ID A0A1S2Y3M1_CICAR Unreviewed; 1031 AA.
AC A0A1S2Y3M1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Histidine kinase 5 {ECO:0000313|RefSeq:XP_004498825.1};
GN Name=LOC101512841 {ECO:0000313|RefSeq:XP_004498825.1};
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_004498825.1};
RN [1] {ECO:0000313|RefSeq:XP_004498825.1}
RP IDENTIFICATION.
RC TISSUE=Etiolated seedlings {ECO:0000313|RefSeq:XP_004498825.1};
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_004498825.1; XM_004498768.3.
DR AlphaFoldDB; A0A1S2Y3M1; -.
DR STRING; 3827.A0A1S2Y3M1; -.
DR PaxDb; 3827-XP_004498825-1; -.
DR GeneID; 101512841; -.
DR KEGG; cam:101512841; -.
DR eggNOG; KOG0519; Eukaryota.
DR OrthoDB; 5476858at2759; -.
DR Proteomes; UP000087171; Chromosome Ca4.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
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; PTHR43047:SF58; HISTIDINE KINASE CYTOKININ RECEPTOR; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
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; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|RefSeq:XP_004498825.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
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 Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 382..687
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 888..1030
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 822..855
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 93..120
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 185..212
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 839..855
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 937
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1031 AA; 116434 MW; FC07B644F3CA7307 CRC64;
MVCEMESDCI EDMMDIEILS SMWPDDVGTD VGKQFNIEKP GRDQDMLKEV TILEEPTIAD
FQRLMELTNY TDKGSSQLAY LMKHWEYKQA NAVRLLREEL DNLSKQRKEV ELRKLEILKD
SNRFEEESYG GDKRPVSILD DVYYTWQDLP VAIRKSDIVV QSKRIEIEAE YDTVIYWKQQ
AVDLERRLEA SIRREQTLME KLQESIETIE RQSSPVEELS QILKRADNFL HFILQNAPVV
IGHQDKELRY RFIYNHFPSL QEEDIIGKTD VEIFTGSGVK ESQDFKREVM EKGLPAKKEI
TFETELFGSK TFLIYVEPVF SKAGETIGVN YMGMEITDQV RKREKMAKLR EEIAVQKAKE
TELNKTIHIT EETMRAKQML ATMSHEIRSP LSGVVSMAEI LTTTKLDKEQ RQLLDVMISS
GDLVLQLIND ILDLSKVESG AMKLEATKFR PREVVRHVLQ TAAASLQKML TLEGNVADDI
PIEVTGDVLR IRQILTNLIS NAVKFTHQGK VGINLYVVPE PQFAKEEECH QKVTEDQSTI
SANGLKEEKH ISSPRSRCDQ NLIDDKKQHD DHPIQNHALS NECRSSFNSE CSMNDDDVTD
EQTHSTETTV WIRCDVYDTG IGIPEKAIPT LFRRYMQVSA DHARKYGGTG LGLAICKQLV
ELMGGRLTVT SKENCGSTFT FILPYKVSTA CDNSDDPDEL SYVNDNEDDT TEGFFQFQPR
TLGSLFTSNG STRPQNILPG YRIAHKFNGF PDNPYSNLSS NIISNGTNSL EDASSVIVDA
LDMPESTSSS SCSPETKHES LVNGNKENRD FKAHAMLQNC SANGNSSQYK EESREMNLAR
TSSEPQQTCQ GQGKEESTSQ CVISSSCSTS STITSSSSEV TESTLKPNIL LVEDNKINIM
VTKSMMKQLG YSMDVVNNGV EAIRAVQNHS YDIILMDVFM PVMNGLQTTK LIRCYEETGS
WDAAKEAGIE QSLLASDECS IPPKKRIHIV AMTANTMSES AEECFANGMD SFVSKPVSFQ
KLRDCVEQYL K
//
