ID G0S3E4_CHATD Unreviewed; 1376 AA.
AC G0S3E4;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE SubName: Full=Tripeptidyl-peptidase-like protein {ECO:0000313|EMBL:EGS22527.1};
GN ORFNames=CTHT_0020710 {ECO:0000313|EMBL:EGS22527.1};
OS Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
OS (Thermochaetoides thermophila).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Thermochaetoides.
OX NCBI_TaxID=759272 {ECO:0000313|Proteomes:UP000008066};
RN [1] {ECO:0000313|EMBL:EGS22527.1, ECO:0000313|Proteomes:UP000008066}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1495 / CBS 144.50 / IMI 039719
RC {ECO:0000313|Proteomes:UP000008066};
RX PubMed=21784248; DOI=10.1016/j.cell.2011.06.039;
RA Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R., Devos D.P.,
RA Arumugam M., Bork P., Hurt E.;
RT "Insight into structure and assembly of the nuclear pore complex by
RT utilizing the genome of a eukaryotic thermophile.";
RL Cell 146:277-289(2011).
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; GL988040; EGS22527.1; -; Genomic_DNA.
DR RefSeq; XP_006692546.1; XM_006692483.1.
DR MEROPS; S53.007; -.
DR GeneID; 18256109; -.
DR KEGG; cthr:CTHT_0020710; -.
DR eggNOG; ENOG502QTN1; Eukaryota.
DR HOGENOM; CLU_255933_0_0_1; -.
DR OrthoDB; 1405251at2759; -.
DR Proteomes; UP000008066; 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:0009116; P:nucleoside metabolic process; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04056; Peptidases_S53; 1.
DR CDD; cd11377; Pro-peptidase_S53; 1.
DR Gene3D; 3.40.50.1580; Nucleoside phosphorylase domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR035994; Nucleoside_phosphorylase_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR015366; S53_propep.
DR InterPro; IPR030400; Sedolisin_dom.
DR PANTHER; PTHR14218; PROTEASE S8 TRIPEPTIDYL PEPTIDASE I CLN2; 1.
DR PANTHER; PTHR14218:SF19; SERINE PROTEASE AORO, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G10250)-RELATED; 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}; Protease {ECO:0000256|PROSITE-ProRule:PRU01032};
KW Reference proteome {ECO:0000313|Proteomes:UP000008066};
KW Serine protease {ECO:0000256|PROSITE-ProRule:PRU01032}.
FT DOMAIN 944..1375
FT /note="Peptidase S53"
FT /evidence="ECO:0000259|PROSITE:PS51695"
FT REGION 159..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..186
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1021
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT ACT_SITE 1025
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT ACT_SITE 1293
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT BINDING 1334
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT BINDING 1335
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT BINDING 1353
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT BINDING 1355
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
SQ SEQUENCE 1376 AA; 151877 MW; EFE7AF9C4D9982E2 CRC64;
MAFQPQPPAI RASYPIPLFP SSIQAAWLVS SPLDLISAHY CLDQRLPDTF PPGFPDDPNT
YMLGKVGKVF VVVVCLPQRP EDLVERGVRH LLRTFTGLRF AIISGTAAAI PAEPVQLGDV
VIGTKIIPFS SDHSAVVNEF LPPPGYLLAA LGQVLSPNGI RRSTASPRSD TGEGVFEDDS
RRESVGTENT EVSSPETLTP MKIPERLSER VSYTVSIQDG KLTLVPVSIT TYPAESPDWI
SLAPYLKHPW DLPQHRAFSQ HRHPKTGIWF LSSPQVKQWL ELASGRALLV PGAPGTGKSV
LTSLVVDTLR AELTKTETQQ TKGASLVDDR PVVACLYDVY QLPGQETDEW FTKLCASLLG
QIVCSVLDKR QLQDVKPSNI WLNKEQSFRT LVRCLVSPKA LSARPVYILL DGLEQPDSNP
NTESPIFASG ELAAGWGPYT RDFMSILFTL QRTRGVNVFI TTKTPSSMLF KQIIQPLGRM
RASGWSNSPL QIAGVEVLYP NQKFDFEEIR KMLEDKVVLF TQNKRVGLTH QKLMNEVCDG
KSMFLNGDII KGLDEEVIKK CMATGATIMT GEAFGISPDT MFLIAYLVIQ ELFSAASSVP
RDQVGKFLGK LTARLKKTVL PNRKKCLNSR FDGQVLSLAS MYKHIYSRLA CSNAVHDVEC
CEANAKARKG HLTEKILFLS WYRVRVPADH LGCQDGGIGD EDKNSVPIVN VIAETMVASL
ECWSQRVGRA CLALQQPTSN HHREEECPAD MFVMSGMNSI TLKDGSSGGQ SDPKSPKFGK
YLSPREVVDL FTPKQESIDE VVSWLRGEGV DGRRLGMSYN KQWIGFDAPV DEIERLLHTQ
YHIYEHVESG VLSIACSEYH VPHNISHLID YITPGIKLAT SHRDVKIAKR AIRIEDERQS
RRLMIERRNA KRNDNVASAT DAPQLNVPQI EDKWFKPSGW CSGDVTPQCI RAQYQIPVGS
KSTPGNELGI FQSLGQHYNQ HDLDTYFRNI APWVPKGTFP SLRSINGALG PTNDVSKAGF
EADLDFEVAI PLVWPQKTVL FQVDDEWYQQ EQTRSDSKYP GFFNTFFDAL DASYCHLTAY
NLTGNCRTSS CRDPEYPNPN VPPLNLSSST PLLSPDAFII LNAYHGPLMC GAHPPTKVIS
ISYSGTEHTW PANYMRRQCL EIMKLTLQGI TVVESSGDVG VGGGRYNSQV GCLGANRTVY
APRVMSNCPY VLSVGATMLV DKDDGTASWR EVAAEGIKEK GYILKGEEGF SNSSVPEGKV
FNLAGRAYPD VAAIGENFKV VWKGYPNRMD GTSVAVPIWA SILTLINEER LAVGKGPVGF
VHPVLYAHPE VFTDITEGSN PGCGSEGFPA TKGWDPVTGL GTPIFPKLLE LFMSLP
//
