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
//