ID A0A1V8UGC2_9PEZI Unreviewed; 568 AA.
AC A0A1V8UGC2;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Alpha-MPP {ECO:0000256|ARBA:ARBA00030006};
DE AltName: Full=Inactive zinc metalloprotease alpha {ECO:0000256|ARBA:ARBA00032315};
GN ORFNames=B0A51_11604 {ECO:0000313|EMBL:OQO22462.1};
OS Rachicladosporium sp. CCFEE 5018.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Cladosporiales; Cladosporiaceae; Rachicladosporium.
OX NCBI_TaxID=1974281 {ECO:0000313|EMBL:OQO22462.1, ECO:0000313|Proteomes:UP000192386};
RN [1] {ECO:0000313|Proteomes:UP000192386}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCFEE 5018 {ECO:0000313|Proteomes:UP000192386};
RA Coleine C., Masonjones S., Stajich J.E.;
RT "Genomes of endolithic fungi from Antarctica.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Substrate recognition and binding subunit of the essential
CC mitochondrial processing protease (MPP), which cleaves the
CC mitochondrial sequence off newly imported precursors proteins.
CC {ECO:0000256|ARBA:ARBA00002123}.
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|RuleBase:RU004447}.
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:OQO22462.1}.
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DR EMBL; NAEU01000475; OQO22462.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V8UGC2; -.
DR STRING; 1974281.A0A1V8UGC2; -.
DR Proteomes; UP000192386; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; 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; IPR001431; Pept_M16_Zn_BS.
DR InterPro; IPR007863; Peptidase_M16_C.
DR PANTHER; PTHR11851; METALLOPROTEASE; 1.
DR PANTHER; PTHR11851:SF49; MITOCHONDRIAL-PROCESSING PEPTIDASE SUBUNIT ALPHA; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 2.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
DR PROSITE; PS00143; INSULINASE; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000192386}.
FT DOMAIN 54..201
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 207..269
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 346..466
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT REGION 16..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 251..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..267
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 568 AA; 62204 MW; 369D85E9CB2A13EA CRC64;
MSKSILAPAR VLRTATRAAR SAKRTRSYAT VTSTPSEKEP TDLDSITTLP NGLRVATEAL
PGHFSGIGVY VDAGSRYEND GLRGVSHIID RLAFKSTEQH TGDEVLEKID ALGGNIQCAS
SRESLMYQSA TFNSAVPEAV ALLAETIRSP KITEEEVERQ LETADYEIGE IWGKPELILP
ELVHMAAYKD NTLGNPLLCP KERLDSINKR TVEAYRKAFF KPERIVVAFA GVEHEEAVRL
AEQHFGDMKT PSLTTSTATQ AQQVQPPYPT SQMPPQKDPR LVSRLPFFKN LSTSASQKAT
ISAIDPSRII SHPLDEPIAY DAVSQYTGGF LTLPPLPIPA NPALPRVSHI HLAFEALPIN
SPDIYTLATL QTLLGGGGSF SAGGPGKGMY SRLYTNVLNQ YGWVENCMAF NHAYTDSGLF
GISAACGTTY VPRMLDTMAR ELSLLSAETG LGRLSETEVK RAKNQLRSSL LMNLESRMVE
LEDLGRQVQV HGRRVPVKEM VANIEAVTIK DLRRVAKQVF SGEVRNPGGG SGAPTVVLQQ
GEEEGVKFKE VGWEEIQERI GRFKLGRR
//
