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Database: UniProt
Entry: F9X6A8_ZYMTI
LinkDB: F9X6A8_ZYMTI
Original site: F9X6A8_ZYMTI 
ID   F9X6A8_ZYMTI            Unreviewed;       354 AA.
AC   F9X6A8;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=Peptidase M48 domain-containing protein {ECO:0000259|Pfam:PF01435};
GN   ORFNames=MYCGRDRAFT_69961 {ECO:0000313|EMBL:EGP88862.1};
OS   Zymoseptoria tritici (strain CBS 115943 / IPO323) (Speckled leaf blotch
OS   fungus) (Septoria tritici).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX   NCBI_TaxID=336722 {ECO:0000313|EMBL:EGP88862.1, ECO:0000313|Proteomes:UP000008062};
RN   [1] {ECO:0000313|EMBL:EGP88862.1, ECO:0000313|Proteomes:UP000008062}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 115943 / IPO323 {ECO:0000313|Proteomes:UP000008062};
RX   PubMed=21695235; DOI=10.1371/journal.pgen.1002070;
RA   Goodwin S.B., Ben M'barek S., Dhillon B., Wittenberg A.H.J., Crane C.F.,
RA   Hane J.K., Foster A.J., Van der Lee T.A.J., Grimwood J., Aerts A.,
RA   Antoniw J., Bailey A., Bluhm B., Bowler J., Bristow J., van der Burgt A.,
RA   Canto-Canche B., Churchill A.C.L., Conde-Ferraez L., Cools H.J.,
RA   Coutinho P.M., Csukai M., Dehal P., De Wit P., Donzelli B.,
RA   van de Geest H.C., van Ham R.C.H.J., Hammond-Kosack K.E., Henrissat B.,
RA   Kilian A., Kobayashi A.K., Koopmann E., Kourmpetis Y., Kuzniar A.,
RA   Lindquist E., Lombard V., Maliepaard C., Martins N., Mehrabi R.,
RA   Nap J.P.H., Ponomarenko A., Rudd J.J., Salamov A., Schmutz J.,
RA   Schouten H.J., Shapiro H., Stergiopoulos I., Torriani S.F.F., Tu H.,
RA   de Vries R.P., Waalwijk C., Ware S.B., Wiebenga A., Zwiers L.-H.,
RA   Oliver R.P., Grigoriev I.V., Kema G.H.J.;
RT   "Finished genome of the fungal wheat pathogen Mycosphaerella graminicola
RT   reveals dispensome structure, chromosome plasticity, and stealth
RT   pathogenesis.";
RL   PLoS Genet. 7:E1002070-E1002070(2011).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU003983};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|RuleBase:RU003983};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004167}. Mitochondrion
CC       inner membrane {ECO:0000256|ARBA:ARBA00004434}; Single-pass membrane
CC       protein {ECO:0000256|ARBA:ARBA00004434}.
CC   -!- SIMILARITY: Belongs to the peptidase M48 family.
CC       {ECO:0000256|RuleBase:RU003983}.
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DR   EMBL; CM001198; EGP88862.1; -; Genomic_DNA.
DR   RefSeq; XP_003853886.1; XM_003853838.1.
DR   AlphaFoldDB; F9X6A8; -.
DR   STRING; 336722.F9X6A8; -.
DR   EnsemblFungi; Mycgr3T69961; Mycgr3P69961; Mycgr3G69961.
DR   GeneID; 13404224; -.
DR   KEGG; ztr:MYCGRDRAFT_69961; -.
DR   VEuPathDB; FungiDB:ZTRI_3.626; -.
DR   eggNOG; KOG2661; Eukaryota.
DR   HOGENOM; CLU_029002_1_0_1; -.
DR   InParanoid; F9X6A8; -.
DR   OMA; NVCRSED; -.
DR   OrthoDB; 5490879at2759; -.
DR   Proteomes; UP000008062; Chromosome 3.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:EnsemblFungi.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:EnsemblFungi.
DR   GO; GO:0035694; P:mitochondrial protein catabolic process; IEA:EnsemblFungi.
DR   GO; GO:0033108; P:mitochondrial respiratory chain complex assembly; IEA:EnsemblFungi.
DR   GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IEA:EnsemblFungi.
DR   GO; GO:0031929; P:TOR signaling; IEA:EnsemblFungi.
DR   CDD; cd07331; M48C_Oma1_like; 1.
DR   Gene3D; 3.30.2010.10; Metalloproteases ('zincins'), catalytic domain; 1.
DR   InterPro; IPR001915; Peptidase_M48.
DR   PANTHER; PTHR22726; METALLOENDOPEPTIDASE OMA1; 1.
DR   PANTHER; PTHR22726:SF1; METALLOENDOPEPTIDASE OMA1, MITOCHONDRIAL; 1.
DR   Pfam; PF01435; Peptidase_M48; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003983};
KW   Membrane {ECO:0000256|ARBA:ARBA00022792};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000256|RuleBase:RU003983};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003983};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008062};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003983}.
FT   DOMAIN          141..321
FT                   /note="Peptidase M48"
FT                   /evidence="ECO:0000259|Pfam:PF01435"
FT   REGION          21..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   354 AA;  39341 MW;  855C085BE7A056C4 CRC64;
     MSAPRILSAL FRPSSSRTFT STATSTFRSQ PSYRPRPSTQ WRTNPSSSRS YRRQAFNYQR
     FSTTKSYLRA WSQRPTFYYE VGGLGATCGG FYIYNLEPVA VTGRRRFNVV SPGREAEMGL
     QMYNQTLQEF SSKLLPAHSS EHRMVSRVLE RLIPHSGLSD EENKWELHVV DDPIPNAFVI
     PGGKVFVFRG ILDIARGEDG LAAVLGHEIA HNVAHHAAER MSRSFIILPF AVIGSLIVGL
     DVGIGNGLAK LAFELPGSRK EESEADYIGL LMMAQACFDP KAAIGLWQRM ESMEGKQGGA
     PPAFLSTHPS SHDRGEKIRG WLGKAEEVYQ RGECGGMGGY MSGFKEVTDF SRWS
//
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