ID Q2HV70_MEDTR Unreviewed; 771 AA.
AC Q2HV70; A0A0C3W9M2; G7KQJ4;
DT 21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE SubName: Full=Proteinase inhibitor I9, subtilisin propeptide {ECO:0000313|EMBL:ABD28577.1};
DE SubName: Full=Subtilisin-like serine protease {ECO:0000313|EMBL:AES80322.2};
GN Name=11416905 {ECO:0000313|EnsemblPlants:AES80322};
GN OrderedLocusNames=MTR_7g079300 {ECO:0000313|EMBL:AES80322.2};
GN ORFNames=MtrDRAFT_AC148994g19v2 {ECO:0000313|EMBL:ABD28577.1};
OS Medicago truncatula (Barrel medic) (Medicago tribuloides).
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; Hologalegina; IRL clade; Trifolieae; Medicago.
OX NCBI_TaxID=3880 {ECO:0000313|EMBL:ABD28577.1};
RN [1] {ECO:0000313|EMBL:ABD28577.1}
RP NUCLEOTIDE SEQUENCE.
RA Town C.D.;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABD28577.1}
RP NUCLEOTIDE SEQUENCE.
RG The International Medicago Genome Annotation Group;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:AES80322.2, ECO:0000313|Proteomes:UP000002051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A17 {ECO:0000313|EMBL:AES80322.2}, and cv. Jemalong A17
RC {ECO:0000313|EnsemblPlants:AES80322,
RC ECO:0000313|Proteomes:UP000002051};
RX PubMed=22089132; DOI=10.1038/nature10625;
RA Young N.D., Debelle F., Oldroyd G.E., Geurts R., Cannon S.B., Udvardi M.K.,
RA Benedito V.A., Mayer K.F., Gouzy J., Schoof H., Van de Peer Y., Proost S.,
RA Cook D.R., Meyers B.C., Spannagl M., Cheung F., De Mita S.,
RA Krishnakumar V., Gundlach H., Zhou S., Mudge J., Bharti A.K., Murray J.D.,
RA Naoumkina M.A., Rosen B., Silverstein K.A., Tang H., Rombauts S.,
RA Zhao P.X., Zhou P., Barbe V., Bardou P., Bechner M., Bellec A., Berger A.,
RA Berges H., Bidwell S., Bisseling T., Choisne N., Couloux A., Denny R.,
RA Deshpande S., Dai X., Doyle J.J., Dudez A.M., Farmer A.D., Fouteau S.,
RA Franken C., Gibelin C., Gish J., Goldstein S., Gonzalez A.J., Green P.J.,
RA Hallab A., Hartog M., Hua A., Humphray S.J., Jeong D.H., Jing Y.,
RA Jocker A., Kenton S.M., Kim D.J., Klee K., Lai H., Lang C., Lin S.,
RA Macmil S.L., Magdelenat G., Matthews L., McCorrison J., Monaghan E.L.,
RA Mun J.H., Najar F.Z., Nicholson C., Noirot C., O'Bleness M., Paule C.R.,
RA Poulain J., Prion F., Qin B., Qu C., Retzel E.F., Riddle C., Sallet E.,
RA Samain S., Samson N., Sanders I., Saurat O., Scarpelli C., Schiex T.,
RA Segurens B., Severin A.J., Sherrier D.J., Shi R., Sims S., Singer S.R.,
RA Sinharoy S., Sterck L., Viollet A., Wang B.B., Wang K., Wang M., Wang X.,
RA Warfsmann J., Weissenbach J., White D.D., White J.D., Wiley G.B.,
RA Wincker P., Xing Y., Yang L., Yao Z., Ying F., Zhai J., Zhou L., Zuber A.,
RA Denarie J., Dixon R.A., May G.D., Schwartz D.C., Rogers J., Quetier F.,
RA Town C.D., Roe B.A.;
RT "The Medicago genome provides insight into the evolution of rhizobial
RT symbioses.";
RL Nature 480:520-524(2011).
RN [4] {ECO:0000313|EMBL:AES80322.2, ECO:0000313|Proteomes:UP000002051}
RP GENOME REANNOTATION.
RC STRAIN=cv. Jemalong A17 {ECO:0000313|EnsemblPlants:AES80322,
RC ECO:0000313|Proteomes:UP000002051};
RX PubMed=24767513; DOI=10.1186/1471-2164-15-312;
RA Tang H., Krishnakumar V., Bidwell S., Rosen B., Chan A., Zhou S.,
RA Gentzbittel L., Childs K.L., Yandell M., Gundlach H., Mayer K.F.,
RA Schwartz D.C., Town C.D.;
RT "An improved genome release (version Mt4.0) for the model legume Medicago
RT truncatula.";
RL BMC Genomics 15:312-312(2014).
RN [5] {ECO:0000313|EnsemblPlants:AES80322}
RP IDENTIFICATION.
RC STRAIN=cv. Jemalong A17 {ECO:0000313|EnsemblPlants:AES80322};
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR EMBL; AC148994; ABD28577.1; -; Genomic_DNA.
DR EMBL; CM001223; AES80322.2; -; Genomic_DNA.
DR RefSeq; XP_003624104.2; XM_003624056.2.
DR AlphaFoldDB; Q2HV70; -.
DR STRING; 3880.Q2HV70; -.
DR MEROPS; S08.150; -.
DR PaxDb; 3880-AES80322; -.
DR EnsemblPlants; AES80322; AES80322; MTR_7g079300.
DR GeneID; 11416905; -.
DR Gramene; AES80322; AES80322; MTR_7g079300.
DR KEGG; mtr:11416905; -.
DR eggNOG; ENOG502QT5U; Eukaryota.
DR HOGENOM; CLU_000625_4_6_1; -.
DR OrthoDB; 11910at2759; -.
DR Proteomes; UP000002051; Chromosome 7.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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:SF514; SUBTILISIN-LIKE PROTEASE; 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:UP000002051};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..771
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014586153"
FT DOMAIN 29..119
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 145..590
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 664..765
FT /note="Subtilisin-like protease fibronectin type-III"
FT /evidence="ECO:0000259|Pfam:PF17766"
FT ACT_SITE 154
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 226
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 551
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 771 AA; 84214 MW; E2D5C1AB8BC3866F CRC64;
MEPNFMFSLL LIISLWLLLT FHSNAETSTY IIHMNKSFFP QVFTNHHDWF KSTIHSLKSK
TLVLDDHDQQ EEASMQSQKQ LVYTYDNAMY GFSALLSSNE LETLNNTDGF VAAYQDRTAT
MDTTHTFEFL SLDSPSGLWH ASNFGDDIII GVIDSGVWPE SQSFKDDGMT KKIPNKWKGT
CETGHKFNAS MCNFKLIGAR SFNKGVIASN PNVRIRMNSA RDSIGHGTHT SSTVAGNYVN
GTSYFGYAKG VARGIAPRAR LAMYKVIWEE GLLASDVLAG MDQAIADGVD VISISMGFDG
VPLYEDAIAI ASFAAMEKGI VVSSSAGNSG PKHGTLHNGI PWVLTVAAGT IDRTFGSLVL
GNGQNIIGWT LFASNSTIVE NLPLVYDNTL SSCNSVKRLS QVNKQVIIIC DSISNSSSVF
DQIDVVTQTN MLGAVFLSDS PELIDLRHIY APGIVIKTKD AESVIKYAKR NKNNPTASIK
FQQTFLGIKP APIAAHYSSR GPSHGFPWIL KPDIMAPGSR VLAAFVPYKP TARIGTDVFL
SSDYNFMSGT SMACPHASGV AALLKAVHPQ WSSAAIRSAL ITTANPLDNT KNLIRDNGYP
SQYASPLAIG AGEIDPNRAM NPGLIYDATP QDYVNFLCGL KFTKNQILTI TRSSSYGCEN
PSLDLNYPSF IAFYNKKTRS MVHTFNRTVT NVGDGAATYS ANVTHPKGCV MTVLPDILTF
KYRNEKQSYS LVIKCVMYKK DNVSFGDLVW IEYGGAHTVR SPIVVAPRGI I
//