ID   DAPB_COLGM              Reviewed;         921 AA.
AC   E3QKD2;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, 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=GLRG_06464;
OS   Colletotrichum graminicola (strain M1.001 / M2 / FGSC 10212) (Maize
OS   anthracnose fungus) (Glomerella graminicola).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum graminicola species complex.
OX   NCBI_TaxID=645133;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M1.001 / M2 / FGSC 10212;
RX   PubMed=22885923; DOI=10.1038/ng.2372;
RA   O'Connell R.J., Thon M.R., Hacquard S., Amyotte S.G., Kleemann J.,
RA   Torres M.F., Damm U., Buiate E.A., Epstein L., Alkan N., Altmueller J.,
RA   Alvarado-Balderrama L., Bauser C.A., Becker C., Birren B.W., Chen Z.,
RA   Choi J., Crouch J.A., Duvick J.P., Farman M.A., Gan P., Heiman D.,
RA   Henrissat B., Howard R.J., Kabbage M., Koch C., Kracher B., Kubo Y.,
RA   Law A.D., Lebrun M.-H., Lee Y.-H., Miyara I., Moore N., Neumann U.,
RA   Nordstroem K., Panaccione D.G., Panstruga R., Place M., Proctor R.H.,
RA   Prusky D., Rech G., Reinhardt R., Rollins J.A., Rounsley S., Schardl C.L.,
RA   Schwartz D.C., Shenoy N., Shirasu K., Sikhakolli U.R., Stueber K.,
RA   Sukno S.A., Sweigard J.A., Takano Y., Takahara H., Trail F.,
RA   van der Does H.C., Voll L.M., Will I., Young S., Zeng Q., Zhang J.,
RA   Zhou S., Dickman M.B., Schulze-Lefert P., Ver Loren van Themaat E.,
RA   Ma L.-J., Vaillancourt L.J.;
RT   "Lifestyle transitions in plant pathogenic Colletotrichum fungi deciphered
RT   by genome and transcriptome analyses.";
RL   Nat. Genet. 44:1060-1065(2012).
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; GG697354; EFQ31320.1; -; Genomic_DNA.
DR   RefSeq; XP_008095340.1; XM_008097149.1.
DR   AlphaFoldDB; E3QKD2; -.
DR   SMR; E3QKD2; -.
DR   STRING; 645133.E3QKD2; -.
DR   ESTHER; colgm-dapb; DPP4N_Peptidase_S9.
DR   GlyCosmos; E3QKD2; 4 sites, No reported glycans.
DR   EnsemblFungi; EFQ31320; EFQ31320; GLRG_06464.
DR   GeneID; 24411829; -.
DR   VEuPathDB; FungiDB:GLRG_06464; -.
DR   eggNOG; KOG2100; Eukaryota.
DR   HOGENOM; CLU_006105_0_1_1; -.
DR   OrthoDB; 2876738at2759; -.
DR   Proteomes; UP000008782; Unassembled WGS sequence.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; IEA:EnsemblFungi.
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; alpha/beta hydrolase; 1.
DR   Gene3D; 2.140.10.30; Dipeptidylpeptidase IV, N-terminal domain; 1.
DR   InterPro; IPR029058; AB_hydrolase.
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.
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..921
FT                   /note="Probable dipeptidyl-aminopeptidase B"
FT                   /id="PRO_0000412144"
FT   TOPO_DOM        1..108
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        109..129
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        130..921
FT                   /note="Vacuolar"
FT                   /evidence="ECO:0000255"
FT   REGION          1..87
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        13..34
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        35..49
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        768
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        845
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        878
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        131
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        364
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        577
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        827
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   921 AA;  103378 MW;  92129EF1EB01470B CRC64;
     MDAPATASRQ PIAEEPRMSQ ESSLSTVSTT SLVFDRLHEH NEKSYHSSSQ RRRAPSASRG
     GYADHPDDDD DDDESYKEAD TNDLETGPFL APASVMMRRV GVDRGLKKVI LILAAAFLFA
     WGAALFVFLS NKSYKHASTI DHDPSATSRG SGKPVTLDQV ISGFWYPTSH SISWIEGPNG
     EDGLLLEQGA RGKDYLVVED VRSGNKDSQV SANVVQSRTL MKNPWINVGG RQLAPSDTRP
     SKDMKKVLVS TDRQRNWRYS YTALYWIFDV ETQTAEALDP EHPDGRVQLA TWSPQSNAIV
     FTRDNNLFLR KLDGDKKVTQ ITNDGGPEYF YGIPDWVYEE EVFATNSATW YSEDGKYVAF
     LRTNETGVPE YPLQYFLSRP SGKEKPPGEE TYPDEKRIKY PRAGSHNPVV DLLFFDVERG
     DVFSVDIDGG FADDDRLINM VLWANDKVLI KETNRVSDIM RVVLVDVVAR TGKTVNTIDV
     GELDGGWFEI SHTTQFIPAD PANGRPQDGY IDTVVHGNGD HIAYFSPMDN AEPVYLTGGD
     WEVDDGPSAV DLKNNLVYFV ATKESSIQRH VYSVHLNRSD LKPFTDTKFE SYYDISFSSG
     AGYALLSYQG PKIPWQKVVS TPSSPVSYEH VVEKNEDLAE NAKKYELPIL NYGTLKVDGV
     ELNYVERRPP HFDEKKKYPV LFQQYSGPGS QSVHKKFAVD FQSYVASALG YLVVTVDGRG
     TGFIGRKNRV LIRDHLGYWE AHDQIAAAQA WAAKKYVDPA RIAIWGWSYG GFNTLKTLEM
     DAGRTFSYGM AVAPVTDWRF YDSIYTERYM RTPQLNPSGY DQTAVSNVSA LAGNVRWLMM
     HGVGDDNVHY QNTLTLLDKL DLNGIENYDV HVFPDSDHGI YFHGANRIVY DKLSNWLINA
     FNGEWLKVAG AKPIVEPKAR V
//