DAPB_TRIVH
ID DAPB_TRIVH Reviewed; 899 AA.
AC D4DCG0;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=Probable dipeptidyl-aminopeptidase B;
DE Short=DPAP B;
DE EC=3.4.14.5;
GN Name=DAPB; ORFNames=TRV_04813;
OS Trichophyton verrucosum (strain HKI 0517).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663202;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HKI 0517;
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(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; 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; ACYE01000244; EFE40482.1; -; Genomic_DNA.
DR RefSeq; XP_003021100.1; XM_003021054.1.
DR AlphaFoldDB; D4DCG0; -.
DR SMR; D4DCG0; -.
DR ESTHER; artbc-dapb; DPP4N_Peptidase_S9.
DR EnsemblFungi; EFE40482; EFE40482; TRV_04813.
DR GeneID; 9577942; -.
DR KEGG; tve:TRV_04813; -.
DR HOGENOM; CLU_006105_0_1_1; -.
DR Proteomes; UP000008383; 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 Serine protease; Signal-anchor; Transmembrane; Transmembrane helix;
KW Vacuole.
FT CHAIN 1..899
FT /note="Probable dipeptidyl-aminopeptidase B"
FT /id="PRO_0000412165"
FT TOPO_DOM 1..99
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 100..120
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 121..899
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT REGION 1..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 765
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
FT ACT_SITE 842
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
FT ACT_SITE 875
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
FT CARBOHYD 212
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 308
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 360
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 819
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 824
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 827
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 893
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 899 AA; 101076 MW; CD9AF2AD45BBFCB8 CRC64;
MKLDRMRVGS RINDEEAMPL TAPESRARDS IDSSSTASIS LTLVEGASHA TTEPSKPAHN
HNGRTQGNYA EKYRDDLEED WEENNYIPTN GKSSQRRTLI VFWLLVALCV GGWAVAFLFF
VTSPGNKTST SPHSGSNSPE GDVTKPGIPA TGKKIPLDDA IGGVWSPAEH TISWIAGAKG
EDGLLLQKSE GGTGPYLHVE DVRNIHGTQS NNNSIVLMKE SVFFVNDERI SPEKVWPSPD
LKTVLAMTRE KKNWRHSFTG LYWLFDVETQ TAQPLDPDAP NGRIQLATWS PTSDAVAFTR
DNNLYIRNLT SKSVKAITTD GGTNLFYGIP DWVYEEEVFE GNIATWWSLD GKYISYLRTN
ETLVPEFPID FYLSSPPGYS PKPGEESYPY VQQIKYPKAG APNPTVSLQF YDIEREESFS
VDVKDTLKDD DRLIVEVIPG SKGKVLVRET NRESYIVKVA VIDANKREGK IVRSDNIDEI
DGGWVEPSHT TTYIPADPSA GRPDDGYIDT VIHEGYIHLA YFTPLENPKP KMLTTGKWEV
VAAPSGVDLK NNVVYFVATK ESPIDRHVYS VKLDGSELRM LKDSDKSAYY DVSFSHGAGY
MLLKYQGPQI PWQKLISSPS NADNYIEILE ENKKLAKLSN EFALPSLHYS TITVDGFELP
VVERRPPNFD ETKKYPVLFQ LYGGPGSQTV NKKFLVNFQT YVASNLGYIV VTVDGRGTGF
NGRKFKCIVR RNLGHYEAHD QIQAAKAWGK KPYVDKTRMA IWGWSYGGFM TLKTLEQDAG
ETFQYGMAVA PVTNWRYYDS VYTERYMHMP QNNEGGYENA SISNATNLSQ NTRFLIMHGS
ADDNVHFQNT LTLLDKLDIL GVHNYDMHVF PDSNHGIYFH HAYKMVHQRK YFNLSFLGH
