ID A0A1S3V184_VIGRR Unreviewed; 999 AA.
AC A0A1S3V184;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=LOC106770782 {ECO:0000313|RefSeq:XP_014512070.1};
OS Vigna radiata var. radiata (Mung bean) (Phaseolus aureus).
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; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=3916 {ECO:0000313|Proteomes:UP000087766, ECO:0000313|RefSeq:XP_014512070.1};
RN [1] {ECO:0000313|RefSeq:XP_014512070.1}
RP IDENTIFICATION.
RC TISSUE=Leaf {ECO:0000313|RefSeq:XP_014512070.1};
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};
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00169}.
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DR RefSeq; XP_014512070.1; XM_014656584.2.
DR AlphaFoldDB; A0A1S3V184; -.
DR STRING; 3916.A0A1S3V184; -.
DR GeneID; 106770782; -.
DR KEGG; vra:106770782; -.
DR OrthoDB; 5476858at2759; -.
DR Proteomes; UP000087766; Chromosome 1.
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; -; 2.
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:SF51; HISTIDINE KINASE 4; 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; 2.
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; 2.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|RefSeq:XP_014512070.1};
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:UP000087766};
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 TRANSMEM 20..41
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 316..337
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 93..305
FT /note="CHASE"
FT /evidence="ECO:0000259|PROSITE:PS50839"
FT DOMAIN 373..663
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 688..818
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 843..979
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 893
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 999 AA; 111430 MW; 84DF4B8F55E78C88 CRC64;
MKSEQAGSNG KNTFIQAHRA WLPKLLMLWI LLMALIGWCI YTKMDADTKV RRKEVLGSLC
DQRARMLQDQ FSVSVNHVHA LAILVSTFHY YRTPSAIDQE TFAEYTARTA FERPLLSGVA
YAQRVVNSER ESFEKQHGWV IKTMERKPSQ VRDEYAPVIF AQETLSYLES LDMMSGEEDR
ENILRARATG KAVLTSPFKL LGSHHLGVVL TFPVYKSKLP TKPTMEERIK ATAGYVGGSF
DVESLVENLL GQLAGNQAIL VNVYDITNFT DPLIMYGKQD EEGDMSLVHE SKLDFGDPYR
KHKMICRYHQ KAPTNWIALT TAFLFFVILL LVGYILYSAG NRIVKVEDDF HKMAELKVRA
ESADIAKSQF LATVSHEIRT PMNGILGMLG LLLGTELSST QLDYAQTAQA CGMALIALIN
EVLDRAKIEA GKLELETVPF DIRSILDDVL SLFSEKSRHK GLELAVFVSD KVPDIVMGDP
GRFRQIVTNL VGNSVKFTER GHILVKVHLA ENRMSTMNGK METFLNGRSD EVVHVSSGGY
NFKTLSGHEA ADERNSWDNF KHLIADEEFF FDDSVKKVAS ESYEQVTLMV SVEDTGNGIP
FIAQDKIFMP FVQADSSTSR HYGGTGIGLS ISKCLVELMG GEISFISRPQ VGSTFSFTAD
FGTIKKNSIT DMKKHNLEDL RSSFRGFKAI VVDGKPVRAA VTRYHLKRLG IQAKVANSIN
KAVSLCGKNW SLTSGIFQPD MIFVEKDSWI CGEDGIFNVW QLDWKQNGHM FKIPQMILLA
TNITNTEFDK AKAAGFSDTV IMKPLRASMV AACLQQVLGT GKKRQLGKDT GSSFARSLLC
GKKILVVDDN RVNRRVAAGA LQNFGAHVTC AESGKIALEM LQLPHNFDAC FMDIQMPEMD
GFQATGKIRE MERKANELLM NGECGEGNGW KKEYHLPILA MTADVIQATY EKCVECGMDG
YVTKPFEEEN LYQAVAKFFN PKPTSDNSLQ NGNRTGKAP
//
