SPIK1_ADEG1
ID SPIK1_ADEG1 Reviewed; 710 AA.
AC Q64761;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 02-JUN-2021, entry version 89.
DE RecName: Full=Fiber protein 1;
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; AAC54917.1; -; Genomic_DNA.
DR RefSeq; NP_043891.1; NC_001720.1.
DR PDB; 2IUM; X-ray; 1.60 A; A/B/C=496-710.
DR PDB; 2IUN; X-ray; 2.80 A; A/B/C/D/E/F=496-710.
DR PDBsum; 2IUM; -.
DR PDBsum; 2IUN; -.
DR SMR; Q64761; -.
DR GeneID; 1476564; -.
DR KEGG; vg:1476564; -.
DR EvolutionaryTrace; Q64761; -.
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; IPR000939; Adenobir_fibre_prot_rpt/shaft.
DR InterPro; IPR031822; AdHead_fibreRBD.
DR InterPro; IPR009013; Attachment_protein_shaft_sf.
DR InterPro; IPR010537; Avian_adenovirus_fibre_N.
DR InterPro; IPR038486; Fiber_prot_C_sf.
DR Pfam; PF00608; Adeno_shaft; 3.
DR Pfam; PF16812; AdHead_fibreRBD; 1.
DR Pfam; PF06536; Av_adeno_fibre; 6.
DR SUPFAM; SSF51225; SSF51225; 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..710
FT /note="Fiber protein 1"
FT /id="PRO_0000221808"
FT STRAND 502..508
FT /evidence="ECO:0007829|PDB:2IUM"
FT STRAND 517..521
FT /evidence="ECO:0007829|PDB:2IUM"
FT TURN 522..524
FT /evidence="ECO:0007829|PDB:2IUM"
FT STRAND 525..538
FT /evidence="ECO:0007829|PDB:2IUM"
FT STRAND 541..551
FT /evidence="ECO:0007829|PDB:2IUM"
FT HELIX 552..554
FT /evidence="ECO:0007829|PDB:2IUM"
FT STRAND 557..559
FT /evidence="ECO:0007829|PDB:2IUM"
FT HELIX 561..564
FT /evidence="ECO:0007829|PDB:2IUM"
FT STRAND 566..572
FT /evidence="ECO:0007829|PDB:2IUM"
FT HELIX 574..577
FT /evidence="ECO:0007829|PDB:2IUM"
FT HELIX 580..582
FT /evidence="ECO:0007829|PDB:2IUM"
FT STRAND 590..594
FT /evidence="ECO:0007829|PDB:2IUM"
FT HELIX 599..602
FT /evidence="ECO:0007829|PDB:2IUM"
FT HELIX 606..609
FT /evidence="ECO:0007829|PDB:2IUM"
FT TURN 610..612
FT /evidence="ECO:0007829|PDB:2IUM"
FT HELIX 627..629
FT /evidence="ECO:0007829|PDB:2IUM"
FT STRAND 633..639
FT /evidence="ECO:0007829|PDB:2IUM"
FT HELIX 644..646
FT /evidence="ECO:0007829|PDB:2IUM"
FT STRAND 648..659
FT /evidence="ECO:0007829|PDB:2IUM"
FT STRAND 664..666
FT /evidence="ECO:0007829|PDB:2IUN"
FT STRAND 669..678
FT /evidence="ECO:0007829|PDB:2IUM"
FT STRAND 695..697
FT /evidence="ECO:0007829|PDB:2IUM"
FT STRAND 701..707
FT /evidence="ECO:0007829|PDB:2IUM"
SQ SEQUENCE 710 AA; 72928 MW; 5B1E603D5212416E CRC64;
MTSPLTLSQR ALALKTDSTL TLNTQGQLGV SLTPGDGLVL NTNGLSINAD PQTLAFNNSG
ALEVNLDPDG PWSKTATGID LRLDPTTLEV DNWELGVKLD PDEAIDSGPD GLCLNLDETL
LLATNSTSGK TELGVHLNTS GPITADDQGI DLDVDPNTMQ VNTGPSGGML AVKLKSGGGL
TADPDGISVT ATVAPPSISA TAPLTYTSGT IALTTDTQTM QVNSNQLAVK LKTGGGLTAD
ADGISVSVAP TPTISASPPL TYTNGQIGLS IGDQSLQVSS GQLQVKLKSQ GGIQQSTQGL
GVAVDQTLKI VSNTLEVNTD PSGPLTSGNN GLSLAAVTPL AVSSAGVTLN YQSPLTVTSN
SLGLSIAAPL QAGAQGLTVN TMEPLSASAQ GIQLHYGQGF QVVAGTLQLL TNPPIVVSSR
GFTLLYTPAF TVSNNMLGLN VDGTDCVAIS SAGLQIRKEA PLYVTSGSTP ALALKYSSDF
TITNGALALA NSGGGGSSTP EVATYHCGDN LLESYDIFAS LPNTNAAKVA AYCRLAAAGG
VVSGTIQVTS YAGRWPKVGN SVTDGIKFAI VVSPPMDKDP RSNLSQWLGA TVFPAGATTA
LFSPNPYGSL NTITTLPSIA SDWYVPESNL VTYTKIHFKP TGSQQLQLAS GELVVAAAKS
PVQTTKYELI YLGFTLKQNS SGTNFFDPNA SSDLSFLTPP IPFTYLGYYQ
