ID   SPIK2_ADEG1             Reviewed;         410 AA.
AC   Q64762;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   02-JUN-2021, entry version 79.
DE   RecName: Full=Fiber protein 2;
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 [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: Forms spikes that protrude from each vertex of the
CC       icosahedral capsid. Interacts with host receptor to provide virion
CC       initial attachment to target cell. Fiber proteins are shed during virus
CC       entry, when virus is still at the cell surface (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Homotrimer. Interacts (via N-terminal tail region) with
CC       pentons (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000250}. Host nucleus {ECO:0000250}.
CC       Note=Anchored to the pentons, protrudes from the virion surface.
CC       {ECO:0000250}.
CC   -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC   -!- DOMAIN: The tail region anchors the fiber to penton base capsomers,
CC       whereas the shaft, built from several repeated motifs, allows the knob
CC       to protrude from the virion. {ECO:0000250}.
CC   -!- MISCELLANEOUS: All late proteins expressed from the major late promoter
CC       are produced by alternative splicing and alternative polyadenylation of
CC       the same gene giving rise to non-overlapping ORFs. A leader sequence is
CC       present in the N-terminus of all these mRNAs and is recognized by the
CC       viral shutoff protein to provide expression although conventional
CC       translation via ribosome scanning from the cap has been shut off in the
CC       host cell (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the adenoviridae fiber family. {ECO:0000305}.
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DR   EMBL; U46933; AAC54918.1; -; Genomic_DNA.
DR   RefSeq; NP_043892.1; NC_001720.1.
DR   PDB; 2VTW; X-ray; 2.00 A; A/B/C/D/E/F=206-410.
DR   PDBsum; 2VTW; -.
DR   SMR; Q64762; -.
DR   GeneID; 1476564; -.
DR   EvolutionaryTrace; Q64762; -.
DR   Proteomes; UP000001594; Genome.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
DR   GO; GO:0098671; P:adhesion receptor-mediated virion attachment to host cell; IEA:UniProtKB-KW.
DR   GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.90.30; -; 1.
DR   InterPro; IPR031822; AdHead_fibreRBD.
DR   InterPro; IPR010537; Avian_adenovirus_fibre_N.
DR   InterPro; IPR038486; Fiber_prot_C_sf.
DR   Pfam; PF16812; AdHead_fibreRBD; 1.
DR   Pfam; PF06536; Av_adeno_fibre; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Capsid protein; Host nucleus; Host-virus interaction;
KW   Late protein; Reference proteome;
KW   Viral attachment to host adhesion receptor; Viral attachment to host cell;
KW   Virion; Virus entry into host cell.
FT   CHAIN           1..410
FT                   /note="Fiber protein 2"
FT                   /id="PRO_0000221809"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   STRAND          208..215
FT                   /evidence="ECO:0007829|PDB:2VTW"
FT   STRAND          224..228
FT                   /evidence="ECO:0007829|PDB:2VTW"
FT   STRAND          233..245
FT                   /evidence="ECO:0007829|PDB:2VTW"
FT   STRAND          248..258
FT                   /evidence="ECO:0007829|PDB:2VTW"
FT   TURN            259..261
FT                   /evidence="ECO:0007829|PDB:2VTW"
FT   HELIX           269..272
FT                   /evidence="ECO:0007829|PDB:2VTW"
FT   STRAND          276..281
FT                   /evidence="ECO:0007829|PDB:2VTW"
FT   TURN            285..287
FT                   /evidence="ECO:0007829|PDB:2VTW"
FT   STRAND          297..300
FT                   /evidence="ECO:0007829|PDB:2VTW"
FT   HELIX           305..308
FT                   /evidence="ECO:0007829|PDB:2VTW"
FT   HELIX           322..324
FT                   /evidence="ECO:0007829|PDB:2VTW"
FT   STRAND          333..340
FT                   /evidence="ECO:0007829|PDB:2VTW"
FT   STRAND          342..345
FT                   /evidence="ECO:0007829|PDB:2VTW"
FT   STRAND          352..362
FT                   /evidence="ECO:0007829|PDB:2VTW"
FT   STRAND          368..381
FT                   /evidence="ECO:0007829|PDB:2VTW"
FT   STRAND          390..406
FT                   /evidence="ECO:0007829|PDB:2VTW"
SQ   SEQUENCE   410 AA;  42942 MW;  154ABBA7A8AE8AF4 CRC64;
     MADQKRKLAD PDAEAPTGKM ARAGPGELDL VYPFWYQVAA PTEITPPFLD PNGPLYSTDG
     LLNVRLTAPL VIIRQSNGNA IGVKTDGSIT VNADGALQIG ISTAGPLTTT ANGIDLNIDP
     KTLVVDGSSG KNVLGVLLKG QGALQSSAQG IGVAVDESLQ IVDNTLEVKV DAAGPLAVTA
     AGVGLQYDNT QFKVTNGTLQ LYQAPTSSVA AFTSGTIGLS SPTGNFVSSS NNPFNGSYFL
     QQINTMGMLT TSLYVKVDTT TMGTRPTGAV NENARYFTVW VSSFLTQCNP SNIGQGTLEP
     SNISMTSFEP ARNPISPPVF NMNQNIPYYA SRFGVLESYR PIFTGSLNTG SIDVRMQVTP
     VLATNNTTYN LIAFTFQCAS AGLFNPTVNG TVAIGPVVHT CPAARAPVTV