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Database: UniProt
Entry: A0A397TNL1_9GLOM
LinkDB: A0A397TNL1_9GLOM
Original site: A0A397TNL1_9GLOM 
ID   A0A397TNL1_9GLOM        Unreviewed;       747 AA.
AC   A0A397TNL1;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Dipeptidyl peptidase IV N-terminal region-domain-containing protein {ECO:0000313|EMBL:RIA99029.1};
GN   ORFNames=C1645_685268 {ECO:0000313|EMBL:RIA99029.1};
OS   Glomus cerebriforme.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC   Glomeromycetes; Glomerales; Glomeraceae; Glomus.
OX   NCBI_TaxID=658196 {ECO:0000313|EMBL:RIA99029.1, ECO:0000313|Proteomes:UP000265703};
RN   [1] {ECO:0000313|EMBL:RIA99029.1, ECO:0000313|Proteomes:UP000265703}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DAOM 227022 {ECO:0000313|EMBL:RIA99029.1,
RC   ECO:0000313|Proteomes:UP000265703};
RA   Morin E., San Clemente H., Chen E.C.H., De La Providencia I., Hainaut M.,
RA   Kuo A., Kohler A., Murat C., Tang N., Roy S., Loubradou J., Henrissat B.,
RA   Grigoriev I.V., Corradi N., Roux C., Martin F.M.;
RT   "Comparative genomics reveals the genomic features of Rhizophagus
RT   irregularis, R. cerebriforme, R. diaphanum and Gigaspora rosea, and their
RT   symbiotic lifestyle signature.";
RL   Submitted (JUN-2018) 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:RIA99029.1}.
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DR   EMBL; QKYT01000008; RIA99029.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A397TNL1; -.
DR   STRING; 658196.A0A397TNL1; -.
DR   Proteomes; UP000265703; 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:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
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; 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.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022825};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Protease {ECO:0000256|ARBA:ARBA00022825};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265703};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW   Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW   Vacuole {ECO:0000256|ARBA:ARBA00022554}.
FT   DOMAIN          85..455
FT                   /note="Dipeptidylpeptidase IV N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00930"
FT   DOMAIN          550..740
FT                   /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00326"
SQ   SEQUENCE   747 AA;  85862 MW;  BCAB298BE01E9754 CRC64;
     MSGTDNFANR IQFDHLYNGS FFPEYQSLEW SKAVGDDDGA FVYRDHDDSI ILEHVADKKK
     KILVKGDDLI DSNGDHLYYD DFLVSPDSKY ILFSTNRTKQ WRYSHFSNYW IFNITSSSPF
     PLTKSIDKDH QAVIAFAQWS PVGHTVAFVK DNDLYVSVDL LDERRLTFDG SAVVFNGMPD
     WIYEEEVLKA DNAIWWSNEG KRLAYLRLNE SEVPEYRFPL YLTGFNATPY PREVVMRYPK
     PGYPNPIATF HVYDLESPLA SQFGAITFEN DFSDDERIIT EVMWAGDDTV LVKVMNRVQD
     IARVVLVDTN TRKGKIVREE NADKMDGGWY EINQSMFYVK KSGSLKQDGY IDIVVNRGYD
     HLALFSPVDS STPKFLTSGE WEVDGKVVSV DYERELIYFI STEKSSIERH LYSVNFDGTN
     RTALTDINNE GHYSVSFSPG GQYYNLKYEG PDIPWQKVLK IGDPNFAMVL HENNDLRKLM
     GSLETPTKRH LTIESDGNIL NAVEIRPPGM DESGRVKYPV LFNVYGGPNS QLVQKKFKVD
     WHMFIASSDR LKYITVIVDT RGTGFKGRKF RVGVRKRLGE LESKDVINAG RYWSKLPYVD
     SNKIAVWGWS FGAFLTSKVI ESDSRVFQVG MAVAPVTDWR YYDSIYTERY MKTPAQNPEG
     YEYSAITNMT GFENAKFLLV HGTGDVHFQN TANLIDRLTL ASVHNYRVQF YSDNDHNIDI
     HNANRELYYL LTEYLWQSFG TGGTTEH
//
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