DAPB_VERA1
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 03-AUG-2022, entry version 55.
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 EnsemblFungi; EEY18938; EEY18938; VDBG_05047.
DR GeneID; 9532123; -.
DR KEGG; val:VDBG_05047; -.
DR eggNOG; KOG2100; Eukaryota.
DR HOGENOM; CLU_006105_0_1_1; -.
DR OMA; MRTPQEN; -.
DR Proteomes; UP000008698; 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:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
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.
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
