PHOSP_PI1HB
ID PHOSP_PI1HB Reviewed; 568 AA.
AC P32530;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 02-JUN-2021, entry version 75.
DE RecName: Full=Phosphoprotein;
DE Short=Protein P;
GN Name=P/C;
OS Human parainfluenza 1 virus (strain C35) (HPIV-1).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC Respirovirus.
OX NCBI_TaxID=31605;
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; M74081; AAA46834.1; -; Genomic_RNA.
DR PIR; A40234; RRNZ35.
DR SMR; P32530; -.
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_0000142699"
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..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 113..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; 64671 MW; 2CDA4E170E5D2AB8 CRC64;
MDQDAFFFER DPEAEGEAPR KQESLSDVIG LLDVVLSYKP TEIGEDRSWL HGIIDNPKEN
KPSCKADDNN KDRAISTPTQ DHRSGEESGI SRRTSESKTE THARILDQQG IHRASRRGTS
PNPLPENMGN ERNTRIDEDS PNERRHQRSV LTDEDRKMAE DSNKREEDQV EGFPEEIRRS
TPLSDDGESR TNNNGRSMET SSTHSTRITD VIINPSPELE DAVLQRNKRR PTIIRRNQTR
SERTQNSELH KSTSENSSNL EDHNTKTSPK GPPPKNEESA 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