ID F7VKY5_SORMK Unreviewed; 878 AA.
AC F7VKY5;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
GN ORFNames=SMAC_00380 {ECO:0000313|EMBL:CCC06162.1};
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:CCC06162.1, ECO:0000313|Proteomes:UP000001881};
RN [1] {ECO:0000313|EMBL:CCC06162.1, 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:CCC06162.1};
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|PIRSR:PIRSR634016-3,
CC ECO:0000256|RuleBase:RU364040};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR634016-3,
CC ECO:0000256|RuleBase:RU364040};
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000256|ARBA:ARBA00010136, ECO:0000256|RuleBase:RU364040}.
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:CCC06162.1}.
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DR EMBL; CABT02000001; CCC06162.1; -; Genomic_DNA.
DR RefSeq; XP_003351833.1; XM_003351785.1.
DR AlphaFoldDB; F7VKY5; -.
DR STRING; 771870.F7VKY5; -.
DR MEROPS; M01.007; -.
DR GeneID; 10809419; -.
DR KEGG; smp:SMAC_00380; -.
DR VEuPathDB; FungiDB:SMAC_00380; -.
DR eggNOG; KOG1046; Eukaryota.
DR HOGENOM; CLU_003705_0_1_1; -.
DR InParanoid; F7VKY5; -.
DR OMA; MMEYVAI; -.
DR OrthoDB; 3085317at2759; -.
DR Proteomes; UP000001881; Unassembled WGS sequence.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09601; M1_APN-Q_like; 1.
DR Gene3D; 1.25.50.20; -; 1.
DR Gene3D; 2.60.40.1910; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 1.
DR InterPro; IPR045357; Aminopeptidase_N-like_N.
DR InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR InterPro; IPR024571; ERAP1-like_C_dom.
DR InterPro; IPR034016; M1_APN-typ.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR PANTHER; PTHR11533:SF174; PUROMYCIN-SENSITIVE AMINOPEPTIDASE-RELATED; 1.
DR Pfam; PF11838; ERAP1_C; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR Pfam; PF17900; Peptidase_M1_N; 1.
DR PRINTS; PR00756; ALADIPTASE.
DR SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW ECO:0000256|RuleBase:RU364040};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364040};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR634016-3};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU364040};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU364040};
KW Reference proteome {ECO:0000313|Proteomes:UP000001881};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT DOMAIN 28..212
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 247..464
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 537..854
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT ACT_SITE 320
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 319
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 323
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 342
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT SITE 405
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 878 AA; 98492 MW; CD096AB770AA3B1B CRC64;
MCRTHAQADV ASGVNILGRE LLPTNVIPRH YHITLEPDFQ KLTFDGTVVI DLDVEEDSKS
IALHTLEIDI HNAKVTSGGQ TVSSNPKVTY NETTQVSTFD FDNAVTKGTK AQLEIQFTGQ
LNDKMAGFYR STYNNPDGTQ GLLAVSQMEP TDARRAFPCF DEPSLKAEFT VTLVADKKLT
CLSNMDVASE SETKDGKKAV TFNKSPLMST YLVAFVVGEL NYIETNDFRV PVRVYAPPGQ
NIEHGRFSLN LAAKTLAFYE KVFGIEFPLP KMDQIAIPDF AQGAMENWGL VTYRVVDLLL
DEKVSGAATK ERVAEVVQHE LAHQWFGNLV TMDWWDGLWL NEGFATWASW YSCNIFYPEW
KVWETYVTDN LQRALALDSL RSSHPIEVPV KRADEINQIF DAISYSKGSC VLRMISTYLG
EDVFLEGVRR YLKKHAYGNT QTGDLWAALG DASGKSVEEV MDVWTKHVGY PVVTVTEKDE
KTIQVKQNRF LRTGDVKPEE DKVLFPVFLG LRSKDGIDES LTLDKREDTF EVPGTEFFKL
NANHTGLYRT SYTPERLEKL GEAAKKGLLS VEDRAGMIAD AGALASSGYQ KTSGVLNLLK
GFDSEKEFIV WSEIISRVAA VQTAWIFEDK AVRDGLEAFQ RELVSARAHQ MGWEFTENDG
HIEQQFKAML FGNAGLCGDE KIIAAAKDMF KKFIAGDKSA VHPNIRGSVF SMALKYGGKE
EYDAILNFYR TSTNSDERNT ALRCLGRAKS PELIKSTLNL LFSGEIKDQD VYMPTAGLRS
HPEGIEALFT WMTENWDELV KRFPPQLSML GTLVTIFTSS FTKKEQLAKV EKFFEGKSTN
GFEMSLAQSL DAIRSKVAWI ERDGEDVAKW VKDNKYSA
//
