DAPB_SORMK
ID DAPB_SORMK Reviewed; 924 AA.
AC D1Z9B4; F7VTE6;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Probable dipeptidyl-aminopeptidase B;
DE Short=DPAP B;
DE EC=3.4.14.5;
GN Name=DAPB; ORFNames=SMAC_05958;
OS Sordaria macrospora (strain ATCC MYA-333 / DSM 997 / K(L3346) / K-hell).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Sordaria.
OX NCBI_TaxID=771870;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-333 / DSM 997 / K(L3346) / K-hell;
RX PubMed=20386741; DOI=10.1371/journal.pgen.1000891;
RA Nowrousian M., Stajich J.E., Chu M., Engh I., Espagne E., Halliday K.,
RA Kamerewerd J., Kempken F., Knab B., Kuo H.-C., Osiewacz H.D., Poeggeler S.,
RA Read N.D., Seiler S., Smith K.M., Zickler D., Kueck U., Freitag M.;
RT "De novo assembly of a 40 Mb eukaryotic genome from short sequence reads:
RT Sordaria macrospora, a model organism for fungal morphogenesis.";
RL PLoS Genet. 6:E1000891-E1000891(2010).
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; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10084};
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}.
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; CABT02000006; CCC08602.1; -; Genomic_DNA.
DR RefSeq; XP_003351079.1; XM_003351031.1.
DR AlphaFoldDB; D1Z9B4; -.
DR SMR; D1Z9B4; -.
DR STRING; 771870.D1Z9B4; -.
DR ESTHER; neucr-q7shu8; DPP4N_Peptidase_S9.
DR EnsemblFungi; CCC08602; CCC08602; SMAC_05958.
DR GeneID; 10808655; -.
DR KEGG; smp:SMAC_05958; -.
DR VEuPathDB; FungiDB:SMAC_05958; -.
DR eggNOG; KOG2100; Eukaryota.
DR HOGENOM; CLU_006105_0_1_1; -.
DR InParanoid; D1Z9B4; -.
DR OMA; MRTPQEN; -.
DR OrthoDB; 269253at2759; -.
DR Proteomes; UP000001881; 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:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002471; Pept_S9_AS.
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.
DR PROSITE; PS00708; PRO_ENDOPEP_SER; 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..924
FT /note="Probable dipeptidyl-aminopeptidase B"
FT /id="PRO_0000412163"
FT TOPO_DOM 1..111
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 112..132
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 133..924
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT REGION 1..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..78
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 768
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
FT ACT_SITE 845
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
FT ACT_SITE 878
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
FT CARBOHYD 231
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 364
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 827
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 924 AA; 104058 MW; 70999F5B74E9B34C CRC64;
MPPFTYSDDT LRSGRDRFRD HSPSQHRRSM SQETDSSAST TSIVFDRIQE RLDTKEFTPR
GTDGDDDGSL KDELNNDDLE TGPFLGNADS SSRSDQRSPG DGQRMDRSLR RWLFIVSGVL
VATWVIGLFV FVSSKAYKPS SSFAHDPQAT VTHGTGKKVT LDQVLNNQWR AKSHSISWIA
GANGEDGLLL EKEGVGKDYL VVEDVRAQNP SSVQASKSKA LIKEKLFEFA NKTYWPSITV
PSRDLKKVLL ATDVKNNWRH SYYAVYWIFD VETQQVEPLV PYDVEARLQL ASWSPTSDAI
VYTRDNNMFL RKLGSDKIVQ ITRDGSADVF NGVPDWVYEE EVLASGVATW WSEDGQYVAF
LRTNETGVPE YPIQYFVSRP SGEEPKPGEE NYPEVRQIKY PKAGAHNPIV DLKFYDVKRG
DVFSVDISGR FADDDRLITE VVWAGKQVLI KETNRVSDVM RVVLVDVGSR TGKAVRTVDV
NAIDGGWFEI SHKTKFIPAD PVNGRPDDGY VDTIIHDNGD HLAYFTPLDN PEPIMLTSGD
YEVVDAPSAV DLQRNLVYFV STKESSIQRH VYQVKLTGED MTPVTDTSKE GYYAISFSTG
AGYAMVSYQG PDIPWQKVIS TPSNPDKYEY VVEENKDLAE AAKKHELPIN IYGTINVDGV
DLNYVERRPP HFDKNKKYPV LFQQYSGPVS QTVKKTFAVD FQSFVAAGLG YICVTVDGRG
TGFIGRKNRV IIRGDLGHWE SHDQIAAAKH WAQKDYIDED RLAIWGWSYG GYMTLKTLEQ
DAGQTFKYGM AVAPVTDWRF YDSIYTERYM RTPQTNLEGY DSAAVTNATA LSQNVRFLLM
HGVADDNVHM QNSLTLLDAL DQRSVENYDV HVFPDSDHGI YFHNANRIVF DKLTNWLVNA
FNGEWLKIAN AQPNGMKKRA APTA
