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 27-MAR-2024, entry version 100.
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; 227321.Q5B934; -.
DR ESTHER; emeni-q7si80; DPP4N_Peptidase_S9.
DR GlyCosmos; Q5B934; 3 sites, No reported glycans.
DR EnsemblFungi; CBF83695; CBF83695; ANIA_02946.
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; 2876738at2759; -.
DR Proteomes; UP000000560; Chromosome VI.
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:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
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; 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..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
//
