DAPB_NEUCR
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 03-AUG-2022, entry version 100.
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; 5141.EFNCRP00000002047; -.
DR ESTHER; neucr-q7shu8; DPP4N_Peptidase_S9.
DR MEROPS; S09.006; -.
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 Proteomes; UP000001805; Chromosome 1, Linkage Group I.
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; IBA:GO_Central.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002471; Pept_S9_AS.
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.
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