GenomeNet

Database: UniProt
Entry: Q2H127_CHAGB
LinkDB: Q2H127_CHAGB
Original site: Q2H127_CHAGB 
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system