ID A1DJ89_NEOFI Unreviewed; 498 AA.
AC A1DJ89;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE RecName: Full=Peptide hydrolase {ECO:0000256|RuleBase:RU361240};
DE EC=3.4.-.- {ECO:0000256|RuleBase:RU361240};
GN ORFNames=NFIA_001250 {ECO:0000313|EMBL:EAW16778.1};
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117 {ECO:0000313|EMBL:EAW16778.1, ECO:0000313|Proteomes:UP000006702};
RN [1] {ECO:0000313|Proteomes:UP000006702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 /
RC NRRL 181 / WB 181 {ECO:0000313|Proteomes:UP000006702};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M28 family. M28A subfamily.
CC {ECO:0000256|ARBA:ARBA00005957}.
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DR EMBL; DS027697; EAW16778.1; -; Genomic_DNA.
DR RefSeq; XP_001258675.1; XM_001258674.1.
DR AlphaFoldDB; A1DJ89; -.
DR STRING; 331117.A1DJ89; -.
DR MEROPS; M28.001; -.
DR EnsemblFungi; EAW16778; EAW16778; NFIA_001250.
DR GeneID; 4585734; -.
DR KEGG; nfi:NFIA_001250; -.
DR VEuPathDB; FungiDB:NFIA_001250; -.
DR eggNOG; KOG2195; Eukaryota.
DR HOGENOM; CLU_024336_0_0_1; -.
DR OMA; VRFCFWT; -.
DR OrthoDB; 51543at2759; -.
DR Proteomes; UP000006702; Unassembled WGS sequence.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008235; F:metalloexopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd03876; M28_SGAP_like; 1.
DR CDD; cd02130; PA_ScAPY_like; 1.
DR Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR045175; M28_fam.
DR InterPro; IPR041756; M28_SGAP-like.
DR InterPro; IPR046450; PA_dom_sf.
DR InterPro; IPR003137; PA_domain.
DR InterPro; IPR007484; Peptidase_M28.
DR PANTHER; PTHR12147; METALLOPEPTIDASE M28 FAMILY MEMBER; 1.
DR PANTHER; PTHR12147:SF55; PEPTIDE HYDROLASE; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
DR SUPFAM; SSF52025; PA domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW ECO:0000313|EMBL:EAW16778.1}; Hydrolase {ECO:0000256|RuleBase:RU361240};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU361240};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU361240};
KW Reference proteome {ECO:0000313|Proteomes:UP000006702};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|RuleBase:RU361240}.
FT SIGNAL 1..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..498
FT /note="Peptide hydrolase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012655157"
FT DOMAIN 121..209
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 235..442
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
FT REGION 473..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..487
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 498 AA; 53759 MW; A2B233FF0264F556 CRC64;
MKLLYLTSFA SLAVANGPGW DWKPPVHPKV LPQMIHLWDL MHGAQKLEDF AYAYPERNRV
FGGPAHEDTV NYLYRELKKT GYYDVYKQPQ VHQWTRADQA LTVDGKSYVA TTMTYSPSVN
VTAPLAVVNN LGCVESDYPA DLKGKIALVS RGECPFATKS VLSAKAGAAA ALVYNNIEGS
MAGTLGGPTS ELGPYAPIAG ISLADGQALI QMIQAGTVTA NLWIDSKVEN RTTYNVIAQT
KGGDPNNVVA LGGHTDSVEA GPGINDDGSG IISNLVVAKA LTRFSVKNAV RFCFWTAEEF
GLLGSSYYVN SLNATEKAKI RLYLNFDMIA SPNYALMIYD GDGSAFNLTG PAGSAQIERL
FEDYYKSIRK PFVPTEFNGR SDYEAFILNG IPAGGIFTGA EAIKTEEQAK LFGGQAGVAL
DANYHAKGDN MTNLNREAFL INSKATAFAV ATYANSLDSI PSRNMSTVVK RSQLEQAKKS
TPHTHTGGTG CYKDRVEQ
//
