DPP5_EMENI
ID DPP5_EMENI Reviewed; 722 AA.
AC Q5BA58; C8VPV9;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Probable dipeptidyl-peptidase 5;
DE EC=3.4.14.-;
DE AltName: Full=Dipeptidyl-peptidase V;
DE Short=DPP V;
DE Short=DppV;
DE Flags: Precursor;
GN Name=dpp5; ORFNames=AN2572;
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 [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 [2]
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).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=19286987; DOI=10.1128/ec.00368-08;
RA Shin K.S., Kwon N.J., Kim Y.H., Park H.S., Kwon G.S., Yu J.H.;
RT "Differential roles of the ChiB chitinase in autolysis and cell death of
RT Aspergillus nidulans.";
RL Eukaryot. Cell 8:738-746(2009).
CC -!- FUNCTION: Extracellular dipeptidyl-peptidase which removes N-terminal
CC dipeptides sequentially from polypeptides having unsubstituted N-
CC termini. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase S9C family. {ECO:0000305}.
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DR EMBL; AACD01000043; EAA64677.1; -; Genomic_DNA.
DR EMBL; BN001307; CBF87122.1; -; Genomic_DNA.
DR RefSeq; XP_660176.1; XM_655084.1.
DR AlphaFoldDB; Q5BA58; -.
DR SMR; Q5BA58; -.
DR STRING; 162425.CADANIAP00009305; -.
DR ESTHER; emeni-q5ba58; Prolyl_oligopeptidase_S9.
DR EnsemblFungi; CBF87122; CBF87122; ANIA_02572.
DR EnsemblFungi; EAA64677; EAA64677; AN2572.2.
DR GeneID; 2875174; -.
DR KEGG; ani:AN2572.2; -.
DR VEuPathDB; FungiDB:AN2572; -.
DR eggNOG; KOG2100; Eukaryota.
DR HOGENOM; CLU_008615_0_1_1; -.
DR InParanoid; Q5BA58; -.
DR OMA; STRWNPK; -.
DR OrthoDB; 265965at2759; -.
DR Proteomes; UP000000560; Chromosome VII.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.120.10.30; -; 1.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001375; Peptidase_S9.
DR Pfam; PF00326; Peptidase_S9; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Aminopeptidase; Glycoprotein; Hydrolase; Protease; Reference proteome;
KW Secreted; Serine protease; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..722
FT /note="Probable dipeptidyl-peptidase 5"
FT /id="PRO_0000397821"
FT ACT_SITE 558
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 641
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 673
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 151
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 253
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 448
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 605
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 722 AA; 79446 MW; CA106CDDDAD0A2AA CRC64;
MGALRWLSLA AAASSALALT PEQLISAPRR SEAIPNPSGN IAVFSSSQYS FDTHESSSAW
NLLDLRSGKI TPLTNDSNVS EIVWLNDSTL LYINGTNAQI PGGSELWVSG LSNFPSGYKA
ASLPASFSGL KAVTTKSGDI KFVAYAQSYR NGTAYNEELA ETYLSSARIY DSIYVRHWDT
YLTTTFNAVF SGTLKKTQHA RYASAGSLKN LVAPIPNAES PYPPFGGSSD YDISADGKWV
AYKSKAPDVP QANHTTAYIY LVPHDGSETP VPINGPGSAP EGIEGDSNNP VFSPDSKSLA
YLQMKDPTYE SDRRVIYIYD LASKKITPLA TEWDRSPDSL KWTDKSTIVA GSEDEGSGNL
FLIPVKKATG DFIPEKLTNG KYASAFYLAS GNTLVVTGST LYSSWYVDLV SLNPKRGTIK
NLVSAHEIDP ELSGLGPEDI SDIWFAGNWT DIHAWVIYPE GFDKSKTYPL AFLIHGGPQG
AWYNSWSSRW NPKVFADQGY VVVAPNPTGS TGYGDELTDA IQNNWGGAPY EDLVKAWEYV
RDNLDYVDTD RGVAAGASYG GFMVNWIQGS DLGREFKALV THDGTFVADA KISTEELWFM
EREFNGTFWD VRDNYRRFDP SAPERILRFA TPHLIIHNDL DYRLPVAEGL SLFNVLQERG
VPSRFLNFPD ENHWVTSPEN SLVWHQQVLG WLNKYSGIAE DNEDAVTLED TVVPVVNINP
PA
