ID D2VDU6_NAEGR Unreviewed; 463 AA.
AC D2VDU6;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Peptidase S1 domain-containing protein {ECO:0000259|PROSITE:PS50240};
GN ORFNames=NAEGRDRAFT_67046 {ECO:0000313|EMBL:EFC45059.1};
OS Naegleria gruberi (Amoeba).
OC Eukaryota; Discoba; Heterolobosea; Tetramitia; Eutetramitia;
OC Vahlkampfiidae; Naegleria.
OX NCBI_TaxID=5762 {ECO:0000313|Proteomes:UP000006671};
RN [1] {ECO:0000313|EMBL:EFC45059.1, ECO:0000313|Proteomes:UP000006671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEG-M {ECO:0000313|EMBL:EFC45059.1,
RC ECO:0000313|Proteomes:UP000006671};
RX PubMed=20211133; DOI=10.1016/j.cell.2010.01.032;
RA Fritz-Laylin L.K., Prochnik S.E., Ginger M.L., Dacks J.B., Carpenter M.L.,
RA Field M.C., Kuo A., Paredez A., Chapman J., Pham J., Shu S., Neupane R.,
RA Cipriano M., Mancuso J., Tu H., Salamov A., Lindquist E., Shapiro H.,
RA Lucas S., Grigoriev I.V., Cande W.Z., Fulton C., Rokhsar D.S., Dawson S.C.;
RT "The genome of Naegleria gruberi illuminates early eukaryotic
RT versatility.";
RL Cell 140:631-642(2010).
CC -!- SIMILARITY: Belongs to the peptidase S1 family.
CC {ECO:0000256|ARBA:ARBA00007664}.
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 EMBL; GG738865; EFC45059.1; -; Genomic_DNA.
DR RefSeq; XP_002677803.1; XM_002677757.1.
DR AlphaFoldDB; D2VDU6; -.
DR STRING; 5762.D2VDU6; -.
DR MEROPS; S01.103; -.
DR EnsemblProtists; EFC45059; EFC45059; NAEGRDRAFT_67046.
DR GeneID; 8853049; -.
DR VEuPathDB; AmoebaDB:NAEGRDRAFT_67046; -.
DR eggNOG; KOG3627; Eukaryota.
DR InParanoid; D2VDU6; -.
DR OMA; QEMTHEA; -.
DR OrthoDB; 5392320at2759; -.
DR Proteomes; UP000006671; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR24276:SF91; AT26814P-RELATED; 1.
DR PANTHER; PTHR24276; POLYSERASE-RELATED; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000256|RuleBase:RU363034};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|RuleBase:RU363034};
KW Reference proteome {ECO:0000313|Proteomes:UP000006671};
KW Serine protease {ECO:0000256|RuleBase:RU363034};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 440..461
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 61..295
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT REGION 308..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 382..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..424
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 463 AA; 49055 MW; FCF73882950AD637 CRC64;
MNHPIGSVQA SSLFNINKKE QISKELTRYF TPAFQSYKQS YRPSSLTIAS IILRGIKDSK
IAGGTQASSH EFPFLVSIQS SSRQHYCGGS LIAPNFVLSA AHCFVSGTTV DNPTTVYILP
GSNDRTCSTC TRYRGKAITV HPNYDEQTTR NDIAILELQS SIPVDGTLVK LAKVEGGTYP
IDGSKSLTVS GWGYTTGTSL PTMLMKTNVV VNPVSVCLLL DMITPNQICA GGNGHDSCAG
DSGGPLFRVD SSNDFIVLGI VSYGDDGCGE AQTYNNKGVY TNTTHYLSFI KSVVPSVGVK
SYSVVTPSSL STPTVNNTTN TTTISNNTNT PTVNNTTNTT SSNNGASNST TNSNSSISVN
NSTSNCTASN CTLTNSNTTI NSNSSIPLPI PTPIPSPSTP SLSNSTSNSS HWFNSTSSNS
TKNSTTTFLG PNGSNIASPY FHYIISTLIM LFISTCFNNF ATI
//
