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[1]
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NUCLEOTIDE SEQUENCE [GENOMIC RNA].
DOI=10.1016/0042-6822(90)90356-V; PubMed=2219708 [NCBI, ExPASy, EBI, Israel, Japan]
Thornbury D.W.,
Patterson C.A.,
Dessens J.T.,
Pirone T.P.;
"Comparative sequence of the helper component (HC) region of potato virus Y and a HC-defective strain, potato virus C.";
Virology 178:573-578(1990).
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[2]
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FUNCTION OF HELPER COMPONENT PROTEINASE.
PubMed=9880030 [NCBI, ExPASy, EBI, Israel, Japan]
Blanc S.,
Ammar E.D.,
Garcia-Lampasona S.,
Dolja V.V.,
Llave C.,
Baker J.,
Pirone T.P.;
"Mutations in the potyvirus helper component protein: effects on interactions with virions and aphid stylets.";
J. Gen. Virol. 79:3119-3122(1998).
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[3]
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REVIEW.
DOI=10.1016/S0168-1702(01)00220-9; PubMed=11226583 [NCBI, ExPASy, EBI, Israel, Japan]
Urcuqui-Inchima S.,
Haenni A.L.,
Bernardi F.;
"Potyvirus proteins: a wealth of functions.";
Virus Res. 74:157-175(2001).
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- FUNCTION: HC is inactive with respect to its ability to effect aphid transmission of either PVC or PVY. Between the 2 amino acid changes which are specific to PVC-HC, the Lys to Glu-334 is more probably responsible of loss of binding to aphid stylet and thereby loss of aphid transmissibility. Displays proteolytic activity. Acts as a suppressor of RNA-mediated gene silencing, also known as post-transcriptional gene silencing (PTGS), a mechanism of plant viral defense that limits the accumulation of viral RNAs. May have RNA-binding activity (By similarity).
- CATALYTIC ACTIVITY: Hydrolyzes a Gly-|-Gly bond at its own C-terminus, commonly in the sequence -Tyr-Xaa-Val-Gly-|-Gly, in the processing of the potyviral polyprotein.
- DOMAIN: The N-terminus of helper component proteinase is involved in interaction with stylets. The central part is involved in interaction with virions and the C-terminus is involved in cell-to cell movement of the virus.
- PTM: The viral RNA of potyviruses is expressed as a single polyprotein which undergoes post-translational proteolytic processing by the main proteinase NIa-pro resulting in the production of at least ten individual proteins. The P1 proteinase and the HC-pro cleave only their respective C-termini autocatalytically (By similarity).
- SIMILARITY: Belongs to the potyviruses polyprotein family.
- SIMILARITY: Contains 1 peptidase C6 domain [view classification].
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Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms.
Distributed under the Creative Commons Attribution-NoDerivs License.
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| Length: 856 AA [This is the length of the partial sequence of the unprocessed precursor] |
Molecular weight: 96829 Da [This is the MW of the partial sequence of the unprocessed precursor] |
CRC64: 959EAE29BA0D60A8 [This is a checksum on the sequence] |
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10 20 30 40 50 60
MAIYMSTICF GSIECKLPYS PASCGHVTEE REVLASVEPF MDLEAQLSAR LLRQKHATVR
70 80 90 100 110 120
VLKNGTCAYR YKTDAQIVRI QKKLERKERD EYHFQMAAPS IVSKITIAGG DPPSKYEPQT
130 140 150 160 170 180
PKRVIHTTPR VRKVKKHSII KLTESQMNHL IKQVKRIMSA KKGSVHLINK KSTHVQYKEI
190 200 210 220 230 240
LGTTRAAVRT AHMMGLRRRV DFRCDMWTTE RLKCLARTDK WSNRVHTINI RKGDSGVILN
250 260 270 280 290 300
ADSLKGHFGR SSGGLFIVRG SHEGKLYDAR SKVTQGVLNS MVQFSNAENF WKGLDDNWAR
310 320 330 340 350 360
MRYPSDHTCI DGLPVEDCGR VAALMTHSIL PCYEITCPTC AQQYANLPAS DLFKLLHKHA
370 380 390 400 410 420
RDGLSRLGSD KDRFVHVNKF LVALEHLTEP VDLNLELFNE IFKSIGEKQQ APFKNLNVLN
430 440 450 460 470 480
NFFLKGKENT AHEWQVAQLS LLELARFQKN RTDNIKKGDI SFFRNKLSAK ANWNLYLSCD
490 500 510 520 530 540
NQLDKNANFL WGQREYHAKR FFSNFFEEVD PAKGYSAYEI RKHPNGTRKL SIGNLVVPLD
550 560 570 580 590 600
LAEFRQKMKG DYRKQPGVSK RCTSSKDGNY VYPCCCTTLD DGSAIESTFY PPTKKHLVIG
610 620 630 640 650 660
NSGDQKYVDL PKGDSEMLYI AKQGYCYINV FLAMLINVSE EDAKDFTKKV RDMCVPKLGT
670 680 690 700 710 720
WPTMMDLATT CAQMRIFYPD VHDAELPRIL VDHDTQTCHV VDSFGSQTTG YHILKASSVS
730 740 750 760 770 780
QLILFANDEL ESEIKHYRVG GVPNACPELG STISPFREGG VIMSESAALK LLLKGIFRPK
790 800 810 820 830 840
VMRQLLLDEP HLLILSILSP GILMAMYNNG IFELAVRLWI NEKQSIAMIA SLLSALALRV
850
SAAETLVAQR IIIDAA
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P22601 in FASTA format |
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