ID   DAPB_FUSV7              Reviewed;         912 AA.
AC   C7YYG9;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   13-OCT-2009, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   RecName: Full=Probable dipeptidyl-aminopeptidase B;
DE            Short=DPAP B;
DE            EC=3.4.14.5;
GN   Name=DAPB; ORFNames=NECHADRAFT_47100;
OS   Fusarium vanettenii (strain ATCC MYA-4622 / CBS 123669 / FGSC 9596 / NRRL
OS   45880 / 77-13-4) (Fusarium solani subsp. pisi).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium solani species complex; Fusarium vanettenii.
OX   NCBI_TaxID=660122;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4622 / CBS 123669 / FGSC 9596 / NRRL 45880 / 77-13-4;
RX   PubMed=19714214; DOI=10.1371/journal.pgen.1000618;
RA   Coleman J.J., Rounsley S.D., Rodriguez-Carres M., Kuo A., Wasmann C.C.,
RA   Grimwood J., Schmutz J., Taga M., White G.J., Zhou S., Schwartz D.C.,
RA   Freitag M., Ma L.-J., Danchin E.G.J., Henrissat B., Coutinho P.M.,
RA   Nelson D.R., Straney D., Napoli C.A., Barker B.M., Gribskov M., Rep M.,
RA   Kroken S., Molnar I., Rensing C., Kennell J.C., Zamora J., Farman M.L.,
RA   Selker E.U., Salamov A., Shapiro H., Pangilinan J., Lindquist E.,
RA   Lamers C., Grigoriev I.V., Geiser D.M., Covert S.F., Temporini E.,
RA   VanEtten H.D.;
RT   "The genome of Nectria haematococca: contribution of supernumerary
RT   chromosomes to gene expansion.";
RL   PLoS Genet. 5:E1000618-E1000618(2009).
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; GG698903; EEU43005.1; -; Genomic_DNA.
DR   RefSeq; XP_003048718.1; XM_003048672.1.
DR   AlphaFoldDB; C7YYG9; -.
DR   SMR; C7YYG9; -.
DR   STRING; 660122.C7YYG9; -.
DR   ESTHER; nech7-dapb; DPP4N_Peptidase_S9.
DR   GlyCosmos; C7YYG9; 2 sites, No reported glycans.
DR   EnsemblFungi; NechaT47100; NechaP47100; NechaG47100.
DR   GeneID; 9665490; -.
DR   KEGG; nhe:NECHADRAFT_47100; -.
DR   VEuPathDB; FungiDB:NECHADRAFT_47100; -.
DR   eggNOG; KOG2100; Eukaryota.
DR   HOGENOM; CLU_006105_0_1_1; -.
DR   InParanoid; C7YYG9; -.
DR   OMA; MRTPQEN; -.
DR   OrthoDB; 2876738at2759; -.
DR   Proteomes; UP000005206; 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..912
FT                   /note="Probable dipeptidyl-aminopeptidase B"
FT                   /id="PRO_0000412150"
FT   TOPO_DOM        1..85
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        86..106
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        107..912
FT                   /note="Vacuolar"
FT                   /evidence="ECO:0000255"
FT   REGION          1..74
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          892..912
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        16..30
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        31..52
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        895..912
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        749
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        826
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        859
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        344
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        808
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   912 AA;  102536 MW;  316574CA966658A3 CRC64;
     MSSALSPEGD RRYSDDSLSS VSTTSLVFER IQEKTEMDAD NDKEKDPRAL DDEDPLRDED
     DLETGPFLGP GASLHREPMD RGLRRILIIV AVVFIGGWLA GLGIFIASGS YHHESDTEHD
     PDANSRGSGK SLSMDQLFDG TWSPKYHSIS WIAGPKGEDG LLLEVGASNK PYIVVEDIRS
     DKNVATRDDA EPKASNSRTL MEHPYFEYDG KQYSPSWSEP SPDLTKVLLG VDRKKNWRHS
     FSAIYFVLDV KTQEAEPLVP DQVDARIQLA SWSPKSDAVS FTRENNLYIR RLTGDKDVTQ
     ITKDGGPEYF YGIPDWVYEE EVFSGRSATW WSDDGKYLAF LRTNETGVPE YPVQFFIERP
     SGTTPEDGEE AYPEVEQIKY PKAGAHNPVV DLQFYDIGKK DTFSVEIDGA FADDDRIINN
     LLWAGDKAIV KQTNRVSDVL KVVLVDVPSR KGKTINTINI NEIDGGWFEI SHKMTYIPAD
     PKNGREHDGY VDSVIHEGYD HLAYFTPLDN SEPIMLTKGN WEVDDAPSAV DLANNLVYFI
     AAKESSIQRH VYSVKLDGSD LQALTDPKTE AYYDASFSKG AGFVFLSYRG PKVPTQKVIS
     TPVSASSYER IIEDNAELAD RARRHELPIL KYGTLDLDTG VKVNYVERRP PHFDAKKQYP
     VLFHQYSGPG SQSVTKRFAV DFQAYVAAAL GYLVITVDPR GTGFLGRKHR VTVRSKLGVH
     EAHDHIAAAA SFASRPYVDA ERLAIWGWSY GGFTTLKTLE QDAGRTFSYG MAVAPVTDWR
     FYDSIYTERY MRTPQDNPDG YDLSKVANAT ALGENKRFLL MHGVADDNVH FQNSLTLLDD
     LDLAGVENYD VHVFPDSDHS IYFHNGNRIV YDKLRNWLIN AFNGEWLKVS NPQPQKDPVE
     KEKRHMVPQA LV
//