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Database: UniProt
Entry: M2QYJ2_CERS8
LinkDB: M2QYJ2_CERS8
Original site: M2QYJ2_CERS8 
ID   M2QYJ2_CERS8            Unreviewed;      1065 AA.
AC   M2QYJ2;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   13-SEP-2023, entry version 31.
DE   RecName: Full=Mitochondrial presequence protease {ECO:0008006|Google:ProtNLM};
GN   ORFNames=CERSUDRAFT_79827 {ECO:0000313|EMBL:EMD42233.1};
OS   Ceriporiopsis subvermispora (strain B) (White-rot fungus) (Gelatoporia
OS   subvermispora).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Gelatoporiaceae; Gelatoporia.
OX   NCBI_TaxID=914234 {ECO:0000313|EMBL:EMD42233.1, ECO:0000313|Proteomes:UP000016930};
RN   [1] {ECO:0000313|EMBL:EMD42233.1, ECO:0000313|Proteomes:UP000016930}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B {ECO:0000313|EMBL:EMD42233.1,
RC   ECO:0000313|Proteomes:UP000016930};
RX   PubMed=22434909; DOI=10.1073/pnas.1119912109;
RA   Fernandez-Fueyo E., Ruiz-Duenas F.J., Ferreira P., Floudas D.,
RA   Hibbett D.S., Canessa P., Larrondo L.F., James T.Y., Seelenfreund D.,
RA   Lobos S., Polanco R., Tello M., Honda Y., Watanabe T., Watanabe T.,
RA   Ryu J.S., Kubicek C.P., Schmoll M., Gaskell J., Hammel K.E., St John F.J.,
RA   Vanden Wymelenberg A., Sabat G., Splinter BonDurant S., Syed K.,
RA   Yadav J.S., Doddapaneni H., Subramanian V., Lavin J.L., Oguiza J.A.,
RA   Perez G., Pisabarro A.G., Ramirez L., Santoyo F., Master E., Coutinho P.M.,
RA   Henrissat B., Lombard V., Magnuson J.K., Kuees U., Hori C., Igarashi K.,
RA   Samejima M., Held B.W., Barry K.W., LaButti K.M., Lapidus A.,
RA   Lindquist E.A., Lucas S.M., Riley R., Salamov A.A., Hoffmeister D.,
RA   Schwenk D., Hadar Y., Yarden O., de Vries R.P., Wiebenga A., Stenlid J.,
RA   Eastwood D., Grigoriev I.V., Berka R.M., Blanchette R.A., Kersten P.,
RA   Martinez A.T., Vicuna R., Cullen D.;
RT   "Comparative genomics of Ceriporiopsis subvermispora and Phanerochaete
RT   chrysosporium provide insight into selective ligninolysis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:5458-5463(2012).
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DR   EMBL; KB445791; EMD42233.1; -; Genomic_DNA.
DR   AlphaFoldDB; M2QYJ2; -.
DR   STRING; 914234.M2QYJ2; -.
DR   HOGENOM; CLU_006065_0_0_1; -.
DR   OrthoDB; 227593at2759; -.
DR   Proteomes; UP000016930; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 4.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR011765; Pept_M16_N.
DR   InterPro; IPR007863; Peptidase_M16_C.
DR   PANTHER; PTHR43016:SF16; METALLOPROTEASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_4G07610)-RELATED; 1.
DR   PANTHER; PTHR43016; PRESEQUENCE PROTEASE; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 1.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000016930}.
FT   DOMAIN          73..150
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          211..406
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   REGION          1034..1065
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1042..1065
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1065 AA;  117780 MW;  91D5FB23BF364566 CRC64;
     MSPVSINGVI PHDQVHETHG NFELVKRLKL DYADIVVSKW KSSVTGLSVV HLDYDAPIVN
     GYFVVATEIF DDTGCPHTLE HLIFLGSEKY PYKGIIDHFA NRGFSNGTNA WTDIDHTAYT
     VSTAGEQGFL QLLPIYVDHI LYPTLTNAGF VTEVHHINGK GEDSGVVYSE MQGRENTSSD
     IMALHSQRLL NPPGSAYRSE TGGLMSALRV LTIDQIRDYH KTYYAPHNFC LVVAGKLASG
     TKSLLDVVQK QVEPSIIAHK QDKGPRPQGW KRPFLETASA IRAISSTVKH VVEFPEKDES
     VGEVMISLLG PPPNAFLERK ALDILSLYLT SSATAPLNKE FVEIENPLCT YIWFGEDTRA
     TRIDLPIYAG SVPTEHLESF NEKLMASLRR IIEEGVDLER IARVINRDER QLRSKLEASK
     GDTFSNAIIA DFIYGAEDGS ELTEALNEFH QYNELRNWSS KQWTNLLADL INQPHVVTLG
     KPSAKLAEKL EKDEQARIAA QKDRLGPNGL AAAEQLLEEA KKEHDKEIPK DVLASFPVPD
     VKSISWIPVQ SLQEPGKGEG RRRLVEQSDN AELAKHIQGD GQELPFFVQY DHVQSDFVSI
     NAYFSLANLP DRLRPHMTVY LASFFSLPVR RSTGERLSYE EVVNKLDDET VSFEVALGIG
     NIFTETVRVT LKVETAMYEV GIAWLKDLVY GSEFDKDRLA VTIAKTQQAL PELKRDGDNV
     LTSVTAELLY NEQSTQRAGA VLPQVEFIPK LAQQLQVSPE EVIKDFEEIR KHITDPSGVR
     FSVTGNVLDL QQPRSLWGKY FNEQLPAANL APVPLISGTL SEVGKNPVQQ AIVVSLPTIE
     SSYVAHTTKG ILGFQHPDFP AIRVAAEVLN ATESFLWRYI RGSGLAYGAS VSIDNEAGLL
     WFNLYRSSNC IEAFKQGASV LKGITDGSIP LDDTTLDTAK SSIVYSVTRT VATPTRAASA
     SFYNQALKGV PQDWQRQLLQ QYQAVSKEDV VEALRKYFLP LFDSSTSVAV VVTAPSKSKE
     IGDDLTAAGF VVQQRTVEAD AGEDEEGSES GSDEGSESGS EEESD
//
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