PHOSP_PI1HD
ID PHOSP_PI1HD Reviewed; 568 AA.
AC P32531;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Phosphoprotein;
DE Short=Protein P;
GN Name=P/C;
OS Human parainfluenza 1 virus (strain CI-5/73) (HPIV-1).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC Respirovirus.
OX NCBI_TaxID=31607;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=1318610; DOI=10.1016/0042-6822(92)90712-x;
RA Power U.F., Ryan K.W., Portner A.;
RT "The P genes of human parainfluenza virus type 1 clinical isolates are
RT polycistronic and microheterogeneous.";
RL Virology 189:340-343(1992).
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}.
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DR EMBL; M74082; AAA46838.1; -; Genomic_RNA.
DR SMR; P32531; -.
DR PRIDE; P32531; -.
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 3: Inferred from homology;
KW Phosphoprotein; Viral RNA replication.
FT CHAIN 1..568
FT /note="Phosphoprotein"
FT /id="PRO_0000142701"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 55..322
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 REGION 494..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..111
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..193
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..213
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..263
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..281
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..513
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 568 AA; 64644 MW; FACC2D694E9ACE0C CRC64;
MDQDAFFSER DPEAEGETPR KQESLSDVIG LLDVVLSYKP TEIGEDRSWL HSIIDNSKEN
KPSCKADDNN KDRAISTPTQ DHRSSEESGI SRRTGESKTE THARILDQQG IHRASRRGTS
PNPLPENMGN ERNTRIDEDS PNERRHQRSV PTDEDRKMAE NSNKREEDQV EGFPEEVRRG
TPLSDDREGR TNNNGRSMET SSTHSTRITD VITNPSPELE DAVLQRNKRR PTTIKRSQTR
SERTQNSELH KSTSEDSSNL EDHNTKTSPK VLPSKNEESV ATQKNNHNHR KTKYTTNNAN
NNTKSLPTPE HDTTANEEGT SNTSVDEMAK LLVSLGVIKS QHEFELSRSA SHVFAKRMLK
SANYKEMTFN LCGMLLSVEK SLENKVEENR TLLKQIQEEI DSSRDLHKRF SEYQKEQNSL
MMANLSTLHI ITDRGGKTGD PSDTTRSPSV FTKGKDNKVK KTRFDPSMEA LGGQEFKPDL
IREDELRDDI RNPVLEEHNN EPQASNASRL IPSTEKHTLH SLKLVIENSP LSRVEKKAYI
KSLYKCRTNQ EVKNVMELFE EDIDSLTN