ID   F4S789_MELLP            Unreviewed;      1153 AA.
AC   F4S789;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   SubName: Full=Zinc metalloprotease {ECO:0000313|EMBL:EGF99472.1};
GN   ORFNames=MELLADRAFT_94306 {ECO:0000313|EMBL:EGF99472.1};
OS   Melampsora larici-populina (strain 98AG31 / pathotype 3-4-7) (Poplar leaf
OS   rust fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Pucciniomycetes; Pucciniales; Melampsoraceae; Melampsora.
OX   NCBI_TaxID=747676 {ECO:0000313|Proteomes:UP000001072};
RN   [1] {ECO:0000313|Proteomes:UP000001072}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=98AG31 / pathotype 3-4-7 {ECO:0000313|Proteomes:UP000001072};
RX   PubMed=21536894; DOI=10.1073/pnas.1019315108;
RA   Duplessis S., Cuomo C.A., Lin Y.-C., Aerts A., Tisserant E.,
RA   Veneault-Fourrey C., Joly D.L., Hacquard S., Amselem J., Cantarel B.L.,
RA   Chiu R., Coutinho P.M., Feau N., Field M., Frey P., Gelhaye E.,
RA   Goldberg J., Grabherr M.G., Kodira C.D., Kohler A., Kuees U.,
RA   Lindquist E.A., Lucas S.M., Mago R., Mauceli E., Morin E., Murat C.,
RA   Pangilinan J.L., Park R., Pearson M., Quesneville H., Rouhier N.,
RA   Sakthikumar S., Salamov A.A., Schmutz J., Selles B., Shapiro H.,
RA   Tanguay P., Tuskan G.A., Henrissat B., Van de Peer Y., Rouze P.,
RA   Ellis J.G., Dodds P.N., Schein J.E., Zhong S., Hamelin R.C.,
RA   Grigoriev I.V., Szabo L.J., Martin F.;
RT   "Obligate biotrophy features unraveled by the genomic analysis of rust
RT   fungi.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:9166-9171(2011).
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DR   EMBL; GL883158; EGF99472.1; -; Genomic_DNA.
DR   RefSeq; XP_007417246.1; XM_007417184.1.
DR   AlphaFoldDB; F4S789; -.
DR   STRING; 747676.F4S789; -.
DR   EnsemblFungi; EGF99472; EGF99472; MELLADRAFT_94306.
DR   GeneID; 18936845; -.
DR   KEGG; mlr:MELLADRAFT_94306; -.
DR   VEuPathDB; FungiDB:MELLADRAFT_94306; -.
DR   eggNOG; KOG0961; Eukaryota.
DR   HOGENOM; CLU_006065_0_0_1; -.
DR   InParanoid; F4S789; -.
DR   OrthoDB; 227593at2759; -.
DR   Proteomes; UP000001072; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; 2.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:EGF99472.1};
KW   Metalloprotease {ECO:0000313|EMBL:EGF99472.1};
KW   Protease {ECO:0000313|EMBL:EGF99472.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001072};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..1153
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003318306"
FT   DOMAIN          168..220
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          327..510
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          886..1052
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   REGION          69..109
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1153 AA;  128125 MW;  E20D717B2372B4C7 CRC64;
     MFTMLLMVIK NMSVVGLPTL PKGINTGQGV AEHLIEDMNG ANEGTHRDVV PHMQKQDRHQ
     DLQFDSQARE NEKVPNHKDE SSSSAHEDKD TLPSEEITAS SVKKEEDVEI PDTVGNFDRV
     IEPFKMDSAP IKVAKWKSRE TGLSVVWADI DGPIVNGYLT VATEIFNDSG VPHTLEHLIF
     MGSEKYPYKG ILASLANRSF ATGINAWTET THTAYTVKTA GSEGFFKLLP SMQFHPIYKF
     RTANSMKNLS LSTEQSTSTT IPSSAFTTEV YHINGEGEDA GVVYSEMQGR ENSSTDLMSL
     RSLREIYPPT SAYQSETSGK MAALRTLTVE QIRKYHSDYY HPHNLQLLVT GKVDPTTLLS
     VLQEEVEPSL IKHGQDKFPA EWKRPFLETA SKGGAVLTKD KVVEVPFPEK DESTGQVQIS
     WVGPSINDYL LQDALKILET YLTKTAISPL AKKFIDIEDP LCTGITFYPT EGEKTVISAC
     ISSVPAEHLS DFGKMFKDAL AHEAENLDMQ RMRMTIECDA LEIANQLEAN AHSILSSAII
     SNFLYGSGEQ LVADLSTVLE RYKTLASWSR EQWSSMFKKW LVESPSVTVI GKPSGKLADQ
     LVADNKARIE ETKKKYGPEG LKQLQAKLEA AQKTNDTPHP QTILSNYPIP KMESIKWIEV
     ESARADGSLK GDLQAQIDKK DSTILPYFIQ FDHIDSNFLR ISVHLSPTDL PADLVKYLYI
     WLALFFSLPV KRSDGTLLPF DQVVKELTKE TIEYKTHMGS SISQTSEICF KIEKSKYPTM
     IGWLKDLLWG SQFDIDRLRI IVANNLQHIP SMKRSGAGVC AALFQELLYS PYTAPYMSSN
     LFKLDEWLPE IMEQLKSNPQ EVIKNLEQLR KHCRSSPISS HTLTVLQPST MRLSVVGDIK
     TLQDPKKSWL EHFQKIPSST LRPPLYSSDV LSADGLKPSG KAIVMSMPSI ESSFAYHVAK
     GAQGFNHPDR PALAVAVSLL NSMESHLWKA IRGTGLAYGA SMRSIPESGH VCVQIYSSPD
     SWKAFEEAGK VMSDLISKKL ILDELSLEAA KSSLAYATAE LESTMGSAAF STFTNMALKG
     IEKDASRQLL DKTKDITIDQ VLEVIEKYFL PIFDAQTSVA VVTSSPGKAK STAASLRNAG
     YRVEERDLNV ASQ
//