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Database: UniProt
Entry: G9NMU1_HYPAI
LinkDB: G9NMU1_HYPAI
Original site: G9NMU1_HYPAI 
ID   G9NMU1_HYPAI            Unreviewed;       703 AA.
AC   G9NMU1;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   24-JAN-2024, entry version 51.
DE   RecName: Full=Peptidase M3A/M3B catalytic domain-containing protein {ECO:0000259|Pfam:PF01432};
GN   ORFNames=TRIATDRAFT_155050 {ECO:0000313|EMBL:EHK48221.1};
OS   Hypocrea atroviridis (strain ATCC 20476 / IMI 206040) (Trichoderma
OS   atroviride).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=452589 {ECO:0000313|EMBL:EHK48221.1, ECO:0000313|Proteomes:UP000005426};
RN   [1] {ECO:0000313|EMBL:EHK48221.1, ECO:0000313|Proteomes:UP000005426}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 20476 / IMI 206040 {ECO:0000313|Proteomes:UP000005426};
RX   PubMed=21501500; DOI=10.1186/gb-2011-12-4-r40;
RA   Kubicek C.P., Herrera-Estrella A., Seidl-Seiboth V., Martinez D.A.,
RA   Druzhinina I.S., Thon M., Zeilinger S., Casas-Flores S., Horwitz B.A.,
RA   Mukherjee P.K., Mukherjee M., Kredics L., Alcaraz L.D., Aerts A., Antal Z.,
RA   Atanasova L., Cervantes-Badillo M.G., Challacombe J., Chertkov O.,
RA   McCluskey K., Coulpier F., Deshpande N., von Doehren H., Ebbole D.J.,
RA   Esquivel-Naranjo E.U., Fekete E., Flipphi M., Glaser F.,
RA   Gomez-Rodriguez E.Y., Gruber S., Han C., Henrissat B., Hermosa R.,
RA   Hernandez-Onate M., Karaffa L., Kosti I., Le Crom S., Lindquist E.,
RA   Lucas S., Luebeck M., Luebeck P.S., Margeot A., Metz B., Misra M.,
RA   Nevalainen H., Omann M., Packer N., Perrone G., Uresti-Rivera E.E.,
RA   Salamov A., Schmoll M., Seiboth B., Shapiro H., Sukno S.,
RA   Tamayo-Ramos J.A., Tisch D., Wiest A., Wilkinson H.H., Zhang M.,
RA   Coutinho P.M., Kenerley C.M., Monte E., Baker S.E., Grigoriev I.V.;
RT   "Comparative genome sequence analysis underscores mycoparasitism as the
RT   ancestral life style of Trichoderma.";
RL   Genome Biol. 12:R40.1-R40.15(2011).
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:EHK48221.1}.
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DR   EMBL; ABDG02000019; EHK48221.1; -; Genomic_DNA.
DR   RefSeq; XP_013946385.1; XM_014090910.1.
DR   AlphaFoldDB; G9NMU1; -.
DR   MEROPS; M03.009; -.
DR   GeneID; 25776296; -.
DR   eggNOG; KOG2089; Eukaryota.
DR   HOGENOM; CLU_001805_1_1_1; -.
DR   OMA; RSGAWCS; -.
DR   OrthoDB; 735202at2759; -.
DR   Proteomes; UP000005426; 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:UP000005426};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT   DOMAIN          224..699
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   703 AA;  80355 MW;  96EC1A745A17DC16 CRC64;
     MAPEQFRNPP QSPPVFTATA DSILADAKKS AEKSKSILDQ IVATVTPETA TFDNTLKPIL
     IDGNDSTGPQ NIQTFFQHVS TNESLREAST KAEELLNDFY IEAKMREDVF KLVDAAYSTR
     DSQNLDKESL HILEKERQKY IRNGLLLPPG EKRDRFKEIK KRLSQLCILG KKNLNEEKGG
     FWFTREELEG VPKDDIDVDT LEKGTGENEG KFKVTFKYNH YTPLMKYAIH EDTRRRYIIA
     DANKSNNNVE IFKEIMELRD EAARLLGYPD HASVRIEEKM AKSPTRVNDF LGDLQVRLAP
     GGKKEVEVLR GYKKRDYEER GIPFDGEFYM WDTSYYSRIM KEVEYSVDEV AISQYFPAES
     TFAGMLKIFE EIFGFVFVEL GKEDRARLSP SGKADDISWH EDVIMYSVWD EAAKGGEFCG
     YLYLDLFPRD NKYGHYANFG IEPGFTTVDG KRSYPSTSLV CNFSKPTATK PSLLKHHEVV
     TFFHELGHGI HDLAGRSRFS YTHGTATVAD FVEAPSQMLE NWCWTPSVLK SLSKHWESGE
     SIPDELVEKL VKTKHLNSAI GALGQLVIGT FDMTIHGPKT HEEAKTRNYG KLWNQIRHDI
     SQIKGPEDIG ETMEWGNRYA NIGHFLGGYD AGYYGYLYSE VFSLDMFHSF FKKNPMDGKE
     GRRYRHTVLE RGGSIDEMEF LKEFLGREPS TEAFYEELGI AAK
//
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