ID A0A0C9Z423_9AGAM Unreviewed; 891 AA.
AC A0A0C9Z423;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Dipeptidyl-peptidase IV {ECO:0008006|Google:ProtNLM};
GN ORFNames=PISMIDRAFT_687695 {ECO:0000313|EMBL:KIK14773.1};
OS Pisolithus microcarpus 441.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Sclerodermatineae; Pisolithaceae; Pisolithus.
OX NCBI_TaxID=765257 {ECO:0000313|EMBL:KIK14773.1, ECO:0000313|Proteomes:UP000054018};
RN [1] {ECO:0000313|EMBL:KIK14773.1, ECO:0000313|Proteomes:UP000054018}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=441 {ECO:0000313|EMBL:KIK14773.1,
RC ECO:0000313|Proteomes:UP000054018};
RG DOE Joint Genome Institute;
RA Kuo A., Kohler A., Costa M.D., Nagy L.G., Floudas D., Copeland A.,
RA Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A.,
RA Lipzen A., Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA Hua S.X.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000054018}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=441 {ECO:0000313|Proteomes:UP000054018};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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; KN833923; KIK14773.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C9Z423; -.
DR STRING; 765257.A0A0C9Z423; -.
DR MEROPS; S09.006; -.
DR HOGENOM; CLU_006105_0_0_1; -.
DR OrthoDB; 2876738at2759; -.
DR Proteomes; UP000054018; 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:UP000054018};
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 93..117
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 201..598
FT /note="Dipeptidylpeptidase IV N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00930"
FT DOMAIN 683..883
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
FT REGION 1..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..32
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 891 AA; 99172 MW; 87B6AE1E49346D62 CRC64;
MAPHAYQHLS NAEEGCLDRE SDYPRDRSPS LSDHTARPLT YYGEGPFDAP SSDDEDEEYL
VKEARDQGEV GDSEPVSGLR VGGGGKRPTA LRALVISLAS LVLFSAFIGV FAATVLYNGK
PFHGPGAQKL ALDHIFNGTF SASLRSVHWV PEAGDGVFSM MENGRIVLVD LKINETKPLI
SIADVKDENG NQLNWTEWKL SPDMRYILVK ADKVKQWRHS SFGNYYVHDL ETKATNPLLP
PTDPPVTAYA TWAPTGQSIA FVASNDLYVL PSPRSTMSPI RVTNTGNASL FHGIPDWIYE
EEVFSSDYAL WWSPDSARIA FLRLDETAVD EYRFPIYNPT NDAYAVVPYT EDVVIKYPKP
GYNNPIASVH VFNLASYLEY SNIFSAAAST VELVWTGRFS LDNSVISQVT WVDDSSLIVK
EVNRAADNGS VIFFSLDTLI PEQGTASGVV VRRLGVNGEE ADGGWIEPHQ NIYPLPSGLR
SGGSPAYLDI VPSEDGYDHI ALFDPADSTT PRFLTSGPWE VTGGIQVVDA QRGLIYFQAA
RSSIERHLYS VPISSPNTAS PIMPSPLTDE STTSSYSVNF SPGAGFYLLN YRGPGVPWQR
LVRVDRPDFD YVLTDNTALN ATLSVFETAT VTYTTIVSDG YELNVKEMRP PRMDDSGRTK
YPVLFHVYGG PESQQVNVEY KRDWHDYLVC TLQYIVVVVD GRGTGFKGRH LRNPVRNNLG
FWETRDQINA ARIWAGKPYV DTKRIGIWGW SYGGFMASKV AEADVGIHSL AMAVAPVTSW
RLYDSIYTER YMGLPNDNPG GYINASISSV EGFRNVDYLL MHGSGDDNVH FANSAHLLDM
LTKAQIRNFK FRMFTDSDHS INRRGANREV YEYMSLFLLE KWGKGGHRRG W
//
