DAPB_PENRW
ID DAPB_PENRW Reviewed; 903 AA.
AC B6HFS8;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Probable dipeptidyl-aminopeptidase B;
DE Short=DPAP B;
DE EC=3.4.14.5;
GN Name=dapB; ORFNames=Pc20g06070;
OS Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS 54-1255) (Penicillium chrysogenum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC Penicillium chrysogenum species complex.
OX NCBI_TaxID=500485;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255;
RX PubMed=18820685; DOI=10.1038/nbt.1498;
RA van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J.,
RA van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA Bovenberg R.A.L.;
RT "Genome sequencing and analysis of the filamentous fungus Penicillium
RT chrysogenum.";
RL Nat. Biotechnol. 26:1161-1168(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; AM920435; CAP85936.1; -; Genomic_DNA.
DR RefSeq; XP_002563136.1; XM_002563090.1.
DR AlphaFoldDB; B6HFS8; -.
DR SMR; B6HFS8; -.
DR STRING; 1108849.XP_002563136.1; -.
DR ESTHER; pencw-dapb; DPP4N_Peptidase_S9.
DR MEROPS; S09.006; -.
DR EnsemblFungi; CAP85936; CAP85936; PCH_Pc20g06070.
DR GeneID; 8310705; -.
DR KEGG; pcs:Pc20g06070; -.
DR VEuPathDB; FungiDB:PCH_Pc20g06070; -.
DR eggNOG; KOG2100; Eukaryota.
DR HOGENOM; CLU_006105_0_1_1; -.
DR OMA; MRTPQEN; -.
DR OrthoDB; 269253at2759; -.
DR BioCyc; PCHR:PC20G06070-MON; -.
DR Proteomes; UP000000724; Contig Pc00c20.
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..903
FT /note="Probable dipeptidyl-aminopeptidase B"
FT /id="PRO_0000412156"
FT TOPO_DOM 1..90
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 91..111
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 112..903
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT REGION 1..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 121..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..46
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 268
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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"
SQ SEQUENCE 903 AA; 100902 MW; D00566741A21990E CRC64;
MGKFEDDGNS ESVPLTRQRS ESLASQTSTD SGLSIASESF MKNHKGGNTM PTDGGDGDRY
LDVEDGGETG LDEPLISSGT KTGSSSRLRK IVWLLVLLCV GGWVLSFVLF LTQKRPDTAA
LSSASTVEIH EPGPATGGTS HGKPVTLEQV LSGTWSPKSH AISWIAGPDG EDGLLVEQGE
KQDAFLRVKD IRSSEDGVDN LETRVLMKKG YIWFDGEAML SAKTWPSPDM NRVLVMTDIQ
SNWRHSYFGK YWILDVATQK AEPLDPGNLS GRVQLAAWSP TSDAVVFVRE NNLYLRKLTS
LEVTPITKDG DENLFYGVPD WVYEEEVFSG NTGTWWSDDG KFVAFLRTNE TAVPEYPIQY
FRSRPSGKQP PPGLENYPEV RQIKYPKPGS PNPIVNLQFY DVEKNEVFSF EMPEDFVDDE
RIIIEVVWAS EGKVLIRETN RESDVVKIFV MDTKARTGKL VRSDDIAALD GGWVEPTQST
RVIPADPKNG RPHDGYVDTV IYEGYDHLAY FTPFDNPEPV MLTKGNWEVV NAPSAVDLKK
GLVYFVATKE APTQRHVYSV KLDGSDLRPL TDTSAPGFFD VSFSHGAGYG LLSYKGPAVP
WQAVINTQGD EIDFINLIEE NVELAKMVEE SAIPTEVYSN VTIDGYTLQV LERRPPNFNP
EKKYPVLFFL YGGPGSQTVD RKFTIDFQTY VASNLGYIVV TVDGRGTGFI GREARCLVRG
NIGHYEAIDQ IETAKIWASK SYVDESRMAV WGWSYGGYMT LKVLEQDAGE TFQYGMAVAP
VTDWRFYDSI YTERYMHTPE HNPSGYANAS IDDVMALGHS VRFLIMHGVA DDNVHLQNTL
VLIDKLDLKN IDNYDMQVFP DSDHSIQFHM AHALVYERLS SWLINAFNGE WHRTANPKPQ
EST
