ID A0A1E4SX98_9ASCO Unreviewed; 464 AA.
AC A0A1E4SX98;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=mitochondrial processing peptidase {ECO:0000256|ARBA:ARBA00012299};
DE EC=3.4.24.64 {ECO:0000256|ARBA:ARBA00012299};
DE AltName: Full=Beta-MPP {ECO:0000256|ARBA:ARBA00031018};
GN ORFNames=CANARDRAFT_29306 {ECO:0000313|EMBL:ODV84135.1};
OS [Candida] arabinofermentans NRRL YB-2248.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Ogataea; Ogataea/Candida clade.
OX NCBI_TaxID=983967 {ECO:0000313|EMBL:ODV84135.1, ECO:0000313|Proteomes:UP000094801};
RN [1] {ECO:0000313|Proteomes:UP000094801}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL YB-2248 {ECO:0000313|Proteomes:UP000094801};
RG DOE Joint Genome Institute;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goker M.,
RA Salamov A., Wisecaver J., Long T.M., Aerts A.L., Barry K., Choi C.,
RA Clum A., Coughlan A.Y., Deshpande S., Douglass A.P., Hanson S.J.,
RA Klenk H.-P., Labutti K., Lapidus A., Lindquist E., Lipzen A.,
RA Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J., Peng Y.,
RA Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C., Stielow J.B.,
RA Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V., Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of N-terminal transit peptides from precursor proteins
CC imported into the mitochondrion, typically with Arg in position P2.;
CC EC=3.4.24.64; Evidence={ECO:0000256|ARBA:ARBA00001098};
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DR EMBL; KV453858; ODV84135.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E4SX98; -.
DR STRING; 983967.A0A1E4SX98; -.
DR OrthoDB; 167798at2759; -.
DR Proteomes; UP000094801; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
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; PTHR11851:SF149; GH01077P; 1.
DR PANTHER; PTHR11851; METALLOPROTEASE; 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 Reference proteome {ECO:0000313|Proteomes:UP000094801}.
FT DOMAIN 41..188
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 194..382
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 464 AA; 51422 MW; F280E0B15F1614CF CRC64;
MLRLASRELK RNFKFARSLA SAAVSAVPTT KTTVLKNGLT VATEEIPNSL TATVGVWIDA
GSRADVTDST SGTAHFLEHL AFKGTNTRTQ LNLELEVENC GSHLNAYTSR ENTVYYAKSL
RDDIPRAVDI LSDILTRSKL EKIAIEKERP VIIRESEEVD KMYDEVIFDR LHEIVFKDQP
LGRTILGPLE NIRSITQQDL KNYIKTNYKG DRMVLVGAGA VKHEELVSLA QRSFGHVPIS
SNPLPLGTPR SNIPKFYGDE IKIKDESLPN TYMALCVEGC SWSSNDYFKA LVTQAIVGNW
DRATNSSVSP LSQSISNNGE PLCNSFMSFS TSYSDTGLWG IYIVADKTAD CKPLIDSVLN
EWERLRKGSI TNEEVETAKS QLKGSLLLSL DGTTAIAEDI GRQLVTTGER LTPESIFQIV
NDITKSDIVD WCERYLQDKS VGLAALGSID SIPDHKYIND GMKR
//