ID A0A0D1ECZ9_USTMA Unreviewed; 1298 AA.
AC A0A0D1ECZ9;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=tripeptidyl-peptidase II {ECO:0000256|ARBA:ARBA00012462};
DE EC=3.4.14.10 {ECO:0000256|ARBA:ARBA00012462};
GN ORFNames=UMAG_12106 {ECO:0000313|EMBL:KIS72095.1};
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631 {ECO:0000313|EMBL:KIS72095.1, ECO:0000313|Proteomes:UP000000561};
RN [1] {ECO:0000313|EMBL:KIS72095.1, ECO:0000313|Proteomes:UP000000561}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021 {ECO:0000313|Proteomes:UP000000561};
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kamper J., Kahmann R., Bolker M., Ma L.J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Muller O., Perlin M.H., Wosten H.A.,
RA de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G., Snetselaar K., McCann M.,
RA Perez-Martin J., Feldbrugge M., Basse C.W., Steinberg G., Ibeas J.I.,
RA Holloman W., Guzman P., Farman M., Stajich J.E., Sentandreu R.,
RA Gonzalez-Prieto J.M., Kennell J.C., Molina L., Schirawski J.,
RA Mendoza-Mendoza A., Greilinger D., Munch K., Rossel N., Scherer M.,
RA Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B., Meng S.,
RA Ho E.C., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J., Deelstra H.J.,
RA Ortiz-Castellanos L., Li W., Sanchez-Alonso P., Schreier P.H.,
RA Hauser-Hahn I., Vaupel M., Koopmann E., Friedrich G., Voss H., Schluter T.,
RA Margolis J., Platt D., Swimmer C., Gnirke A., Chen F., Vysotskaia V.,
RA Mannhaupt G., Guldener U., Munsterkotter M., Haase D., Oesterheld M.,
RA Mewes H.W., Mauceli E.W., DeCaprio D., Wade C.M., Butler J., Young S.,
RA Jaffe D.B., Calvo S., Nusbaum C., Galagan J., Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [2] {ECO:0000313|Proteomes:UP000000561}
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021 {ECO:0000313|Proteomes:UP000000561};
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR EMBL; CM003140; KIS72095.1; -; Genomic_DNA.
DR RefSeq; XP_011386833.1; XM_011388531.1.
DR STRING; 237631.A0A0D1ECZ9; -.
DR MEROPS; S08.A56; -.
DR EnsemblFungi; KIS72095; KIS72095; UMAG_12106.
DR GeneID; 23567869; -.
DR KEGG; uma:UMAG_12106; -.
DR VEuPathDB; FungiDB:UMAG_12106; -.
DR eggNOG; KOG1114; Eukaryota.
DR InParanoid; A0A0D1ECZ9; -.
DR OrthoDB; 662485at2759; -.
DR Proteomes; UP000000561; Chromosome 1.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008240; F:tripeptidyl-peptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04857; Peptidases_S8_Tripeptidyl_Aminopeptidase_II; 1.
DR Gene3D; 1.25.40.710; -; 1.
DR Gene3D; 2.20.25.690; -; 1.
DR Gene3D; 2.60.40.3170; -; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 2.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR034051; TPP_II_domain.
DR InterPro; IPR046939; TPPII_C_sf.
DR InterPro; IPR048384; TPPII_GBD.
DR InterPro; IPR048383; TPPII_Ig-like-1.
DR InterPro; IPR022229; TPPII_Ig-like-2.
DR InterPro; IPR046940; TPPII_Ig-like_sf.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR PANTHER; PTHR43806:SF14; TRIPEPTIDYL-PEPTIDASE 2; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR Pfam; PF12580; TPPII; 1.
DR Pfam; PF21316; TPPII_GBD; 1.
DR Pfam; PF21223; TPPII_Ig-like-1; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000000561};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 37..523
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 578..683
FT /note="Tripeptidyl-peptidase II first Ig-like"
FT /evidence="ECO:0000259|Pfam:PF21223"
FT DOMAIN 701..791
FT /note="Tripeptidyl-peptidase II galactose-binding"
FT /evidence="ECO:0000259|Pfam:PF21316"
FT DOMAIN 833..1024
FT /note="Tripeptidyl peptidase II second Ig-like"
FT /evidence="ECO:0000259|Pfam:PF12580"
FT REGION 1149..1168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 184..211
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1154..1168
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 46
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 305
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 495
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1298 AA; 142291 MW; 9B026F027266087A CRC64;
MPSARAVPSE PFPLGGLLPK DTTEALSFLR KYPDFDGRNV RVAILDTGVD PAAIGLNVPG
KVVDVIDCTG AGDIPLQPIE PVANTGDSSS KHIEFKSPFT GRIIRLSSKL SNPKGEWKIG
FKKAYDLWPG ELKSRRSAER QKAFLVSHQA LLCKAQSELN ALESPASSKA SDAISSNADH
NIVKDNAKLQ KDEIKARIQT LKDLAASYKD DGPLIEAIVF HNGKHWYAVV GGGEGQTHDP
STGQPEDVLK PLEQQTLDLT TVDPITDFRT ERQWQSFGEQ DLLTYTVNIE DNGNLLSLVT
VAGSHGTHVA GIVGARHDEQ PELNGVAPGC EIVSMKIGDS RLGSMEQGQA MLRSAQALID
TKCDIANLSY GEDGAFGAED KGAFAKALRD IVIRQRDILF VSSAGNNGPA LTTVGQPGGT
TSSVLSVGAY VNAGAMQKAE YALVEKGVPD SVTTWCSRGP TADGDRGVSI YAPGAAITSI
PRYCLQSTQL MNGTSMSSPN ACGSIALLLS GLKAQKVPIT PARVFNAVRV TGKDVNDPLG
VPFIRVDAAW DYLMQNKDRV EQDAEYRVGV TRAGKALGRM DKRGIYLREK DETYNVQQTN
VTVRPTFKQG ETEKAFHLEL RCALAASKPW VSVPDFLLLG GNGRTFEVRV DPTNLTPGLH
HAWLEAYDTE RPGHKLFDIP VTVAKPEVFA SPTVKFDTVR FEAGKIERRF ISVPEGATWA
SLTVRSSNHS SAGTSARFWL HCVQLEPLQR LSEVEKAFVL ALQENEPVTK KFNVRGGMTM
EVCSAQFWSN KSAFDLDLDI EFHGITASLV PASGRQELTL IGGQGHAKIE CQSTVRIEDF
KPSITFDTRR TFHRPSSSTI RPLTTPRDLQ PSGNHMFELV TTYHISVKED SNKLSYSFPA
LGNHLYDSSV PLLTQLFDLR KKRVHFGDVY MKEIDLPKGD YVLKAQLLNE SMKVLESLKN
VTLMIDQKLS KPESAALKLY DNHVDLHSEA PPAKYAGVKL QPGERIVLTL DLNLEGDAVP
KEAQPGDILV GTFGFAAEGK GQIRYIVPPA VKNADEGSDD GATAGKNDKE IPELLTATAK
KIKDPKEKLD FMDKLISDYP KFLGALVAKL EALDADDKDA TKRKEVITTV DQVLSLIDET
EVKLWLATQK PSASEQTDEE KKHSKEMEEK KKALILALNR KTRVLMTDAE SSSGSSADLE
SSWKTYRSYF SADTKNKDYT ILFVRWSILH RRFALALQAV HKLKKDLGAG TAETLAELEK
LKQLELRLVG KQGLDWPLWA SHLERLERVA APKAYAPF
//
