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   27-MAR-2024, entry version 50.
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   GlyCosmos; D4DCG0; 7 sites, No reported glycans.
DR   GeneID; 9577942; -.
DR   KEGG; tve:TRV_04813; -.
DR   HOGENOM; CLU_006105_0_1_1; -.
DR   OrthoDB; 2876738at2759; -.
DR   Proteomes; UP000008383; Unassembled WGS sequence.
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; alpha/beta hydrolase; 1.
DR   Gene3D; 2.140.10.30; Dipeptidylpeptidase IV, N-terminal domain; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR002471; Pept_S9_AS.
DR   InterPro; IPR001375; Peptidase_S9.
DR   InterPro; IPR002469; Peptidase_S9B_N.
DR   PANTHER; PTHR11731:SF200; DIPEPTIDYL PEPTIDASE FAMILY MEMBER 2; 1.
DR   PANTHER; PTHR11731; PROTEASE FAMILY S9B,C DIPEPTIDYL-PEPTIDASE IV-RELATED; 1.
DR   Pfam; PF00930; DPPIV_N; 1.
DR   Pfam; PF00326; Peptidase_S9; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF82171; DPP6 N-terminal domain-like; 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
//