NCAP_TPMV
ID NCAP_TPMV Reviewed; 552 AA.
AC Q9WS40;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 02-JUN-2021, entry version 73.
DE RecName: Full=Nucleoprotein;
DE AltName: Full=Nucleocapsid protein;
DE Short=NP;
DE Short=Protein N;
GN Name=N; Synonyms=Np;
OS Tupaia paramyxovirus (TPMV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC Narmovirus; Tupaia narmovirus.
OX NCBI_TaxID=92129;
OH NCBI_TaxID=37347; Tupaia belangeri (Common tree shrew) (Tupaia glis belangeri).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=10366580; DOI=10.1006/viro.1999.9693;
RA Tidona C.A., Kurz H.W., Gelderblom H.R., Darai G.;
RT "Isolation and molecular characterization of a novel cytopathogenic
RT paramyxovirus from tree shrews.";
RL Virology 258:425-434(1999).
CC -!- FUNCTION: Encapsidates the genome, protecting it from nucleases. The
CC nucleocapsid (NC) has a helical structure. The encapsidated genomic RNA
CC is termed the NC and serves as template for transcription and
CC replication. During replication, encapsidation by N is coupled to RNA
CC synthesis and all replicative products are resistant to nucleases.
CC -!- SUBUNIT: Homomultimerizes to form the nucleocapsid. Binds to viral
CC genomic RNA. In nucleocapsid, binds the P protein and thereby positions
CC the polymerase on the template (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}. Host cytoplasm
CC {ECO:0000250}.
CC -!- DOMAIN: Ncore is globular and carries regions required for N self-
CC assembly and RNA-binding. Ntail is an intrinsically disordered
CC monomeric domain (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the paramyxoviruses nucleocapsid family.
CC {ECO:0000305}.
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DR EMBL; AF079780; AAD28694.1; -; Genomic_RNA.
DR RefSeq; NP_054690.1; NC_002199.1.
DR SMR; Q9WS40; -.
DR GeneID; 1452635; -.
DR KEGG; vg:1452635; -.
DR Proteomes; UP000136220; Genome.
DR GO; GO:0019029; C:helical viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR InterPro; IPR002021; Paramyx_ncap.
DR Pfam; PF00973; Paramyxo_ncap; 1.
PE 3: Inferred from homology;
KW Capsid protein; Helical capsid protein; Host cytoplasm; Reference proteome;
KW Ribonucleoprotein; RNA-binding; Viral nucleoprotein; Virion.
FT CHAIN 1..552
FT /note="Nucleoprotein"
FT /id="PRO_0000142687"
FT REGION 1..400
FT /note="Ncore"
FT /evidence="ECO:0000250"
FT REGION 401..552
FT /note="Ntail"
FT /evidence="ECO:0000250"
FT REGION 423..552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..447
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..485
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 526..552
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 552 AA; 61516 MW; E471D28B9F277063 CRC64;
MADLFSKVND FQKYRTNLGR QGGLTVKLVG VRSTVVVLVP STKDHRLRWK LIRLLTLAVY
NDSLPDSISI GALLSLLAIS FEQPAAVIRG LLSDPDLEVQ MIEVSLDDQG EIRFAARGDI
LTRYKDAYFE KIRDFPNPDD DLAIFEDPEL GDYSDITQDE YQAMITTITI QLWILLTKAV
TAPDTAHDSE QRRFIKYLQQ RKAYAAFKFT TIFTERVRRK IAQSLSIRKF MVSIMLEVRK
SGSAKGRISE CIADVSAYIE EAGLSGFILT LKYGIGTRFP VLALNAFQSD LSVIRNLIDL
YKSMGTIAPF MVLIEDATQV KFAPGNYSLL WSFAMGVGTA LDHAMNNLNI NRDYLEPSYF
RLGQEVVRLS ESTVDRSMAQ ELGIDPTSED LIMRAVQAAG VGSRDPDAAR RTGRFQVADI
QIDEGPVDLA TEAEDQTTKD NEQRIKVPDP RGSIGQSNAQ FQPPKPQLRG RVMPPERKPT
DQQKNLQDQR PRPSATPRRL TKDAEDNIDQ LFAQYDSGVA APEDVTLVTS DSTSPARSSG
TGSDMDLINQ SP