ID A0A0V0WK82_9BILA Unreviewed; 825 AA.
AC A0A0V0WK82;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Inactive dipeptidyl peptidase 10 {ECO:0000313|EMBL:KRX75918.1};
GN Name=Dpp10 {ECO:0000313|EMBL:KRX75918.1};
GN ORFNames=T06_17041 {ECO:0000313|EMBL:KRX75918.1};
OS Trichinella sp. T6.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92179 {ECO:0000313|EMBL:KRX75918.1, ECO:0000313|Proteomes:UP000054673};
RN [1] {ECO:0000313|EMBL:KRX75918.1, ECO:0000313|Proteomes:UP000054673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS34 {ECO:0000313|EMBL:KRX75918.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
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}.
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:KRX75918.1}.
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DR EMBL; JYDK01000112; KRX75918.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0WK82; -.
DR Proteomes; UP000054673; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008236; F:serine-type peptidase 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; 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 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000054673};
KW Signal {ECO:0000256|SAM:SignalP};
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}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..825
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006871780"
FT TRANSMEM 54..79
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 159..525
FT /note="Dipeptidylpeptidase IV N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00930"
FT DOMAIN 616..824
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 825 AA; 94792 MW; 22B41E70C0D9FFDA CRC64;
MRIFPVGIHW LSFLRVGCGV CLLCRMSEED DFSAEVEYVS DKELMTGDAP QRNWWGIGIA
LLVILTITAI ISVTIVLLAP NSDRSNDNVT PFTIEDIVHP KANEVNPGII WLSVDTFAYK
DAKCNIWLVS IFNHQINRTL LIDDRSCQNR HIVSYKPSAT AQYIAFSYET RQFVRQRWST
LVKVRVLNSH FDYPVGPSKT GDEFIQLFLW NSQELSNDLV YVYEYNIYYQ ANVTAPSEQI
TFSGVENKIS NGIADWLYEE EIFGTHKAVW WSPSGNHLAF VVFNDTQVSN ITMSYYSEEP
YPTNVNIPYP KVGASLPEAK VHVWNKKTKQ TITFSPPDEV QRLKENYVYH VSWLKGGFSE
FSNEDTLLVV WSNRVQNSVF ISLCKLSSEQ CILNYNQNFT NFWAEPLNFV VRFADEQNYF
VILPKSVEDE SEKQHYWYSH IAKINVPQSG QNGKAVFLTD GPWEVIEIVG YSEKDKEFVS
IFETTTSPKC WTCNMTKDGC SYVDVHFAPK GDHYILYCQG PETPTVHLKS LHSAEFCKNS
VFLAYEIENN TALRQFYSTK LFPVVSYKEI QLPNQQKALL KILYPPGFEE NANKEFYPAV
LRVYAGPNSQ QVVEKWSVSF DTYLASAQKY IVLYIDARGS AYRGSKYTAP LYKNIGQLEI
EDQIDAFKAF CSQYGQVDLQ RTAVWGWVIF CFKSYGGFAA ARIVQMDEFQ IFKCASSVAP
VTDFRFYDAA YTERYLGLYE DNVVSYEKTN LMKNVTAFKL GKYLLIHGSF DDNVHYQNTA
AFISALTANN VNFQLMVYTN ENHSIGNRRM HLNTLLDRFF KSCFA
//