ID H1VL60_COLHI Unreviewed; 514 AA.
AC H1VL60;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Mitochondrial presequence protease {ECO:0000313|EMBL:CCF40963.1};
GN ORFNames=CH063_11388 {ECO:0000313|EMBL:CCF40963.1};
OS Colletotrichum higginsianum (strain IMI 349063) (Crucifer anthracnose
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum destructivum species complex.
OX NCBI_TaxID=759273 {ECO:0000313|EMBL:CCF40963.1, ECO:0000313|Proteomes:UP000007174};
RN [1] {ECO:0000313|Proteomes:UP000007174}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMI 349063 {ECO:0000313|Proteomes:UP000007174};
RX PubMed=22885923; DOI=10.1038/ng.2372;
RA O'Connell R.J., Thon M.R., Hacquard S., Amyotte S.G., Kleemann J.,
RA Torres M.F., Damm U., Buiate E.A., Epstein L., Alkan N., Altmueller J.,
RA Alvarado-Balderrama L., Bauser C.A., Becker C., Birren B.W., Chen Z.,
RA Choi J., Crouch J.A., Duvick J.P., Farman M.A., Gan P., Heiman D.,
RA Henrissat B., Howard R.J., Kabbage M., Koch C., Kracher B., Kubo Y.,
RA Law A.D., Lebrun M.-H., Lee Y.-H., Miyara I., Moore N., Neumann U.,
RA Nordstroem K., Panaccione D.G., Panstruga R., Place M., Proctor R.H.,
RA Prusky D., Rech G., Reinhardt R., Rollins J.A., Rounsley S., Schardl C.L.,
RA Schwartz D.C., Shenoy N., Shirasu K., Sikhakolli U.R., Stueber K.,
RA Sukno S.A., Sweigard J.A., Takano Y., Takahara H., Trail F.,
RA van der Does H.C., Voll L.M., Will I., Young S., Zeng Q., Zhang J.,
RA Zhou S., Dickman M.B., Schulze-Lefert P., Ver Loren van Themaat E.,
RA Ma L.-J., Vaillancourt L.J.;
RT "Lifestyle transitions in plant pathogenic Colletotrichum fungi deciphered
RT by genome and transcriptome analyses.";
RL Nat. Genet. 44:1060-1065(2012).
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000256|ARBA:ARBA00004305}.
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DR EMBL; CACQ02004407; CCF40963.1; -; Genomic_DNA.
DR AlphaFoldDB; H1VL60; -.
DR STRING; 759273.H1VL60; -.
DR MEROPS; M16.A19; -.
DR EnsemblFungi; CCF40963; CCF40963; CH063_11388.
DR VEuPathDB; FungiDB:CH63R_04061; -.
DR eggNOG; KOG2019; Eukaryota.
DR HOGENOM; CLU_529972_0_0_1; -.
DR Proteomes; UP000007174; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 2.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR007863; Peptidase_M16_C.
DR PANTHER; PTHR43016; PRESEQUENCE PROTEASE; 1.
DR PANTHER; PTHR43016:SF13; PRESEQUENCE PROTEASE, MITOCHONDRIAL; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:CCF40963.1};
KW Protease {ECO:0000313|EMBL:CCF40963.1};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 71..160
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 224..410
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 514 AA; 57407 MW; 365222D79578AF8B CRC64;
MLRNAVNTAK KAVTELSQYP KPGDKLHGFT LLRTKHVPEL ELTALHLQHD KTGADYLHIA
RDDSNNVFSI GFKTNPPDDT GVPHILEHTT LCGSQKFPIR DPFFKMLPRT LSNFMNAFTA
SDHTFYPFAT TNAQDFKNLM SVYMDATLHP LLKESDYTQE GWRIGPENPQ AASGEESNLV
FKGVVYNEMK GQMSDAGYLF YIRFQDHIFP DINNSGGDPQ KITDLTYEQL RKFHAEHYHP
SNAKLFTYGD MPLSDHLQEV NAQLSAFERI QEDKTIHQPI DLSSGPREVT AKGPLDPLVD
PDRQYKTSVS WIMGDTSDVV ESFSLALLST LLMDGYGSPL YRGLVEAGLG TDFSPNAGYD
SSAKLGIFSI GLTGVQEADV PKLKAEAQRI LQEVRQKGFD RTKIDGSLHQ LELALKHKTA
NFGMNMLHRL KPKWFTGVDP FDSLAWNDTI SAFETQLAKG GYLESLIEKY LLNDNTLSFT
MSPSTTFSED LGLATKTHVD AEAELETNDS ASPH
//
