ID   DAPB_CHAGB              Reviewed;         925 AA.
AC   Q2HF90;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Probable dipeptidyl-aminopeptidase B;
DE            Short=DPAP B;
DE            EC=3.4.14.5;
GN   Name=DAPB; ORFNames=CHGG_01114;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970;
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   -!- FUNCTION: Type IV dipeptidyl-peptidase which removes N-terminal
CC       dipeptides sequentially from polypeptides having unsubstituted N-
CC       termini provided that the penultimate residue is proline.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, from a
CC         polypeptide, preferentially when Yaa is Pro, provided Zaa is neither
CC         Pro nor hydroxyproline.; EC=3.4.14.5;
CC   -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000250}; Single-pass type
CC       II membrane protein {ECO:0000250}. Note=Lysosome-like vacuoles.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S9B family. {ECO:0000305}.
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DR   EMBL; CH408029; EAQ92879.1; -; Genomic_DNA.
DR   RefSeq; XP_001220335.1; XM_001220334.1.
DR   AlphaFoldDB; Q2HF90; -.
DR   SMR; Q2HF90; -.
DR   STRING; 38033.XP_001220335.1; -.
DR   ESTHER; chagb-q2hf90; DPP4N_Peptidase_S9.
DR   PRIDE; Q2HF90; -.
DR   EnsemblFungi; EAQ92879; EAQ92879; CHGG_01114.
DR   GeneID; 4388188; -.
DR   eggNOG; KOG2100; Eukaryota.
DR   HOGENOM; CLU_006105_0_1_1; -.
DR   InParanoid; Q2HF90; -.
DR   OMA; MRTPQEN; -.
DR   OrthoDB; 269253at2759; -.
DR   Proteomes; UP000001056; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008239; F:dipeptidyl-peptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR001375; Peptidase_S9.
DR   InterPro; IPR002469; Peptidase_S9B_N.
DR   Pfam; PF00930; DPPIV_N; 1.
DR   Pfam; PF00326; Peptidase_S9; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase; Glycoprotein; Hydrolase; Membrane; Protease;
KW   Reference proteome; Serine protease; Signal-anchor; Transmembrane;
KW   Transmembrane helix; Vacuole.
FT   CHAIN           1..925
FT                   /note="Probable dipeptidyl-aminopeptidase B"
FT                   /id="PRO_0000412141"
FT   TOPO_DOM        1..110
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        111..131
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        132..925
FT                   /note="Vacuolar"
FT                   /evidence="ECO:0000255"
FT   REGION          1..104
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        28..44
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        50..68
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        773
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        850
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        883
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        369
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        832
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   925 AA;  102583 MW;  A6C59C5AB4BE82DF CRC64;
     MTPYRDVPPV SSRTHSSNRD RSQSRSRMSH ESGSSVSTTS IVFDRISERV AAGDLSEKQP
     RGDDNEDALK DEPDNDDLET GPFLGNASGN GNSPRHAQKK GPGMDRGMRR ALLIAAGLLV
     SAWVAGLFVY IATKSYKPAS ATAHDPQATI VRGSGKAVTL DQVMGSFWRP EVRSIQWIAG
     PEGEDGLLLE RDAAGKDYLV VEDIRSQDAA AVDSSADAQA ADARTLMEKG SFEYGKRVYN
     AVKVAPSRDL QRVLVATDVK SNWRHSSYAA YWIFDVKTQT ADPLVPGEPD ARIQLAQWNP
     TGDAVAFTRD NNLYLRKVGS DNIIQVTKDG GSEVFNGVPD WVYEEEVFSG SSATWWSEDG
     DYIAFLRTNE TGVPEFPIDY FLKRPSGTEP KPGEEAYPET RKIKYPKAGA HNPVVELKFY
     DVVRGDVFSV DISGGFADDD RLITEVVWAG KQILVKETNR VSDVMRVVLV DVAARSGKTV
     RTTDVKAIDG GWFEITHQTK HIPADPSKGR EHDGYIDLII HGDGNHLAYF TPLDNPDPVM
     LTSGDWEVVD SPYAVDLDKN VVYFMATKES SIQRHVYQVK LTGEDLTAVS DTSSEGYYAA
     SFSIGGGYAL LTYQGPGIPW QKVISTPSNP RKYEHTVEEN KDLADNAKKH ELPIKIYGTI
     NVDGVELNYV ERRPAHFDAS KKYPVLFQQY SGPGSQTVNK KFTVDFQSYV AAGLGYICVT
     VDGRGTGYIG RKNRVIVRGN LGQWEAHDQI AAAKIWAKKK YIDETRLAIW GWSFGGFNAL
     KTLEQDAGET FRYGMAVAPV TDWRFYDSIY TERYMLTPQA NGHGYDTSAI YNTTALGQNV
     RFLLMHGLAD DNVHFQSSLT LLDKLNLAGV ENYDVHVFPD SDHSIYFHNA NRIVYDKLTN
     WLINAFNGEW IKVASPKPNG KRRAA