ID A0A0N7L932_9BASI Unreviewed; 517 AA.
AC A0A0N7L932;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Peptide hydrolase {ECO:0000256|RuleBase:RU361240};
DE EC=3.4.-.- {ECO:0000256|RuleBase:RU361240};
OS Ceraceosorus bombacis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Exobasidiomycetes; Ceraceosorales; Ceraceosoraceae; Ceraceosorus.
OX NCBI_TaxID=401625 {ECO:0000313|EMBL:CEH12658.1, ECO:0000313|Proteomes:UP000054845};
RN [1] {ECO:0000313|EMBL:CEH12658.1, ECO:0000313|Proteomes:UP000054845}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Magalhaes I.L.F., Oliveira U., Santos F.R., Vidigal T.H.D.A.,
RA Brescovit A.D., Santos A.J.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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; CCYA01000181; CEH12658.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N7L932; -.
DR STRING; 401625.A0A0N7L932; -.
DR OrthoDB; 51543at2759; -.
DR Proteomes; UP000054845; 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; 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:CEH12658.1}; Hydrolase {ECO:0000256|RuleBase:RU361240};
KW Metal-binding {ECO:0000256|RuleBase:RU361240};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU361240};
KW Reference proteome {ECO:0000313|Proteomes:UP000054845};
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..517
FT /note="Peptide hydrolase"
FT /evidence="ECO:0000256|RuleBase:RU361240"
FT /id="PRO_5005962245"
FT DOMAIN 142..230
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 257..471
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
SQ SEQUENCE 517 AA; 54702 MW; E2B3CA7719D637B5 CRC64;
MRLSTFLTAV VAGTAVSVAL PQSSDVSSDS SRLLPGFPGF NFPKPLVSSI VLRNLITRRD
LSSKAQTLQR FADASPGRNR VFGSPGHNAT VNWLYDELVK LDAYDVYLQP FTETYAENSA
KVTVDAVDQG AGPFTYAPGG QVTEQLVQVA NVGCAASDFP AAVSGKIALI SRGTCPFASK
VGLAGAAGAK AALIYNNADG ALSGTLGGTS TPEGPYVPVA SLDKARGDAL VGRLAAGETV
TAALDIVGIT EDRETYNVIA QTRTGDPNEV YFVGSHTDSV IAGPGINDNG SGTISLLTIA
QKLKNFRTNK AIRFGFWSAE EFGLLGAEHY VRTLSTEERN KIRVYGNFDM VASPNYVYGV
YDGSGRAFNI TGPAGSTEGQ DLLQSYFRSQ RLNTVPSGFD GRSDYGPFLE ANIACLGLFT
GAEELKTEEE ARLFGGQAGV ALDANYHKAG DDINNLNYDA FLANAKAIAH TIATYGRGFQ
SLPPKEQAVP QPQLRIANAQ HAHKGSIKRC GETLLEA
//
