DAPB_ASPFN
ID DAPB_ASPFN Reviewed; 916 AA.
AC B8N076;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, 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=AFLA_087160;
OS Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS / JCM 12722 / SRRC 167).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=332952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC 167;
RX PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT aflatoxin contamination of food and feed.";
RL Genome Announc. 3:E0016815-E0016815(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; EQ963472; EED58018.1; -; Genomic_DNA.
DR RefSeq; XP_002373630.1; XM_002373589.1.
DR AlphaFoldDB; B8N076; -.
DR SMR; B8N076; -.
DR STRING; 5059.CADAFLAP00001495; -.
DR ESTHER; aspor-q2upw4; DPP4N_Peptidase_S9.
DR MEROPS; S09.006; -.
DR EnsemblFungi; EED58018; EED58018; AFLA_087160.
DR VEuPathDB; FungiDB:AFLA_087160; -.
DR eggNOG; KOG2100; Eukaryota.
DR HOGENOM; CLU_006105_0_1_1; -.
DR OMA; MRTPQEN; -.
DR Proteomes; UP000001875; 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 Serine protease; Signal-anchor; Transmembrane; Transmembrane helix;
KW Vacuole.
FT CHAIN 1..916
FT /note="Probable dipeptidyl-aminopeptidase B"
FT /id="PRO_0000412134"
FT TOPO_DOM 1..92
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..113
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 114..916
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 67..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 754
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 831
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 864
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 349
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 640
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 808
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 813
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 916 AA; 103230 MW; 483BB24C1B0F377E CRC64;
MGRTGDLENA EFFPMTRRRS TSGTSSRSST DSGLSVDTAY LEDNKHNNFA NGTSGLTDET
KYRDVEDAEA DVDEPFLPTS SKKLGSGSRT RQIFWALVIL CLGGWVLALV LFLTHGRASS
QTASETLQQQ ESDSGSTSAG RPVTLQQVLT GSWNPRAHAI SWIAGPDGED GLLVQRAEVD
KEGYMRVDDI RSQEGDDVDS QSGRILIDKA AVRVNGETLM PTFTWPSPDL NKVLLMSNHE
KNWRYSFTGR YWIFDVATQT AQPLDPSVPD GRVQLALWSP SSDAVVFVRD NNMYLRKLSS
ESVVSITKDG GEDLFYGIPD WVYEEEVITD KSVTWWSNDG KYVAFLRTNE SAVPEFPVQY
FVSRPSGKRP PPGLENYPEV RQIKYPKAGS PNPVVNLLFY DVEKDEVFPV DVPDDFPDDD
RIIIEVLWAS EGKVIVRATN RESDRVKVFL IDTKSRTGKL VRFEDIANLD GGWVEPSHYT
KFIPADPSNG RPDDGYIDTV IHDGYDHLAY FTPLDNPDPI MLTTGEWEVV EAPSAVDLRR
GIVYFVATKE SPTQRHVYRV HLDGSNLQAL TDTSKPGFYD VSFSDGAGYA LLSYNGPSVP
WQAIINTGGD EITFEKTIEK NPRLASMVET YALPTEIYQN VTIDGFTLQL VERRPPHFNP
AKKYPVVFQL YNGPTSQRVD RKFTIDFQSY IASNLGYIVV TLDARGTGYS GRKVRCAVRG
NLGHYEAHDQ ITTAKMWAKK PYVDETRMAI WGWSYGGFMT LKVLEQDAGE TFQYGMAVAP
VTDWRFYDSV YTERYMHTPE HNPSGYENST ITNVSALSKA TRFLLIHGAS DDNVHIQNTL
TFVDKLDLLN VQNYDMHFYP DSDHNIYFHN AHFMIYERLS NWLINAFNGE WHQIANPVPE
DSIWDSVKRS VPAFAH
