DAPB_ASPTN
ID DAPB_ASPTN Reviewed; 914 AA.
AC Q0CXB1;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Probable dipeptidyl-aminopeptidase B;
DE Short=DPAP B;
DE EC=3.4.14.5;
GN Name=dapB; ORFNames=ATEG_01673;
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10084};
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; CH476595; EAU38430.1; -; Genomic_DNA.
DR RefSeq; XP_001209038.1; XM_001209038.1.
DR AlphaFoldDB; Q0CXB1; -.
DR SMR; Q0CXB1; -.
DR STRING; 341663.Q0CXB1; -.
DR ESTHER; asptn-dapb; DPP4N_Peptidase_S9.
DR MEROPS; S09.006; -.
DR EnsemblFungi; EAU38430; EAU38430; ATEG_01673.
DR GeneID; 4315814; -.
DR VEuPathDB; FungiDB:ATEG_01673; -.
DR eggNOG; KOG2100; Eukaryota.
DR HOGENOM; CLU_006105_0_1_1; -.
DR OMA; MRTPQEN; -.
DR OrthoDB; 269253at2759; -.
DR Proteomes; UP000007963; 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:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002471; Pept_S9_AS.
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.
DR PROSITE; PS00708; PRO_ENDOPEP_SER; 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_0000412139"
FT TOPO_DOM 1..89
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 90..110
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 111..914
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT REGION 1..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..73
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 752
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
FT ACT_SITE 829
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
FT ACT_SITE 862
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
FT CARBOHYD 347
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 638
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 806
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 914 AA; 102747 MW; 549E8ABBD3DE5314 CRC64;
MGKSEADEDA QFLPMNRPRS SSAASQTSSD SGLSVESALI RNSTYGKTPD EAYNPAGDPR
YRDIEDGEAE SDQPFLPSRK GSGARARRVF WGLLLLCLAG WVLAFVLFLI QGRSGYSATS
EELQQHEADS SAGVTSDGKP VTLKQVLSGD WLPRSHGIAW IAGPDGEDGL LVEAGEDGGE
GFLRVKDIRA RHGDDAGTLK SRVLMKKSTF YAGQRSILTR LTWPSPDLKK VLVLSDYEKN
WRHSYTGLYW IFDVDSQTAE PLDPDVPEGR VQLASWSPNS DAVVFVRDNN MFLRKLSSDK
VVPITKDGGK DLFYGVPDWV YEEEVLSGNS ATWWSNDAKY VAFLRTNEST VPEYPVQYFL
SRPSGKKPLP GLEDYPDVRQ IKYPKAGAPN PVVNLQFYNV EKNEVFSVEV PDDFADDDRI
IIEVLWAAES NVLVRATNRE SDVLKIFLID TESRTGKMVR LEDIVGLDGG WVEPSQSTRF
IPADPAAGRP NDGYIDTVIH DGYDHLAYFT PLDNPEPIML TTGEWEVVEA PTAVDLRRGL
VYFVATKEAP TQRHVYQVQL DGSNLKPLTD TSKPGYYHVS FSDGTAYALL SYQGPSIPWQ
AIINTEGDDV VFEETIEENP ELARMVETYA IPSKVFSNIT IDGFTLQMVE RRPPHFNPHK
KYPVLFFLYG GPGSQTVDRK FTIDFQSYVA SNLGYIVVTL DGRGTGFIGR EARCIIRGNL
GYYEAHDQIT AAKMFAEKSY VDESRMAIWG WSYGGFMTLK TLEQDAGQTF QYGMAVAPVT
DWRFYDSIYT ERYMHTPQHN PSGYDNSSIT DMAALEENVR FLVMHGASDD NVHLQNTLTL
IDKLDLSNVQ NYDVHFYPDS DHSIFFHNAH YMVYERLSNW LVNAFNGEWH RIAAPVPDNS
MWQRFKRALP VFVH
