ID D8Q2B4_SCHCM Unreviewed; 915 AA.
AC D8Q2B4;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Dipeptidyl aminopeptidase {ECO:0008006|Google:ProtNLM};
GN ORFNames=SCHCODRAFT_82141 {ECO:0000313|EMBL:EFI98654.1};
OS Schizophyllum commune (strain H4-8 / FGSC 9210) (Split gill fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Schizophyllaceae; Schizophyllum.
OX NCBI_TaxID=578458 {ECO:0000313|Proteomes:UP000007431};
RN [1] {ECO:0000313|EMBL:EFI98654.1, ECO:0000313|Proteomes:UP000007431}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H4-8 / FGSC 9210 {ECO:0000313|Proteomes:UP000007431};
RX PubMed=20622885; DOI=10.1038/nbt.1643;
RA Ohm R.A., de Jong J.F., Lugones L.G., Aerts A., Kothe E., Stajich J.E.,
RA de Vries R.P., Record E., Levasseur A., Baker S.E., Bartholomew K.A.,
RA Coutinho P.M., Erdmann S., Fowler T.J., Gathman A.C., Lombard V.,
RA Henrissat B., Knabe N., Kuees U., Lilly W.W., Lindquist E., Lucas S.,
RA Magnuson J.K., Piumi F., Raudaskoski M., Salamov A., Schmutz J.,
RA Schwarze F.W.M.R., vanKuyk P.A., Horton J.S., Grigoriev I.V.,
RA Woesten H.A.B.;
RT "Genome sequence of the model mushroom Schizophyllum commune.";
RL Nat. Biotechnol. 28:957-963(2010).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-
CC pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}. Vacuole
CC membrane {ECO:0000256|ARBA:ARBA00004576}; Single-pass type II membrane
CC protein {ECO:0000256|ARBA:ARBA00004576}.
CC -!- SIMILARITY: Belongs to the peptidase S9B family.
CC {ECO:0000256|ARBA:ARBA00006150}.
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DR EMBL; GL377305; EFI98654.1; -; Genomic_DNA.
DR RefSeq; XP_003033557.1; XM_003033511.1.
DR AlphaFoldDB; D8Q2B4; -.
DR STRING; 578458.D8Q2B4; -.
DR ESTHER; schcm-d8q2b4; DPP4N_Peptidase_S9.
DR GeneID; 9592808; -.
DR KEGG; scm:SCHCO_02687101; -.
DR VEuPathDB; FungiDB:SCHCODRAFT_02687101; -.
DR eggNOG; KOG2100; Eukaryota.
DR HOGENOM; CLU_006105_0_0_1; -.
DR InParanoid; D8Q2B4; -.
DR OMA; DKYKATT; -.
DR OrthoDB; 2876738at2759; -.
DR Proteomes; UP000007431; Unassembled WGS sequence.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
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 {ECO:0000256|ARBA:ARBA00022438};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022438};
KW Reference proteome {ECO:0000313|Proteomes:UP000007431};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Vacuole {ECO:0000256|ARBA:ARBA00022554}.
FT TRANSMEM 101..124
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 212..621
FT /note="Dipeptidylpeptidase IV N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00930"
FT DOMAIN 706..907
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
FT REGION 1..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 915 AA; 101259 MW; D5A4BDD5BEAC5EEC CRC64;
MAPRGGITAH DDDEDVEEHL LDTRSIRSTA SSSKTLVRPP TYYGDGPFDA PSSDSSEEGD
ALLEDKESLD EEIPRTRSPG RAEDGLYVGG APQSRKGPTR YLVIALASLV GLSAIIGIFA
SLSYSAKGSV YRAPGVKKIT MDHVFNGTFS AETRDLHWVK EAGDGVFSVQ EDGYIKLVDL
KNNKTMTNLV NMLDVKRENG EPITDWADWQ LSADMKYILV KTDYVKQWRH SSLGNYYIHD
IDAGETQPLV GPNHPPTTAY AAWSPVGDIA YVDSGDLYLL QGSDLYNPIR VTYTGSPTVT
NGVPDWVYEE EVYGGPSALW FSPTGDRLAF LSFNDTEVDI FRFEIFNPTD DNDAVIPYTQ
PTEVPYPKPG YSNPIVGAYV FDIANHVYAE EMPESVVLGE TLHLLQWSPS LPADDQIIME
VAWVGIQSLI VKEVNRNADN GHVVFVDFSE GAPEGIVVRT LGKDGEEGDD GWIEQAQTVF
PLPRDVLSTA AFQGSKNAYL DIVPTKEGYN HIALFPVADT AEPVWLTNGE WEVTSSIKGV
GQNSKDEWVV YFEAANPMST ARNLYSVAIP SNLTSSAVPD ITPLTYSEDA PLAEQEAYYS
TSFSPEAGFY LLSYKGPGVP YQKVVHVGDE DFEYTLTTND RLSNVTAEFE TPTIIRGTIE
IDGIELNYRE IRPPRMDDSG RTKYAVLFNV YGGPGSQTVD LRFAGYDWHG YLACGLQYIV
VAVDGRGTGF EGRGLRSVVK GDLGFWETQD QVAAARIWAG RNYVDPRRIG IWGWSYGGFM
AGKVVEADAG IHSLAMSVAP VTSWRLYDSI YTERYMNTPE LNPGGYVNAS ITDVEPFKKV
DYLLAHGTGD DNVHFANSAH LLDMFVKGHV RDYAFRMFTD SDHAIRTRGA YRELHEFLTG
FLLEKWGKGG RKRGW
//
