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Database: UniProt
Entry: A0A5J9TXV3_9POAL
LinkDB: A0A5J9TXV3_9POAL
Original site: A0A5J9TXV3_9POAL 
ID   A0A5J9TXV3_9POAL        Unreviewed;      1753 AA.
AC   A0A5J9TXV3;
DT   11-DEC-2019, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2019, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
DE   Flags: Fragment;
GN   ORFNames=EJB05_39784 {ECO:0000313|EMBL:TVU16232.1};
OS   Eragrostis curvula (weeping love grass).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Chloridoideae; Eragrostideae; Eragrostidinae; Eragrostis.
OX   NCBI_TaxID=38414 {ECO:0000313|EMBL:TVU16232.1, ECO:0000313|Proteomes:UP000324897};
RN   [1] {ECO:0000313|EMBL:TVU16232.1, ECO:0000313|Proteomes:UP000324897}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Victoria {ECO:0000313|Proteomes:UP000324897};
RC   TISSUE=Leaf {ECO:0000313|EMBL:TVU16232.1};
RX   PubMed=31308395; DOI=.1038/s41598-019-46610-0;
RA   Carballo J., Santos B.A.C.M., Zappacosta D., Garbus I., Selva J.P.,
RA   Gallo C.A., Diaz A., Albertini E., Caccamo M., Echenique V.;
RT   "A high-quality genome of Eragrostis curvula grass provides insights into
RT   Poaceae evolution and supports new strategies to enhance forage quality.";
RL   Sci. Rep. 9:10250-10250(2019).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001433};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|RuleBase:RU004432}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:TVU16232.1}.
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DR   EMBL; RWGY01000031; TVU16232.1; -; Genomic_DNA.
DR   Proteomes; UP000324897; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0048544; P:recognition of pollen; IEA:InterPro.
DR   GO; GO:0051707; P:response to other organism; IEA:UniProt.
DR   CDD; cd00009; AAA; 1.
DR   CDD; cd00028; B_lectin; 1.
DR   CDD; cd01098; PAN_AP_plant; 1.
DR   CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR   Gene3D; 1.10.8.60; -; 2.
DR   Gene3D; 2.90.10.10; Bulb-type lectin domain; 1.
DR   Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   Gene3D; 4.10.860.10; UVR domain; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR001480; Bulb-type_lectin_dom.
DR   InterPro; IPR036426; Bulb-type_lectin_dom_sf.
DR   InterPro; IPR019489; Clp_ATPase_C.
DR   InterPro; IPR036628; Clp_N_dom_sf.
DR   InterPro; IPR004176; Clp_R_dom.
DR   InterPro; IPR001270; ClpA/B.
DR   InterPro; IPR018368; ClpA/B_CS1.
DR   InterPro; IPR028299; ClpA/B_CS2.
DR   InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR003609; Pan_app.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR000858; S_locus_glycoprot_dom.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR   PANTHER; PTHR11638:SF155; CLP PROTEASE ATP-BINDING SUBUNIT; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF07724; AAA_2; 1.
DR   Pfam; PF17871; AAA_lid_9; 1.
DR   Pfam; PF01453; B_lectin; 1.
DR   Pfam; PF02861; Clp_N; 2.
DR   Pfam; PF10431; ClpB_D2-small; 1.
DR   Pfam; PF08276; PAN_2; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF00954; S_locus_glycop; 1.
DR   PRINTS; PR00300; CLPPROTEASEA.
DR   SMART; SM00382; AAA; 2.
DR   SMART; SM00108; B_lectin; 1.
DR   SMART; SM01086; ClpB_D2-small; 1.
DR   SMART; SM00473; PAN_AP; 1.
DR   SUPFAM; SSF51110; alpha-D-mannose-specific plant lectins; 1.
DR   SUPFAM; SSF81923; Double Clp-N motif; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50927; BULB_LECTIN; 1.
DR   PROSITE; PS51903; CLP_R; 1.
DR   PROSITE; PS00870; CLPAB_1; 1.
DR   PROSITE; PS00871; CLPAB_2; 1.
DR   PROSITE; PS50948; PAN; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU004432};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000324897};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..1753
FT                   /note="non-specific serine/threonine protein kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5023911432"
FT   DOMAIN          28..148
FT                   /note="Bulb-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50927"
FT   DOMAIN          341..424
FT                   /note="Apple"
FT                   /evidence="ECO:0000259|PROSITE:PS50948"
FT   DOMAIN          925..1068
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   REGION          426..445
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          698..728
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        428..442
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        714..728
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         544
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:TVU16232.1"
SQ   SEQUENCE   1753 AA;  194736 MW;  4E63FF8AD25DC805 CRC64;
     MDSNRSKNHL NLLLSFVLLL SPRSTLAVDT FSKGRNITDN NTTLVSADGA FTMGFFSPGV
     STKRYLGIWF TVSRDAVCWV ANGDHPINDN SGVLFVSDTE NLLLLDGTGQ VAWSSNSAST
     SPVEAQLLNS GDLVVRNQGS TDALWHSFNF PQNVFLSGMK VGKDFFSGAE WYLTSWRSPD
     DPSPGAYTRR LDIAGLPDNI VWQGNVKTFR SDPWNGVKFG GIPEVRSYMG GLFDYQMVIS
     SREITYGYQV RPGATYTYIM LRDDGKARRL AWDASSRTWQ EYYRGPRDVC DDYGKCGAFG
     VCNISAAETL YCSCLTGYSP ASPLVWPRIT SDGCRRNVKR CGQTSDGFWP VRSVKLPDTH
     NATVDTNITV DGCRARCLSD CSCLAYAAAE VRAGGNFSGC VMWSDDLIDL RYIDSGQDLY
     LRLTESELPP ASPPPPSPPP SAKSLSTATV ASASVASIVG ITLIALLILC VIKRRRRSAS
     SSSRRPPTAV HSVELTVPPP VPFAELSSLK EATGDFSESN IIGRGGFGIV YEGHFPDGRK
     VAVKRLNQSS PDDERGDDFM REVEVMSKLR GYTAPEYIME CRLLTLKCDV YSFGVILLEV
     VSGKRNWNTP TLLPDAWESW NQHKINELLD SAVTQPEPEL LLELEKCVQV GLLCVQQSAD
     DRPTMSAVVT MLNNTSLIHR PKKPVLFDSR NGSPLREAAD LTVEEASGRS RDSQTLGQER
     ENISHGDHQP RLLNDFLLDR SWYADMFPYE STSMQPRRGD VRVRRAKAGA PLSRLLHTDA
     GVVQRLVWGA DMHTRVAHLL PGPQGRRQRL RKCGAFGVHV VLRLRQGVRP RVPRGVEDEM
     REASDDDDGW VPAAARGEAP QHEQRGLRET EALDCLWLAQ HGGGSSSVCN RSNRIQKQFW
     SFPCTRKGQD KCYHGAQHAN TDTYSRRFPR VAADKFSGHK EEARRLGHNF VGTEQILLGL
     IGEGTGIAAK VLKSMGINLK DARVEVEKII GRGSGFVAVE IPFTPRAKRV LELSLEEARQ
     LGHNYIGSEH LLLGLLREGE GVAARVLESL GADPNNIRGG TSGQKMPTLE EYGTNLTKLA
     EEGKLDPVVG RQDQIERVTQ ILGRRTKNNP CLIGEPGVGK TAIAEGLAQR IANGDVPETI
     EGKKVITLDM GLLVAGTKYR GEFEERLKKL MEEIKQNEDI ILFIDEVHTL IGAGAAEGAI
     DAANILKPAL ARGELQCIGA TTLDEYRKHI EKDPALERRF QPVKVPEPTV DESIQILRGL
     RERYELHHKL RYTDDALIAA AQLSYQYISD RFLPDKAIDL IDEAGSRVRL RHAQLPDEAK
     ELDKELRQIT KQKNEAVRGQ DFEKVCPNFK VYEKCSEFWT KAGELRDREM ELKAQITAII
     DKSKEMIKAE TESGEVGPLV TEADIQHIVS SWTGIPVEKV SSDESDRLLK MEETLHTRII
     GQDEAVKAIS RAIRRARVGL KNPNRPIASF IFSGPTGVGK SELAKALASY YFGSEEAMIR
     LDMSEFMERH TVSKLIGSPP GYVGYTEGGQ LTEAVRRRPY TVVLFDEIEK AHPDVFNMML
     QILEDGRLTD SKGRTVDFKN TLLIMTSNVG SSVIEKGGRK IGFDLDYDEK DTSYNRIKSL
     VTEELKQYFR PEFLNRLDEM IVFRQLTKLE VKEIADIMLK EVFDRLKAKE IDLQVTERFR
     DRVVDEGYNP SYGARPLRRA IMRLLEDSLA EKILAGEVKE GDSAIVDVDS EGKVIVLNGG
     SGVAEPLEPA LSI
//
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