ID   I7_VARV                 Reviewed;         423 AA.
AC   P0DOL4; P33003;
DT   16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT   16-OCT-2019, sequence version 1.
DT   03-AUG-2022, entry version 12.
DE   RecName: Full=Core protease I7;
DE            EC=3.4.22.-;
GN   ORFNames=I7L;
OS   Variola virus.
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus.
OX   NCBI_TaxID=10255;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Bangladesh-1975;
RX   PubMed=8264798; DOI=10.1038/366748a0;
RA   Massung R.F., Esposito J.J., Liu L.I., Qi J., Utterback T.R., Knight J.C.,
RA   Aubin L., Yuran T.E., Parsons J.M., Loparev V.N., Selivanov N.A.,
RA   Cavallaro K.F., Kerlavage A.R., Mahy B.W.J., Venter J.C.;
RT   "Potential virulence determinants in terminal regions of variola smallpox
RT   virus genome.";
RL   Nature 366:748-751(1993).
CC   -!- FUNCTION: Late protein responsible for processing most or all of the
CC       viral core and membrane proteins known to undergo morphogenesis-
CC       associated proteolysis. These proteolytic events are involved in the
CC       transformation of immature virions (IV) into mature virions (MV).
CC       Probably cleaves at least the A3, A10, L4, and A17 precursors
CC       preferentially at Ala-Gly-|-Ala motifs. Also seems to process Ala-
CC       Gly-|-Ser and Ala-Gly-|-Thr motifs (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000250}. Note=Present in the virion
CC       core. {ECO:0000250}.
CC   -!- INDUCTION: Expressed late in the viral replicative cycle.
CC   -!- SIMILARITY: Belongs to the peptidase C57 family. {ECO:0000305}.
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DR   EMBL; L22579; AAA60809.1; -; Genomic_DNA.
DR   PIR; T28499; T28499.
DR   RefSeq; NP_042105.1; NC_001611.1.
DR   GeneID; 1486462; -.
DR   KEGG; vg:1486462; -.
DR   Proteomes; UP000119805; Genome.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR004970; Peptidase_C57.
DR   Pfam; PF03290; Peptidase_C57; 1.
DR   SUPFAM; SSF54001; SSF54001; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Late protein; Protease; Thiol protease; Virion.
FT   CHAIN           1..423
FT                   /note="Core protease I7"
FT                   /id="PRO_0000448203"
FT   ACT_SITE        241
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        248
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        328
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   423 AA;  49142 MW;  E9434483CB999826 CRC64;
     MERYTDLVIS KIPELGFTNL LCHIYSLAGL CSNIDVSKFL TNCNGYVVEK YDKSTTAGKV
     SCIPIGMMLE LVESRHLSRP NSSDELDQKK ELTDELKTRY HSIYDVFELP TSIPLAYFFK
     PRLREKVSKA IDFSQMDLKI DDLSRKGIHT GENPKVVKMK IEPERGAWMS NRSIKNLVSQ
     FAYGSEVDYI GQFDMRFLNS LAIHEKFDAF MNKHILSYIL KDKIKSSTSR FVMFGFCYLS
     HWKCVIYDKK QCLVSFYDSG GNIPTEFHHY NNFYFYSFSD GFNTNHRHSV LDNTNCDIDV
     LFRFFECIFG AKIGCINVEV NQLLESECGM FISLFMILCT RTPPKSFKSL KKVYTFFKFL
     ADKKMTLFKS ILFNLQDLSL DITETDNAGL KEYKRMEKWT KKSINVICDK LTTKLNRIVD
     DDE