ID A0A0D7AM90_9AGAR Unreviewed; 912 AA.
AC A0A0D7AM90;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Dipeptidyl aminopeptidase {ECO:0008006|Google:ProtNLM};
GN ORFNames=FISHEDRAFT_70393 {ECO:0000313|EMBL:KIY51898.1};
OS Fistulina hepatica ATCC 64428.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Fistulinaceae; Fistulina.
OX NCBI_TaxID=1128425 {ECO:0000313|EMBL:KIY51898.1, ECO:0000313|Proteomes:UP000054144};
RN [1] {ECO:0000313|EMBL:KIY51898.1, ECO:0000313|Proteomes:UP000054144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 64428 {ECO:0000313|EMBL:KIY51898.1,
RC ECO:0000313|Proteomes:UP000054144};
RX PubMed=25683379; DOI=10.1016/j.fgb.2015.02.002;
RA Floudas D., Held B.W., Riley R., Nagy L.G., Koehler G., Ransdell A.S.,
RA Younus H., Chow J., Chiniquy J., Lipzen A., Tritt A., Sun H., Haridas S.,
RA LaButti K., Ohm R.A., Kues U., Blanchette R.A., Grigoriev I.V., Minto R.E.,
RA Hibbett D.S.;
RT "Evolution of novel wood decay mechanisms in Agaricales revealed by the
RT genome sequences of Fistulina hepatica and Cylindrobasidium torrendii.";
RL Fungal Genet. Biol. 76:78-92(2015).
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; KN881647; KIY51898.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D7AM90; -.
DR MEROPS; S09.006; -.
DR OrthoDB; 2876738at2759; -.
DR Proteomes; UP000054144; 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:UP000054144};
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 95..118
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 205..619
FT /note="Dipeptidylpeptidase IV N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00930"
FT DOMAIN 704..904
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 912 AA; 101657 MW; 18DEA65266D682AF CRC64;
MAPEPEYIPL HGEADGEGDT RSIRSTTSTL VRPHIYYDDG PFEASSSDSS EEDLLLTAKQ
DVEVQPEPNP SPGAAERGAV FELPVKEKRA SSLRVLVIIL ASLVGAAALI GIVASLTYTG
GSGLYHAPGT RKITMEHIFN GTFSPEHVSL HWVKEAGDGV FSVEEGEFIR LVDFKSNKTT
DLVNRQDVTD ENGEPITKWA EWRLSPDMKH IIVKTDQVKL WRHSSFGNFY VHTIASKETR
SLSTPRHPPT ATYATWSPKG DVAYVDNGDL YVLPLASGNF DGPIRITTTG STLQTNAIPD
WVYEEEVLGG PFALWFSPDG GKIAFMSFDD TNVDVFQFEV FNPTEDNDAI IPYTTPTKVR
YPKPGYTNPT VDAYMFDLEA YVKARPTVSA PHVVALAKSL HRLSWTPRAP SDDRVLMEVA
WVSDMRVIVK EVNRNADIGR VVLFDFANDR LRPGVLQGTI ARKLGREGEQ GDNGWIDATQ
TIHSLPAALR DKMDGYLDVV PSKDGYNHVA LFSPASSSKP IWLTSGSWEV TGKIQGVRVD
EKGDGVVYFT AANPLSTSRH LYSVTFTPGA EVKVGKVTAL TYDQDATDNV KDRETLYRSS
FSPNAGFYLL NYEGPGVPWQ KVKASADKGF NLDVGMNEVL VNRTAEYEAP TIVYGTIEID
GIEFNYRETR PPRMDDSGRT KYAVLFQVYG GPASQMVDLT FSPDWHWYLS CRLQYIIVSV
DGRGTGYKGR KIRNFVKSNL GFWETHDQIE AGRMWAAKDY VDPKRIGIWG WSYGGFMSSK
VAEANAGVHS LAMAVAPVTS WRLYDSIYTE RYMNLPDVNP GGYINASITD VEGFKHINYL
LAHGTADDNV HFANTAHLLD MFVKAQVRGY RFRIFVDSDH SIRKRGANRE VYEFMTDFLI
EKWGKGGKRR GW
//
