ID A0A1S2YGC9_CICAR Unreviewed; 1007 AA.
AC A0A1S2YGC9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 2.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=LOC101506212 {ECO:0000313|RefSeq:XP_004504407.3};
OS Cicer arietinum (Chickpea) (Garbanzo).
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; Cicereae; Cicer.
OX NCBI_TaxID=3827 {ECO:0000313|Proteomes:UP000087171, ECO:0000313|RefSeq:XP_004504407.3};
RN [1] {ECO:0000313|RefSeq:XP_004504407.3}
RP IDENTIFICATION.
RC TISSUE=Etiolated seedlings {ECO:0000313|RefSeq:XP_004504407.3};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
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DR RefSeq; XP_004504407.3; XM_004504350.3.
DR STRING; 3827.A0A1S2YGC9; -.
DR PaxDb; 3827-XP_004504407-1; -.
DR KEGG; cam:101506212; -.
DR eggNOG; KOG0519; Eukaryota.
DR OrthoDB; 5476858at2759; -.
DR Proteomes; UP000087171; Chromosome Ca6.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 6.10.250.1190; -; 1.
DR Gene3D; 3.30.450.350; CHASE domain; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR006189; CHASE_dom.
DR InterPro; IPR042240; CHASE_sf.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43719:SF73; HISTIDINE KINASE 3; 1.
DR PANTHER; PTHR43719; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF03924; CHASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM01079; CHASE; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50839; CHASE; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|RefSeq:XP_004504407.3};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000087171};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..1007
FT /note="histidine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018683053"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 371..393
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 135..362
FT /note="CHASE"
FT /evidence="ECO:0000259|PROSITE:PS50839"
FT DOMAIN 430..698
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 872..1004
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 922
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1007 AA; 113016 MW; 291818AC8912413F CRC64;
MLCFWLVSFF YLNSEVLKET KMGFLGNGSK MWLKCWEKIS VHGYKIHQQY YLYIGSKKVK
RELWRKLLLT WVLGWIVVSL WIFCCMRLQV VEKRKETLAS LCDERARIVQ DQFNVSMNHI
QAMSILISSF HHAKSPSAID QRTFARYTER TAFERPLTSG VAYAVRVLHS EREQFEKQQG
WIIKRMDTLE QNPVHKDDYA TEALEQSFIQ EEYAPVIFAQ DTISHVISVD VLSGKEDRDN
VLRARESGKG VLTEPFRLLK SNRLGVILTF AVYKRYLPSN ATPNERIQAT NGYLGGVFDV
ESLVEKLLQQ LASKQSVIVN VYDTTNHTHP IVMYGSTNVS GDVFCHVSTL NFGDPFRKHE
MHCRFKQKPP WPWLAITTSI GILVIALLVG HIFHATVNRI AKVEDDCREM TELKKRAEAA
DVAKSQFLAT VSHEIRTPMN GVLGMLHMLM DTDLDVTQQE YVRTAQESGK ALVSLINEVL
DQAKIEFGKL ELEAVLFDIR SILDDVLSLF SDKSQGKGVE LAAYVSDHVP ELLIGDPGRF
RQIITNLMGN SIKFTDKGHI FVTIHLVEEI VHSIEVDNES NPENTLSGFA VTNSCLSWKG
FKAFSQEGPL GSFSSSSTDL INLIVSVEDT GEGIPREAQS LIFTPFMQVG SSISRKHGGT
GIGLSISKCL VGLMNGEIGF ASEPKIGSTF TFTSVFTNGL LSSNECRIQQ INRSQPASSE
FEGMNALVID PRPVRAKVSR YHXXXXXXXX XMVSDLNQGL STIKNGNAVI NMVLIEQEVW
YRDSSMSSHF FNNTRKIDRG FPPKLFILVN SSCSSKTSSV ISDVHNPTII TKPLRASMLA
VSLERAMNVG NKRIPNRDVQ SLSLSHLLFG RKILIVDDNG VNRAVAAGAL KKYGADVVCV
SSGKDAISSL KPPHQFDACF MDIQMPEMDG FEATNIIREM EHNVNREVSN DGFENTSNWH
VPILAMTADV IQATHEKCLR CGMDGYVSKP FEAEQLYREV SWFFSSS
//
