ID M2XWT5_GALSU Unreviewed; 582 AA.
AC M2XWT5;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE SubName: Full=Aspartyl protease {ECO:0000313|EMBL:EME27874.1};
GN ORFNames=Gasu_45390 {ECO:0000313|EMBL:EME27874.1};
OS Galdieria sulphuraria (Red alga).
OC Eukaryota; Rhodophyta; Bangiophyceae; Galdieriales; Galdieriaceae;
OC Galdieria.
OX NCBI_TaxID=130081 {ECO:0000313|EMBL:EME27874.1, ECO:0000313|Proteomes:UP000030680};
RN [1] {ECO:0000313|Proteomes:UP000030680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=074W {ECO:0000313|Proteomes:UP000030680};
RX PubMed=23471408; DOI=10.1126/science.1231707;
RA Schonknecht G., Chen W.H., Ternes C.M., Barbier G.G., Shrestha R.P.,
RA Stanke M., Brautigam A., Baker B.J., Banfield J.F., Garavito R.M., Carr K.,
RA Wilkerson C., Rensing S.A., Gagneul D., Dickenson N.E., Oesterhelt C.,
RA Lercher M.J., Weber A.P.;
RT "Gene transfer from bacteria and archaea facilitated evolution of an
RT extremophilic eukaryote.";
RL Science 339:1207-1210(2013).
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR EMBL; KB454526; EME27874.1; -; Genomic_DNA.
DR RefSeq; XP_005704394.1; XM_005704337.1.
DR AlphaFoldDB; M2XWT5; -.
DR EnsemblPlants; EME27874; EME27874; Gasu_45390.
DR GeneID; 17086752; -.
DR Gramene; EME27874; EME27874; Gasu_45390.
DR KEGG; gsl:Gasu_45390; -.
DR eggNOG; KOG1339; Eukaryota.
DR OMA; GASHAYG; -.
DR OrthoDB; 3528209at2759; -.
DR Proteomes; UP000030680; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05471; pepsin_like; 1.
DR CDD; cd12087; TM_EGFR-like; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR034164; Pepsin-like_dom.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR47966:SF51; NAPSIN-A; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|RuleBase:RU000454};
KW Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|RuleBase:RU000454, ECO:0000313|EMBL:EME27874.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030680};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 528..552
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 171..495
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 187
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 383
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 582 AA; 63532 MW; B23C2799A93950D9 CRC64;
MKTLSRKKVE QNESMSWVSL ATHMLRLLPG IFLFLVLCCP SGGQTSRTNN CYNTLRQRTL
IQMGNELFLE PRQNVVRKQM DNDEILVIPL AYRVPLGRQD ILRNIFTSES RKRHLLGNNR
ENLFRQLEQR VIQKNNDWED SPRFQTEESG IGVKRYFEQV VLGNVVNMAE YYVSLQVNGE
SFYVQLDTGS SNLLISTTNC SHCQANKKLQ LNGLTSVSCS SSDCCQQSSS CCSKQDPSLC
GVLVEYGSGF ASGALVKGTV TISNISVYTT FGGILNSSSD FEPTSVSGIL GMASSQLACN
PTCVTPLFDA IVQQKSIANV FSVLLNPDNG VLVLGGVDGN FSNGSISYTD MPSSDPGYYE
VTVSSVSVDG DDVYQTSFTA VVDTGTTLVY LPETCYNDLV KYFQSHYNNS FWDSLGALLG
SLSSSYISSL PNVDIQLSGS VKVSIPPDSY LVSVGDGNYM FGIQSSGGSS SILGDVLLQN
YYTVFDRVNS RIGFGPAVDV KSVNLSNVPG VGNISIPSPS TSPTLPTYGI VLIVVAGVLG
AILLSMAVFL LVRRRRKSII PRTNVWSSQP YGVYGDSYYY YR
//