ID   M1249_ASFB7             Reviewed;        1249 AA.
AC   Q65152;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   23-FEB-2022, entry version 56.
DE   RecName: Full=Minor capsid protein M1249L {ECO:0000303|PubMed:31624094};
DE            Short=pM1249L;
GN   OrderedLocusNames=Ba71V-060; ORFNames=M1249L;
OS   African swine fever virus (strain Badajoz 1971 Vero-adapted) (Ba71V)
OS   (ASFV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Asfuvirales; Asfarviridae; Asfivirus.
OX   NCBI_TaxID=10498;
OH   NCBI_TaxID=6937; Ornithodoros (relapsing fever ticks).
OH   NCBI_TaxID=9823; Sus scrofa (Pig).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=11831707; DOI=10.1006/viro.1995.1149;
RA   Yanez R.J., Rodriguez J.M., Nogal M.L., Yuste L., Enriquez C.,
RA   Rodriguez J.F., Vinuela E.;
RT   "Analysis of the complete nucleotide sequence of African swine fever
RT   virus.";
RL   Virology 208:249-278(1995).
RN   [2]
RP   SUBCELLULAR LOCATION.
RX   PubMed=30185597; DOI=10.1128/jvi.01293-18;
RA   Alejo A., Matamoros T., Guerra M., Andres G.;
RT   "A Proteomic Atlas of the African Swine Fever Virus Particle.";
RL   J. Virol. 92:0-0(2018).
RN   [3]
RP   INDUCTION.
RX   PubMed=32075923; DOI=10.1128/jvi.00119-20;
RA   Cackett G., Matelska D., Sykora M., Portugal R., Malecki M., Baehler J.,
RA   Dixon L., Werner F.;
RT   "The African Swine Fever Virus Transcriptome.";
RL   J. Virol. 94:0-0(2020).
RN   [4]
RP   STRUCTURE BY ELECTRON MICROSCOPY (4.8 ANGSTROMS) OF THE ASFV CAPSID,
RP   FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION, INTERACTION WITH HEXON
RP   CAPSID PROTEIN P72, AND INTERACTION WITH MINOR CAPSID PROTEIN P17.
RX   PubMed=31624094; DOI=10.1126/science.aaz1439;
RA   Wang N., Zhao D., Wang J., Zhang Y., Wang M., Gao Y., Li F., Wang J.,
RA   Bu Z., Rao Z., Wang X.;
RT   "Architecture of African swine fever virus and implications for viral
RT   assembly.";
RL   Science 366:640-644(2019).
CC   -!- FUNCTION: Together with the penton and the other minor capsid proteins
CC       (p17, p49), forms a complicated network immediately below the outer
CC       capsid shell, stabilizing the whole capsid.
CC       {ECO:0000269|PubMed:31624094}.
CC   -!- SUBUNIT: Interacts with the minor capsid protein p17 and with the hexon
CC       capsid protein p72 capsomers; these interactions form a rigid zipper
CC       structure that stabilizes the capsomers. {ECO:0000269|PubMed:31624094}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:30185597,
CC       ECO:0000269|PubMed:31624094}.
CC   -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC       {ECO:0000269|PubMed:32075923}.
CC   -!- SIMILARITY: Belongs to the asfivirus M1249L family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U18466; AAA65290.1; -; Genomic_DNA.
DR   RefSeq; NP_042754.1; NC_001659.2.
DR   GeneID; 22220290; -.
DR   KEGG; vg:22220290; -.
DR   Proteomes; UP000000624; Genome.
PE   1: Evidence at protein level;
KW   Late protein; Reference proteome; Virion.
FT   CHAIN           1..1249
FT                   /note="Minor capsid protein M1249L"
FT                   /id="PRO_0000373609"
SQ   SEQUENCE   1249 AA;  144337 MW;  A3CB7B11F6DE8EE8 CRC64;
     MEEVITIAQI VHRGTDILSL NNEEIEALVD EIYSTLKGSN DIKNIRLIDF LFTLKDFVNH
     VRAEQSKLPD LSMPMEAYIR QLLVDPDVVP IVSEKKKELR VRPSTRKEIF LINGTHLAVP
     AEAPIEIYGL KLRLKSFSPQ CFMRMAEIGS FSPETLGYVA SGANLTNFIR VFMKCVDQET
     WKKNGEGVVV TTKENIIQFT HQYIELYKFL RSGGHSWLIN RLAEEMVHRK LDREDQGSHI
     SNIVETEEIE PEENIKRVIF FLKELSTMYS VSPVFTSGYM PLLYDLYRAG YLEVLWNPVE
     QKFLQHAEQR EKEQMILQQV DMKLTEVITQ ARQYFKIMEE KIGRVQSDAI REILTMEGKV
     DDPNSILQEV IKACGKQEAE LITTEYLNIK KQWELQEKNA CAHLKLVKQL RSGLQYAELL
     KVLESIRVLY KEKNNTTNWN LCKACGFKLL CPHVDMLIQL QAAEASYDTM RTKLMKFSGI
     NKEKENNQGL IYSYFCKICG EELAHFIQED RTADVGVIGD LNSKLRIFIW QETMKACTFI
     HFGKLVDVKQ FANIAVNVCL PLVYSIENIK KEEDYDPLTQ LYAVIYIYAY ILNLIYSSQK
     NKEFLTITIH GMKADSSLNA YVTFLLEKMM QQYSGIINQL SEITDQWIAN NFREAFKKII
     HQNGLQGLSV QDDTKVLLTE ILLGPMYDYA ATVARIDGSI PMHKPRTPKE AEYEFKTVIG
     RTPAELLSQK EFYDKIYTSK YRPDFTQLAR LNDIYFQEES LRVWWGGRDE EKTSTLIYLR
     AYELFLKYLQ NAPNFNSELA EFKTYENAYG EQKALLAQQG FYNIFDPNTG RADQRTRLFE
     YKRLPISTLY DERGLPHKWT IYVYKAVDSS QKPAEIEVTR KDVIKKIDNH YALADLRCSV
     CHVLQHEVGQ LNIKKVQTAL KASLEFNTFY AFYESRCPKG GLHDFQDKKC VKCGLFTYII
     YDHLSQPELV HDYYNNYKDQ YDKEKMSIRS IQIKKDMTTP SSETQPKPPQ EPWTFDYGKI
     IKTAKILDIS PAVIEAIGAM EGRSYADIRE GQGAPPPPTS MDDPRLMAVD SAVRIFLYNY
     NCLRHVSTFN KPPMHVERLV KHLSYEEKED LEKVLPNVVN EYHTTFKHLR VTDPASALLY
     SIEFLCVSFL TLYEIKEPSW VVNIVREFAL TELNTIIQSE KLLSKPGAFN FMIFGEDFVC
     SGEDSSMDDI SAYSSPGLFG EDIIDRLDDP FSIEDVDISL DVLDNLAPQ