ID Q2H789_CHAGB Unreviewed; 434 AA.
AC Q2H789;
DT 21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2006, sequence version 1.
DT 24-JAN-2024, entry version 76.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN ORFNames=CHGG_05476 {ECO:0000313|EMBL:EAQ88857.1};
OS Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS NRRL 1970) (Soil fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX NCBI_TaxID=306901 {ECO:0000313|EMBL:EAQ88857.1, ECO:0000313|Proteomes:UP000001056};
RN [1] {ECO:0000313|Proteomes:UP000001056}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970
RC {ECO:0000313|Proteomes:UP000001056};
RX PubMed=25720678; DOI=10.1128/genomeA.00021-15;
RA Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL Genome Announc. 3:E0002115-E0002115(2015).
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447}.
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DR EMBL; CH408031; EAQ88857.1; -; Genomic_DNA.
DR RefSeq; XP_001221571.1; XM_001221570.1.
DR AlphaFoldDB; Q2H789; -.
DR MEROPS; A01.082; -.
DR GeneID; 4391016; -.
DR VEuPathDB; FungiDB:CHGG_05476; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_9_4_1; -.
DR InParanoid; Q2H789; -.
DR OMA; DQRFCRA; -.
DR OrthoDB; 615305at2759; -.
DR Proteomes; UP000001056; Unassembled WGS sequence.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd05474; SAP_like; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR033876; SAP-like.
DR PANTHER; PTHR47966:SF65; ASPARTIC-TYPE ENDOPEPTIDASE; 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; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000001056};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 9..328
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 380..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 27
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 222
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 257..293
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 434 AA; 45315 MW; 329BC23251F21E07 CRC64;
MPQHSNKPST TTVSLGTPPQ PVFVQLDTGS FELWVNPDCT TVSGGDAVFC QRAGRYESTA
SSTATSLGTT RTLRYGIGAA NISYFTDTIS LAGSPMSLQD VQFGVATASV DAFSGILGIG
YGKGIATRYP NFVDQLREQN ATRVKAYTLA LGSKDAQEGV IVFGGVDTSK FAGKLAKLPI
LPAAQAPDGV PRFWVDMQAL SITPPNGVTT VYEGSSMPVF LDSGSTMTLL PANLTAAVAR
DFGAESPDSN GFYMIDCALT ALNGTLDFVF DGVTVKVPYK ELTREVASTP PSCFLGIMAS
DRFTLLGDTF LRSAYTVFDL ETDSIWMTQA TNCGSSPAAL SNIQDLSVVV GECGAGASED
IDTTSSTQFP STAVEDFESG AIPTSTGSFG PQVSEVAPPD QARPLPENSG PSLRAAGFIW
NLGMAGAVHL LAGL
//
