ID   DAPB_VERA1              Reviewed;         875 AA.
AC   C9SJ15;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   24-NOV-2009, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   RecName: Full=Probable dipeptidyl-aminopeptidase B;
DE            Short=DPAP B;
DE            EC=3.4.14.5;
GN   Name=DAPB; ORFNames=VDBG_05047;
OS   Verticillium alfalfae (strain VaMs.102 / ATCC MYA-4576 / FGSC 10136)
OS   (Verticillium wilt of alfalfa) (Verticillium albo-atrum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX   NCBI_TaxID=526221;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VaMs.102 / ATCC MYA-4576 / FGSC 10136;
RX   PubMed=21829347; DOI=10.1371/journal.ppat.1002137;
RA   Klosterman S.J., Subbarao K.V., Kang S., Veronese P., Gold S.E.,
RA   Thomma B.P.H.J., Chen Z., Henrissat B., Lee Y.-H., Park J.,
RA   Garcia-Pedrajas M.D., Barbara D.J., Anchieta A., de Jonge R., Santhanam P.,
RA   Maruthachalam K., Atallah Z., Amyotte S.G., Paz Z., Inderbitzin P.,
RA   Hayes R.J., Heiman D.I., Young S., Zeng Q., Engels R., Galagan J.,
RA   Cuomo C.A., Dobinson K.F., Ma L.-J.;
RT   "Comparative genomics yields insights into niche adaptation of plant
RT   vascular wilt pathogens.";
RL   PLoS Pathog. 7:E1002137-E1002137(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;
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; DS985218; EEY18938.1; -; Genomic_DNA.
DR   RefSeq; XP_003005441.1; XM_003005395.1.
DR   AlphaFoldDB; C9SJ15; -.
DR   SMR; C9SJ15; -.
DR   STRING; 526221.C9SJ15; -.
DR   ESTHER; vera1-dapb; DPP4N_Peptidase_S9.
DR   GlyCosmos; C9SJ15; 3 sites, No reported glycans.
DR   GeneID; 9532123; -.
DR   KEGG; val:VDBG_05047; -.
DR   eggNOG; KOG2100; Eukaryota.
DR   HOGENOM; CLU_006105_0_1_1; -.
DR   OMA; MRTPQEN; -.
DR   OrthoDB; 2876738at2759; -.
DR   Proteomes; UP000008698; 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: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..875
FT                   /note="Probable dipeptidyl-aminopeptidase B"
FT                   /id="PRO_0000412168"
FT   TOPO_DOM        1..98
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        99..119
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        120..875
FT                   /note="Vacuolar"
FT                   /evidence="ECO:0000255"
FT   REGION          1..90
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          689..715
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        33..70
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        726
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        803
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        836
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        354
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        567
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        785
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   875 AA;  98704 MW;  6ED2051D22DBFEB2 CRC64;
     MSEPKPIQDT LDRRHSRESS ISSASTTSLV FDRLAEESEK NHDASSRPHP SAARHAYTDD
     NSDAIKESDI NDPETGPFLG ASSETTPPRK GVDRKLKKVL LIVGGFFVAA WIVSLVVFLT
     NKSYKHGSQI DHDPAATNRK SGKRVTLDQV QSGFWRPTSH TFSWIPGPDG EDGLLLEQEA
     RGKHFLVVED VRSQGSADGE AHPDAAESRT LIKDPWFYWG DQQHSILQTW PSKNQKKVLV
     ATQKQRNWRH SFTALYWVFD VESQSAEPLD PAHPEERVQL ATWNAQSDAI VFTRSNNLFL
     RKLADDKVTP ITTDGGPEYF YGIPDWVYEE EVFSGNSATW WSADGKHVAF LRTNETEVPE
     YPIQYFVSRP SGAEPEVGEE NYPEVRQIKY PKVGSPNPVV DLLFYDVEKG DVFTVDIDGD
     FPEKDKLINF VMWADGNVLV KTTNRVSDVL QVNLIDIVAR TGKTVQHVDV AKIDGGWFEI
     SHVMYIPADP KNGRPHDGYV DTVIHNDGDH LAYFTPMDNP KPVYITEGPG WEVDGSASAV
     DLKNNLVYFR STKESSIQRH IYSVHLNGTD MKPFTDTTHE SYYDVSFSSG AGFGLLSYQG
     PKVPWQKVVS TPSNPKSYER IIEENKDLTQ QAKKHELPVL EYGTIKVDDV ELNYVERRPP
     HFDKNKKYPV LFQQYSGPGS QTVTKKFAVD FQSSDGGRRT TRSPRRATGR PSATSTPTAF
     AIWGWSYGGF ATLKTLETDA GRTFRYGMAV APVTDWRFYD SIYTERYMRT PDLNRNGYQQ
     TAISNTTALG ANERFLVMHG VADDNVHMQN TLTLLDELDL AGVENYDVHV FPDSDHSIYF
     HNANRIVYDK LSNWLINAFN GEWVKVNDAK PKIES
//