PHOSP_PI1HC
ID PHOSP_PI1HC Reviewed; 568 AA.
AC P28054;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 02-JUN-2021, entry version 74.
DE RecName: Full=Phosphoprotein;
DE Short=Protein P;
GN Name=P/C;
OS Human parainfluenza 1 virus (strain C39) (HPIV-1).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC Respirovirus.
OX NCBI_TaxID=11210;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1851888; DOI=10.1128/jvi.65.6.3406-3410.1991;
RA Matsuoka Y., Curran J., Pelet T., Kolakofsky D., Ray R., Compans R.W.;
RT "The P gene of human parainfluenza virus type 1 encodes P and C proteins
RT but not a cysteine-rich V protein.";
RL J. Virol. 65:3406-3410(1991).
CC -!- FUNCTION: This protein is probably a component of the active
CC polymerase. It may function in template binding.
CC -!- SIMILARITY: Belongs to the respirovirus P protein family.
CC {ECO:0000305}.
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; M37792; AAA46868.1; -; mRNA.
DR PIR; A39929; RRNZ39.
DR SMR; P28054; -.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:InterPro.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0019079; P:viral genome replication; IEA:InterPro.
DR Gene3D; 1.10.287.320; -; 1.
DR InterPro; IPR002693; Paramyxo_PProtein_C.
DR InterPro; IPR043097; PProtein_oligomer_dom1.
DR InterPro; IPR016075; RNA_pol_Pprot-P_XD_paramyxovir.
DR Pfam; PF01806; Paramyxo_P; 1.
DR SUPFAM; SSF101089; SSF101089; 1.
PE 2: Evidence at transcript level;
KW Phosphoprotein; Viral RNA replication.
FT CHAIN 1..568
FT /note="Phosphoprotein"
FT /id="PRO_0000142700"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 45..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 434..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..111
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..185
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..249
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..272
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..310
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 568 AA; 64660 MW; C5E3CE2B83AE197A CRC64;
MDQDAFFFER DPEAEGEAPR KQESLSGVIG LLDVVLSYKP TEIGEDRSWL HGIIDNPEEN
KPSCKADDNN KDRAISTPTQ DHRSGEESGI SRRTSESKTE THARLLDQQS IHRASRRGTS
PNPLPENMGN ERNTRIDEDS PNERRHQRSV LTDEDRKMAE DSNKREEDQV EGFPEEIRRS
TPLSDDGESR TNNNGRSMET SSTHSTRITD VIINPSPELE DAVLQRNKRR PTIIRRNQTR
SERTQNSELH KSTSENSSNL EDHNTKTSPK GLPPKNEESA ATPKNNHNHR KTKYTMNNAN
NNTKSPPTPE HDTTANEEET SNTSVDEMAK LLVSLGVMKS QHEFELSRSA SHVFAKRMLK
SANYKEMTFN LCGMLISVEK SLENKVEENR TLLKQIQEEI NSSRDLHKRF SEYQKEQNSL
MMANLSTLHI ITDRGGKTGD PSDTTRSPSV FTKGKDNKVK KTRFDPSMEA LGGQEFKPDL
IREDELRDDI KNPVLEENNN DLQASNASRL IPSTEKHTLH SLKLVIENSP LSRVEKKAYI
KSLYKCRTNQ EVKNVMELFE EDIDSLTN