ID A0A2U9C6Q4_SCOMX Unreviewed; 913 AA.
AC A0A2U9C6Q4;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE SubName: Full=Putative dipeptidyl peptidase 9-like {ECO:0000313|EMBL:AWP10772.1};
GN ORFNames=SMAX5B_022524 {ECO:0000313|EMBL:AWP10772.1};
OS Scophthalmus maximus (Turbot) (Psetta maxima).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC Scophthalmus.
OX NCBI_TaxID=52904 {ECO:0000313|EMBL:AWP10772.1, ECO:0000313|Proteomes:UP000246464};
RN [1] {ECO:0000313|EMBL:AWP10772.1, ECO:0000313|Proteomes:UP000246464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Martinez P.;
RT "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT evaluation of genetic and physical mapping variation across individuals.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP026254; AWP10772.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U9C6Q4; -.
DR STRING; 52904.ENSSMAP00000034397; -.
DR Proteomes; UP000246464; Chromosome 12.
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; IPR045785; Dpp_8/9_N.
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; PF19520; Dpp_8_9_N; 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 Reference proteome {ECO:0000313|Proteomes:UP000246464}.
FT DOMAIN 64..187
FT /note="Dipeptidyl peptidase 8 /9 ,N-terminal"
FT /evidence="ECO:0000259|Pfam:PF19520"
FT DOMAIN 199..618
FT /note="Dipeptidylpeptidase IV N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00930"
FT DOMAIN 713..913
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 913 AA; 104232 MW; 190B8CE2488DCEC5 CRC64;
MKQQRDVCPQ WGRHLRCRVW SRLVERLMHR VKRLKVEDRT EDAEESIRGV AAGMTGLDEL
SDSTEVVEME DVIPTQFQVE KHTWDGLRKI IHQSHKTTGM IISKAPHDFQ FIQKDEGSPH
SHRVYYLGMP NIFMENALLY SDIPKKIRKD SLLVLSWKMM LDHFQASPHH GGLSREEELL
RERKRLGVSG ITSYDFHRPS GLFLFQANSS LYYCRDGGND SLTTSPMNPS EIKSQNSGTR
MDPKICPGDP DFIGFIINND IWVTNIKTGE ERRLTFCHKG SENPKDDPKS AGVATFVTQE
EFDRFTGYWW SPAAREESDG GKTLQILYEE VDESEVEIIH VPSPALEERK TDVYRYPRAG
SKNPDITLKI AEIRTDNLGK IVSAQEKELP VPFTSLFPCA EYITRAGWTK DGRYAWAVMM
DRRQQRLQLV LLPPAFFIPS HQDEASRQES LEALGDAVQP FIIYQETSNI WINVHDIFHP
FIQTSDEEIT FITVNESKTG FCHLYKITSV LQRGSYHWAK GYTHSEEDFK CPVKEELTVT
SGEWEVLANQ GAKIWVDEAA KLVYFQGTKD SPLEHHLYVV SYDSPGEIAR LTKPGFSHSC
SVSQTFDMFI SHYSSLTSSP CVHIFKLNGS DSDPLHKEPQ FWASMKEPPG FTFDYTPPEI
FSFTGKSGFE LYGMLYKPHH LVPGRKHPTV VFVYGGPQVQ LVNNSFKGVK YLRLNTLASL
GYAVLVIDGR GSCQRGLQFE GAVKDKMGQV EIEDQVEGLH YVADKYKFVD LSRVAIHGWS
YGGFLSLMGL VHKPDVFKVA IAGAPVTLWM AYDTGYTERY LDTPEKNKQG YEACSVALHV
DKLPNEPNRL LILHGFLDEN VHFFHTNFLV SQMIRAGKPY NLQVYPNERH SIRCPESGEH
YEITLLHFLQ QNL
//