus Res. 165:219-224(2012).
CC -!- FUNCTION: An RNA-dependent RNA polymerase that plays an essential role
CC in the virus replication. {ECO:0000256|ARBA:ARBA00029404}.
CC -!- FUNCTION: Has RNA-binding and proteolytic activities.
CC {ECO:0000256|ARBA:ARBA00029399}.
CC -!- FUNCTION: Has helicase activity. It may be involved in replication.
CC {ECO:0000256|ARBA:ARBA00029422}.
CC -!- FUNCTION: Indispensable for virus replication.
CC {ECO:0000256|ARBA:ARBA00034080}.
CC -!- FUNCTION: Involved in aphid transmission, cell-to-cell and systemis
CC movement, encapsidation of the viral RNA and in the regulation of viral
CC RNA amplification. {ECO:0000256|ARBA:ARBA00029405}.
CC -!- FUNCTION: Mediates the cap-independent, EIF4E-dependent translation of
CC viral genomic RNAs (By similarity). Binds to the cap-binding site of
CC host EIF4E and thus interferes with the host EIF4E-dependent mRNA
CC export and translation (By similarity). VPg-RNA directly binds EIF4E
CC and is a template for transcription (By similarity). Also forms
CC trimeric complexes with EIF4E-EIF4G, which are templates for
CC translation. {ECO:0000256|ARBA:ARBA00037225}.
CC -!- FUNCTION: Required for aphid transmission and also has proteolytic
CC activity. Only cleaves a Gly-Gly dipeptide at its own C-terminus.
CC Interacts with virions and aphid stylets. Acts as a suppressor of RNA-
CC mediated gene silencing, also known as post-transcriptional gene
CC silencing (PTGS), a mechanism of plant viral defense that limits the
CC accumulation of viral RNAs. May have RNA-binding activity.
CC {ECO:0000256|ARBA:ARBA00029420}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolyzes a Gly-|-Gly bond at its own C-terminus, commonly in
CC the sequence -Tyr-Xaa-Val-Gly-|-Gly, in the processing of the
CC potyviral polyprotein.; EC=3.4.22.45;
CC Evidence={ECO:0000256|ARBA:ARBA00001848};
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: Cytoplasmic vesicle
CC {ECO:0000256|ARBA:ARBA00004541}. Host cytoplasmic vesicle
CC {ECO:0000256|ARBA:ARBA00034108}. Host nucleus
CC {ECO:0000256|ARBA:ARBA00004147}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}. Vesicle
CC {ECO:0000256|ARBA:ARBA00004373}. Virion
CC {ECO:0000256|ARBA:ARBA00004328}.
CC -!- SIMILARITY: Belongs to the potyviridae genome polyprotein family.
CC {ECO:0000256|ARBA:ARBA00006064, ECO:0000256|RuleBase:RU003351}.
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; JQ403609; AFC17879.1; -; Genomic_RNA.
DR MEROPS; C04.011; -.
DR GO; GO:0019029; C:helical viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0044161; C:host cell cytoplasmic vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0031982; C:vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
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:UniProtKB-KW.
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; 3.90.70.150; Helper component proteinase; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR001456; HC-pro.
DR InterPro; IPR031159; HC_PRO_CPD_dom.
DR InterPro; IPR042308; HC_PRO_CPD_sf.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR002540; Pept_S30_P1_potyvir.
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; IPR039560; Potyvirid-P3.
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 PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR PANTHER; PTHR18934:SF83; PRE-MRNA-SPLICING FACTOR ATP-DEPENDENT RNA HELICASE DHX16; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00863; Peptidase_C4; 1.
DR Pfam; PF00851; Peptidase_C6; 1.
DR Pfam; PF01577; Peptidase_S30; 1.
DR Pfam; PF00767; Poty_coat; 1.
DR Pfam; PF08440; Poty_PP; 1.
DR Pfam; PF13608; Potyvirid-P3; 1.
DR Pfam; PF00680; RdRP_1; 1.
DR PRINTS; PR00966; NIAPOTYPTASE.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS51744; HC_PRO_CPD; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51436; POTYVIRUS_NIA_PRO; 1.
DR PROSITE; PS51871; PV_P1_PRO; 1.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Capsid protein {ECO:0000256|ARBA:ARBA00022561};
KW Covalent protein-RNA linkage {ECO:0000256|ARBA:ARBA00022520};
KW Helical capsid protein {ECO:0000256|ARBA:ARBA00022497};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Host cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00022488};
KW Host-virus interaction {ECO:0000256|ARBA:ARBA00022463};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Inhibition of host innate immune response by virus
KW {ECO:0000256|ARBA:ARBA00022463};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Ribosomal frameshifting {ECO:0000256|ARBA:ARBA00022758};
KW RNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022484};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Suppressor of RNA silencing {ECO:0000256|ARBA:ARBA00022463};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Viral immunoevasion {ECO:0000256|ARBA:ARBA00022463};
KW Viral RNA replication {ECO:0000256|ARBA:ARBA00022953};
KW Virion {ECO:0000256|ARBA:ARBA00022844}.
FT DOMAIN 99..233
FT /note="Peptidase S30"
FT /evidence="ECO:0000259|PROSITE:PS51871"
FT DOMAIN 571..693
FT /note="Peptidase C6"
FT /evidence="ECO:0000259|PROSITE:PS51744"
FT DOMAIN 1182..1334
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1353..1512
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1988..2206
FT /note="Peptidase C4"
FT /evidence="ECO:0000259|PROSITE:PS51436"
FT DOMAIN 2472..2596
FT /note="RdRp catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50507"
FT REGION 2752..2796
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2752..2785
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 579
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01080"
FT ACT_SITE 652
FT /note="For helper component proteinase activity"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01080"
FT UNSURE 483
FT /note="I or L"
FT /evidence="ECO:0000313|EMBL:AFC17879.1"
FT UNSURE 1592
FT /note="D or N"
FT /evidence="ECO:0000313|EMBL:AFC17879.1"
SQ SEQUENCE 3022 AA; 343570 MW; 2E63897848501F68 CRC64;
MAGTWTHVTY KWQPNLDNPR DVRKSMELFV AKRQVYDEKR ALEHNSKLLR RAQMVDVKPI
ITAQPKKCAQ MWKEVADHNP THDFVYARFS EIKKQQPVKP VAISVNELVR KTLEIREKFP
VNVEFIGKRR KNTTKVSLKK VFNKTFLHCS TRHEDNQFKR IDTNITRDWI PVLSSVAKCY
ATLSSNXMHN VHKGHSGLTF IQNGELFIIR GRLRGELCNS LDYTTNIQEI EHYADPQAAD
FWRGYTNAYV ANRNISTTHT EHTPTINLEM CGKRMALLEV LFHSTFKITC KHCNTDDLEL
ADDEFGGKLY KNIQXIEEQQ SEYLAXDQKL KRMLSFIKAR CTPKFDHLPL NWQVADVIGH
YSDNQTKQIL DVNEALIKVN TLTPSDALKA SAALLELSRW YKNRKESAKX DNLSTFRNKI
SPKSTINLAL MCDNQLDSNG NFVWGKREYH AKRFFSNYFE AVDPTDAYEK HVTRFNPNGQ
RKLSIGKLVI PLDFQRIRDS FXGIPVTKQP LSNACLSRID KTYVYPCCCV TTEFGQPTYS
EXIPPTKGHL TIGNSVDPKI VDLPNTDPPT MYISKDGYCY INIFLAAMIN VNEDSAKDYT
KFIRDELIER LGKWPKLKNV ATACYALSVM FPEIKNAELP QILVDHENKT MHVVDSYGSL
SVGYHILKAN TVGQLIKMQY ESMESEMREY AVGGTITHKS FSTLISHLIK NMFKPHEMRK
XIEEEPFLIM LSVVSPTVLI ALYNNCHIEN AMXYWITKNQ GVAAMFAQLE ALAKETSKAE
LLIQQMTILE KASSQLKLAV MGLNHVDPAK RLLWSHLEVM SSRAXTNKEL LDQGYALYSD
RLYAIXEKTY VDQLNQAWAE LSLFGKFSET WRVYKDKKYY KPSLILRKSV DLGAVYNISA
THQISNLVQX SRSQXSSXLT KLHQSSCDRL HALRIXAINT IYWFIPDIFR LIHIFIILSL
LSXVANTIIX TMQDYKKLQK QVREEEYEKE XXEVRAIHAK LLKIHENDLT CEQFLQYIQE
NHPRLIEAAI ELSGVGVIHE GKSNLEINLE QAMAXGTLIT MIFDPTKSDA VYKVLNKMRT
ILSTVEQDAP FPRIDFTNIF RTQVTHQSLD LDDPLTIXTD KKXTVDFDTT QDLPADTFSN
DVTFDQWWSN QLEXNRTVPH YRLGGEFIEF TREKAASVSI XIAHSQIEKE YLLRGAVGSG
KSTGLPYHLS QRGKVLLLEP TRPLAENVCR QLQGAPFNVS PTLQMRGLSS FGSTPITIMT
SGFALHMYAN NPDKLSNYDF VIFDECHIME APAMAFYCLL KEYAFNGKII KVSATPPGRE
CEFSTQHPVD IHVCENLTQN QFVLELGTGS KADATKYGNN VLVYVASYND VDSLSRALIE
RHYSVIKVDG RTMKQNTNGI XPNGHDGKKC FIVATNIIEN GVTLDVDVVV DFGLKVTAEL
DVDNRAVMYR KVSISYGERI QRLGRVGRTK PGTVIRIGTT XKGLQEIPAM IATEAAFLCF
AYGLKVITHN VSTTHLSKCT VKQARTMMHF ELSPFIMSEL XKFDGSMHPQ IHEVLKKYKL
RESVIMLRPN AIPHTNVHNW LTVKDYNKIG CDLELDDYIK VPYFIRGIPE KVYSDIYKIV
LEYGSTSCYG RLSSACAGKV AYTLRTDPFA LPRTIAIVNQ LIAEEHAKRD HYNSITANPS
SSHAFSLAGI CNMLASRYMK DHSRENIEKL TRVKDQLIEF RGTGAEFKNP EDLLEFGGLV
TVIHQGLDSI AQCLQLKGRW NGDLIQRDLM ISAGVFTGGL LMLWFLFRKW STTDVKHEAK
TKRSRQKLKF RQARDNKYAY DVTGSKDAIE ENFGSAYVKK DKKKGTKVGL GVKQHKFYML
YNFDPQDYNL IRFVDPLTGA TLDEQLNADI KMVQEHFAEI REAAINNDQL EYQHIYSNPG
IKAYFIRNGS QNALKVDMTP HEPLRVVTGN NIAGFPEYEG TLRQTGKAQV VPLEQVPAPN
EVEVEHEAKS MLTGLVDYTP IANQICIIEN HSDDVRLCMY AIGYGSYLIT PAHLFKANNG
ELTFRSTRGV YKMRNSVEVK LHHVKGRDLV IIQLPKDFPP FPQKLKFQAP NRENKVCLIG
VNFQQNHSSC VISESSTIAP KGNNTFWSHW ISTTDGQCGL PLVDIKTRSI VGVHSLASVN
TNVNFFVSMP EDFNTYLGEL VSKNEWEKGW QYNPNLISWN GLNLVSSAPK GAFKTAKLVE
DLSFDVTEQG IQHETWLTKN IQQNLQVVAK CPGQLVTKHV VKGPCPHFAL YLSTHEEAEK
FFRPLMGKYD KSRLNKAAFV KDLTKYAKPT YIGEVNTDLF ERAVEHVIRI LRDVGIQTCE
YITDEDEIFK SLNMNAAVGA LYTGKKREYF SEYTQEDKAE IIKQSCERIY EGKLGIWNGS
LKAEIRPKEK TEANKTRTFT AAPLETLLAG KVCVDDFNGQ FYSQHLNGPW TVGITKFYGG
WNKLLEKLPD GWIYCDADGS QFDSSLTPYL INAVLNIRLQ FMEPWNIGEQ MLRNLYTEIV
FTPIATPDGS VIKKFKGNNS GQPSTVVDNT LMVIIAFNYT LLSCGVDLEK ADEVCRMYAN
GDDLLLAVNP THVNILDEFG KHFAALGLNF DFESRTRDKS ELWFMSTRGI KYEEMYIPKL
EKERIVAILE WDRSLLPQYR LEAICAAMVE AWGYKDLLHE IRKFYAWLLE MQPFSSLAKE
GSAPYIAESA LRNLYTGAKV SEDELNVYAR QFFDDLPSYL ADEVIDVKHQ AGENVDAGQK
TEAQKEAEKK AAEEKKADGG STGKDKDVDA GTSGSVSVPK LKAMSKKMRL PQAKGKNILH
LDFLLKYKPQ QQDLSNTRAT RAEFDRWYEA VQKEYELDDT QMTVVMSGLM VWCIENGCSP
NINGVWTMMD GDEQRTFPLK PVIENASPTF RQIMHHFSDA AEAYIEYRNS TEKYMPRYGL
QRNLTDFSLA RYAFDFYEIS SRTPARAKEA HMQMKAAAVR GSNTRMFGLD GNVGEAHENT
ERHTAGDVSR NMHSLLGVQQ GH
//
