DAPB_METAQ
ID DAPB_METAQ Reviewed; 934 AA.
AC E9ED72;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 39.
DE RecName: Full=Probable dipeptidyl-aminopeptidase B;
DE Short=DPAP B;
DE EC=3.4.14.5;
GN Name=DAPB; ORFNames=MAC_07820;
OS Metarhizium acridum (strain CQMa 102).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=655827;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CQMa 102;
RX PubMed=21253567; DOI=10.1371/journal.pgen.1001264;
RA Gao Q., Jin K., Ying S.-H., Zhang Y., Xiao G., Shang Y., Duan Z., Hu X.,
RA Xie X.-Q., Zhou G., Peng G., Luo Z., Huang W., Wang B., Fang W., Wang S.,
RA Zhong Y., Ma L.-J., St Leger R.J., Zhao G.-P., Pei Y., Feng M.-G., Xia Y.,
RA Wang C.;
RT "Genome sequencing and comparative transcriptomics of the model
RT entomopathogenic fungi Metarhizium anisopliae and M. acridum.";
RL PLoS Genet. 7:E1001264-E1001264(2011).
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; GL698555; EFY86155.1; -; Genomic_DNA.
DR RefSeq; XP_007814160.1; XM_007815969.1.
DR AlphaFoldDB; E9ED72; -.
DR SMR; E9ED72; -.
DR STRING; 92637.XP_007814160.1; -.
DR ESTHER; metaq-dapb; DPP4N_Peptidase_S9.
DR EnsemblFungi; EFY86155; EFY86155; MAC_07820.
DR GeneID; 19252131; -.
DR KEGG; maw:MAC_07820; -.
DR eggNOG; KOG2100; Eukaryota.
DR HOGENOM; CLU_006105_0_1_1; -.
DR InParanoid; E9ED72; -.
DR OMA; MRTPQEN; -.
DR OrthoDB; 269253at2759; -.
DR Proteomes; UP000002499; 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..934
FT /note="Probable dipeptidyl-aminopeptidase B"
FT /id="PRO_0000412148"
FT TOPO_DOM 1..93
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 94..114
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 115..934
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT REGION 1..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..67
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 759
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 836
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 869
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 354
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 576
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 818
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 934 AA; 104515 MW; 89ED7648E4BC6754 CRC64;
MAPPFTDDPE SQRPSTSRLS QDSLSSVSTT SLVFDRIQEE MDRDPSSSRS ARRDLLSATK
DEGDYEDASE TGAFLGQPGV PLQRQPMDRG FRRILIIIGA VFVGAWLAGL GVFVLSGSYR
HESDSEHDPD AISRGSGKAV TMDQVFGGFW SAKSRSISWI ADPDGGDGLL LEVGTANGYL
VVEDVRADKQ GTDTTSRQTA DTQPAKPRVL MKDPYFMYNG EIKRPEWNEP SPDLKKVLLA
VNLEKNWRHS FQATYFILHV ETAQIQPLVP DNVNAKVQLA NWSPKSDAIS FTMDNNIYIR
RLNQANDVVQ ITKDGGPEYF YGIPDWVYEE EVLAGRSATW WSDDGNYLAF LRTNETAVPE
YAIEYYIQRP SGKKPAVGEE AYPEIRKIKY PKPGAHNPVV DVQYYDVSKG DVFSISAPDE
FPDKDRIISN VLWAGNKVLL KQSNRVGDFL KVILVDPSER KAKIVNSINI AEIDGGWFEI
SHTMTYIPAD PSKGRQQDGY VDTVIHEGYE HIGYFTPIDN PKPIMLTSGS WEVEDAPSAV
DLDNNLVYFV ATKESSIQRH VYSVKLDGSN LTPLTNTSSE GYYAVSFSSR SGFALLSYQG
PKIPYQKVIS TPSIPIEFSR TIEDNAGLAD KAKKHELPIL KYGTLQLPNG ISVNYLERRP
PHFNPKKKYP ILFQQYSGPK SQTVTKKFAV NFQSYVASSL GYLVVTIDPR GTGFLGRQHR
VVVRSQLGVL EAQDHIAAAK HYSSLPYVDP SRLAIWGWSY GGFQTLKTLE VDAGDTFSYG
MAVAPVTDWR FYDSIYTERY MRLPQDNAAG YDASAVHNAT ALGMSKRFLI MHGSADDNVH
FQNSLKLLDY LDLARIENYD VHVFPDSDHG IAFHGANRMV YDSKSEFSVL FSWILSPMLT
LSGLNNWLVN AFNGEWLKIA DPKPIDTKKR RHVS
