ID A0A094HI84_9PEZI Unreviewed; 701 AA.
AC A0A094HI84;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 13-SEP-2023, entry version 35.
DE RecName: Full=Peptidase M3A/M3B catalytic domain-containing protein {ECO:0000259|Pfam:PF01432};
GN ORFNames=V502_05982 {ECO:0000313|EMBL:KFZ14622.1};
OS Pseudogymnoascus sp. VKM F-4520 (FW-2644).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420915 {ECO:0000313|EMBL:KFZ14622.1, ECO:0000313|Proteomes:UP000029308};
RN [1] {ECO:0000313|EMBL:KFZ14622.1, ECO:0000313|Proteomes:UP000029308}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4520 (FW-2644) {ECO:0000313|Proteomes:UP000029308};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU003435};
CC Note=Binds 1 zinc ion. {ECO:0000256|RuleBase:RU003435};
CC -!- SIMILARITY: Belongs to the peptidase M3 family.
CC {ECO:0000256|ARBA:ARBA00006040, ECO:0000256|RuleBase:RU003435}.
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:KFZ14622.1}.
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DR EMBL; JPKE01002277; KFZ14622.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094HI84; -.
DR STRING; 1420915.A0A094HI84; -.
DR MEROPS; M03.009; -.
DR HOGENOM; CLU_001805_1_1_1; -.
DR OrthoDB; 735202at2759; -.
DR Proteomes; UP000029308; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd06455; M3A_TOP; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 1.10.1370.10; Neurolysin, domain 3; 1.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR024077; Neurolysin/TOP_dom2.
DR InterPro; IPR024080; Neurolysin/TOP_N.
DR InterPro; IPR045090; Pept_M3A_M3B.
DR InterPro; IPR001567; Pept_M3A_M3B_dom.
DR PANTHER; PTHR11804; PROTEASE M3 THIMET OLIGOPEPTIDASE-RELATED; 1.
DR PANTHER; PTHR11804:SF84; SACCHAROLYSIN; 1.
DR Pfam; PF01432; Peptidase_M3; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003435};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU003435};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU003435};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003435};
KW Reference proteome {ECO:0000313|Proteomes:UP000029308};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 226..697
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 701 AA; 78362 MW; 705072868499B4DA CRC64;
MAPAQYRTPP QAPPLFTATT SSLVADAKKL CANSKNVMDI IVGSVKPENA AFETVVLPMA
VDENEGSLEA RIIGFYQAVS TDKALRDAST EAEKIMDEFA IEASMREDVY KLVEAAFQKG
AELDPESQRL LEKERKSYIR NGLGLPAGPK RDRFKEIKLR LSQISTDFQK NLNEEDGGIW
VTREEMAGVP EDVLGGLEKG TGAEEGKLRL SFKYPDLFPT LKFALSAELR QKLFIENENK
CNVNVPLFKE AIVLRDEAAR LLGYPDHATF RIEDKMAKTP KTVLDFLGDL RTQLAPGGIK
ETEHLKELKI ADLKSRGLEN TYDGNYYLWD HRFYDRLMVE QEYTIDEQKI AEYFPLESTV
NSMLNIFESL FGLVFVEIEG EARDALSPTA KRDDIVWHED VKLFSVWDDA GEGGAFSGYL
YLDLHPRPGK YGHAANFNLQ SGFVAANGTR RYPATALVCN FSKPTADKPS LLKHDEVVTL
FHELGHGIHD LVGRTQYSRF HGTSVVRDFV EAPSQMLENW CWAPAQLKGL SKHYVSGEAI
PDELIEKLIS TKHVNDALFN LRQLHFGTFD MAVHTPKTHE EAVGLEISEL YNTLRMQISG
MKGPEALGQG NAWGNGPATF GHLIGGYDAG YYGYLSSQVY SADMFHSVFA KDPMSAVEGR
RYRHMVLEKG GSQDEMVTLE AFLGRKPSTE AFYRELGLGG N
//