ID A1CFX3_ASPCL Unreviewed; 506 AA.
AC A1CFX3;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=Peptide hydrolase {ECO:0000256|RuleBase:RU361240};
DE EC=3.4.-.- {ECO:0000256|RuleBase:RU361240};
GN ORFNames=ACLA_094720 {ECO:0000313|EMBL:EAW11772.1};
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612 {ECO:0000313|EMBL:EAW11772.1, ECO:0000313|Proteomes:UP000006701};
RN [1] {ECO:0000313|EMBL:EAW11772.1, ECO:0000313|Proteomes:UP000006701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1
RC {ECO:0000313|Proteomes:UP000006701};
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; DS027052; EAW11772.1; -; Genomic_DNA.
DR RefSeq; XP_001273198.1; XM_001273197.1.
DR AlphaFoldDB; A1CFX3; -.
DR STRING; 344612.A1CFX3; -.
DR MEROPS; M28.001; -.
DR EnsemblFungi; EAW11772; EAW11772; ACLA_094720.
DR GeneID; 4704832; -.
DR KEGG; act:ACLA_094720; -.
DR VEuPathDB; FungiDB:ACLA_094720; -.
DR eggNOG; KOG2195; Eukaryota.
DR HOGENOM; CLU_024336_0_1_1; -.
DR OMA; PNYEYEV; -.
DR OrthoDB; 51543at2759; -.
DR Proteomes; UP000006701; 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 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:SF17; AMINOPEPTIDASE Y; 1.
DR PANTHER; PTHR12147; METALLOPEPTIDASE M28 FAMILY MEMBER; 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:EAW11772.1}; 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:UP000006701};
KW Signal {ECO:0000256|RuleBase:RU361240};
KW Zinc {ECO:0000256|RuleBase:RU361240}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|RuleBase:RU361240"
FT CHAIN 22..506
FT /note="Peptide hydrolase"
FT /evidence="ECO:0000256|RuleBase:RU361240"
FT /id="PRO_5005120939"
FT DOMAIN 148..231
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 260..469
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
SQ SEQUENCE 506 AA; 54392 MW; FDD63AB75508E47E CRC64;
MTITTSSLIA SVLALSGEVS ALQLPLFSSS EAQIPVAGQD LISSSALQSQ VNVDNLLRRA
EELYRIAELG QDEYNHPTRV IGSKGHLGTL DYIYATLQEF DDYYTISNQS FPAVTGNVLE
SRLVLGHSVP ESALPMGLTP PTKDNEPVYG PLVLVANLGC DAADYPANLT GAIAFISRGS
CPFGTKSALA GQAGAVAAVI YNNEKGGLGG TLGTPSPHHV ATFGISDRDA APFLDRLRHG
KSVDAIAYMD ATVETIMTTN IIAQTQAGDP DNCVMAGAHS DSVMEGPGIN DDGSGSLTLL
EVASLLPQYR VNNCVRLAWW AAEEEGLLGS DYYVSVLSEE ENLQIRLFMD YDMLASPNFA
YQVYNATNAV NPVGSEQLRD LYTEFYEAQG LNFTYIPFDG RSDYDAFIRN GIPGGGIATG
AEVIKTEEEQ RMFGGVAGDA FDPCYHQLCD DVGNVNRTAW EVNTKLVAHS IATYALSFEG
FPKRTGVASK AMEEKPRKYR GHALLF
//
