ID F8NG20_SERL9 Unreviewed; 514 AA.
AC F8NG20;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=Alpha-MPP {ECO:0000256|ARBA:ARBA00030006};
DE AltName: Full=Inactive zinc metalloprotease alpha {ECO:0000256|ARBA:ARBA00032315};
GN ORFNames=SERLADRAFT_455468 {ECO:0000313|EMBL:EGO30990.1};
OS Serpula lacrymans var. lacrymans (strain S7.9) (Dry rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Coniophorineae; Serpulaceae; Serpula.
OX NCBI_TaxID=578457;
RN [1] {ECO:0000313|EMBL:EGO30990.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=S7.9 {ECO:0000313|EMBL:EGO30990.1};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Eastwood D.C., Floudas D., Binder M., Majcherczyk A., Schneider P.,
RA Aerts A., Asiegbu F.O., Baker S.E., Barry K., Bendiksby M., Blumentritt M.,
RA Coutinho P.M., Cullen D., Cullen D., Gathman A., Goodell B., Henrissat B.,
RA Ihrmark K., Kauserud H., Kohler A., LaButti K., Lapidus A., Lavin J.L.,
RA Lee Y.-H., Lindquist E., Lilly W., Lucas S., Morin E., Murat C.,
RA Oguiza J.A., Park J., Pisabarro A.G., Riley R., Rosling A., Salamov A.,
RA Schmidt O., Schmutz J., Skrede I., Stenlid J., Wiebenga A., Xie X.,
RA Kues U., Hibbett D.S., Hoffmeister D., Hogberg N., Martin F.,
RA Grigoriev I.V., Watkinson S.C.;
RT "Evolution of plant cell wall degrading machinery underlies the functional
RT diversity of forest fungi.";
RL Submitted (APR-2011) 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|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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DR EMBL; GL945428; EGO30990.1; -; Genomic_DNA.
DR RefSeq; XP_007312874.1; XM_007312812.1.
DR AlphaFoldDB; F8NG20; -.
DR GeneID; 18817176; -.
DR KEGG; sla:SERLADRAFT_455468; -.
DR HOGENOM; CLU_009902_5_2_1; -.
DR OrthoDB; 7099at2759; -.
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; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
DR PROSITE; PS00143; INSULINASE; 1.
PE 3: Inferred from homology;
FT DOMAIN 36..182
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 189..426
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 514 AA; 56513 MW; D273057146C97EEA CRC64;
MRKAPASLIR RSHGVSRRQY SQVLQPQITT LPNKIRVATE STPGHFSSVG LYVDAGSRYE
DLTTSGVSHF LDRMAFKSTR SRTDADMATA MDALGGQIMC SSSRESMMYQ SSHFHQATPL
ALSLISDTVL NPAFLEEEID VQRDAARYET REINGKPEMI LPEILHDVAY GGKALGNSLL
CSEERIDLIN ADLLRDTLTD WYRPERMVFA GAGMQHEQLV ELVDKYFSSL KCSPPLAPPS
ARTTPSQSVP PHLLPSTSPS LYKSLTRAAS SYLYPTSDPS ASPIDYHSRY VGGFRHIPST
TLEFDQLYVG YEGVGIHDDD IYDLATMQVL LGGGGSFSAG GPGKGMYSRL YTHILNHFPQ
IDHCASFHHI YTDSSLFGLF ASFVPNAPGQ RGNTPAQILP HLIHQLSLLI YQPVPKAELE
RAKNQLKSSL MMALESRAVE VEDLGRQILV HGRKIPITDM TAAIDQVTPE SVRRVANRLF
GPESANKASI VTMGRGDIGD WKSVLRKYGV AGGA
//