DAPB_ASPCL
ID DAPB_ASPCL Reviewed; 914 AA.
AC A1CJQ1;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Probable dipeptidyl-aminopeptidase B;
DE Short=DPAP B;
DE EC=3.4.14.5;
GN Name=dapB; ORFNames=ACLA_035780;
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027056; EAW09375.1; -; Genomic_DNA.
DR RefSeq; XP_001270801.1; XM_001270800.1.
DR AlphaFoldDB; A1CJQ1; -.
DR SMR; A1CJQ1; -.
DR STRING; 5057.CADACLAP00003660; -.
DR ESTHER; aspcl-dapb; DPP4N_Peptidase_S9.
DR MEROPS; S09.006; -.
DR EnsemblFungi; EAW09375; EAW09375; ACLA_035780.
DR GeneID; 4703117; -.
DR KEGG; act:ACLA_035780; -.
DR VEuPathDB; FungiDB:ACLA_035780; -.
DR eggNOG; KOG2100; Eukaryota.
DR HOGENOM; CLU_006105_0_1_1; -.
DR OMA; MRTPQEN; -.
DR OrthoDB; 269253at2759; -.
DR Proteomes; UP000006701; 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..914
FT /note="Probable dipeptidyl-aminopeptidase B"
FT /id="PRO_0000412132"
FT TOPO_DOM 1..91
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..112
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 113..914
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 753
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 830
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 863
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 348
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 565
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 639
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 807
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 914 AA; 102054 MW; B72E64B88D3C541D CRC64;
MATFSDHETS EFLPMTRPRS TSSASQTSSD SGLSSEPAFQ EDQKQPFSAP NGTTGMDNGD
RYRDLEDGEA EANEPFLASS KKAATGGRAR RIFWLLVLLC FGGWLLAFVL FLTGGRANYQ
SASDALQAQE PESASGSTSS GKPVTLEQVL TGQWSPRYHA ITWVAGPNDE DGLLVEKGGG
EQEGYLRVDD IQSRKNKDGK GGRVLMRKPI VHVDGKLVVP GNAWPSPDLK KVLLISDQEK
NWRHSFTGKY WVLDVESQTA QPLDPSLPDG RVQLALWSPK SDAVIFVREN DVYLRKLSSD
RVVTVTKDGG ENLFYGVPDW VYEEEVISGR SVTWWSNDAK YVAFFRTNES AVSDFPVDYF
LSRPSGKKPD PGLENYPEVR QIKYPKAGAS NPVVDLQFYD VEKNEVFSVD VADDFDNDDR
IIIEVVWASE GKVLVRSTNR ESDILKVFLI DTKSRTGRVV RTEDVASLDG GWVEPSQSTR
FIPADPSNGR PDDGYIDTVP YKGYDHLAYF SPLDSPKGVM LTSGDWEVVD APAAVDLQRG
LVYFVAAKEA PTERHIYRVQ LDGSNMTAIT DTSKPGYFGV SFSHGAGYAL LTYNGPSVPW
QAIINTHGDE ITFEERIEEN PQLTSMIEAY ALPTEIYQNV TVDGFTLQVV ERRPPHFNPA
KKYPVLFYLY GGPGSQTVDR KFSIDFQSYV ASSLGYIVVT VDGRGTGHIG RKARCIVRGN
LGFYEARDQI ATAKIWAAKS YVDESRMAIW GWSFGGFMTL KTLELDAGET FQYGMAVAPV
TDWRFYDSIY SERYMHTPQH NPSGYANSTI TDMAALTHPV RFLVMHGTAD DNVHLQNTLV
LTDKLDLSNV KNYDLHFFPD SDHSIFFHNA HAMVYDRLSS WLVNAFNGEW HRIAHPVPGE
SMWTRFKRSL PVLV
