ID G0SGN4_CHATD Unreviewed; 463 AA.
AC G0SGN4;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 03-MAY-2023, entry version 52.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN ORFNames=CTHT_0066970 {ECO:0000313|EMBL:EGS17373.1};
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:EGS17373.1, 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 -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR EMBL; GL988047; EGS17373.1; -; Genomic_DNA.
DR RefSeq; XP_006696991.1; XM_006696928.1.
DR AlphaFoldDB; G0SGN4; -.
DR GeneID; 18260735; -.
DR KEGG; cthr:CTHT_0066970; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_0_3_1; -.
DR OMA; FPFAIYG; -.
DR OrthoDB; 2900143at2759; -.
DR Proteomes; UP000008066; Unassembled WGS sequence.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd06097; Aspergillopepsin_like; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR034163; Aspergillopepsin-like_cat_dom.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966:SF2; ASPERGILLOPEPSIN-1-RELATED; 1.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|ARBA:ARBA00022750,
KW ECO:0000256|RuleBase:RU000454}; Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000008066};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..463
FT /note="Peptidase A1 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003409229"
FT DOMAIN 137..459
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 87..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 155
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 347
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 463 AA; 49973 MW; 94D9E2860B734518 CRC64;
MRFSLLAAAA ALLSPAFAAP RVVKVDPKDI KPRHPGGIHF KVAQVHNDHF RQHGKGPRAL
AKVYQKYDVK MPTSLLRVLR TIYDEIEHPS NDDDPSGYAA GDGSYGGGGA GGDDSDTPRV
PDTGEVTAIP QLFDVEYLAP VEIGTPPQTL MLNFDTGSSD LWVFSSETPA RYVAGQKLYQ
IENSTTATRL ANHTWAIQYG DGSRSAGNVW LDTVSIGGIA VDRQAVESAT SVSSSFTRDN
ASSGILGLAF DHLNQVRPNK QKTWFSNALD VLEMPVFSAN LKKAEPGNYN FGFIDTTEFL
GPLHFVDVNS TDGFWKFEAT GFSIQNANST DNTSSLFVPV AHTAIADTGT TLLLLPSAIT
QAYYWQVANA TDSPMLGGWV FPCGTYLPDL TLHIGTYKAV IPGELMVFAP VDTDDLATAT
TCYGGIQSSS GFPFAIYGDV FLKAQWTVFD MGEERLGFAA KPI
//
