ID K7TME9_MAIZE Unreviewed; 294 AA.
AC K7TME9;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=Aspartic proteinase A1 {ECO:0000313|EMBL:AQK41998.1};
GN ORFNames=ZEAMMB73_Zm00001d024767 {ECO:0000313|EMBL:AQK41998.1};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577 {ECO:0000313|EMBL:AQK41998.1};
RN [1] {ECO:0000313|EMBL:AQK41998.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Seedling {ECO:0000313|EMBL:AQK41998.1};
RG Maize Genome Sequencing Project;
RA Ware D.;
RT "Update maize B73 reference genome by single molecule sequencing
RT technologies.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR EMBL; CM000786; AQK41995.1; -; Genomic_DNA.
DR EMBL; CM000786; AQK41998.1; -; Genomic_DNA.
DR AlphaFoldDB; K7TME9; -.
DR MEROPS; A01.020; -.
DR HOGENOM; CLU_013253_3_1_1; -.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR Gene3D; 1.10.225.10; Saposin-like; 1.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR007856; SapB_1.
DR InterPro; IPR008138; SapB_2.
DR InterPro; IPR011001; Saposin-like.
DR InterPro; IPR008139; SaposinB_dom.
DR PANTHER; PTHR47966:SF9; ASPARTIC PROTEINASE; 1.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR Pfam; PF00026; Asp; 1.
DR Pfam; PF05184; SapB_1; 1.
DR Pfam; PF03489; SapB_2; 1.
DR PRINTS; PR00792; PEPSIN.
DR SMART; SM00741; SapB; 2.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR SUPFAM; SSF47862; Saposin; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
DR PROSITE; PS50015; SAP_B; 2.
PE 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|ARBA:ARBA00022750,
KW ECO:0000256|RuleBase:RU000454};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR601461-2};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454}.
FT DOMAIN 1..291
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT DOMAIN 105..145
FT /note="Saposin B-type"
FT /evidence="ECO:0000259|PROSITE:PS50015"
FT DOMAIN 164..216
FT /note="Saposin B-type"
FT /evidence="ECO:0000259|PROSITE:PS50015"
FT DISULFID 213..250
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 294 AA; 31674 MW; 288E4705643AC72A CRC64;
MQEQELLAED VFSFWLNRSP DAAAAGGELV FGGVDPAHFS GNHTYVPVSR KGYWQFDMGD
LLIDGHSTGF CAKGCAAIVD SGTSLLAGPT AIIAQVNEAI GADGIISTEC KEVVSQYGEM
ILDMLIAQTD PQRVCSQVGL CVFDGARSVS EGIESVVGKE NLGSDVMCSA CQMAVVWIEN
QLRENKTKEL ILQYANQLCE RLPSPNGEST VSCQEISKMP SLAFTIANKT FTLTPQQYIV
KLEQGGQTVC ISGFMAYDVP PPRGPLWILG DVFMGAYHTV FDFGNDRIGF AESA
//
