ID I1MJG1_SOYBN Unreviewed; 521 AA.
AC I1MJG1;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 2.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN Name=100814747 {ECO:0000313|EnsemblPlants:KRH13812};
GN ORFNames=GLYMA_15G265500 {ECO:0000313|EMBL:KRH13812.1};
OS Glycine max (Soybean) (Glycine hispida).
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=3847 {ECO:0000313|EnsemblPlants:KRH13812};
RN [1] {ECO:0000313|EMBL:KRH13812.1, ECO:0000313|EnsemblPlants:KRH13812}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH13812};
RC TISSUE=Callus {ECO:0000313|EMBL:KRH13812.1};
RX PubMed=20075913; DOI=10.1038/nature08670;
RA Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA Stacey G., Shoemaker R.C., Jackson S.A.;
RT "Genome sequence of the palaeopolyploid soybean.";
RL Nature 463:178-183(2010).
RN [2] {ECO:0000313|EnsemblPlants:KRH13812}
RP IDENTIFICATION.
RC STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH13812};
RG EnsemblPlants;
RL Submitted (FEB-2018) to UniProtKB.
RN [3] {ECO:0000313|EMBL:KRH13812.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Callus {ECO:0000313|EMBL:KRH13812.1};
RA Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA Jackson S.;
RT "WGS assembly of Glycine max.";
RL Submitted (JUL-2018) 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; CM000848; KRH13812.1; -; Genomic_DNA.
DR RefSeq; XP_006598230.1; XM_006598167.2.
DR AlphaFoldDB; I1MJG1; -.
DR SMR; I1MJG1; -.
DR MEROPS; A01.A30; -.
DR PaxDb; 3847-GLYMA15G41970-1; -.
DR EnsemblPlants; KRH13812; KRH13812; GLYMA_15G265500.
DR GeneID; 100814747; -.
DR Gramene; KRH13812; KRH13812; GLYMA_15G265500.
DR KEGG; gmx:100814747; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_005738_8_0_1; -.
DR InParanoid; I1MJG1; -.
DR OMA; EVRCLGF; -.
DR OrthoDB; 469863at2759; -.
DR Proteomes; UP000008827; Chromosome 15.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05476; pepsin_A_like_plant; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR034161; Pepsin-like_plant.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR032799; TAXi_C.
DR InterPro; IPR032861; TAXi_N.
DR PANTHER; PTHR47967:SF69; ASPARTIC PROTEINASE NANA, CHLOROPLAST; 1.
DR PANTHER; PTHR47967; OS07G0603500 PROTEIN-RELATED; 1.
DR Pfam; PF14541; TAXi_C; 1.
DR Pfam; PF14543; TAXi_N; 2.
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|ARBA:ARBA00022750,
KW ECO:0000256|RuleBase:RU000454}; Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000008827}.
FT DOMAIN 114..516
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 150..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..193
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 132
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 397
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 521 AA; 57631 MW; 1C2B20E1C9D4C1EC CRC64;
MMGRRMMQWN TITKASILVT ITLLLILPVA VNSMRLELVH RHHERFAGGG GDVDRVEAVK
GFVKRDKLRR QRMNQRWGVV SNYDSRRKGF EMTTTPAEVE MPMHSGRDDA LGEYFAEVKV
GSPGQRFWLV VDTGSEFTWL NCVMQNATTT TTTRKNKTKK KQQQHHHHVH KHHSKRNNRT
RTRRTRKKKV KSSKSNKSDP CKGVFCPHKS KSFEAVTCAS RKCKVDLSEL FSLSVCPKPS
DPCLYDISYA DGSSAKGFFG TDSITVGLTN GKQGKLNNLT IGCTKSMLNG VNFNEETGGI
LGLGFAKDSF IDKAANKYGA KFSYCLVDHL SHRSVSSNLT IGGHHNAKLL GEIRRTELIL
FPPFYGVNVV GISIGGQMLK IPPQVWDFNA EGGTLIDSGT TLTSLLLPAY EAVFEALTKS
LTKVKRVTGE DFDALEFCFD AEGFDDSVVP RLVFHFAGGA RFEPPVKSYI IDVAPLVKCI
GIVPIDGIGG ASVIGNIMQQ NHLWEFDLST NTVGFAPSTC T
//
