ID   DAPB_NEUCR              Reviewed;         924 AA.
AC   Q7SHU8;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   19-MAR-2014, sequence version 2.
DT   27-MAR-2024, entry version 106.
DE   RecName: Full=Probable dipeptidyl-aminopeptidase B;
DE            Short=DPAP B;
DE            EC=3.4.14.5;
GN   Name=dapB; ORFNames=NCU02515;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
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; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU10084};
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; CM002236; EAA36410.2; -; Genomic_DNA.
DR   RefSeq; XP_965646.2; XM_960553.2.
DR   AlphaFoldDB; Q7SHU8; -.
DR   SMR; Q7SHU8; -.
DR   STRING; 367110.Q7SHU8; -.
DR   ESTHER; neucr-q7shu8; DPP4N_Peptidase_S9.
DR   MEROPS; S09.006; -.
DR   GlyCosmos; Q7SHU8; 3 sites, No reported glycans.
DR   PaxDb; 5141-EFNCRP00000002047; -.
DR   EnsemblFungi; EAA36410; EAA36410; NCU02515.
DR   GeneID; 3881844; -.
DR   KEGG; ncr:NCU02515; -.
DR   VEuPathDB; FungiDB:NCU02515; -.
DR   HOGENOM; CLU_006105_0_1_1; -.
DR   InParanoid; Q7SHU8; -.
DR   OrthoDB; 2876738at2759; -.
DR   Proteomes; UP000001805; Chromosome 1, Linkage Group I.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; IEA:EnsemblFungi.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008239; F:dipeptidyl-peptidase activity; IBA:GO_Central.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
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; IPR002471; Pept_S9_AS.
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.
DR   PROSITE; PS00708; PRO_ENDOPEP_SER; 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..924
FT                   /note="Probable dipeptidyl-aminopeptidase B"
FT                   /id="PRO_0000412152"
FT   TOPO_DOM        1..111
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        112..132
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        133..924
FT                   /note="Vacuolar"
FT                   /evidence="ECO:0000255"
FT   REGION          1..102
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        12..28
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        29..47
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        48..78
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        85..102
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        768
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
FT   ACT_SITE        845
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
FT   ACT_SITE        878
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
FT   CARBOHYD        231
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        827
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   924 AA;  104094 MW;  D11B8E601522811D CRC64;
     MPSTYSDDNT LRSGLDRFRD HSPSQHRRSM SQETDSTVST TSIVFDRIQE RLDTKEFPAR
     GTDGDDNDSL KDELNNDDLE TGPFLGNASP SSRSNQRSSA DGQRMDRSLR RWLFIVSGAL
     VATWVIGLIF FVSSKAYKPS SSFAHDPQAT VTHGSGKKVT LDQVLNNEWR AKSHSISWIA
     GVNGEDGLLL EKEGANKDYL VVEDVRAQNP SSVEASKSKT LIKDKLFEFA NKTYWPTVTV
     PSRDLKKVLL ATDVQNNWRH SYYAVYWIFD VETQQAEPLV PYDADARLQL ASWSPTSDAI
     VYTRDNNMFL RKLDSDKIVQ ITRDGSADVF NGVPDWVYEE EVLASGVATW WSEDGNYVAF
     LRTNETGVPE YPIQYFVSRP SGEEPKPGEE NYPEVRQIKY PKAGAHNPIV DLKFYDVKRG
     DVFSVDISGR FADDDRLITE VIWAGKQVLI KETNRVSDVM RVVLVDVGSR TGKAVRTVDV
     NDIDGGWFEI SHKTKFIPAD PANGRPDDGY VDTIIHNNGD HLAYFTPLDN PNPIMLTSGD
     YEVVDAPSAV DLQRNLVYFV STKESSIQRH VYQVKLTGED MTPVTDTSKE GYYAISFSTG
     AGYALVSYQG PNIPWQKVIS TPSNPDKYEH VVEENKDLAE AAKKHELPIN IYGTINVDGV
     ELNYIERRPP HFDKNKKYPV LFQQYSGPVS QTVKKTFAVD FQSFVAAGLG YICVTVDGRG
     TGFIGRKNRV IIRGNLGTWE SHDQIAAAKH WAQKDYIDED RLAIWGWSYG GYMTLKTLEQ
     DAGQTFKYGM AVAPVTDWRF YDSIYTERYM RTPQTNPEGY ESAAVTNVTA LSQNVRFLLM
     HGVADDNVHM QNSLTLLDAL DQRSVENYDV QVFPDSDHGI YFHNANRIVF DKLTNWLVNA
     FNGEWLKIAN AQPNGMKRRA LPTA
//