ID E9QRW5_ASPFU Unreviewed; 581 AA.
AC E9QRW5;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=Alpha-MPP {ECO:0000256|ARBA:ARBA00030006};
DE AltName: Full=Inactive zinc metalloprotease alpha {ECO:0000256|ARBA:ARBA00032315};
GN ORFNames=AFUA_1G11870 {ECO:0000313|EMBL:EAL90515.1};
OS Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 /
OS Af293) (Neosartorya fumigata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879 {ECO:0000313|EMBL:EAL90515.1, ECO:0000313|Proteomes:UP000002530};
RN [1] {ECO:0000313|EMBL:EAL90515.1, ECO:0000313|Proteomes:UP000002530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100
RC {ECO:0000313|Proteomes:UP000002530};
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.,
RA Fedorova N., Fedorova N., Feldblyum T.V., Fischer R., Fosker N., Fraser A.,
RA Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B., Haas H., Harris D., Horiuchi H.,
RA Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K.,
RA Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafon A., Latge J.P.,
RA Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y.,
RA Molina M., Monod M., Mouyna I., Mulligan S., Murphy L., O'Neil S.,
RA Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A.,
RA Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H.,
RA Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M.,
RA Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D.,
RA Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G.,
RA Vazquez de Aldana C.R., Weidman J., White O., Woodward J., Yu J.H.,
RA Fraser C., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.,
RA Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
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:EAL90515.1}.
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DR EMBL; AAHF01000004; EAL90515.1; -; Genomic_DNA.
DR RefSeq; XP_752553.1; XM_747460.1.
DR AlphaFoldDB; E9QRW5; -.
DR STRING; 330879.E9QRW5; -.
DR EnsemblFungi; EAL90515; EAL90515; AFUA_1G11870.
DR GeneID; 3510432; -.
DR KEGG; afm:AFUA_1G11870; -.
DR VEuPathDB; FungiDB:Afu1g11870; -.
DR eggNOG; KOG2067; Eukaryota.
DR HOGENOM; CLU_009902_5_2_1; -.
DR InParanoid; E9QRW5; -.
DR OMA; LKYHHSP; -.
DR OrthoDB; 7099at2759; -.
DR Proteomes; UP000002530; Chromosome 1.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006627; P:protein processing involved in protein targeting to mitochondrion; IBA:GO_Central.
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 Hydrolase {ECO:0000313|EMBL:EAL90515.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002530}.
FT DOMAIN 49..196
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 202..272
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 359..479
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT REGION 266..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 581 AA; 63651 MW; 9A4B606A134AF45E CRC64;
MRRSVLRAIE SAKPLARVPR SASRSFATLN ESKDPAELDQ ITTLPNGIRV ATESLPGPFA
GVGVYVDAGS RYEDESLRGV SHIMDRLAFK STKSRTSDEM LETLESLGGN IQCASSRESL
MYQSASFNSA VPATLGLLAE TIRDPLITDE EVLQQLATAE YEINEIWAKP ELILPELVHM
AAYKDNTLGN PLLCPRERLE EINKAVVERY REVFFKPERM VVAFAGVPHE EAVKLTEQYF
GDMKAANQAK GPVLSGTGIE TTLSDSETAA QEGQVPTVPQ FTPSSTITTT PTSKTQSVLS
RLPFLKNLST TASKPASVAP LDPSLVQPSS LDLTRPSHYT GGFLSLPPIP PPANPMLPRL
SYIHLAFEAL PISSPDIYAL ATLQTLLGGG GSFSAGGPGK GMYSRLYTNV LNQHGWVESC
IAFNHSYTDS GIFGISASCS PTRTTEMLEV MCRELQALTL DTGYSALQPQ EVNRAKNQLR
SSLLMNLESR MVELEDLGRQ VQVHGHKVGV KEMCDRIEAL TVDDLRRVAR HVFGGHVQNK
GQGTGIPTVV LQEGELEGYK LRPFPWEEIQ ERIARWKLGR R
//
