ID A0A0D1YT38_9EURO Unreviewed; 1054 AA.
AC A0A0D1YT38;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Mitochondrial presequence protease {ECO:0008006|Google:ProtNLM};
GN ORFNames=PV11_09797 {ECO:0000313|EMBL:KIV78033.1};
OS Exophiala sideris.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=1016849 {ECO:0000313|EMBL:KIV78033.1, ECO:0000313|Proteomes:UP000053599};
RN [1] {ECO:0000313|EMBL:KIV78033.1, ECO:0000313|Proteomes:UP000053599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121828 {ECO:0000313|EMBL:KIV78033.1,
RC ECO:0000313|Proteomes:UP000053599};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala sideris CBS121828.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KN846954; KIV78033.1; -; Genomic_DNA.
DR EMBL; KN846954; KIV78034.1; -; Genomic_DNA.
DR STRING; 1016849.A0A0D1YT38; -.
DR HOGENOM; CLU_006065_0_0_1; -.
DR OrthoDB; 227593at2759; -.
DR Proteomes; UP000053599; 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:UP000053599}.
FT DOMAIN 58..141
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 198..375
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT REGION 1010..1054
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1023..1054
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1054 AA; 117405 MW; 28D2FC4C290B92DF CRC64;
MVASRANPRF RHLQKISPDY SPSTITQYES ERTGMRVVVV DQEGPKLHGY FVLATEIHDD
SGAPHTLEHL CFMGSKSYKY KGFLDKLATR AYSNTNAWTA TDHTAYTLET AGWAGFAQIL
PVYLEHVILP TLTDAGCTTE VHHIDGDGND AGVVYSEMQG VQNMASELIE LRSKRILYPE
GVGFRYETGG MMEQLRVLTS DRIRQFHHDM YQPRNLCLAL FGEVNHKELL AILDDFESSI
ISDIPSPDAP FKRPWIDSKH TPALTKSTLE RVEFPEEDES FGEVDIRFLG PDCSDALPTA
ALSVALLYLA GSSAAVLDNA LVEKEQLASG VYFTVDSRPR TEIAFSMSGV ETGRLEEVEK
RFFEVLNEAV EKPLDMKFMR DCIDRQVRTY KFNAEATPTA FADAIISDYL FGKRDGSTLA
SLQSLEQYTK ALVSWSELQW KDFLKQYISD APHVSILGVP STRLSEKLKT DEASRIEQQK
SKLGPDGLKK MQEKLDQAKA ENDLEIPRDL LGQFKVPSTD SIHFVTTSGA RAGLALEVGK
PKNRYQNVID NDAGHVALFL DFEHIPTNFA RVNMIISTET LPDELRPLLS IYMEAFFNLP
VKRGSKVIDF EQVVVELERD TVGYNIDSAG SLGNSEGIRV SFQVEIEKYK VAIKWLSELL
YNSVFDVERL KAINTRLLAD VPDAKRSGDD MMTAVRVMTH LAPKSIGRAR STLVKALYLK
RLKQLLATDP DQVVRQLERL RGHLCRFENY RVLVITDLDQ VQEPVSAWAS FLEGMETNRK
LAPIGKRIER LSEAGENPGK LAYVVPMPTI DSSFAYAAAR GPTSYDDPKM PAVMVAMAYM
NAVEGPLWVA VRGTGLAYGT NMGYDIDSGY IHLDVYRSPD AYKAFEASQK VVRGHMGGEI
EFDPLMLEGA ISSIVVAFAN EQQTLASAAG ASFVRAIMKG LPEDHMERLL KKVRAVEVED
IKDALKSVVY DMFTPGKADI FITCAPGLKQ AIADGLRGAG FSPEIHDLNH FQDDYGLKPT
NGDDENDDEE DDEEDEDGDE EDDESEDIGG SEGF
//