ID   DAPB_EMENI              Reviewed;         906 AA.
AC   Q5B934; C8VJ32; Q7SI80;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Probable dipeptidyl-aminopeptidase B;
DE            Short=DPAP B;
DE            EC=3.4.14.5;
GN   Name=dapB; Synonyms=ste13; ORFNames=AN2946;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=12949156; DOI=10.1099/mic.0.c0119-0;
RA   Dyer P.S., Paoletti M., Archer D.B.;
RT   "Genomics reveals sexual secrets of Aspergillus.";
RL   Microbiology 149:2301-2303(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=DAA01787.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=EAA63517.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; BK001296; DAA01787.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AACD01000051; EAA63517.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BN001306; CBF83695.1; -; Genomic_DNA.
DR   RefSeq; XP_660550.1; XM_655458.1.
DR   AlphaFoldDB; Q5B934; -.
DR   SMR; Q5B934; -.
DR   STRING; 162425.CADANIAP00010138; -.
DR   ESTHER; emeni-q7si80; DPP4N_Peptidase_S9.
DR   EnsemblFungi; CBF83695; CBF83695; ANIA_02946.
DR   EnsemblFungi; EAA63517; EAA63517; AN2946.2.
DR   GeneID; 2873731; -.
DR   KEGG; ani:AN2946.2; -.
DR   VEuPathDB; FungiDB:AN2946; -.
DR   eggNOG; KOG2100; Eukaryota.
DR   HOGENOM; CLU_006105_0_1_1; -.
DR   InParanoid; Q5B934; -.
DR   OMA; MRTPQEN; -.
DR   OrthoDB; 269253at2759; -.
DR   Proteomes; UP000000560; Chromosome VI.
DR   Proteomes; UP000005890; 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; IBA:GO_Central.
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..906
FT                   /note="Probable dipeptidyl-aminopeptidase B"
FT                   /id="PRO_0000412145"
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..906
FT                   /note="Vacuolar"
FT                   /evidence="ECO:0000255"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        17..32
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        743
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        820
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        853
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        338
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        629
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        797
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   906 AA;  101960 MW;  49ACD99EF348E99F CRC64;
     MRSSEDREDS ELLPANRPRS PSRSSYDSDD SGLSVDSILE EQKYNAATNE TLGLPQEMRY
     HDEEGGEAGS NEALHTKASS SRSRRLLWLV VLLCCGGWVV AFVLFITQGR ADYRTATDEL
     QSDNSGSFSD GTSSGKPLTL QQVLSGVFLP RGHAISWVAG PDGEDGLLIE RGEDDEAGYL
     RINDIRQDGK VNRVLMQKPT VGVDGRTIKP SATRPSPDLK KVLIISNQEK NWRHSFTASY
     WIFDVETQTA EPLDPNNIDG RVQLALWSPK SDAIAFVRDN NLYLRKLSSE RVVPITKDGG
     EQLFYGVPDW VYEEEVFSGN SVTWWSEDGS QIAFIRTNES AVPEFPVQYF LSRPSGKKPQ
     PGLENYPEVR EIKYPKAGAP NPFVNLQFYD VEQGEVFSVD TPDDFDDDDR LIIEVIWAAK
     GKVLVRTTNR ESDILKVFLV DTESRESKLI RIQDISELDG GWVEPTQSVR FIPADPDKGR
     PFDGYLDTVV HEGYDHLAYF TPLDNPEPIM LTSGEWEVVD APTAVDLTRG LVYFIATKEA
     PTERHLYRVR LDGSDLTPLT DTSQPGYYSV SFSDGAGYAL LSYQGPSIPW QSIISTEGEK
     TTTLRIIEDN TDLSKLVAQY ALPTENYQNI TIDGFTLQVV ERRPPHFNPA RKYPVLFHLY
     GGPGSQTVDR RFNVDFQSYV AASLGYIVVT VDGRGTGFIG RAARCIIRGN IGHYEAIDQI
     ATAKNWAQKP YVDESRMAIW GWSYGGFMTL KTLEQDAGET FQYGMAVAPV TDWRFYDSVY
     TERYMHTPQH NPTGYDNTSI SDMAALHNNV RFLVIHGASD DNVHIQNTLT LIDKLDLASV
     QNYDVHFYPD SDHSIFFHNA HTMVYERLAS WLVNAFNGEW HRTANPVPDE SMLRRLAKRV
     WPGFAH