ID   I7_VACCC                Reviewed;         423 AA.
AC   P20501;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Core protease I7;
DE            EC=3.4.22.-;
GN   ORFNames=I7L;
OS   Vaccinia virus (strain Copenhagen) (VACV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX   NCBI_TaxID=10249;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=2219722; DOI=10.1016/0042-6822(90)90294-2;
RA   Goebel S.J., Johnson G.P., Perkus M.E., Davis S.W., Winslow J.P.,
RA   Paoletti E.;
RT   "The complete DNA sequence of vaccinia virus.";
RL   Virology 179:247-266(1990).
RN   [2]
RP   COMPLETE GENOME.
RA   Goebel S.J., Johnson G.P., Perkus M.E., Davis S.W., Winslow J.P.,
RA   Paoletti E.;
RT   "Appendix to 'The complete DNA sequence of vaccinia virus'.";
RL   Virology 179:517-563(1990).
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; M35027; AAA48063.1; -; Genomic_DNA.
DR   PIR; C42511; C42511.
DR   MEROPS; C57.001; -.
DR   Proteomes; UP000008269; 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; Reference proteome; Thiol protease;
KW   Virion.
FT   CHAIN           1..423
FT                   /note="Core protease I7"
FT                   /id="PRO_0000099582"
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;  49040 MW;  633F501637FD80D3 CRC64;
     MERYTDLVIS KIPELGFTNL LCHIYSLAGL CSNIDVSKFL TNCNGYVVEK YDKSTTAGKV
     SCIPIGMMLE LVESGHLSRP NSSDELDQKK ELTDELKTRY HSIYDVFELP TSIPLAYFFK
     PRLREKVSKA IDFSQMDLKI DDLSRKGIHT GENPKVVKMK IEPERGAWMS NRSIKNLVSQ
     FAYGSEVDYI GQFDMRFLNS LAIHEKFDAF MNKHILSYIL KDKIKSSTSR FVMFGFCYLS
     HWKCVIYDKK QCLVSFYDSG GNIPTEFHHY NNFYFYSFSD GFNTNHRHSV LDNTNCDIDV
     LFRFFECTFG AKIGCINVEV NQLLESECGM FISLFMILCT RTPPKSFKSL KKVYTFFKFL
     ADKKMTLFKS ILFNLHDLSL DITETDNAGL KEYKRMEKWT KKSINVICDK LTTKLNRIVD
     DDE