ID   I7_AMEPV                Reviewed;         464 AA.
AC   P29817;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Core protease I7 homolog;
DE            EC=3.4.22.-;
GN   OrderedLocusNames=AMV181; ORFNames=G1;
OS   Amsacta moorei entomopoxvirus (AmEPV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Entomopoxvirinae; Betaentomopoxvirus.
OX   NCBI_TaxID=28321;
OH   NCBI_TaxID=340055; Amsacta.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1942245; DOI=10.1128/jvi.65.12.6516-6527.1991;
RA   Hall R.L., Moyer R.W.;
RT   "Identification, cloning, and sequencing of a fragment of Amsacta moorei
RT   entomopoxvirus DNA containing the spheroidin gene and three vaccinia virus-
RT   related open reading frames.";
RL   J. Virol. 65:6516-6527(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10936094; DOI=10.1006/viro.2000.0449;
RA   Bawden A.L., Glassberg K.J., Diggans J., Shaw R., Farmerie W., Moyer R.W.;
RT   "Complete genomic sequence of the Amsacta moorei entomopoxvirus: analysis
RT   and comparison with other poxviruses.";
RL   Virology 274:120-139(2000).
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) (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Virion. Note=Present in the virion core.
CC       {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; M77182; AAA42379.1; -; Genomic_DNA.
DR   EMBL; AF250284; AAG02887.1; -; Genomic_DNA.
DR   PIR; A41561; WZVZG1.
DR   RefSeq; NP_064963.1; NC_002520.1.
DR   PRIDE; P29817; -.
DR   GeneID; 1494771; -.
DR   KEGG; vg:1494771; -.
DR   Proteomes; UP000000872; 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..464
FT                   /note="Core protease I7 homolog"
FT                   /id="PRO_0000099586"
FT   ACT_SITE        258
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        269
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        353
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   464 AA;  55541 MW;  4FF09F3BB23307EE CRC64;
     MNNKIRRFPN KNLKMPESGI NFMSMLFFSK IDNMVYFINP IKYNTNANIA ILEKIDDDDE
     TRGKVTFIPI KYLEILYNEL VLDPNHINNI NFENNIKRKF FLFWTIKKYL QDKNININTF
     ITSKKYKGIP LVYMRKSFLK SELSKTRDFS TFATIYDDLD AQIGIPPLGF NPKPKAYPRK
     HDKSTWLSSG DIYNCIYPLT MINTDYDYFH LILFEKTDKN IATVASSMRC YKLEDRVKFF
     LMNDKKRFFM FPIIYNDHFT CCVIDKHFDK DKKAAYFFNS SGYIPELIKQ NKKYMFIESD
     MTIKSHKHYN STPNTNYAYL YIDVLSEYLN DIFKNVNYYF FNTFELQYDS PDCGMFNIIF
     LYYIVYFNIK SKFEFKKLYY SMSFIGDLLA SSYRGALFIS RYDINSIDEF KNTLEIFNIK
     NKKFMELIDM YKKNSNRIMN VCSKIKNDYD SYIDNEKNSL ESNI