PHOSP_PI1HE
ID PHOSP_PI1HE Reviewed; 568 AA.
AC P32532;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Phosphoprotein;
DE Short=Protein P;
GN Name=P/C;
OS Human parainfluenza 1 virus (strain CI-14/83) (HPIV-1).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC Respirovirus.
OX NCBI_TaxID=31606;
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; M74080; AAA46830.1; -; Genomic_RNA.
DR PIR; E40234; RRNZ83.
DR SMR; P32532; -.
DR PRIDE; P32532; -.
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_0000142702"
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 REGION 493..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 45..111
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..174
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..213
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..281
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..324
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; 64586 MW; 8795D10C1CD3CCD7 CRC64;
MDQDAFFFER DPEAEGEAPR KQESLSDVIG LLDVVLSYKP TEIGEDRSWL HNIIDNPKEN
KSSCKSDDNN KDRAISTSTQ DHRSSEESGI SRRTGESKTE THARILDQQG IHRASRRGTS
PNPLPENMGD ERNTRIDEDS PNERRHQRSV PTDEDRKMAE NSNKREEDQV EGFPEEVRGS
TSLSDDGEGR TNNNGRSMET SSTHSTRITD VITNPSPELE EAVLQRKKRR PTTIKRNQTR
SERTQNSELH KSTSGDSSNL EDHNTKTSQK IPPSKNEEPA VTQKNNHNHR KTKHTTNNAN
NNAKCLPTPE HDTTSNEEGT SNTSVDEMAK LLVSLGVMKS QHEFELSRRA SHQFAKRMLK
SANYKEMTFN LCGMLLSVEK SLGNKVEENR TLLKQIQEEI DSSRDLHKRF SEYQKEQNSL
MMANLSTLHI ITDRGGKTGD PSDTTRSPSV FTKGKDNKVK KTRFDPSMEA LGGQEFKPDL
IREDELREDI RNPVLEEHNN EPQASNASRL IPSTEKHTLH SLKLVIENSP LSRVEKKAYI
KSLYKCRTNQ EVKNVMELFE EDIDSLTN