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Database: UniProt
Entry: A0A075AD77_9TREM
LinkDB: A0A075AD77_9TREM
Original site: A0A075AD77_9TREM 
ID   A0A075AD77_9TREM        Unreviewed;      1000 AA.
AC   A0A075AD77;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Peptidase M28 domain-containing protein {ECO:0000259|Pfam:PF04389};
GN   ORFNames=T265_06749 {ECO:0000313|EMBL:KER25894.1};
OS   Opisthorchis viverrini.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Opisthorchiida; Opisthorchiata; Opisthorchiidae; Opisthorchis.
OX   NCBI_TaxID=6198 {ECO:0000313|EMBL:KER25894.1, ECO:0000313|Proteomes:UP000054324};
RN   [1] {ECO:0000313|EMBL:KER25894.1, ECO:0000313|Proteomes:UP000054324}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Young N.D., Nagarajan N., Lin S.J., Korhonen P.K., Jex A.R., Hall R.S.,
RA   Safavi-Hemami H., Kaewkong W., Bertrand D., Gao S., Seet Q., Wongkham S.,
RA   Teh B.T., Wongkham C., Intapan P.M., Maleewong W., Yang X., Hu M., Wang Z.,
RA   Hofmann A., Sternberg P.W., Tan P., Wang J., Gasser R.B.;
RT   "Opisthorchis viverrini - life in the bile duct.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the peptidase M28 family.
CC       {ECO:0000256|ARBA:ARBA00010918}.
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DR   EMBL; KL596763; KER25894.1; -; Genomic_DNA.
DR   RefSeq; XP_009170358.1; XM_009172094.1.
DR   AlphaFoldDB; A0A075AD77; -.
DR   STRING; 6198.A0A075AD77; -.
DR   GeneID; 20320928; -.
DR   KEGG; ovi:T265_06749; -.
DR   CTD; 20320928; -.
DR   OrthoDB; 277019at2759; -.
DR   Proteomes; UP000054324; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008235; F:metalloexopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd03875; M28_Fxna_like; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR048024; Fxna-like_M28_dom.
DR   InterPro; IPR045175; M28_fam.
DR   InterPro; IPR007484; Peptidase_M28.
DR   PANTHER; PTHR12147:SF26; ENDOPLASMIC RETICULUM METALLOPEPTIDASE 1; 1.
DR   PANTHER; PTHR12147; METALLOPEPTIDASE M28 FAMILY MEMBER; 1.
DR   Pfam; PF04389; Peptidase_M28; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054324};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        437..455
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        461..494
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        506..525
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        655..675
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          175..360
FT                   /note="Peptidase M28"
FT                   /evidence="ECO:0000259|Pfam:PF04389"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..34
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1000 AA;  111577 MW;  DFD131E7AA519EEF CRC64;
     MDARRRSSTS PGGGGANATT DPDNQSSASI DLKSHSSYDE GDTPIPLSFW LKSISLFFLL
     TLMSSSVYRP CLSSTDRNVT PAPHQFIGAN ARRHLQKVTF LGSRTSGSLA NEVLAPEYLL
     SELYDIARLG KSNGADIFVD EQLSSAASFR TGYAVQSYKN VKNLLIRFHN SSLSNHTTAF
     LVNCHYDSFL GSPGATDTFV NCAILLEAGR AIATGKVQLV NDLIFLFNGA EESGLLTSHA
     FVTQHRWSND VKSFLNLEGT GAGGRLFVFQ SSSDESSQLL LGTYESCFHY PYADVFGEEI
     FQSGLIPSDT DFRIFRDFGF VPGLDMAYVR DGYAYHTPFD TEARISEECL QQNGEEILRF
     LSAVGGDKRL ESVSKLKSVN DTGLPSSGPP LNELSSTKIS RSQLPKPKVQ TSAHHRHVYF
     DILGIKLFVV SWTRWKLFNW FISLLVCCRL CFIRGSLPSR WVGLGISLVL HCLSQALGLI
     FSLLLGFVVH SFGFRMSWYS NQYNVVGLYI LPLLCWFICY STWFFHTLHR HNGLLRKICA
     YAKWSVTGDR RWNYALIEAD FFDAATLLLT VLVSVLTVLD RPAVFLFTLW LTSTVLGRFT
     YKFIFSGSTF SSLSNFLLTL MPTLTLWHVY FSRTILEFFI PVFGRSGHLV RQDVLMSGFV
     FFCVAPVALF ILGPLHCSST NCGKTLRLLF LNACVTYAVL VHSSSYGFPY TFTTGGNIND
     SSVSPRFQRL SVFHIDRTFH GSLGSKELEG QESFITILAW DGNGIQYLKP QTGLKFLDDN
     ENGKPNGLRE LLEATPAYCN FSLPYCGIPF FRPLFHFFTD FYHIPAKQHG SKPVAQLDVI
     SRIPLASSQL QSGRVAWNFT FSLRPGPPQT PLALRFDVPH VRLLNWSFAV DTSVPVPVPL
     TKSPSDPHVE SVGAHYFLDF IDARASISLP VEPWVFWLVI DRPSDMESSH FDIAVMGTYL
     DTKLPSCVSA QLDDVVSRLP PWISLSSGCA SYDHYRVGLS
//
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