DAPB_FUSV7
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 03-AUG-2022, entry version 58.
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; 140110.NechaP47100; -.
DR ESTHER; nech7-dapb; DPP4N_Peptidase_S9.
DR PRIDE; C7YYG9; -.
DR EnsemblFungi; NechaT47100; NechaP47100; NechaG47100.
DR GeneID; 9665490; -.
DR KEGG; nhe:NECHADRAFT_47100; -.
DR eggNOG; KOG2100; Eukaryota.
DR HOGENOM; CLU_006105_0_1_1; -.
DR InParanoid; C7YYG9; -.
DR OMA; MRTPQEN; -.
DR OrthoDB; 269253at2759; -.
DR Proteomes; UP000005206; 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..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
