ID H9AAW3_9ADEN Unreviewed; 366 AA.
AC H9AAW3;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 08-NOV-2023, entry version 27.
DE RecName: Full=Core-capsid bridging protein {ECO:0000256|HAMAP-Rule:MF_04053};
DE AltName: Full=Core protein V {ECO:0000256|HAMAP-Rule:MF_04053};
GN Name=L2 {ECO:0000256|HAMAP-Rule:MF_04053};
OS Simian adenovirus A1327.
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Rowavirales; Adenoviridae; Mastadenovirus; Simian adenovirus B.
OX NCBI_TaxID=1159193 {ECO:0000313|EMBL:AFD22107.1, ECO:0000313|Proteomes:UP000167733};
RN [1] {ECO:0000313|EMBL:AFD22107.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A1327 {ECO:0000313|EMBL:AFD22107.1};
RX PubMed=22709783; DOI=10.3201/eid1807.111665;
RA Roy S., Sandhu A., Medina A., Clawson D.S., Wilson J.M.;
RT "Adenoviruses in fecal samples from asymptomatic rhesus macaques, United
RT States.";
RL Emerg. Infect. Dis. 18:1081-1088(2012).
CC -!- FUNCTION: Associates loosely with the viral DNA to form an outer shell
CC around the nucleoprotein-DNA complex and links it with the capsid by
CC binding the endosome lysis protein. Dissociates from the viral genome
CC during entry. Might be involved in nuclear capsid assembly of the viral
CC particles through its association with NPM1/nucleophosmin.
CC {ECO:0000256|HAMAP-Rule:MF_04053}.
CC -!- SUBUNIT: Monomer. Homodimer. Exists in equilibrium between monomers and
CC dimers in solution. Interacts with the histone-like nucleoprotein; this
CC interactions bridge the virus core to the capsid. Interacts with core
CC protein X; this interactions bridge the virus core to the capsid.
CC Interacts with the endosome lysis protein VI; this interactions bridge
CC the virus core to the capsid. Interacts with the peripentonal hexons.
CC Interacts with host NPM1; this interaction might play a role in virus
CC assembly. {ECO:0000256|HAMAP-Rule:MF_04053}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000256|HAMAP-Rule:MF_04053}. Host
CC nucleus, host nucleolus {ECO:0000256|HAMAP-Rule:MF_04053}. Note=Located
CC inside the capsid (core). Present in 157 copies per virion. Localizes
CC in the nucleoli during infection, then translocates from the nucleoli
CC to the nucleoplasm as the infection progresses and is finally
CC incorporated into the viral particles. {ECO:0000256|HAMAP-
CC Rule:MF_04053}.
CC -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC {ECO:0000256|HAMAP-Rule:MF_04053}.
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. {ECO:0000256|HAMAP-Rule:MF_04053}.
CC -!- MISCELLANEOUS: This protein is only encoded by mastadenoviruses, and
CC may therefore play a role in mammals tropism. {ECO:0000256|HAMAP-
CC Rule:MF_04053}.
CC -!- SIMILARITY: Belongs to the adenoviridae core-capsid bridging protein
CC family. {ECO:0000256|ARBA:ARBA00008293, ECO:0000256|HAMAP-
CC Rule:MF_04053}.
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DR EMBL; JN880455; AFD22107.1; -; Genomic_DNA.
DR Proteomes; UP000167733; Genome.
DR GO; GO:0044196; C:host cell nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0044423; C:virion component; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019076; P:viral release from host cell; IEA:UniProtKB-UniRule.
DR HAMAP; MF_04053; ADV_CORE5; 1.
DR InterPro; IPR005608; Adeno_V.
DR Pfam; PF03910; Adeno_PV; 1.
PE 2: Evidence at transcript level;
KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_04053};
KW Host nucleus {ECO:0000256|HAMAP-Rule:MF_04053};
KW Late protein {ECO:0000256|HAMAP-Rule:MF_04053};
KW Viral capsid assembly {ECO:0000256|HAMAP-Rule:MF_04053};
KW Viral release from host cell {ECO:0000256|HAMAP-Rule:MF_04053};
KW Virion {ECO:0000256|HAMAP-Rule:MF_04053}.
FT REGION 308..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..330
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 366 AA; 40903 MW; 1B91602B99715856 CRC64;
MSKRKFKEEL LQAVAPEIYG PPDVKPLRDL KRAIKKREKK EEKKEEAAAE AWGDAVEFVR
ATAPRRRVQW KGRRVRRVLR PGTAVVFSPG ERSALRALKR DYDEVYADED LLEQAERHEG
EFAYGKRGRY GDVALALDES NPTPSLKAVT LQQVLPVAES KKGIKREAAE LQPTMQLMVP
KRQRLEEVLE QMKVDPTVQP DVKIRPIKQV APGLGVQTVD IQIPVRTAAV EAMETQTEPA
VVGPSATAAA LGAALGRAAT AEVGIQTDPR YEYVAVAAST PRVRRRRATA AAASALLPDY
VLHPSIAPTP GYPGRPYRPR RRRRATTTTR RRRRLPTLAP VRVRRVTRRG RTLVLPTARY
HPSILV
//