ID   A0A3B4BMB1_9GOBI        Unreviewed;       813 AA.
AC   A0A3B4BMB1;
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=Uncharacterized protein {ECO:0000313|Ensembl:ENSPMGP00000029615.1};
OS   Periophthalmus magnuspinnatus.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Gobiaria; Gobiiformes; Gobioidei; Gobiidae; Oxudercinae; Periophthalmus.
OX   NCBI_TaxID=409849 {ECO:0000313|Ensembl:ENSPMGP00000029615.1, ECO:0000313|Proteomes:UP000261520};
RN   [1] {ECO:0000313|Ensembl:ENSPMGP00000029615.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; A0A3B4BMB1; -.
DR   STRING; 409849.ENSPMGP00000029615; -.
DR   Ensembl; ENSPMGT00000031522.1; ENSPMGP00000029615.1; ENSPMGG00000023820.1.
DR   Proteomes; UP000261520; Unplaced.
DR   GO; GO:0016020; C:membrane; 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:SF206; DIPEPTIDYL AMINOPEPTIDASE-LIKE PROTEIN 6 ISOFORM X1; 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|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        73..94
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          189..521
FT                   /note="Dipeptidylpeptidase IV N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00930"
FT   DOMAIN          599..794
FT                   /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00326"
FT   REGION          1..64
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        38..62
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   813 AA;  92799 MW;  4348E1496DF1F551 CRC64;
     MASLYQRFRS GTIETNKSFP DPPEASHLLG QSAEGQRGPE SHRARLQQQY RRQHDDEDEL
     VGSNPPQRNW KGIAIALLVI LVICSLIVTS VILLTPREDD RLALKSKLTV TDLFKKDFKV
     HDPNAKWISV LTQNLIVSMN FNAILWNIHD KTVTSMEKSR WQTQRPRDAP PEMLHSATLR
     YKRVSFYRET WNLNPPEVRN AQLQFAGWGP QDQQLIFIFE NNIYFRSKVE SRSIRLVSTG
     KEGVIFNGLS DWLYEEEIFH SHIAHWWSPD GARLAYATIN DSLVPKMELP MFTGTPYPMG
     KEYHYPKAGE ENPVITIYVV NLNGPLHTIE MRRPDDTRIG EYYVTMVKWA TATKLAINWM
     NRPQNISVLT LCEATTGVCT KKHEDESEGW LHTQNESPLF SRDGLKLFFT RAIPQGGRGK
     FFHISMSTSQ VNTSTDTLQS ITSGDWDVTQ VLAFNEESQL IYFLSTEDGP KRRHLYSADT
     SGSFNRRCLT CSLPNTCGYV SGSFSLNMTY FLLECKGPDV PFVSIFRTQI DEDAQDGESE
     RILDSMQMPT VEYKEVNMDD YILSMQILKP AGFMDTSHYP LLLLVDGTPG GQSVSEQFHL
     DWSTVLVSSF GAVVLRVDGR GSGFQGTNLL HRIQKRLGIY EEQDQRDAVN LMLREPYIDK
     TRVGAYGKEY GGYITSLLLS AGEGSAVKCG AVLSPITDFE LYGKRFFISG LSFSQMANLE
     HRASQFMDNK FLIIHPTADE KVHFQHTAKF ISRLINAKAN YTLQIYPDEG HFIRSEATRQ
     HLSQSLVNFF EECFRLPERI FEETLEEESE DEV
//