ID   MP44_FOWPN              Reviewed;         626 AA.
AC   Q9J5D0; O72905;
DT   29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Probable metalloendopeptidase G1-type;
DE            EC=3.4.24.-;
GN   OrderedLocusNames=FPV081; ORFNames=FPG1L;
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 [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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 286-626.
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.
CC   -!- FUNCTION: Seems to be involved in viral proteins maturation by cleavage
CC       at Ala-Gly-|-Xaa motifs. {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC       Note=Binds 1 zinc ion. {ECO:0000305};
CC   -!- SIMILARITY: Belongs to the peptidase M44 family. {ECO:0000305}.
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DR   EMBL; AF198100; AAF44425.1; -; Genomic_DNA.
DR   EMBL; AJ223385; CAA11300.1; -; Genomic_DNA.
DR   PIR; H48563; H48563.
DR   RefSeq; NP_039044.1; NC_002188.1.
DR   SMR; Q9J5D0; -.
DR   GeneID; 1486629; -.
DR   KEGG; vg:1486629; -.
DR   Proteomes; UP000008597; Genome.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0019058; P:viral life cycle; IEA:InterPro.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR005072; Peptidase_M44.
DR   Pfam; PF03410; Peptidase_M44; 1.
DR   PIRSF; PIRSF015679; Peptidase_M44; 1.
DR   SUPFAM; SSF63411; SSF63411; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Metalloprotease; Protease; Reference proteome;
KW   Zinc.
FT   CHAIN           1..626
FT                   /note="Probable metalloendopeptidase G1-type"
FT                   /id="PRO_0000218448"
FT   ACT_SITE        45
FT                   /evidence="ECO:0000255"
FT   BINDING         42
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255"
FT   BINDING         46
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   626 AA;  73949 MW;  98EA28BCF318B687 CRC64;
     MIQLNNGIRI FVNHSMKKDI YIGISDFGFE KDINDGILGI AHLLEHILIS FDNKYFNANA
     STSRTYMSFW CVALQKRHYE DAIRTAISWF FDKKYILKTD FSRIVLENYI TELENEYYYR
     TEMYHCMDVL AYLYGGDLYN GGRITMLERL PEIRNMLSNR MKFLSGKNIV IFVKRLTNNI
     LTLLTNTFGS IPKYPIIIPL DPQIQDARRK IIMMPCPFYT LLIQVDNTMN NLLAIICLVE
     NYNLIDYETI SDKLYVCISF ANEDQYEYLL YNIKDMDFNI NRIELDLGED YIMNLYINFP
     WLKNDIFEYI HTMNTKSAML LADLKKNMHN SILEHKFMII YPSFTKLLYN ITDKQNHGIL
     VVGDVSFTPE KDPSMHHSNK ENNNNYSKTV TKRKSKYVMY RKTPTTNNIV IDYTDSSFFD
     YATFYHVMKS KYEKTNLFSR LKTSTGMCYK HCFDNDDLNE LINSDTFIRY NSSKPAVLYQ
     YILLAYFVTE RDIKELVDYK DAIELDMKYY SKNKILFGKN TRYDIRTKSM FVCGLIKGRK
     LSEKVITDYM WKLKSLGLIY YLTSIKLGIS NTFYIFAFTI FPEKVYNFFV GLKEITNRCL
     IVSNKNTKIE EDDYSSLNKQ IVIGIK