ID G1XRH0_ARTOA Unreviewed; 477 AA.
AC G1XRH0;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Peptide hydrolase {ECO:0000256|RuleBase:RU361240};
DE EC=3.4.-.- {ECO:0000256|RuleBase:RU361240};
GN ORFNames=AOL_s00193g169 {ECO:0000313|EMBL:EGX44257.1};
OS Arthrobotrys oligospora (strain ATCC 24927 / CBS 115.81 / DSM 1491)
OS (Nematode-trapping fungus) (Didymozoophaga oligospora).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Orbilia; Orbilia oligospora.
OX NCBI_TaxID=756982 {ECO:0000313|EMBL:EGX44257.1, ECO:0000313|Proteomes:UP000008784};
RN [1] {ECO:0000313|EMBL:EGX44257.1, ECO:0000313|Proteomes:UP000008784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24927 / CBS 115.81 / DSM 1491
RC {ECO:0000313|Proteomes:UP000008784};
RX PubMed=21909256; DOI=10.1371/journal.ppat.1002179;
RA Yang J., Wang L., Ji X., Feng Y., Li X., Zou C., Xu J., Ren Y., Mi Q.,
RA Wu J., Liu S., Liu Y., Huang X., Wang H., Niu X., Li J., Liang L., Luo Y.,
RA Ji K., Zhou W., Yu Z., Li G., Liu Y., Li L., Qiao M., Feng L., Zhang K.-Q.;
RT "Genomic and proteomic analyses of the fungus Arthrobotrys oligospora
RT provide insights into nematode-trap formation.";
RL PLoS Pathog. 7:E1002179-E1002179(2011).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M28 family.
CC {ECO:0000256|RuleBase:RU361240}.
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:EGX44257.1}.
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DR EMBL; ADOT01000288; EGX44257.1; -; Genomic_DNA.
DR RefSeq; XP_011127082.1; XM_011128780.1.
DR AlphaFoldDB; G1XRH0; -.
DR STRING; 756982.G1XRH0; -.
DR GeneID; 22897976; -.
DR eggNOG; KOG2195; Eukaryota.
DR HOGENOM; CLU_024336_1_1_1; -.
DR InParanoid; G1XRH0; -.
DR OMA; HLEINTK; -.
DR OrthoDB; 458841at2759; -.
DR Proteomes; UP000008784; Unassembled WGS sequence.
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 Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR045175; M28_fam.
DR InterPro; IPR007484; Peptidase_M28.
DR PANTHER; PTHR12147; METALLOPEPTIDASE M28 FAMILY MEMBER; 1.
DR PANTHER; PTHR12147:SF55; PEPTIDE HYDROLASE; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW 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:UP000008784};
KW Signal {ECO:0000256|RuleBase:RU361240};
KW Zinc {ECO:0000256|RuleBase:RU361240}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|RuleBase:RU361240"
FT CHAIN 21..477
FT /note="Peptide hydrolase"
FT /evidence="ECO:0000256|RuleBase:RU361240"
FT /id="PRO_5005131298"
FT DOMAIN 248..449
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
SQ SEQUENCE 477 AA; 52800 MW; A1920E5CBE3621E8 CRC64;
MKVSHSTAIL LCAAIASAHP ASFTSEKFQS LISQKSLLSD LKAFDQIASN NNGNRAFGEP
GYVASVNHVK SRLDKSSRFK SWTQKFETPS SNIEHLRLTV NGKSYNLKMP LGWAGGEARD
LDITAPLAVL DWGSPGTCEH PYYNNNTDTT GKIVLNRWVN CHNPGKHSPH VDMSSSSLGY
IFYEDNYEPL GVSKRSVPNM VKREEHPFSF IYMSRADGIE LTRRLHAGEE LIARFQYKTS
PVKIESQNVI AETKAGDPNK VILLGAHLDS GVNSPGINDN ASGAALLLAL FDAINQGKFK
PKNKIRFAWW AGGQEYLNFG SSHYVLNLSK KEADNILLYL NFDMVSRGHF GVYDGDGSRY
GYYGYPGSEI IEKLFEDYFT AMGLPVRPVH WHGDSDYYSF MSPDLLIKPV GGLHGGDGLL
DDACWQQTCD NLANANVTHL EINTKAAAHA LYVLSQTYKE VIPLVPYNHT AAQMAGY
//
