ID F4RPK7_MELLP Unreviewed; 533 AA.
AC F4RPK7;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Peptide hydrolase {ECO:0000256|RuleBase:RU361240};
DE EC=3.4.-.- {ECO:0000256|RuleBase:RU361240};
GN ORFNames=MELLADRAFT_107375 {ECO:0000313|EMBL:EGG05550.1};
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).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M28 family.
CC {ECO:0000256|RuleBase:RU361240}.
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DR EMBL; GL883112; EGG05550.1; -; Genomic_DNA.
DR RefSeq; XP_007411039.1; XM_007410977.1.
DR AlphaFoldDB; F4RPK7; -.
DR STRING; 747676.F4RPK7; -.
DR EnsemblFungi; EGG05550; EGG05550; MELLADRAFT_107375.
DR GeneID; 18923156; -.
DR KEGG; mlr:MELLADRAFT_107375; -.
DR VEuPathDB; FungiDB:MELLADRAFT_107375; -.
DR eggNOG; ENOG502SBCT; Eukaryota.
DR HOGENOM; CLU_038388_0_0_1; -.
DR InParanoid; F4RPK7; -.
DR OrthoDB; 1384212at2759; -.
DR Proteomes; UP000001072; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008235; F:metalloexopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR045175; M28_fam.
DR InterPro; IPR007484; Peptidase_M28.
DR PANTHER; PTHR12147; METALLOPEPTIDASE M28 FAMILY MEMBER; 1.
DR PANTHER; PTHR12147:SF59; PEPTIDASE_M28 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU361240};
KW Metal-binding {ECO:0000256|RuleBase:RU361240};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU361240};
KW Reference proteome {ECO:0000313|Proteomes:UP000001072};
KW Signal {ECO:0000256|RuleBase:RU361240};
KW Zinc {ECO:0000256|RuleBase:RU361240}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|RuleBase:RU361240"
FT CHAIN 23..533
FT /note="Peptide hydrolase"
FT /evidence="ECO:0000256|RuleBase:RU361240"
FT /id="PRO_5005129538"
FT DOMAIN 315..510
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
SQ SEQUENCE 533 AA; 60305 MW; CBE4A95A60B19615 CRC64;
MKTQYPMKTI LLLLLLIKIS ISYQSIFKIK LQPTNSSSSK NRIQSNSTDL TVDGQSIHIN
QNQINLITHD TSIHHHQLQN CPKHYLFSIS PSILDSSLIF QTDHDPLESW KDELNSYVSQ
LQEIETSLQT TTTGSSTEQI VLRSTTTNSR LNECQRSGTR VFFCVNHTAL VLVPYLSLKE
FTERLPNHME LLIHLYPNKT DFSNPYIRSK TLKRSSEKLL NEVIKIHYKP KIDKLISSLN
LNEILKYTRT VVGIDEPSKW ITRHTFSDGI LLALDWLKDR FESGAVGMRC GFEEYQLGFA
PNLVCKILAT DQRNRGDGKE RVVVSAHLDS RGDFGNVFEP GTDDNAFGCS VLLSISKSIQ
AHQLSLKKDL YFVVFSGTHQ GSWGSLGLLN SWKDQLDLVL LHLDLSMIGY RVPGESMQLG
LPIENRFNRV ANWFVGNITN LYLPELLIGP TPVRDLDSQR FERHGILSTI RDLDSQRFGT
HGILSTSLFE RAGKIGNPFY HTSLDLIGKP GYDLVQVLTI GKALYATVLE LVL
//
