ID F4RKI3_MELLP Unreviewed; 674 AA.
AC F4RKI3;
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_86030 {ECO:0000313|EMBL:EGG07175.1};
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; GL883105; EGG07175.1; -; Genomic_DNA.
DR RefSeq; XP_007409617.1; XM_007409555.1.
DR AlphaFoldDB; F4RKI3; -.
DR MEROPS; S53.007; -.
DR EnsemblFungi; EGG07175; EGG07175; MELLADRAFT_86030.
DR GeneID; 18934056; -.
DR KEGG; mlr:MELLADRAFT_86030; -.
DR VEuPathDB; FungiDB:MELLADRAFT_86030; -.
DR eggNOG; ENOG502QZ4I; Eukaryota.
DR HOGENOM; CLU_013783_4_0_1; -.
DR InParanoid; F4RKI3; -.
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:EGG07175.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001072};
KW Serine protease {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT DOMAIN 267..673
FT /note="Peptidase S53"
FT /evidence="ECO:0000259|PROSITE:PS51695"
FT ACT_SITE 345
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT ACT_SITE 349
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT ACT_SITE 589
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT BINDING 632
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT BINDING 633
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT BINDING 651
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT BINDING 653
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
SQ SEQUENCE 674 AA; 75344 MW; 82C2575816260B4D CRC64;
MVNKSKLAIL NWVFPFLFNL PNFIQTLSVS EKITHDRRIP NALWKRTDHL LQSQKEKTVL
RFRFGLKQSN IDNLYDELMR VSSPESPHYA DHWDSDKVSR FFSPSNETIG EVLKWLKKED
KGFKKVELSR SRAWVHVHMS IDQAEKLLDT KFYKYIHTDD HTTHLACEQY KIPGHLSSHI
DIVLPSVHFD TVPVTNKYSS MNDNQASNSL QNDRKMSQSW PTARHVGYPN SGNIPKHSTI
LNHHQLERVR RGVSNCGNVI TLDCLNEVSL EFLRALYKFG RYKIKHPQNN SLAIVEFTPQ
SVLYSDLDHF FSNFSPQAKG SRPSLVPIDG GIVDQEDQDF GLNGESNLDL QYSMPFVHPL
NVSLYQIGDT DMGGSFNNFL DALDSSYCEG HLDPLQDGVY PNPRGYNHRD CGTVKPANII
SISYGMNEAD ATHAYLTRQC NEYGKLGLMG VTFIFSSGDN GVAGNRGICL NRDGTQSENG
PLFNPSFPGT CPYVTSIGAT QLPAGKTVND SEAACYTRIR SGGGFSNLFK LPQYQSRVMK
TYFKRHPPPY NHNTFNASRS TRGFPDISAN GANYVVAVVG RFGLVYGTSA SAPVVASILT
MINDARMARG KKTIGFINPT LYSARFQEAF NDITNGSNPG CGTDGFSAVP GWDPVTGLGT
LDFSKLLPLW TKLR
//
