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Database: UniProt
Entry: D7MRL4_ARALL
LinkDB: D7MRL4_ARALL
Original site: D7MRL4_ARALL 
ID   D7MRL4_ARALL            Unreviewed;       714 AA.
AC   D7MRL4;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   24-JAN-2024, entry version 60.
DE   SubName: Full=Predicted protein {ECO:0000313|EMBL:EFH40404.1};
GN   ORFNames=ARALYDRAFT_684754 {ECO:0000313|EMBL:EFH40404.1};
OS   Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN   [1] {ECO:0000313|Proteomes:UP000008694}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX   PubMed=21478890; DOI=10.1038/ng.807;
RA   Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA   Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA   Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA   Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA   Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA   Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT   "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT   change.";
RL   Nat. Genet. 43:476-481(2011).
CC   -!- SIMILARITY: Belongs to the peptidase S8 family.
CC       {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR   EMBL; GL348720; EFH40404.1; -; Genomic_DNA.
DR   RefSeq; XP_002864145.1; XM_002864099.1.
DR   AlphaFoldDB; D7MRL4; -.
DR   MEROPS; S08.A12; -.
DR   EnsemblPlants; Al_scaffold_0008_1574; Al_scaffold_0008_1574; Al_scaffold_0008_1574.
DR   Gramene; Al_scaffold_0008_1574; Al_scaffold_0008_1574; Al_scaffold_0008_1574.
DR   eggNOG; ENOG502QRA7; Eukaryota.
DR   HOGENOM; CLU_000625_4_3_1; -.
DR   Proteomes; UP000008694; Unassembled WGS sequence.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd02120; PA_subtilisin_like; 1.
DR   CDD; cd04852; Peptidases_S8_3; 1.
DR   Gene3D; 2.60.40.2310; -; 1.
DR   Gene3D; 3.50.30.30; -; 1.
DR   Gene3D; 3.30.70.80; Peptidase S8 propeptide/proteinase inhibitor I9; 1.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   InterPro; IPR034197; Peptidases_S8_3.
DR   InterPro; IPR010259; S8pro/Inhibitor_I9.
DR   InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR   InterPro; IPR045051; SBT.
DR   InterPro; IPR041469; Subtilisin-like_FN3.
DR   PANTHER; PTHR10795; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN; 1.
DR   PANTHER; PTHR10795:SF633; SUBTILISIN-LIKE PROTEASE SBT4.10-RELATED; 1.
DR   Pfam; PF17766; fn3_6; 1.
DR   Pfam; PF05922; Inhibitor_I9; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU01240};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000008694};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..714
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003103527"
FT   DOMAIN          30..108
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000259|Pfam:PF05922"
FT   DOMAIN          132..535
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   DOMAIN          607..708
FT                   /note="Subtilisin-like protease fibronectin type-III"
FT                   /evidence="ECO:0000259|Pfam:PF17766"
FT   ACT_SITE        140
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        195
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        495
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   714 AA;  76952 MW;  EFF7FF2429FDF183 CRC64;
     MAKRADIFCL LVLFLSSVSA IIDDSQNKQV YVVYMGSLPS QLEYTPMSHH MSILQEVTGE
     SSVEGRLVRS YKRSFNGFAA RLTDSERERV AEMEGVVSVF PNMNYKLQTT ASWDFLWLKE
     GKNTKRNLAI ESDIIIGVFD TGIWPESESF SDKGFGPPPK KWKGVCSGGK NFTCNNKLIG
     ARDYTREGAR DLQGHGTHTA STAAGNAVEN TSFYGIGNGT ARGGVPASRI AAYKVCSETD
     CTAASLLSAF DDAIADGVDL ISISLSGNNP QKYEKDPMAI GSFHANVKGI LTVNAAGNSG
     PVPASIESVA PWILSVAAST TNRGFFTKVV LGNGKTLVGR SVNSFDLKGK KYPLVYGDVF
     NESLVQGKIV VSRFTTSEVA VASIRRDGYE HYASISSKPF SVLPPDDFDS LVSYINSTRS
     PQGSVLKTEA FFNQTAPTVA SFSSRGPNII AVDLLKPDVS APGVEILAAY IPLISPSEEE
     SDKRRVKYSV LSGTSMACPH VAGVAAYIKT FHPEWSPSVI KSAIMTTAWP MNDNTTGFES
     TDVLASTEFA SGAGHVDPVA AINPGLVYEL DKSDHIAFLC GLNYTSKTLQ LIAGEAVTCS
     GKTLPRNLNY PSMSAKIYDS NSSFTVTFKR TVTNLGTPNS TYKSKIVLNR GAKLSVKVTP
     RVLSFKRVNE KQSFTVTVSG NNLNRKLPSS ANLIWSDGTH NVRSVIVVYI GDYS
//
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