DAPB_METRA
ID DAPB_METRA Reviewed; 915 AA.
AC E9ETL5;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 04-MAR-2015, sequence version 2.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Probable dipeptidyl-aminopeptidase B;
DE Short=DPAP B;
DE EC=3.4.14.5;
GN Name=DAPB; ORFNames=MAA_03364;
OS Metarhizium robertsii (strain ARSEF 23 / ATCC MYA-3075) (Metarhizium
OS anisopliae (strain ARSEF 23)).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=655844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 23 / ATCC MYA-3075;
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).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ARSEF 23 / ATCC MYA-3075;
RX PubMed=25368161; DOI=10.1073/pnas.1412662111;
RA Hu X., Xiao G., Zheng P., Shang Y., Su Y., Zhang X., Liu X., Zhan S.,
RA St Leger R.J., Wang C.;
RT "Trajectory and genomic determinants of fungal-pathogen speciation and host
RT adaptation.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:16796-16801(2014).
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; ADNJ02000003; EFZ00768.2; -; Genomic_DNA.
DR RefSeq; XP_007819553.2; XM_007821362.2.
DR AlphaFoldDB; E9ETL5; -.
DR SMR; E9ETL5; -.
DR ESTHER; metar-dapb; DPP4N_Peptidase_S9.
DR EnsemblFungi; EFZ00768; EFZ00768; MAA_03364.
DR GeneID; 19257650; -.
DR KEGG; maj:MAA_03364; -.
DR HOGENOM; CLU_006105_0_1_1; -.
DR Proteomes; UP000002498; 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..915
FT /note="Probable dipeptidyl-aminopeptidase B"
FT /id="PRO_0000412149"
FT TOPO_DOM 1..94
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 95..115
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 116..915
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT REGION 1..82
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 760
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 837
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 870
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 355
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 577
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 819
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 915 AA; 102613 MW; 8F1FCAEF3680F64D CRC64;
MAPPFTDDPE SQRPSTSRLS QDSLSSVSTT SLVFDRIQEE MDRDPSASRS ARRDLLPATK
DEGDFDENAS ETGAFLGPPG VPLQRQPMDR GFRRILIIIG AVFVGAWLAG LGIFVLSGSY
KHESDSEHDP DANSRGSGKA VTMDQVFGGF WSARSHSISW IADPDGGDGL LLEVNTANGY
LVVEDVRADK ESTDTNAGQT ADTQPAKPRV LMRDPYFMYH GEIKRPDWNE PSPDLKKVLL
AVKREKNWRH SFQATYFILD VETAQVQPLV PDNVNAKVQL ANWSPTSDAI SFTMDNNIYI
RRLNQANDVV QITKDGGPEY FYGIPDWVYE EEVFAGRSAT WWSDDGKYLA FLRTNETAVP
EYAIEYYIQR PSGKKPAVGE EAYPEIRKIK YPKPGAHNPV VDVQYYDVSK GDVFSISAPD
EFPDHDRIIS NVLWAGNKVL LKQSNRIGDF LKVILVDPSQ REAKIVNSIN IAEIDGGWFE
ISHTMTYIPA DPSKGRQQDG YVDTVIHEGY EHIGYFTPID NPKPIMLTSG SWEVEDAPSA
VDLNNNLVYF VATKESSIQR HVYSVKLDGT NLTPLTNTSS EGYYTVSFSS RSGFALLSYK
GPKIPYQKVI STPSIPIQFS RTIEDNADLA DKAKKHELPI LKYGTLQLPN GISVNYLERR
PPHFNPKKKY PILFQQYSGP KSQTVTKKFA VDFQSYVASS LGYLVVTIDP RGTGFLGRQH
RVVVRSQLGV LEAQDHIAAA KHYSSLPYVD PSRLAIWGWS YGGFQTLKTL EVDAGDTFSY
GMAVAPVTDW RFYDSIYTER YMRLPQDNTA GYDASAVRNA TALGMNKRFL IMHGSADDNV
HFQNSLKLLD YLDLAGIENY DVHVFPDSDH SIAFHGANRM VYDRLNNWLV NAFNGEWLKI
ADPKPIDTKK RRHVS
