ID A0A397U5P5_9GLOM Unreviewed; 962 AA.
AC A0A397U5P5;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Dipeptidyl peptidase IV N-terminal region-domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=C2G38_2047969 {ECO:0000313|EMBL:RIB04981.1};
OS Gigaspora rosea.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC Glomeromycetes; Diversisporales; Gigasporaceae; Gigaspora.
OX NCBI_TaxID=44941 {ECO:0000313|EMBL:RIB04981.1, ECO:0000313|Proteomes:UP000266673};
RN [1] {ECO:0000313|EMBL:RIB04981.1, ECO:0000313|Proteomes:UP000266673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAOM 194757 {ECO:0000313|EMBL:RIB04981.1,
RC ECO:0000313|Proteomes:UP000266673};
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 -!- 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:RIB04981.1}.
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DR EMBL; QKWP01002071; RIB04981.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A397U5P5; -.
DR Proteomes; UP000266673; Unassembled WGS sequence.
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:SF193; DIPEPTIDYL PEPTIDASE 9; 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 Protease {ECO:0000256|ARBA:ARBA00022825};
KW Reference proteome {ECO:0000313|Proteomes:UP000266673};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 290..654
FT /note="Dipeptidylpeptidase IV N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00930"
FT DOMAIN 763..962
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 962 AA; 109958 MW; F30FDA8438125FAF CRC64;
MNCSWEQIRR EIRAYRSSVS PSNIASIKDF CFDERNNRAY VLATDPSRMK TSTLYMVDLP
PLKYKKEKTE STNKVRDQSE STFNFTNNEL CAKEFSFTFC PLTPHDTSIR SESINPSNLD
NSPTIDFSSM NNKTQLKSRQ SCILPKIPTA EWKPLLPESC LREKPFSEAL SREEMFVKER
RRLALQGITS YQFDSRSGQI LFSYGGGIYL GHVSKNAEFY PRPIIPYSLN PVYSGNILNF
SLAHSPQNNR ISPLSSPSTT SSSPSSPCCT SLINTLLPRL DPKLGGRNCD LVAFIRDRDI
WVTTLNGLET QLTFCNEHDP DGSSALSCGV SEFVMQEEFH RFTGYYWAPS TASTCIKEHV
ERILYLQISE SMVDLVLIPR PGQQGEAEEY RYPKAGTPNA VSDLQIVEFI PRYRDEEATT
SPVHKRLWGP AALDKLFPWK EYIVRFGWCP NGKSVWVQLL DRPQRRTAII KVPIANFMSL
SEYQESGGEL DNLCMSRIEV VFEETNDIWI NVTDICYFFN DDEIISSKNT NTNTSLPYTI
QSPTKLIITS ESSGFRHLYL VNKPSAESPH YHVRPITAGN WPIVDRSIYV DTKRELVYFT
AKKDTPLEAH IYVASYAETA DPYSVIRLSE LGYSHFVVMD EKCERYLDWF SNIKEKPRCG
VRYFEWDEGQ IFPKVSETLG ILVKSGNEDE EVRNNEDKPQ NERIPIGEFF NFKNSDGVTI
YGCLYRPINY IEGKKYPTLL SIYGGPKSQM VTNDYKYPRL LRLFLAAHLG FSVVLIDGRG
SSDRGLEFES YLKGRMGTVE LDDQIAGLKY LSSKNMGVDL ERVAITGWSY GGYLSLMALA
QFPQIFKLAV AGAPVTQWEL YDTAYTERYM GLPEENVEGY RNGNVLTWAE KFPDGENRLL
IAHGQIDENV HFKNSELLVA SLVKYNKPHV LQPYPTERHG LRHANVAEHF ETLMFFWLVN
YL
//