ID I1MZL8_SOYBN Unreviewed; 536 AA.
AC I1MZL8;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 2.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN Name=100783825 {ECO:0000313|EnsemblPlants:KRG98063};
GN ORFNames=GLYMA_18G048500 {ECO:0000313|EMBL:KRG98063.1};
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:KRG98063};
RN [1] {ECO:0000313|EMBL:KRG98063.1, ECO:0000313|EnsemblPlants:KRG98063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRG98063};
RC TISSUE=Callus {ECO:0000313|EMBL:KRG98063.1};
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:KRG98063}
RP IDENTIFICATION.
RC STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRG98063};
RG EnsemblPlants;
RL Submitted (FEB-2018) to UniProtKB.
RN [3] {ECO:0000313|EMBL:KRG98063.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Callus {ECO:0000313|EMBL:KRG98063.1};
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; CM000851; KRG98063.1; -; Genomic_DNA.
DR RefSeq; XP_003552901.1; XM_003552853.3.
DR AlphaFoldDB; I1MZL8; -.
DR SMR; I1MZL8; -.
DR STRING; 3847.I1MZL8; -.
DR MEROPS; A01.050; -.
DR PaxDb; 3847-GLYMA18G05510-1; -.
DR EnsemblPlants; KRG98063; KRG98063; GLYMA_18G048500.
DR GeneID; 100783825; -.
DR Gramene; KRG98063; KRG98063; GLYMA_18G048500.
DR KEGG; gmx:100783825; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_005738_5_0_1; -.
DR InParanoid; I1MZL8; -.
DR OMA; KGFFHGA; -.
DR OrthoDB; 889644at2759; -.
DR Proteomes; UP000008827; Chromosome 18.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
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; OS07G0603500 PROTEIN-RELATED; 1.
DR PANTHER; PTHR47967:SF28; PEPTIDASE A1 DOMAIN-CONTAINING PROTEIN; 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; 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};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..536
FT /note="Peptidase A1 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014579199"
FT DOMAIN 170..529
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 47..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..69
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 188
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 411
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 536 AA; 60377 MW; 33A62B0EF290F127 CRC64;
MLMKVSLILV LLSIFCVTFK PYTEVDVQND HNNDPTLANK EFCKKAKSSE STRLNKEEDG
DDAISAKPHK RSAKFHLKRR PINHGNEPKT HALDSALRDL VRIQTLHRKV IEKKDTKSMS
WKQEVKVITI QQQNNLANAV VASLKSSKDE FSGNIMATLE SGASLGTGEY FIDMFVGTPP
KHVWLILDTG SDLSWIQCDP CYDCFEQNGP HYNPNESSSY RNISCYDPRC QLVSSPDPLQ
HCKTENQTCP YFYDYADGSN TTGDFALETF TVNLTWPNGK EKFKHVVDVM FGCGHWNKGF
FHGAGGLLGL GRGPLSFPSQ LQSIYGHSFS YCLTDLFSNT SVSSKLIFGE DKELLNHHNL
NFTKLLAGEE TPDDTFYYLQ IKSIVVGGEV LDIPEKTWHW SSEGVGGTII DSGSTLTFFP
DSAYDVIKEA FEKKIKLQQI AADDFIMSPC YNVSGAMQVE LPDYGIHFAD GAVWNFPAEN
YFYQYEPDEV ICLAILKTPN HSHLTIIGNL LQQNFHILYD VKRSRLGYSP RRCAEV
//
