ID S8AJG0_DACHA Unreviewed; 1059 AA.
AC S8AJG0;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=Mitochondrial presequence protease {ECO:0008006|Google:ProtNLM};
GN ORFNames=H072_2916 {ECO:0000313|EMBL:EPS43054.1};
OS Dactylellina haptotyla (strain CBS 200.50) (Nematode-trapping fungus)
OS (Monacrosporium haptotylum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Dactylellina.
OX NCBI_TaxID=1284197 {ECO:0000313|EMBL:EPS43054.1, ECO:0000313|Proteomes:UP000015100};
RN [1] {ECO:0000313|EMBL:EPS43054.1, ECO:0000313|Proteomes:UP000015100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 200.50 {ECO:0000313|EMBL:EPS43054.1,
RC ECO:0000313|Proteomes:UP000015100};
RX PubMed=24244185;
RA Meerupati T., Andersson K.M., Friman E., Kumar D., Tunlid A., Ahren D.;
RT "Genomic mechanisms accounting for the adaptation to parasitism in
RT nematode-trapping fungi.";
RL PLoS Genet. 9:E1003909-E1003909(2013).
RN [2] {ECO:0000313|Proteomes:UP000015100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 200.50 {ECO:0000313|Proteomes:UP000015100};
RA Ahren D.G.;
RT "Genomic mechanisms accounting for the adaptation to parasitism in
RT nematode-trapping fungi.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
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:EPS43054.1}.
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DR EMBL; AQGS01000089; EPS43054.1; -; Genomic_DNA.
DR RefSeq; XP_011108901.1; XM_011110599.1.
DR AlphaFoldDB; S8AJG0; -.
DR STRING; 1284197.S8AJG0; -.
DR eggNOG; KOG0961; Eukaryota.
DR HOGENOM; CLU_006065_0_0_1; -.
DR OMA; CVEGPFW; -.
DR OrthoDB; 227593at2759; -.
DR Proteomes; UP000015100; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 4.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR007863; Peptidase_M16_C.
DR PANTHER; PTHR43016:SF16; METALLOPROTEASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_4G07610)-RELATED; 1.
DR PANTHER; PTHR43016; PRESEQUENCE PROTEASE; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000015100}.
FT DOMAIN 67..145
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 204..382
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT REGION 1017..1059
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1026..1051
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1059 AA; 117722 MW; 999E3669426D2DFE CRC64;
MAGQMKMGGG GQSSHFKTVT KFTTDYSPTD ITKYESTRTG MSVVVVNKES PKVLGFFALA
TEILDDSGAP HTLEHLCFMG SKNYRFKGIL DKFATRAYST TNAWTATDHT AYTLDTAGWE
GFAQILPVYL EHILFPILTD SGCYTEVHHI DATGHDAGVV YSEMQGVQNE ADTLVSLEAN
RQLYPNGIGF RSETGGMMEQ LRVLTADRIR EFHKDMYQPR NLCLVIIGSI NEPELLDILD
KFEDGIVDHV PKPDSPWKRP WVDSTPAPML KDNILRVVEF PEKDESMGSV TVGYLGPSCV
DPKHMAALDV IGTYLAGSSV SILEKQMVEI PDPYTTGVIW YTEERPNTVI WFELGSVPVK
RLEETEAKLF EVLSQTIKEP LDLDYLRDCL HRSKRQRKSN VENSSNHFAS PVIYDFLFAS
RDGKDLNQLG SLTVYEELEQ WTEEEWRSYI KKWLVDNPHV SVIGKPSAKL AEKIKNDEKD
RVQKQIESLG EEGLKKLAEK LEQAKKDNDP EIPIDVLRGF KTPGVESIKF IHSTSGTAGL
ATSEGPHATN IQNILDGDKP STNPLPLYLH FEHVPSNFVT IIVLLSTKSI PVNLRPLVLL
YFEYLFAAPI VLEDGTKLEY EKVVSLLEKD TVDYGIQGGS GMQASESVRV KMEVEPEKYS
AAIRWLRLVM WNIVFDTERL AVLAKKLRSD IPEEKRSGND MVWSLAYLSG YTSESIGYCG
NTLIKGRFLK QYIELLETKP EEATAQITAF RDGLFTLDNM RVLVVADVEK LPKPVSSWDD
FVAGRSPGGK LKPIDSRLDR LSDVGKNPGN LMYVVPMPTL DSSFSVSVAK GPSSLADPRI
PALLLAMAYL DAVEGPLWRA IRGTGLAYGT GFSRKADSGH MFFSVYRSPD AFKAFEMAKK
IVGEYADGTT QFDEFDLDGA ISGVVSGVVD IEATLASAAT TSFVLQAIQG QSKDYYAEML
RKVRVVTPDE IRKAMKDILL PLFEPDTAVV IVTTATVNTE SLEERFKATG FPVQVKKLSS
FEPKGEGENE DEDEDEGSDD GDDDEDMESG SEGDAEEKK
//