ID A0A168G9A1_CORDF Unreviewed; 408 AA.
AC A0A168G9A1;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Amidohydrolase {ECO:0000313|EMBL:OAA76196.1};
GN ORFNames=LEL_05880 {ECO:0000313|EMBL:OAA76196.1};
OS Akanthomyces lecanii RCEF 1005.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Akanthomyces;
OC Cordyceps confragosa.
OX NCBI_TaxID=1081108 {ECO:0000313|EMBL:OAA76196.1, ECO:0000313|Proteomes:UP000076881};
RN [1] {ECO:0000313|EMBL:OAA76196.1, ECO:0000313|Proteomes:UP000076881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 1005 {ECO:0000313|EMBL:OAA76196.1,
RC ECO:0000313|Proteomes:UP000076881};
RX PubMed=27071652; DOI=10.1093/gbe/evw082;
RA Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT "Divergent and convergent evolution of fungal pathogenicity.";
RL Genome Biol. Evol. 8:1374-1387(2016).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the peptidase M20A family.
CC {ECO:0000256|ARBA:ARBA00006247}.
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:OAA76196.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AZHF01000004; OAA76196.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A168G9A1; -.
DR OrthoDB; 3684955at2759; -.
DR Proteomes; UP000076881; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR017439; Amidohydrolase.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR NCBIfam; TIGR01891; amidohydrolases; 1.
DR PANTHER; PTHR11014:SF63; METALLOPEPTIDASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G09600)-RELATED; 1.
DR PANTHER; PTHR11014; PEPTIDASE M20 FAMILY MEMBER; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR PIRSF; PIRSF005962; Pept_M20D_amidohydro; 1.
DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:OAA76196.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000076881};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 187..279
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 408 AA; 44222 MW; F006434CB5C44D61 CRC64;
MLYFRNVYRQ LHEMPELSGM ERETAQRAAD FLSSLKFFQV HTGIGGYGVV GVFRNGDGPK
LLLRADMDAL PLKEETGLSY ASKKVMKDRF GQEKPVMHAC GQDTHVASLM AVAKLLVDAR
GHWQGTLVCL FQPSEEHLNG AQAMVDDALY ESGRIPRPDV VLAQHVDNDP CGRITMKSGP
ALTASSTLAV RIFGRGGHGS SPQDCVDPIV IGCSTVAKLQ TIVSREIDPN QLAVVTCGSI
HAGDAPNIIP EYLDLTINIR SLSPIIHSRI LDAIGRIVEG ECRTSGCDRP PTITTLQSSP
VTINDESTFE ILKGSFSSYF GTDFTEMDVA TASEDVSILA TAAGAPLVMW FFGGSNSTKW
NDAKERGKLE EIPQNHSELF APVIECLDVA VDAMALAALT LFTSRHRS
//
