ID Q2H127_CHAGB Unreviewed; 926 AA.
AC Q2H127;
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_04519 {ECO:0000313|EMBL:EAQ87900.1};
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:EAQ87900.1, 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; CH408032; EAQ87900.1; -; Genomic_DNA.
DR RefSeq; XP_001223733.1; XM_001223732.1.
DR AlphaFoldDB; Q2H127; -.
DR STRING; 306901.Q2H127; -.
DR GeneID; 4392994; -.
DR VEuPathDB; FungiDB:CHGG_04519; -.
DR eggNOG; ENOG502RV5I; Eukaryota.
DR HOGENOM; CLU_009988_1_0_1; -.
DR InParanoid; Q2H127; -.
DR OMA; WIPSYSY; -.
DR OrthoDB; 1831139at2759; -.
DR Proteomes; UP000001056; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd05471; pepsin_like; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR034164; Pepsin-like_dom.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR15549:SF26; AXIAL BUDDING PATTERN PROTEIN 2-RELATED; 1.
DR PANTHER; PTHR15549; PAIRED IMMUNOGLOBULIN-LIKE TYPE 2 RECEPTOR; 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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000001056};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..926
FT /note="Peptidase A1 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004208807"
FT TRANSMEM 475..497
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 58..432
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 505..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 612..926
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 622..641
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 660..676
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 730..769
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 830..848
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 869..892
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 912..926
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 926 AA; 101474 MW; 3667231C8CA703F9 CRC64;
MRLPYLGAAV VRDVLLLLVL AVSQFGAAVV AASPDPPTPS PLWIQPSGEW YGIDGTWSNF
AFYIGSPAQV VYLSVATALS EIWVVSTGGC VPVQLCIDAR GGVFDISQSD TWRSLGGWQL
GMNYTGMGGN GDYGLETLAF VNRVTRFTSA IDGALVAAIN DTDYYQGYVG VGVTQGRFGA
NLTNPFISQL AQTYGTIPSH GYGYTAGAYY RNDEPNGGTV ASLTLGGYDT LRFEPHNTKF
TLDPVSRLPV VRLRGITAAV PTLDEAPTKN WTSTARPLVK MDDSIIATID SSTPYLWLPT
EVCERFAAAL NLKWREDLGV YVFSDGAQYT NYQSSTSLSF TFSLSSYQNA DNFGQPLNTP
GVVNITLPSA AFAQLLRYPF KNIIQWGDSS VPYFPLKRST KEVNDNRYII GRAFLQEAYI
ITSYDRGTYS LHQARFPKNA TKNYLLEEIT RPADSAYPKY ESEPEPSHGL STGQMVGIVL
GAFVVGSIAA LLLWFCLVRK RKDKQKEVPG QEDEHKDGPQ IIEEDEEEEP ASPVKRMFTK
IIRKKRSRKP AVHETDGQSM QPVEVGADEQ HQVFEMPVPP EPVELDSHDV GDDDTEFGAD
SSRALSQYEI TRRKLDRQLQ GPVPTYTPNA TFPTGLGPEK SMQDTSPVAH YRPVEEPSPA
SSPTYANSNS LPGTLPSPMT PHGDWTNRGF DLPSPMTVAP PTHLLLHTPF TGSDPTYSPV
SPHSPHSPHS PHSPHTYAPS SITRAGSSDS PTSPTGSMQL PSPTFQRTPI DPSRVVCLGP
LPENVQLPRP QQSIPRIVTP AHPPQEADAQ AGPAYSGSQD LPLPQPLGHH RSHTQGSTDT
LGSNFTVEEE TRFRTDEPAL PRQPSMVQDE QQGHHHGHER DRDQDQDVPR TPCSMERIDG
GSELIHVPQV ADKRYSWEED RGGSLN
//