I7_FOWPN
ID I7_FOWPN Reviewed; 421 AA.
AC O72903;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Core protease I7 homolog;
DE EC=3.4.22.-;
DE AltName: Full=Protein FPV083;
GN OrderedLocusNames=FPV083; ORFNames=FPI7L;
OS Fowlpox virus (strain NVSL) (FPV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Avipoxvirus.
OX NCBI_TaxID=928301;
OH NCBI_TaxID=7742; Vertebrata.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=FP-9 / Isolate HP-440;
RA Pollitt E., Skinner M.A., Heaphy S.;
RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10729156; DOI=10.1128/jvi.74.8.3815-3831.2000;
RA Afonso C.L., Tulman E.R., Lu Z., Zsak L., Kutish G.F., Rock D.L.;
RT "The genome of fowlpox virus.";
RL J. Virol. 74:3815-3831(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 {ECO:0000250}. Note=Present in the virion
CC core. {ECO:0000250}.
CC -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC -!- SIMILARITY: Belongs to the peptidase C57 family. {ECO:0000305}.
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DR EMBL; AJ223385; CAA11298.1; -; Genomic_DNA.
DR EMBL; AF198100; AAF44427.1; -; Genomic_DNA.
DR PIR; F48563; F48563.
DR RefSeq; NP_039046.1; NC_002188.1.
DR MEROPS; C57.001; -.
DR GeneID; 1486631; -.
DR KEGG; vg:1486631; -.
DR Proteomes; UP000008597; 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..421
FT /note="Core protease I7 homolog"
FT /id="PRO_0000099585"
FT ACT_SITE 242
FT /evidence="ECO:0000250"
FT ACT_SITE 249
FT /evidence="ECO:0000250"
FT ACT_SITE 329
FT /evidence="ECO:0000250"
SQ SEQUENCE 421 AA; 48621 MW; B58813864F2F10BA CRC64;
MDKYTELVIN KIPELGFVNL LSHIYQTVGL CSSIDISKFK TNCNGYVVER FDKSETAGKV
SCVPISILME LVERGMLSKP DNSKSQLEVK TDLVNELISK NNGFEDIMTI PTSIPMKYFF
KPVLKEKVSK AIDFSVMDIK GDDVSRMGIR YGENDKVVKI KIAPERDAWM TNTSIHQFLI
PMCYGTEVIY IGQFNFNFMN RHAIYEKSSV FNKNTEVFKL KDRIRDNRSS RFIMFGFCYL
HHWKCAIYDK NRDFICFYDS GGNNPNEFNH YRNFFFYSNS DGLNRNSYLS SLANENADID
ILFNFFIDNY GVTAGCINVE VNQLLESECG MFTCLFMAVC CLNPPKGFKG IRKIYTYFKF
LADKKVTMLK SILFNVGKME FTIKEVDGEG MQQYKKMEKW CANTINILAN KITSRVEDII
N