ID   L2MU_ADEG1              Reviewed;         188 AA.
AC   Q64756;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   23-FEB-2022, entry version 61.
DE   RecName: Full=Late L2 mu core protein;
DE   AltName: Full=Protein X;
DE            Short=pX;
DE   AltName: Full=pMu;
DE   Flags: Precursor;
GN   Name=PX;
OS   Fowl adenovirus A serotype 1 (strain CELO / Phelps) (FAdV-1) (Avian
OS   adenovirus gal1 (strain Phelps)).
OC   Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC   Rowavirales; Adenoviridae; Aviadenovirus; Fowl aviadenovirus A.
OX   NCBI_TaxID=10553;
OH   NCBI_TaxID=8976; Galliformes.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8634026; DOI=10.1007/bf01718405;
RA   Akopian T.A., Lazareva S.E., Tikhomirov E.E., Karpov V.A., Naroditsky B.S.;
RT   "Genes for fowl adenovirus CELO penton base and core polypeptides.";
RL   Arch. Virol. 141:357-365(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=8627769; DOI=10.1128/jvi.70.5.2939-2949.1996;
RA   Chiocca S., Kurzbauer R., Schaffner G., Baker A., Mautner V., Cotten M.;
RT   "The complete DNA sequence and genomic organization of the avian adenovirus
RT   CELO.";
RL   J. Virol. 70:2939-2949(1996).
CC   -!- FUNCTION: The role of the precursor might be to condense the viral
CC       prochromatin for encapsidation by virtue of the two basic domains.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the adenoviridae pX family. {ECO:0000305}.
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DR   EMBL; Z67970; CAA91904.1; -; Genomic_DNA.
DR   EMBL; U46933; AAC54910.1; -; Genomic_DNA.
DR   RefSeq; NP_043884.1; NC_001720.1.
DR   SMR; Q64756; -.
DR   GeneID; 1476561; -.
DR   Proteomes; UP000001594; Genome.
DR   GO; GO:0019013; C:viral nucleocapsid; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   InterPro; IPR008393; Adenovirus_late_L2_mu_core.
DR   Pfam; PF05829; Adeno_PX; 1.
PE   3: Inferred from homology;
KW   DNA-binding; Late protein; Reference proteome; Virion.
FT   PROPEP          1..128
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000036537"
FT   PEPTIDE         129..144
FT                   /note="Late L2 mu core protein"
FT                   /id="PRO_0000036538"
FT   PROPEP          145..188
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000036539"
FT   REGION          22..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        25..46
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            14..15
FT                   /note="Cleavage; by adenovirus protease"
FT                   /evidence="ECO:0000255"
FT   SITE            144..145
FT                   /note="Cleavage; by adenovirus protease"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   188 AA;  19789 MW;  B0FFF84FEAD0F55F CRC64;
     MCAVAIHRSD VVMPSVLLTG GRTAKGKKRA SRRRVKVPKL PKGARRKRAS VTPVPTVATA
     TASERAALTN LARRLQRGDY AAWRPADYTS PAVSEAARAA ASSGTPATAR DLATGTLARA
     VPMTGTGGRR RKRTATRRRS LKGGFLPALI PIIAAAIGAI PGIAGTAVGI ANLKEQQRQF
     NKIYGDKK