ID A0A1Y2VGW1_9PEZI Unreviewed; 981 AA.
AC A0A1Y2VGW1;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
GN ORFNames=M434DRAFT_392308 {ECO:0000313|EMBL:OTA96881.1};
OS Hypoxylon sp. CO27-5.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Hypoxylaceae; Hypoxylon.
OX NCBI_TaxID=1001938 {ECO:0000313|EMBL:OTA96881.1, ECO:0000313|Proteomes:UP000194361};
RN [1] {ECO:0000313|EMBL:OTA96881.1, ECO:0000313|Proteomes:UP000194361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO27-5 {ECO:0000313|EMBL:OTA96881.1,
RC ECO:0000313|Proteomes:UP000194361};
RX PubMed=28078400; DOI=10.1007/s00253-017-8091-1;
RA Wu W., Davis R.W., Tran-Gyamfi M.B., Kuo A., LaButti K., Mihaltcheva S.,
RA Hundley H., Chovatia M., Lindquist E., Barry K., Grigoriev I.V.,
RA Henrissat B., Gladden J.M.;
RT "Characterization of four endophytic fungi as potential consolidated
RT bioprocessing hosts for conversion of lignocellulose into advanced
RT biofuels.";
RL Appl. Microbiol. Biotechnol. 101:2603-2618(2017).
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}.
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DR EMBL; KZ112429; OTA96881.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2VGW1; -.
DR STRING; 1001938.A0A1Y2VGW1; -.
DR Proteomes; UP000194361; 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:UP000194361};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT DOMAIN 126..314
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 349..566
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 640..957
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT ACT_SITE 422
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 421
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 425
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 444
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT SITE 507
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 981 AA; 110369 MW; 0086878679BAB9AB CRC64;
MSLRAASRVE FIPRVSTPTR VRLRPFTLRP TISLWRQNHI WCSPALTSPP SYGPSLRLTS
HSSLTSVSRS SPFEKARTTT LSRPPVRHCS YRRNNMCKLA GDIDHTGGAT PDPTQGRELL
PTNVIPRHYD VTLEPNLEKF TFEGKALIDF DVQEDSKSIS LHTIELDIHS AHIKSGETIV
TSSSAITYDE TKQVSKIELK DAIPKGKAQL EIKFTGQLND QMAGFYRSTY KKPDGTEGIL
ATTQMEANDC RRAFPCFDEP MHKAKFTITL IADKHLTCLS NMDVASESEV HSEMSGSTKK
AVKFNTTPLM STYLVAFIIG ELNYIETNNF RVPIRVYAPP SSDIEHGRFS LNLAARTLEY
YEKIFGAEFP LPKMDMVAIP DFAAGAMENW GLITYRVVDL MLDEKASGAA MKERVAEVVQ
HELAHQWFGN LVTMDWWEGL WLNEGFATLM SWLSCNYFYP EWKVWENYVT DNLQSALGLD
SLRSSHPIEV PVKRASEVDQ IFDAISYSKG SCVLRMISTY LGEETFLEGV RRYIKKHAYG
NTRTEDLWAA LEEASGKPVK EIMSIWTKNV GFPVVQVSEN EKDSSIRVKQ NRFLRTGDTK
PEEDQVLYPV FLGLRTKDGV DESLTLTKRE DVFKVKDLDF FKLNANHTSI YRTCYTPDRL
TKLGQSAKEG LLTVEDRAGM IADAGALAVS GYQKTSGVLN LLKGFDTEES FVVWSEIIAR
VATVQSAWVF EDAAVKDGLE AFVKDLISER AHKLGWSFSD KDGHVEQQFK AMLFGAAGMA
GDQKIITAAK EMFKKYMAGD KSAIHPNIRG SVFSMALKYG GQEEYEAVLN FFRTSNNSDE
RNTALRCIGR AKEPALIQRT LDLVLSGEVK SQDIYLPASG LRSHAEGIEA LFSWLTEKWP
EIYKRLSGNP PILGSMVTIC TSSFAKPEQL QKVEEFFKDI DTKTFAQPLA QSKDAIRSKI
AWLERDRDDV AAWVRENGYS K
//
