ID A0A0V0Y579_TRIPS Unreviewed; 807 AA.
AC A0A0V0Y579;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Dipeptidyl aminopeptidase-like protein 6 {ECO:0000313|EMBL:KRX95407.1};
GN Name=DPP6 {ECO:0000313|EMBL:KRX95407.1};
GN ORFNames=T4E_11239 {ECO:0000313|EMBL:KRX95407.1}, T4E_8293
GN {ECO:0000313|EMBL:KRX95371.1};
OS Trichinella pseudospiralis (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6337 {ECO:0000313|EMBL:KRX95407.1, ECO:0000313|Proteomes:UP000054815};
RN [1] {ECO:0000313|EMBL:KRX95407.1, ECO:0000313|Proteomes:UP000054815}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS141 {ECO:0000313|EMBL:KRX95407.1};
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:KRX95407.1}.
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DR EMBL; JYDU01000057; KRX95371.1; -; Genomic_DNA.
DR EMBL; JYDU01000057; KRX95407.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0Y579; -.
DR STRING; 6337.A0A0V0Y579; -.
DR Proteomes; UP000054815; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
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 Aminopeptidase {ECO:0000313|EMBL:KRX95407.1};
KW Hydrolase {ECO:0000313|EMBL:KRX95407.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000313|EMBL:KRX95407.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054815};
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 TRANSMEM 29..54
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 133..520
FT /note="Dipeptidylpeptidase IV N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00930"
FT DOMAIN 604..806
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 807 AA; 92832 MW; 2D7226CAD80A2D0C CRC64;
MSEEDDFSAE VEYVSDKELM TGDAPQRNWW GIGIALLVIL TITAIISVTI VLLAPNSDKS
NDNVTPFTIE DIVYPKANEI NPGVIWLSVD TFAYKDAKCN IWLVSIFNDQ INRTLLIDDR
SCQNRHIISF KPSATAQYIA FSYETRQIYR HSETSLYNIT RVPIFYDDYF DYPVGPSKTG
DEFIQLFLWN SQELSNDLVY VYKNNIYYQA NVTAPSEQIT FNGVENRISN GIADWLYEEE
IFGTHKAVWW SPSGNYLAFV LFNDTQVSNI TMSYYSDQSY PTNVNIPYPK VGASLPEAKV
NVWNKKTKKT ITFSPPDEVQ RLKENYVYQV SWLQGGFSEF SNEDTLLVVW SNRVQNSVFI
SLCKLSNEQC ILNYNQNFTN FWAEPLNFVV RFADEQNYFV ILPKSVEDES EKQHYWYSHI
AKINVPQSGQ NGKAVFLTDG PWEVIEIVGY SEKDKELFFL AALPLPRQKH LYSVSIFETT
TSPKCWTCNM SKDGCSYVDA YFAPKGDHYI LYCQGPETPT VYLKSLHSAE FSFEIENNTA
LRQFYSTKLF PVVSYKEIQL PNQQKALLKI LYPPGFEENA NKEFYPAVLR VYAGPNSQQV
VEKWSVSFDT YLASAQKYIV LYIDARGSAY RGSKYTAPLY KNIGQLEIED QIDAFKAFCS
QYGQVDLQRT AVWGWSYGGF AAARIVQMDE FQIFKCASSV APVTDFRFYD AAYTERYLGL
YEDNVVNYEK TNLMKNVTAF KLGKYLLIHG SFDDNVHYQN TAAFISALTA NNVNFQLMVY
TNENHSISNR RLHLNTLLDR FFKSCFA
//