ID F4R7B9_MELLP Unreviewed; 621 AA.
AC F4R7B9;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=tripeptidyl-peptidase II {ECO:0000256|ARBA:ARBA00012462};
DE EC=3.4.14.10 {ECO:0000256|ARBA:ARBA00012462};
GN ORFNames=MELLADRAFT_46732 {ECO:0000313|EMBL:EGG11812.1};
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 -!- FUNCTION: Secreted tripeptidyl-peptidase which degrades proteins at
CC acidic pHs and is involved in virulence.
CC {ECO:0000256|ARBA:ARBA00002451}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal tripeptide from a polypeptide.;
CC EC=3.4.14.10; Evidence={ECO:0000256|ARBA:ARBA00001910};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|PROSITE-ProRule:PRU01032};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000256|PROSITE-
CC ProRule:PRU01032};
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC {ECO:0000256|ARBA:ARBA00004239}.
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DR EMBL; GL883092; EGG11812.1; -; Genomic_DNA.
DR RefSeq; XP_007405447.1; XM_007405385.1.
DR AlphaFoldDB; F4R7B9; -.
DR MEROPS; S53.007; -.
DR EnsemblFungi; EGG11812; EGG11812; MELLADRAFT_46732.
DR GeneID; 18928368; -.
DR KEGG; mlr:MELLADRAFT_46732; -.
DR VEuPathDB; FungiDB:MELLADRAFT_46732; -.
DR eggNOG; ENOG502QTN1; Eukaryota.
DR HOGENOM; CLU_013783_4_0_1; -.
DR InParanoid; F4R7B9; -.
DR OrthoDB; 2326650at2759; -.
DR Proteomes; UP000001072; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04056; Peptidases_S53; 1.
DR CDD; cd11377; Pro-peptidase_S53; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR015366; S53_propep.
DR InterPro; IPR030400; Sedolisin_dom.
DR PANTHER; PTHR14218:SF42; PEPTIDASE S53 DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR14218; PROTEASE S8 TRIPEPTIDYL PEPTIDASE I CLN2; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR Pfam; PF09286; Pro-kuma_activ; 1.
DR SMART; SM00944; Pro-kuma_activ; 1.
DR SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51695; SEDOLISIN; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PROSITE-
KW ProRule:PRU01032}; Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01032};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU01032};
KW Protease {ECO:0000256|PROSITE-ProRule:PRU01032,
KW ECO:0000313|EMBL:EGG11812.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001072};
KW Serine protease {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT DOMAIN 219..620
FT /note="Peptidase S53"
FT /evidence="ECO:0000259|PROSITE:PS51695"
FT ACT_SITE 292
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT ACT_SITE 296
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT ACT_SITE 536
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT BINDING 579
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT BINDING 580
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT BINDING 598
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT BINDING 600
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
SQ SEQUENCE 621 AA; 69399 MW; 52A3CD4AF2B6A593 CRC64;
MSYVTHERRS ENPLWIRSNQ KFLRPDSHFK IRFGLKQRNL EKLSSELHRV ASPDSTEYAE
HWTNEQIMTF FQPAPESQIK VQEWLKDVLE EGADIQLSAG GAWIDVDLTV SQANQLLKTE
YGIYDHPDGN VHIACEEYSV PEYISDHLDL VIPSVHFDMR SNKGKIEQAS NQKRNNKRRS
TIFKREIHSI DVAQGSPLIR KPVPKPQIIN SESSDPFSTC DQTTTLDCLN FPGLILKHEQ
LILTTNNLVE YSPRAVIFDD LDIFFKGSFQ IVIIPTLCKL DQTAQSYENN LESNLDLSYA
MSMLLIYEFI QVQLYQVGDG IAGSGFNNFL DALDATYCHE KLDPSQDGVY PGYNKRDCGT
VKATHVISSS YSMSEAEATP NYLRRQCEEY GKLALMGVTF LHSSGDYGVA GFRGNCLTED
NRASPQGKRF NPTFPGTCPF VTIIGATQIK PGNSVRDPEE SLSTYFVSGG GFSNLFEIPE
YQKKTLKTYW DLHRPEYSSS QFNNSMKTRG YPDLSANGAN YAVSIDGQLE LVYGTSAAVP
VVASMITLIN DARISMGKSP VGFLNPALYS DGFRDAFNDI TSGSNPGCTT RGFSAVKGWD
PLTGLGTINF PKLLNLFSNL Q
//
