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PHOSP_HENDH
ID   PHOSP_HENDH             Reviewed;         707 AA.
AC   O55778; O89340; Q66759;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 2.
DT   02-JUN-2021, entry version 78.
DE   RecName: Full=Phosphoprotein;
DE            Short=Protein P;
GN   Name=P/V/C;
OS   Hendra virus (isolate Horse/Autralia/Hendra/1994).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC   Henipavirus.
OX   NCBI_TaxID=928303;
OH   NCBI_TaxID=9796; Equus caballus (Horse).
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=9402; Pteropus alecto (Black flying fox).
OH   NCBI_TaxID=9403; Pteropus poliocephalus (Grey-headed flying fox).
OH   NCBI_TaxID=94117; Pteropus scapulatus (Little red flying fox).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 402-707.
RX   PubMed=8822631; DOI=10.1016/0168-1702(96)01308-1;
RA   Gould A.R.;
RT   "Comparison of the deduced matrix and fusion protein sequences of equine
RT   morbillivirus with cognate genes of the Paramyxoviridae.";
RL   Virus Res. 43:17-31(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9445051; DOI=10.1128/jvi.72.2.1482-1490.1998;
RA   Wang L.-F., Michalski W.P., Yu M., Pritchard L.I., Crameri G., Shiell B.,
RA   Eaton B.T.;
RT   "A novel P/V/C gene in a new member of the Paramyxoviridae family, which
RT   causes lethal infection in humans, horses, and other animals.";
RL   J. Virol. 72:1482-1490(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=11024125; DOI=10.1128/jvi.74.21.9972-9979.2000;
RA   Wang L.-F., Yu M., Hansson E., Pritchard L.I., Shiell B., Michalski W.P.,
RA   Eaton B.T.;
RT   "The exceptionally large genome of Hendra virus: support for creation of a
RT   new genus within the family Paramyxoviridae.";
RL   J. Virol. 74:9972-9979(2000).
CC   -!- FUNCTION: Essential component of the RNA polymerase transcription and
CC       replication complex. Binds the viral ribonucleocapsid and positions the
CC       L polymerase on the template (By similarity). {ECO:0000250}.
CC   -!- RNA EDITING: Modified_positions=407; Note=Partially edited. RNA editing
CC       at this position consists of an insertion of one or two guanine
CC       nucleotides. The sequence displayed here is the P protein, derived from
CC       the unedited RNA. The edited RNA gives rise to the V protein (+1G) (AC
CC       O55777), and the W protein (+2G) (AC P0C1C6).;
CC   -!- MISCELLANEOUS: The P/V/C gene has two overlapping open reading frames.
CC       One encodes the P/V/W proteins and the other the C protein.
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DR   EMBL; U49404; AAB39503.1; -; Genomic_RNA.
DR   EMBL; AF010304; AAC04240.1; -; mRNA.
DR   EMBL; AF017149; AAC83188.2; -; Genomic_RNA.
DR   PIR; T08207; T08207.
DR   RefSeq; NP_047107.2; NC_001906.3.
DR   PDB; 4HEO; X-ray; 1.65 A; A/B=654-707.
DR   PDB; 6ILG; X-ray; 2.60 A; C=481-487.
DR   PDB; 6J2D; X-ray; 2.31 A; C=481-488.
DR   PDB; 6J2H; X-ray; 2.30 A; C/F=481-488.
DR   PDB; 6K7T; X-ray; 1.60 A; C=481-488.
DR   PDBsum; 4HEO; -.
DR   PDBsum; 6ILG; -.
DR   PDBsum; 6J2D; -.
DR   PDBsum; 6J2H; -.
DR   PDBsum; 6K7T; -.
DR   SMR; O55778; -.
DR   GeneID; 1446469; -.
DR   KEGG; vg:1446469; -.
DR   Proteomes; UP000008771; Genome.
DR   GO; GO:0032991; C:protein-containing complex; IDA:CAFA.
DR   GO; GO:0097718; F:disordered domain specific binding; IPI:CAFA.
DR   DisProt; DP00700; -.
DR   InterPro; IPR004897; P/V_Pprotein_paramyxoviral.
DR   InterPro; IPR028243; Paramyxo_P/V_N.
DR   InterPro; IPR035430; Paramyxo_PNT.
DR   InterPro; IPR025909; Soyouz_module.
DR   Pfam; PF03210; Paramyx_P_V_C; 1.
DR   Pfam; PF13825; Paramyxo_P_V_N; 1.
DR   Pfam; PF14320; Paramyxo_PNT; 1.
DR   Pfam; PF14313; Soyouz_module; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Coiled coil; Phosphoprotein; Reference proteome; RNA editing;
KW   Viral RNA replication.
FT   CHAIN           1..707
FT                   /note="Phosphoprotein"
FT                   /id="PRO_0000236012"
FT   REGION          26..103
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          193..229
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          254..446
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          454..473
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          558..590
FT                   /note="L protein binding"
FT                   /evidence="ECO:0000250"
FT   COILED          496..574
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        73..94
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        293..314
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        340..354
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        360..377
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         257
FT                   /note="Phosphoserine; by host"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         350
FT                   /note="Phosphoserine; by host"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        408
FT                   /note="A -> V (in Ref. 1; AAB39503)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        474..485
FT                   /note="KYIMPSDDFANT -> NILCHQMILLTL (in Ref. 1; AAB39503)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        574
FT                   /note="I -> M (in Ref. 1; AAB39503)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        688..707
FT                   /note="TDEEVQEVANTVNDIIDGNI -> QMKRFRRWPIQSMILLMGTSKHVSNLIE
FT                   (in Ref. 1; AAB39503)"
FT                   /evidence="ECO:0000305"
FT   HELIX           656..669
FT                   /evidence="ECO:0007829|PDB:4HEO"
FT   HELIX           673..685
FT                   /evidence="ECO:0007829|PDB:4HEO"
FT   HELIX           689..703
FT                   /evidence="ECO:0007829|PDB:4HEO"
SQ   SEQUENCE   707 AA;  78306 MW;  7E8B7E69892C0787 CRC64;
     MDKLDLVNDG LDIIDFIQKN QKEIQKTYGR SSIQQPSTKD RTRAWEDFLQ STSGEHEQAE
     GGMPKNDGGT EGRNVEDLSS VTSSDGTIGQ RVSNTRAWAE DPDDIQLDPM VTDVVYHDHG
     GECTGHGPSS SPERGWSYHM SGTHDGNVRA VPDTKVLPNA PKTTVPEEVR EIDLIGLEDK
     FASAGLNPAA VPFVPKNQST PTEEPPVIPE YYYGSGRRGD LSKSPPRGNV NLDSIKIYTS
     DDEDENQLEY EDEFAKSSSE VVIDTTPEDN DSINQEEVVG DPSDQGLEHP FPLGKFPEKE
     ETPDVRRKDS LMQDSCKRGG VPKRLPMLSE EFECSGSDDP IIQELEREGS HPGGSLRLRE
     PPQSSGNSRN QPDRQLKTGD AASPGGVQRP GTPMPKSRIM PIKKGTDAKS QYVGTEDVPG
     SKSGATRYVR GLPPNQESKS VTAENVQLSA PSAVTRNEGH DQEVTSNEDS LDDKYIMPSD
     DFANTFLPHD TDRLNYHADH LNDYDLETLC EESVLMGIVN AIKLINIDMR LNHIEEQMKE
     IPKIINKIDS IDRVLAKTNT ALSTIEGHLV SMMIMIPGKG KGERKGKTNP ELKPVIGRNI
     LEQQELFSFD NLKNFRDGSL TDEPYGGVAR IRDDLILPEL NFSETNASQF VPLADDASKD
     VVRTMIRTHI KDRELRSELM DYLNRAETDE EVQEVANTVN DIIDGNI
 
 
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