CAPSD_HPBVH
ID CAPSD_HPBVH Reviewed; 552 AA.
AC Q50LE5;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 34.
DE RecName: Full=Capsid protein precursor;
DE Contains:
DE RecName: Full=7 kDa polypeptide;
DE Contains:
DE RecName: Full=Capsid protein;
DE Short=CP;
GN Name=Segment-1; ORFNames=ORF2;
OS Human picobirnavirus (strain Human/Thailand/Hy005102/-) (PBV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Duplopiviricetes;
OC Durnavirales; Picobirnaviridae; Picobirnavirus.
OX NCBI_TaxID=647332;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=15847933; DOI=10.1016/j.jviromet.2005.02.010;
RA Wakuda M., Pongsuwanna Y., Taniguchi K.;
RT "Complete nucleotide sequences of two RNA segments of human
RT picobirnavirus.";
RL J. Virol. Methods 126:165-169(2005).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF CAPSID SHELL, FUNCTION,
RP SUBCELLULAR LOCATION, AUTOCATALYTIC CLEAVAGE, AND PROBABLE ACETYLATION.
RX PubMed=19407816; DOI=10.1038/emboj.2009.109;
RA Duquerroy S., Da Costa B., Henry C., Vigouroux A., Libersou S., Lepault J.,
RA Navaza J., Delmas B., Rey F.A.;
RT "The picobirnavirus crystal structure provides functional insights into
RT virion assembly and cell entry.";
RL EMBO J. 28:1655-1665(2009).
CC -!- FUNCTION: The capsid protein self-assembles to form an icosahedral
CC capsid with a T=2 symmetry made of 120 subunits.
CC {ECO:0000269|PubMed:19407816}.
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: [Capsid protein]: Virion
CC {ECO:0000269|PubMed:19407816}.
CC -!- SUBCELLULAR LOCATION: [7 kDa polypeptide]: Virion
CC {ECO:0000269|PubMed:19407816}.
CC -!- PTM: The 7 kDa polypeptide is acetylated.
CC {ECO:0000269|PubMed:19407816}.
CC -!- PTM: Autocatalytic proteolysis releases a post-translationally modified
CC peptide that remains associated with nucleic acid within the virion.
CC This peptide is observed only when nucleic acid is packaged in the
CC capsid. {ECO:0000269|PubMed:19407816}.
CC -!- MISCELLANEOUS: Picobirnavirus particles are capable of disrupting
CC biological membranes in vitro.
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DR EMBL; AB186897; BAD98235.1; -; Genomic_RNA.
DR RefSeq; YP_239360.1; NC_007026.1.
DR PDB; 6Z8D; EM; 2.63 A; A/B=1-552.
DR PDB; 6Z8E; EM; 2.80 A; A/B=1-552.
DR PDB; 6Z8F; EM; 2.80 A; A/B=41-552.
DR PDBsum; 6Z8D; -.
DR PDBsum; 6Z8E; -.
DR PDBsum; 6Z8F; -.
DR SMR; Q50LE5; -.
DR MEROPS; N05.001; -.
DR GeneID; 5075907; -.
DR KEGG; vg:5075907; -.
DR Proteomes; UP000007252; Genome.
DR GO; GO:0039617; C:T=3 icosahedral viral capsid; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Capsid protein; Reference proteome;
KW T=3 icosahedral capsid protein; Virion.
FT CHAIN 1..552
FT /note="Capsid protein precursor"
FT /id="PRO_0000379521"
FT CHAIN 1..65
FT /note="7 kDa polypeptide"
FT /id="PRO_0000379522"
FT CHAIN 66..552
FT /note="Capsid protein"
FT /id="PRO_0000379523"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 65..66
FT /note="Cleavage"
FT HELIX 49..52
FT /evidence="ECO:0007829|PDB:6Z8D"
FT HELIX 54..60
FT /evidence="ECO:0007829|PDB:6Z8D"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:6Z8D"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:6Z8D"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:6Z8D"
FT TURN 86..88
FT /evidence="ECO:0007829|PDB:6Z8D"
FT STRAND 98..105
FT /evidence="ECO:0007829|PDB:6Z8D"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:6Z8D"
FT HELIX 116..129
FT /evidence="ECO:0007829|PDB:6Z8D"
FT HELIX 140..166
FT /evidence="ECO:0007829|PDB:6Z8D"
FT TURN 175..178
FT /evidence="ECO:0007829|PDB:6Z8D"
FT HELIX 179..184
FT /evidence="ECO:0007829|PDB:6Z8D"
FT HELIX 189..194
FT /evidence="ECO:0007829|PDB:6Z8D"
FT HELIX 196..210
FT /evidence="ECO:0007829|PDB:6Z8D"
FT STRAND 216..219
FT /evidence="ECO:0007829|PDB:6Z8E"
FT HELIX 220..229
FT /evidence="ECO:0007829|PDB:6Z8D"
FT STRAND 232..238
FT /evidence="ECO:0007829|PDB:6Z8D"
FT STRAND 243..253
FT /evidence="ECO:0007829|PDB:6Z8D"
FT STRAND 256..258
FT /evidence="ECO:0007829|PDB:6Z8D"
FT STRAND 261..268
FT /evidence="ECO:0007829|PDB:6Z8D"
FT HELIX 278..288
FT /evidence="ECO:0007829|PDB:6Z8D"
FT TURN 290..292
FT /evidence="ECO:0007829|PDB:6Z8D"
FT HELIX 296..308
FT /evidence="ECO:0007829|PDB:6Z8D"
FT HELIX 311..313
FT /evidence="ECO:0007829|PDB:6Z8D"
FT HELIX 332..339
FT /evidence="ECO:0007829|PDB:6Z8D"
FT STRAND 364..366
FT /evidence="ECO:0007829|PDB:6Z8D"
FT HELIX 371..373
FT /evidence="ECO:0007829|PDB:6Z8D"
FT STRAND 385..388
FT /evidence="ECO:0007829|PDB:6Z8D"
FT HELIX 391..397
FT /evidence="ECO:0007829|PDB:6Z8D"
FT STRAND 401..407
FT /evidence="ECO:0007829|PDB:6Z8D"
FT HELIX 411..416
FT /evidence="ECO:0007829|PDB:6Z8D"
FT TURN 417..420
FT /evidence="ECO:0007829|PDB:6Z8E"
FT STRAND 424..427
FT /evidence="ECO:0007829|PDB:6Z8D"
FT STRAND 431..433
FT /evidence="ECO:0007829|PDB:6Z8D"
FT STRAND 440..443
FT /evidence="ECO:0007829|PDB:6Z8D"
FT STRAND 447..458
FT /evidence="ECO:0007829|PDB:6Z8D"
FT STRAND 460..463
FT /evidence="ECO:0007829|PDB:6Z8F"
FT STRAND 466..471
FT /evidence="ECO:0007829|PDB:6Z8D"
FT STRAND 473..477
FT /evidence="ECO:0007829|PDB:6Z8D"
FT STRAND 479..481
FT /evidence="ECO:0007829|PDB:6Z8D"
FT HELIX 482..494
FT /evidence="ECO:0007829|PDB:6Z8D"
FT STRAND 503..507
FT /evidence="ECO:0007829|PDB:6Z8D"
FT TURN 508..511
FT /evidence="ECO:0007829|PDB:6Z8D"
FT STRAND 512..518
FT /evidence="ECO:0007829|PDB:6Z8D"
FT STRAND 521..525
FT /evidence="ECO:0007829|PDB:6Z8D"
FT HELIX 528..542
FT /evidence="ECO:0007829|PDB:6Z8D"
SQ SEQUENCE 552 AA; 62029 MW; F6D977879662A99C CRC64;
MKQNDTKKTT QRRNSKKYSS KTNRGTKRAP RDQEVGTGAQ ESTRNDVAWY ARYPHILEEA
TRLPFAYPIG QYYDTGYSVA SATEWSKYVD TSLTIPGVMC VNFTPTPGES YNKNSPINIA
AQNVYTYVRH MNSGHANYEQ ADLMMYLLAM DSLYIFHSYV RKILAISKLY TPVNKYFPRA
LLVALGVDPE DVFANQAQWE YFVNMVAYRA GAFAAPASMT YYERHAWMSN GLYVDQDVTR
AQIYMFKPTM LWKYENLGTT GTKLVPLMMP KAGDNRKLVD FQVLFNNLVS TMLGDEDFGI
MSGDVFKAFG ADGLVKLLAV DSTTMTLPTY DPLILAQIHS ARAVGAPILE TSTLTGFPGR
QWQITQNPDV NNGAIIFHPS FGYDGQDHEE LSFRAMCSNM ILNLPGEAHS AEMIIEATRL
ATMFQVKAVP AGDTSKPVLY LPNGFGTEVV NDYTMISVDK ATPHDLTIHT FFNNILVPNA
KENYVANLEL LNNIIQFDWA PQLYLTYGIA QESFGPFAQL NDWTILTGET LARMHEVCVT
SMFDVPQMGF NK
