ID A0A0G2F913_9PEZI Unreviewed; 655 AA.
AC A0A0G2F913;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Extracellular metalloproteinase {ECO:0000256|RuleBase:RU364017};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU364017};
DE AltName: Full=Fungalysin {ECO:0000256|RuleBase:RU364017};
GN ORFNames=UCDDA912_g09361 {ECO:0000313|EMBL:KKY30689.1};
OS Diaporthe ampelina.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Diaporthaceae; Diaporthe.
OX NCBI_TaxID=1214573 {ECO:0000313|EMBL:KKY30689.1, ECO:0000313|Proteomes:UP000034680};
RN [1] {ECO:0000313|EMBL:KKY30689.1, ECO:0000313|Proteomes:UP000034680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DA912 {ECO:0000313|EMBL:KKY30689.1};
RA Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT "Distinctive expansion of gene families associated with plant cell wall
RT degradation and secondary metabolism in the genomes of grapevine trunk
RT pathogens.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KKY30689.1, ECO:0000313|Proteomes:UP000034680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DA912 {ECO:0000313|EMBL:KKY30689.1};
RA Morales-Cruz A., Amrine K.C., Cantu D.;
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR601842-2};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR601842-2};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613,
CC ECO:0000256|RuleBase:RU364017}.
CC -!- SIMILARITY: Belongs to the peptidase M36 family.
CC {ECO:0000256|ARBA:ARBA00006006, ECO:0000256|RuleBase:RU364017}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKY30689.1}.
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DR EMBL; LCUC01000454; KKY30689.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G2F913; -.
DR OrthoDB; 2786251at2759; -.
DR Proteomes; UP000034680; Unassembled WGS sequence.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
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 CDD; cd09596; M36; 1.
DR Gene3D; 3.10.170.10; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR InterPro; IPR011096; FTP_domain.
DR InterPro; IPR001842; Peptidase_M36.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR33478; EXTRACELLULAR METALLOPROTEINASE MEP; 1.
DR PANTHER; PTHR33478:SF1; EXTRACELLULAR METALLOPROTEINASE MEP; 1.
DR Pfam; PF07504; FTP; 1.
DR Pfam; PF02128; Peptidase_M36; 1.
DR PRINTS; PR00999; FUNGALYSIN.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU364017};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR601842-2,
KW ECO:0000256|RuleBase:RU364017};
KW Metalloprotease {ECO:0000256|RuleBase:RU364017};
KW Protease {ECO:0000256|RuleBase:RU364017};
KW Reference proteome {ECO:0000313|Proteomes:UP000034680};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU364017};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU364017};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR601842-2};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145, ECO:0000256|RuleBase:RU364017}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|RuleBase:RU364017"
FT CHAIN 17..655
FT /note="Extracellular metalloproteinase"
FT /evidence="ECO:0000256|RuleBase:RU364017"
FT /id="PRO_5009360662"
FT DOMAIN 85..135
FT /note="FTP"
FT /evidence="ECO:0000259|Pfam:PF07504"
FT ACT_SITE 450
FT /evidence="ECO:0000256|PIRSR:PIRSR601842-1"
FT BINDING 449
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR601842-2"
FT BINDING 453
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR601842-2"
FT BINDING 479
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR601842-2"
SQ SEQUENCE 655 AA; 71319 MW; 5A485B414359F8FD CRC64;
MQSLVLLGLL GSSALAHPAV QSANKKPWKP SLSKRLVDLD QFRPGTAATY VNATETNSSP
DTKLIKRDDY VATATALVKS KVPDAEFRVY DSYVGTNGIG HVYFRQTIFG IDVDNTDFNV
NIAKDGSVFS HGNSFYTGAL PESSPLKKRD FKDPVAALNA ANSVLQLDVK TEGAKAEAKD
GVETYGIAGT TGAQSDPEAR LLYYVKDDGT LALTWRVETD ISSDWLLSYV DAETTEKVYG
VVNYVAQAHN DNKLVPKQAD ISATYLVYPW GVNDPEEGSR VVVTDPWDLE DSPFTWHNDG
SQTYDTTWGN NAVAQVNPTG ATCDTCYTDD YRPESTTFDF EYDYSPSMAD PETYYNASIT
QLFYTVNKYH DLLYELGFTE ATYNFQADNE DKGGKGSDFA IVNAQDGAGT NNADFSTPAD
GRPGRMRMYL WTQSTPVRDC TFEAGVVIHE YTHGVSNRLT GGGTNTRCLT GVESGGLGEG
WGDFMATAIR LKEGDTRATD YSMGAWVYNN PAGIRAYLFS TDMNTNPYTY ASVNGKTEVH
SVGTIWTTIL YEVLWNLIDK YGSNPADKPT FDSNGVPTDG RYLAMKLVID GLALQPCNPT
FVSARDAIID ADLALTGGAN ACELWTGFAK RGLGQGAVYS SSSRTESFVV PSGVC
//
