ID A0A1Y2FF30_PROLT Unreviewed; 846 AA.
AC A0A1Y2FF30;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Dipeptidyl peptidase IV N-terminal region-domain-containing protein {ECO:0000313|EMBL:ORY81906.1};
GN ORFNames=BCR37DRAFT_379801 {ECO:0000313|EMBL:ORY81906.1};
OS Protomyces lactucae-debilis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; Taphrinomycetes;
OC Taphrinales; Protomycetaceae; Protomyces.
OX NCBI_TaxID=2754530 {ECO:0000313|EMBL:ORY81906.1, ECO:0000313|Proteomes:UP000193685};
RN [1] {ECO:0000313|EMBL:ORY81906.1, ECO:0000313|Proteomes:UP000193685}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12-1054 {ECO:0000313|EMBL:ORY81906.1,
RC ECO:0000313|Proteomes:UP000193685};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ORY81906.1}.
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DR EMBL; MCFI01000010; ORY81906.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2FF30; -.
DR STRING; 56484.A0A1Y2FF30; -.
DR OMA; MRTPQEN; -.
DR OrthoDB; 2876738at2759; -.
DR Proteomes; UP000193685; 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:UP000193685};
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 66..86
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 178..543
FT /note="Dipeptidylpeptidase IV N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00930"
FT DOMAIN 629..832
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 846 AA; 95336 MW; EFD54A62FF0489F4 CRC64;
MNSETMSQVQ RPQRTPSSVS TMSSRDSLDA QVEKPEEEEL MRMDEEAAVP VRSKPSRWNL
CARRHLLIIG VIGLVIWSGA LASFVFRGSF DSHTHHPIAE SRRLTLDTAQ SPIWIAHEHQ
VDWTDAHGED GVFLIQSEQD LRLASVNGTN EVFVKASDIR ADQLKGSPPI PATKHWISAD
MKYLLLASEV RPNWRHSFTA KYWVHNVEKK QTISLIPDDP EAILAHAAWA HKGHSIAFVK
DNDVYVRHNM GDVERVTSDG SKNIFNGIAD WVYEEEVFAN DVALWWAPDG KSFAYLKTDE
KRVREYPLEM FVGNGAPQQY PDIEWLKYPK PGTANPIVKL FHYNLESKQS TQVTAEGSLS
DNDRLITEIK WLGPEKLFMR ENNRDSVIQQ TIIATPGKGA KVTQTLNISS IDGGWFEITH
NTHYIPANPA HNRPDDGYID IVISDGHLHL ALFSPVDAAE PKMLTSGNWE ITGGVQAIDL
ERGLVYFLST KKSSTERHLS SVSMVTGEIS DITSTKNEGY FSTSFSPKAG YYLLTYSGPG
VPYQKFLSTN DPSFEIVLEE NSAIKAQVAK YDLPTKHYST ITIDGLEMNV MELRPPNFDG
SGKTKYPVLF NPYGGPASQQ VHKRFKQGWE AYLVSDPALE YLVVTVDGRG TGFKGRSLRT
PIRGHLGRYE AKDQIEAAKI WQAKPYTDKN KFAIWGWSFG GFLTLKVLEA ASGVFQYGMA
VAPVTDWRFY DSVYTERFMG LLEENQAGYE ETAVTNMTAF SEAKRLLVMH GTGDDNVHYQ
NTLTFIDHLN QAGVENYDLH VFPDSDHSIY FHNANRQVYH RLTNWLTRAF GKRDPAGEDR
SWVVPA
//
