ID W9X501_9EURO Unreviewed; 1022 AA.
AC W9X501;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Presequence protease, mitochondrial {ECO:0000256|ARBA:ARBA00020167};
DE AltName: Full=Pitrilysin metalloproteinase {ECO:0000256|ARBA:ARBA00034552};
GN ORFNames=A1O7_01875 {ECO:0000313|EMBL:EXJ65534.1};
OS Cladophialophora yegresii CBS 114405.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=1182544 {ECO:0000313|EMBL:EXJ65534.1, ECO:0000313|Proteomes:UP000019473};
RN [1] {ECO:0000313|EMBL:EXJ65534.1, ECO:0000313|Proteomes:UP000019473}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 114405 {ECO:0000313|EMBL:EXJ65534.1,
RC ECO:0000313|Proteomes:UP000019473};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Cladophialophora yegresii CBS 114405.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Degrades mitochondrial transit peptides after their cleavage
CC in the intermembrane space or in the matrix, and presequence peptides;
CC clearance of these peptides is required to keep the presequence
CC processing machinery running (By similarity). Preferentially cleaves
CC the N-terminal side of paired basic amino acid residues (By
CC similarity). Also degrades other unstructured peptides (By similarity).
CC May function as an ATP-dependent peptidase as opposed to a
CC metalloendopeptidase. {ECO:0000256|ARBA:ARBA00034467}.
CC -!- SUBUNIT: Monomer and homodimer; homodimerization is induced by binding
CC of the substrate. {ECO:0000256|ARBA:ARBA00011853}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space
CC {ECO:0000256|ARBA:ARBA00004569}. Mitochondrion matrix
CC {ECO:0000256|ARBA:ARBA00004305}.
CC -!- SIMILARITY: Belongs to the peptidase M16 family. PreP subfamily.
CC {ECO:0000256|ARBA:ARBA00007575}.
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:EXJ65534.1}.
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DR EMBL; AMGW01000001; EXJ65534.1; -; Genomic_DNA.
DR RefSeq; XP_007754101.1; XM_007755911.1.
DR AlphaFoldDB; W9X501; -.
DR STRING; 1182544.W9X501; -.
DR MEROPS; M16.013; -.
DR GeneID; 19176486; -.
DR VEuPathDB; FungiDB:A1O7_01875; -.
DR eggNOG; KOG2019; Eukaryota.
DR HOGENOM; CLU_009165_0_0_1; -.
DR OrthoDB; 5477696at2759; -.
DR Proteomes; UP000019473; Unassembled WGS sequence.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; 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 InterPro; IPR013578; Peptidase_M16C_assoc.
DR PANTHER; PTHR43016; PRESEQUENCE PROTEASE; 1.
DR PANTHER; PTHR43016:SF13; PRESEQUENCE PROTEASE, MITOCHONDRIAL; 1.
DR Pfam; PF08367; M16C_assoc; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 2.
DR SMART; SM01264; M16C_associated; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000019473}.
FT DOMAIN 489..747
FT /note="Peptidase M16C associated"
FT /evidence="ECO:0000259|SMART:SM01264"
SQ SEQUENCE 1022 AA; 114119 MW; 8171FFAFAEBD6190 CRC64;
MLRHGVRRCA GPHLPRRGYA SVTDLEAYPK SGESIHGFTL KQIKHVPELH LTALRLEHDK
TGAEYLHVAR DDKNNVFAIN FKTNPTDRTG LPHILEHVTL CGSQKYPVRD PFFKMMPRSL
ANFMNAFTSS DYTSYPFATT NLQDFRNLSS VYLDATLHPL LKRSDFLQEG WRLGPEDPRE
PATEDNVKFK GVVYNEMKGQ MSDASYLFYI RFREHLFPSL HNSGGDPEVM TQLTHEQLVD
FSRTHYHPSN AKIFSYGSLS LPEHLQHVDE AISQFEKAAP DSDIKTPISF SDGPLSFEVS
GPVDTMQPPD RQLKSSITWM GCSSADIVET FSVSIMLSLL MNGYGSPLYQ GLIESGLGTT
FSPNSGYDSS AAVGVFSVGL DGMQAEDVAG LKETIQTILR EKAHEAFQQH KIDGYMHQLE
LTLKHKTANF GMGLLEKSLA GWFNGVNPMD SLAWNQIIDT FKQRMTEEKY LERLVEKYLL
NDNCMQFTMK PDDTYGAALE SREEERRKNI LADIKRSASS PEASLSELGQ QELELLEEQE
SAQHKNLDTL PTLRVSDIVR EKERKPRYHS KIGDVDVLWR ETETNGITYF QAKHLLTDLP
EELRLLMPLF TDSLMRLGTK TKSVGDLEAE ILLRTGGISV SSFVAPEPWS LDNYHEGVLL
DGYALDRNVP AMFDLMWTLL TEIDFSSPKA VAAIRELLEA RASGALDTVA ESGHHFAITS
ASAALTQRGR LQDQLSGLSQ IESTAKILDA ARRDPQSLEQ VIQKLKTIQS IAVANSSKLS
MRIVCEPSSV KTNQGLIEGF LAQLPQNNSS AANSTSSNAV AGSSLSRRAF FSLPFQVSYT
GTCLQTAPYS SPDKAPLTVL GQLLVHNFMH PEIREKGGAY GASASASPIS GLFTMSSYRD
PNPRNSLSVF NRAGLYARDK DWSARELEES KLSIFQGIDA PRSVSSEASK EFMYGITEEM
DQQMRERLLG VTKDDVQRVA QQYLVDLPSD QKSVCVLGEK KDWVEQDQEQ WQVKSLNMSA
ES
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