ID G9MF51_HYPVG Unreviewed; 1439 AA.
AC G9MF51;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 61.
DE RecName: Full=tripeptidyl-peptidase II {ECO:0000256|ARBA:ARBA00012462};
DE EC=3.4.14.10 {ECO:0000256|ARBA:ARBA00012462};
DE Flags: Fragment;
GN ORFNames=TRIVIDRAFT_112283 {ECO:0000313|EMBL:EHK27017.1};
OS Hypocrea virens (strain Gv29-8 / FGSC 10586) (Gliocladium virens)
OS (Trichoderma virens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=413071 {ECO:0000313|EMBL:EHK27017.1, ECO:0000313|Proteomes:UP000007115};
RN [1] {ECO:0000313|EMBL:EHK27017.1, ECO:0000313|Proteomes:UP000007115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Gv29-8 / FGSC 10586 {ECO:0000313|Proteomes:UP000007115};
RX PubMed=21501500; DOI=10.1186/gb-2011-12-4-r40;
RA Kubicek C.P., Herrera-Estrella A., Seidl-Seiboth V., Martinez D.A.,
RA Druzhinina I.S., Thon M., Zeilinger S., Casas-Flores S., Horwitz B.A.,
RA Mukherjee P.K., Mukherjee M., Kredics L., Alcaraz L.D., Aerts A., Antal Z.,
RA Atanasova L., Cervantes-Badillo M.G., Challacombe J., Chertkov O.,
RA McCluskey K., Coulpier F., Deshpande N., von Doehren H., Ebbole D.J.,
RA Esquivel-Naranjo E.U., Fekete E., Flipphi M., Glaser F.,
RA Gomez-Rodriguez E.Y., Gruber S., Han C., Henrissat B., Hermosa R.,
RA Hernandez-Onate M., Karaffa L., Kosti I., Le Crom S., Lindquist E.,
RA Lucas S., Luebeck M., Luebeck P.S., Margeot A., Metz B., Misra M.,
RA Nevalainen H., Omann M., Packer N., Perrone G., Uresti-Rivera E.E.,
RA Salamov A., Schmoll M., Seiboth B., Shapiro H., Sukno S.,
RA Tamayo-Ramos J.A., Tisch D., Wiest A., Wilkinson H.H., Zhang M.,
RA Coutinho P.M., Kenerley C.M., Monte E., Baker S.E., Grigoriev I.V.;
RT "Comparative genome sequence analysis underscores mycoparasitism as the
RT ancestral life style of Trichoderma.";
RL Genome Biol. 12:R40.1-R40.15(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}.
CC -!- SIMILARITY: Belongs to the sirtuin family. Class I subfamily.
CC {ECO:0000256|ARBA:ARBA00006924}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00236}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHK27017.1}.
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DR EMBL; ABDF02000001; EHK27017.1; -; Genomic_DNA.
DR RefSeq; XP_013961233.1; XM_014105758.1.
DR STRING; 413071.G9MF51; -.
DR EnsemblFungi; EHK27017; EHK27017; TRIVIDRAFT_112283.
DR GeneID; 25786883; -.
DR VEuPathDB; FungiDB:TRIVIDRAFT_112283; -.
DR eggNOG; KOG2684; Eukaryota.
DR HOGENOM; CLU_251994_0_0_1; -.
DR InParanoid; G9MF51; -.
DR OMA; NFMSARH; -.
DR OrthoDB; 1344271at2759; -.
DR Proteomes; UP000007115; 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:0070403; F:NAD+ binding; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
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 Gene3D; 3.40.50.1220; TPP-binding domain; 2.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
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 InterPro; IPR003000; Sirtuin.
DR InterPro; IPR026590; Ssirtuin_cat_dom.
DR PANTHER; PTHR14218; PROTEASE S8 TRIPEPTIDYL PEPTIDASE I CLN2; 1.
DR PANTHER; PTHR14218:SF15; TRIPEPTIDYL-PEPTIDASE 1; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR Pfam; PF09286; Pro-kuma_activ; 1.
DR Pfam; PF02146; SIR2; 3.
DR SMART; SM00944; Pro-kuma_activ; 1.
DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51695; SEDOLISIN; 1.
DR PROSITE; PS50305; SIRTUIN; 1.
PE 3: Inferred from homology;
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}; NAD {ECO:0000256|ARBA:ARBA00023027};
KW Protease {ECO:0000256|PROSITE-ProRule:PRU01032};
KW Reference proteome {ECO:0000313|Proteomes:UP000007115};
KW Serine protease {ECO:0000256|PROSITE-ProRule:PRU01032};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 182..572
FT /note="Peptidase S53"
FT /evidence="ECO:0000259|PROSITE:PS51695"
FT DOMAIN 600..1195
FT /note="Deacetylase sirtuin-type"
FT /evidence="ECO:0000259|PROSITE:PS50305"
FT REGION 654..763
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 792..856
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 928..947
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 958..1024
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1192..1231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1275..1379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1416..1439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 662..709
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 715..738
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 744..758
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 813..853
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 965..1009
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1195..1224
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1351..1365
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1419..1439
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 261
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT ACT_SITE 265
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT ACT_SITE 482
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT BINDING 525
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT BINDING 526
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT BINDING 550
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT BINDING 552
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EHK27017.1"
FT NON_TER 1439
FT /evidence="ECO:0000313|EMBL:EHK27017.1"
SQ SEQUENCE 1439 AA; 155879 MW; A2F47FF7C9DAA6C6 CRC64;
LAGLGASRRN VEQVVSVPKG WTKFQDVVNP ARHMRLSIAL RQPNIDQLEA KMAESGNRLS
VEEIRQLQAP DQKDVDAVLQ WLSQNKLKGV VDNDFIHFTA TVAQAEPLLG MKVNRFAYQD
KKTVLRTTKY TVPDSVAGAI SFIHPLANFM SAHHGPEVVS APSKPASKGA VTLDNTAYCS
GTVTPSCLAQ LYNITSYTPA NNHSPVIFGV AGFLEENANL QDLQQFLNTS APNVAQAGRS
IKVELVNGGV NSQDLAESGH EAALDVDYAV SVGFPSNVVY YSTGGRGVKL DDNGQPISGE
EDDNEPYLDF LKYLLVKPDH QVPHVLSLSY SDDELSVPRD YAKRVCSLLG LLTSRGTSII
FSSGDGGARG GRDSSCLTHD GTKRPVTMAT FPPTCPWVTS VGAVTNIAEP PSGASFSTGG
FSQYFARPNW QDSAVKGYVQ TLNGHLDGLY NPSMRAIPDV SAVGTSFQII AGGIPRFLQG
TSASAPVFAS LVALINDARL RAGKKSLGFL NNHLYSNKVK GVLQDITAGK SISCVFNDTE
VPGGWPAAKG WDAITGLGVP KEFDKFLKIR ALSLSRRQSR ISVSPLCRFR FEFMPTQHVE
PETHGLLQEV ANSLLKARKV VVVTGAGIST NSGIPDFRSE NGLYSLIQAQ FDAASQPTRS
AERFKTDADG DGGEEPRPTK RRKTSREPSP DLDEVDRQLN EDIRARAEAE RPAASSQAAD
TQPAVAASEP NASENVCLST PRPKPALPST PQPTTTSPLC SPPREEFMLP LALASSSLRT
EDRERIAGVS QNVVSSPLSS PPPVLFDPFH PSSPSDENMS RRSSTTPSEV DETQDLPNAI
PASQASNPGK TTLPNMKGKD LFDASIWSDP TRTSVFYQFA TSLRQKVREA EPTSSHKFIG
HLRDRGKLVR CYTQNIDQIE EKVGLSTSLL AGPGSRGRFS RKSTANTAQL NKMVEEVSSG
EGGNAGDVGA SSQSPPTGSS EQTPADQRQT SSQPNGKTEE DETSTTTPPD QQPKPAPRKE
APTPRSGVEC VFLHGSLQLL RCFLCGQVCS WDDEDREVET LSGQQPECPH CVGATEARQE
RGKRALGVGK LRPDIVLYGE EHPNAHLISP IVTHDLALYP DMLLILGTSL RVHGLKVMVR
EFAKTVHSKG GKVVFVNFTK PPESSWGDII DYWIQWDCDA WVADLQVRIP KLWQDPEPPK
PKKKRDSGGT AEENREEKKK PPAQNPVALR DTKVNGAYCT LKILKELRRI AATSPPPPYS
PPPLSLTISL SPSLPLPPPP LSRDSAAIAT QANPDPKPPT PAEAAPRSAA MDPPTRISTP
RGKAKRPRKS APGALDRPKR TPSTLNPNHG RSKKPVEEVK EQEVPETPET PSQAPVSTVE
EFSSILHSVK SNPRIRKRKM IDGEEFVFPA IGKKRGAVDS LYKGTEEDKK KLPPLRPMP
//
