ID K7LM15_SOYBN Unreviewed; 616 AA.
AC K7LM15;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Prolyl endopeptidase {ECO:0000256|RuleBase:RU368024};
DE EC=3.4.21.- {ECO:0000256|RuleBase:RU368024};
GN ORFNames=GLYMA_10G288500 {ECO:0000313|EMBL:KRH36173.1};
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:KRH36173};
RN [1] {ECO:0000313|EMBL:KRH36173.1, ECO:0000313|EnsemblPlants:KRH36173}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH36173};
RC TISSUE=Callus {ECO:0000313|EMBL:KRH36173.1};
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:KRH36173}
RP IDENTIFICATION.
RC STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH36173};
RG EnsemblPlants;
RL Submitted (FEB-2018) to UniProtKB.
RN [3] {ECO:0000313|EMBL:KRH36173.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Callus {ECO:0000313|EMBL:KRH36173.1};
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 S9A family.
CC {ECO:0000256|ARBA:ARBA00005228, ECO:0000256|RuleBase:RU368024}.
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DR EMBL; CM000843; KRH36173.1; -; Genomic_DNA.
DR AlphaFoldDB; K7LM15; -.
DR SMR; K7LM15; -.
DR STRING; 3847.K7LM15; -.
DR PaxDb; 3847-GLYMA10G43457-1; -.
DR EnsemblPlants; KRH36173; KRH36173; GLYMA_10G288500.
DR Gramene; KRH36173; KRH36173; GLYMA_10G288500.
DR eggNOG; KOG2237; Eukaryota.
DR HOGENOM; CLU_011290_0_1_1; -.
DR InParanoid; K7LM15; -.
DR OMA; PEQSQFG; -.
DR Proteomes; UP000008827; Chromosome 10.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 2.130.10.120; Prolyl oligopeptidase, N-terminal domain; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR023302; Pept_S9A_N.
DR InterPro; IPR001375; Peptidase_S9.
DR InterPro; IPR002470; Peptidase_S9A.
DR PANTHER; PTHR11757:SF22; PROLYL ENDOPEPTIDASE; 1.
DR PANTHER; PTHR11757; PROTEASE FAMILY S9A OLIGOPEPTIDASE; 1.
DR Pfam; PF00326; Peptidase_S9; 1.
DR Pfam; PF02897; Peptidase_S9_N; 1.
DR PRINTS; PR00862; PROLIGOPTASE.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF50993; Peptidase/esterase 'gauge' domain; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU368024};
KW Protease {ECO:0000256|RuleBase:RU368024};
KW Reference proteome {ECO:0000313|Proteomes:UP000008827};
KW Serine protease {ECO:0000256|RuleBase:RU368024}.
FT DOMAIN 2..366
FT /note="Peptidase S9A N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02897"
FT DOMAIN 442..615
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 616 AA; 69761 MW; 1014B4217C41D224 CRC64;
MEMFGDVRIG NYYWLRDDSR TDPEVLSYLH EENAYTDSIM SGRIKEEDVS APLRKGPCYY
YKRTLEGKEY VQYCRRLISD NQKVPYVHDI MPTGPEAPPE HVILDVNVKA QHHQYCTNTT
HTPKTPKEMK YILYVIDAET QATIGEPLVG VTSYFEWAGD NALVYVMMDE ILRPDKAWFH
VLGTEQSKDT CLYVEKDDMF SLDLEAFESK KYLFVASESK NTRFNFYLDV SKLEEGLKVL
TPSVDGIDTT VSHIGACAVN NTSSTTVLIP HRESVKIQEI QLFSDHLVVY ERENGLPKII
VYHLPPISEP LRSLESGQAV SFVDPVYSAE SSGSEFPSSI LGFLYSSLRT PSSVYDDNMK
AGISVLKKID SSNWSTMLRT KLPNDCEIRI KVTKLTYPGA KRLLGSGHYL IPILIVYRKD
LVKLDGSDPL LLYGYGLYEL ISGGGEMGRQ WYENGKLLKK KNTFTDFIAC AEYLIEKNSV
LRKDCIEGRS AGGLLIGAVL NMRPDLCKAA VAGVPFVDVV TTMLDPTIPL TTSEWEEWDD
PRKEEFYFYM KSYSPVDNAK AQNYPNILVT EGLNDTRVLY SEPAKFVAKL RKSKIDDNIL
LFKCEFGAGH SSKSER
//
