ID   F7W2B3_SORMK            Unreviewed;       258 AA.
AC   F7W2B3;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   13-SEP-2023, entry version 50.
DE   SubName: Full=WGS project CABT00000000 data, contig 2.21 {ECO:0000313|EMBL:CCC11763.1};
GN   ORFNames=SMAC_04745 {ECO:0000313|EMBL:CCC11763.1};
OS   Sordaria macrospora (strain ATCC MYA-333 / DSM 997 / K(L3346) / K-hell).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Sordaria.
OX   NCBI_TaxID=771870 {ECO:0000313|EMBL:CCC11763.1, ECO:0000313|Proteomes:UP000001881};
RN   [1] {ECO:0000313|EMBL:CCC11763.1, ECO:0000313|Proteomes:UP000001881}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-333 / DSM 997 / K(L3346) / K-hell
RC   {ECO:0000313|Proteomes:UP000001881};
RC   TISSUE=Mycelium {ECO:0000313|EMBL:CCC11763.1};
RX   PubMed=20386741; DOI=10.1371/journal.pgen.1000891;
RA   Nowrousian M., Stajich J., Chu M., Engh I., Espagne E., Halliday K.,
RA   Kamerewerd J., Kempken F., Knab B., Kuo H.C., Osiewacz H.D., Poeggeler S.,
RA   Read N., Seiler S., Smith K., Zickler D., Kueck U., Freitag M.;
RT   "De novo assembly of a 40 Mb eukaryotic genome from short sequence reads:
RT   Sordaria macrospora, a model organism for fungal morphogenesis.";
RL   PLoS Genet. 6:E1000891-E1000891(2010).
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:CCC11763.1}.
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DR   EMBL; CABT02000021; CCC11763.1; -; Genomic_DNA.
DR   RefSeq; XP_003346572.1; XM_003346524.1.
DR   AlphaFoldDB; F7W2B3; -.
DR   STRING; 771870.F7W2B3; -.
DR   GeneID; 10803962; -.
DR   KEGG; smp:SMAC_04745; -.
DR   VEuPathDB; FungiDB:SMAC_04745; -.
DR   eggNOG; KOG2089; Eukaryota.
DR   HOGENOM; CLU_1078352_0_0_1; -.
DR   InParanoid; F7W2B3; -.
DR   OrthoDB; 735202at2759; -.
DR   Proteomes; UP000001881; 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   Gene3D; 1.10.1370.10; Neurolysin, domain 3; 1.
DR   InterPro; IPR024077; Neurolysin/TOP_dom2.
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:UP000001881};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT   DOMAIN          2..152
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
FT   REGION          165..198
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        165..188
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   258 AA;  29117 MW;  82AC4C1F2F167909 CRC64;
     MAERIAASRH FLKALNNLWQ VSSAIFDMEV HSPKSRTELD DMDFARRHNE LRNELTGLKG
     PEALGEPMTH GHGNLHHLFY EYDAGLYSYH WSNTYTYDMF YSAFAKDPMD KSQGHRYRHM
     VLEKGASQDE MFILEQFLSR KPTTDAFFKE LGLVESVDTP LLKESSFAER DPAMDKGPSS
     EERPAVEARS ILEGSPPVGG NTFVDGGLSV DGAYVVGGRV IETYPSAEGG PVVEPTSPGQ
     RIRHKMRHIA AHFRRNRQ
//