MyHits has reached its end of life and no longer provides data or services. Thank you for your support and trust for more than 23 years!
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
- MyHits
Description | RecName: Full=Genome polyprotein; Contains: RecName: Full=Nuclear inclusion protein B; Short=NI-B; Short=NIB; AltName: Full=RNA-directed RNA polymerase; EC=2.7.7.48; Contains: RecName: Full=Capsid protein; Short=CP; AltName: Full=Coat protein; Flags: Fragment; |
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MyHits synonyms | POLG_WMV2A , P20235 , D3AF006C844EB234 |
![]() Legends: 1, CHAIN Nuclear inclusion protein B. {ECO:0000250}; 2, SITE Cleavage; by NIa-pro. {ECO:0000250}.
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ID POLG_WMV2A Reviewed; 302 AA. AC P20235; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1991, sequence version 1. DT 07-SEP-2016, entry version 64. DE RecName: Full=Genome polyprotein; DE Contains: DE RecName: Full=Nuclear inclusion protein B; DE Short=NI-B; DE Short=NIB; DE AltName: Full=RNA-directed RNA polymerase; DE EC=2.7.7.48; DE Contains: DE RecName: Full=Capsid protein; DE Short=CP; DE AltName: Full=Coat protein; DE Flags: Fragment; OS Watermelon mosaic virus II (isolate Australia). OC Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage; OC Potyviridae; Potyvirus. OX NCBI_TaxID=148358; OH NCBI_TaxID=3654; Citrullus lanatus (Watermelon) (Citrullus vulgaris). OH NCBI_TaxID=3656; Cucumis melo (Muskmelon). OH NCBI_TaxID=3659; Cucumis sativus (Cucumber). OH NCBI_TaxID=3663; Cucurbita pepo (Vegetable marrow) (Summer squash). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RX PubMed=2794980; DOI=10.1099/0022-1317-70-10-2775; RA Frenkel M.J., Ward C.W., Shukla D.D.; RT "The use of 3' non-coding nucleotide sequences in the taxonomy of RT potyviruses: application to watermelon mosaic virus 2 and soybean RT mosaic virus-N."; RL J. Gen. Virol. 70:2775-2783(1989). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 22-302. RX PubMed=2719555; DOI=10.1007/BF01311116; RA Yu M.H., Frenkel M.J., McKern N.M., Shukla D.D., Strike P.M., RA Ward C.W.; RT "Coat protein of potyviruses. 6. Amino acid sequences suggest RT watermelon mosaic virus 2 and soybean mosaic virus-N are strains of RT the same potyvirus."; RL Arch. Virol. 105:55-64(1989). RN [3] RP REVIEW. RX PubMed=11226583; DOI=10.1016/S0168-1702(01)00220-9; RA Urcuqui-Inchima S., Haenni A.L., Bernardi F.; RT "Potyvirus proteins: a wealth of functions."; RL Virus Res. 74:157-175(2001). CC -!- FUNCTION: Capsid protein: involved in aphid transmission, cell-to- CC cell and systemis movement, encapsidation of the viral RNA and in CC the regulation of viral RNA amplification. CC -!- FUNCTION: Nuclear inclusion protein B: an RNA-dependent RNA CC polymerase that plays an essential role in the virus replication. CC -!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate CC + RNA(n+1). CC -!- SUBCELLULAR LOCATION: Capsid protein: Virion {ECO:0000305}. CC -!- PTM: Genome polyprotein of potyviruses undergoes post- CC translational proteolytic processing by the main proteinase NIa- CC pro resulting in the production of at least ten individual CC proteins. The P1 proteinase and the HC-pro cleave only their CC respective C-termini autocatalytically. 6K1 is essential for CC proper proteolytic separation of P3 from CI (By similarity). CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the potyviridae genome polyprotein family. CC {ECO:0000305}. DR EMBL; D00535; BAA00423.1; -; Genomic_RNA. DR PIR; PS0084; PS0084. DR ProteinModelPortal; P20235; -. DR GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW. DR GO; GO:0003968; F:RNA-directed RNA polymerase activity; IEA:UniProtKB-KW. DR InterPro; IPR001592; Poty_coat. DR Pfam; PF00767; Poty_coat; 1. PE 3: Inferred from homology; KW Capsid protein; Nucleotidyltransferase; RNA-directed RNA polymerase; KW Transferase; Virion. FT CHAIN <1 21 Nuclear inclusion protein B. FT {ECO:0000250}. FT /FTId=PRO_0000040493. FT CHAIN 1 302 Genome polyprotein. FT /FTId=PRO_0000420032. FT CHAIN 22 302 Capsid protein. {ECO:0000250}. FT /FTId=PRO_0000040494. FT SITE 21 22 Cleavage; by NIa-pro. {ECO:0000250}. FT NON_TER 1 1 CC -------------------------------------------------------------------------- CC The following FT lines are automated annotations from the MyHits database. CC -------------------------------------------------------------------------- FT MYHIT 67 297 ipfam:Poty_coat [T] SQ SEQUENCE 302 AA; 33860 MW; D3AF006C844EB234 CRC64; KYLEVLDFNH IDGCCESVSL QSGKEAVENL DTGKDSKKDT SGKGDKPQNS QTGQGSKEQT KIGTVSKDVN VGSKGKEVPR LQKITKKMNL PTVGGKIILS LDHLLEYKPN QVDLFNTRAT KTEFESWYSA VKIEYDLNDE QMGVIMNGFM VWCIDNGTSP DVNGVWVMMD GEEQVEYPLK PIVENAKPTL RQIMHHFSDA AEAYIEMRNS ESPYMPRYGL LRNLRDRELA RYAFDFYEVT SKTPNRAREA IAQMKAAALA GINSRLFGLD GNISTNSENT ERHTARDVNQ NMHTLLGMGP PQ // |