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Database: UniProt
Entry: F8NG20_SERL9
LinkDB: F8NG20_SERL9
Original site: F8NG20_SERL9 
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
//
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