ID A0A0B2RC85_GLYSO Unreviewed; 572 AA.
AC A0A0B2RC85;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Aspartic proteinase Asp1 {ECO:0000313|EMBL:KHN32026.1};
DE EC=2.7.1.- {ECO:0000313|EMBL:KHN32026.1};
DE SubName: Full=Aspartyl protease APCB1 {ECO:0000313|EMBL:RZB92685.1};
GN ORFNames=D0Y65_024582 {ECO:0000313|EMBL:RZB92685.1}, glysoja_034889
GN {ECO:0000313|EMBL:KHN32026.1};
OS Glycine soja (Wild soybean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3848 {ECO:0000313|EMBL:KHN32026.1};
RN [1] {ECO:0000313|EMBL:KHN32026.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Root {ECO:0000313|EMBL:KHN32026.1};
RA Lam H.-M., Qi X., Li M.-W., Liu X., Xie M., Ni M., Xu X.;
RT "Identification of a novel salt tolerance gene in wild soybean by whole-
RT genome sequencing.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:RZB92685.1, ECO:0000313|Proteomes:UP000289340}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. W05 {ECO:0000313|Proteomes:UP000289340};
RC TISSUE=Hypocotyl of etiolated seedlings {ECO:0000313|EMBL:RZB92685.1};
RA Xie M., Chung C.Y.L., Li M.-W., Wong F.-L., Chan T.-F., Lam H.-M.;
RT "A high-quality reference genome of wild soybean provides a powerful tool
RT to mine soybean genomes.";
RL Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447}.
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DR EMBL; KN650338; KHN32026.1; -; Genomic_DNA.
DR EMBL; QZWG01000009; RZB92685.1; -; Genomic_DNA.
DR SMR; A0A0B2RC85; -.
DR OrthoDB; 335768at2759; -.
DR Proteomes; UP000053555; Unassembled WGS sequence.
DR Proteomes; UP000289340; Chromosome 9.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR032799; TAXi_C.
DR InterPro; IPR032861; TAXi_N.
DR PANTHER; PTHR13683:SF316; ASPARTYL PROTEASE APCB1; 1.
DR PANTHER; PTHR13683; ASPARTYL PROTEASES; 1.
DR Pfam; PF14541; TAXi_C; 1.
DR Pfam; PF14543; TAXi_N; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:RZB92685.1};
KW Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:RZB92685.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000289340};
KW Transferase {ECO:0000313|EMBL:KHN32026.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 89..106
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 192..549
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 210
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 418
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 572 AA; 63083 MW; FA311AFD99F8F67F CRC64;
MEDDESPQIK GVVIISLPPP DNPSLGKTIT AFTFSNPSPQ PSIQPHQHQS QPTHPNAQHN
TDPPLQSYPS NPQLSFSFRR LFHSTPVKLF SFFGILLFAL FLYGSVSSTT TVELRGRNND
DDDDDKATSF LFPLFPKFGV LGQKDLKLQL GKLSQKEKFL THRDDGDGSG VVAVDSSSVF
PVSGNVYPDG LYFTILRVGN PPKSYFLDVD TGSDLTWMQC DAPCISCGKG AHVLYKPTRS
NVVSSVDALC LDVQKNQKNG HHDESLLQCD YEIQYADHSS SLGVLVRDEL HLVTTNGSKT
KLNVVFGCGY DQAGLLLNTL GKTDGIMGLS RAKVSLPYQL ASKGLIKNVV GHCLSNDGAG
GGYMFLGDDF VPYWGMNWVP MAYTLTTDLY QTEILGINYG NRQLRFDGQS KVGKMVFDSG
SSYTYFPKEA YLDLVASLNE VSGLGLVQDD SDTTLPICWQ ANFPIKSVKD VKDYFKTLTL
RFGSKWWILS TLFQISPEGY LIISNKGHVC LGILDGSNVN DGSSIILGDI SLRGYSVVYD
NVKQKIGWKR ADCGMPSRRL RKKNNFIPDS ML
//
