ID A0A2I1GX85_9GLOM Unreviewed; 1555 AA.
AC A0A2I1GX85;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=RhiirA4_407281 {ECO:0000313|EMBL:PKY51237.1};
OS Rhizophagus irregularis.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC Glomeromycetes; Glomerales; Glomeraceae; Rhizophagus.
OX NCBI_TaxID=588596 {ECO:0000313|EMBL:PKY51237.1, ECO:0000313|Proteomes:UP000234323};
RN [1] {ECO:0000313|EMBL:PKY51237.1, ECO:0000313|Proteomes:UP000234323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A4 {ECO:0000313|EMBL:PKY51237.1,
RC ECO:0000313|Proteomes:UP000234323};
RA Ropars J., Sedzielewska K., Noel J., Charron P., Farinelli L., Marton T.,
RA Kruger M., Pelin A., Brachmann A., Corradi N.;
RT "Genome analyses suggest a sexual origin of heterokaryosis in a supposedly
RT ancient asexual fungus.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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: 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:PKY51237.1}.
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DR EMBL; LLXI01000983; PKY51237.1; -; Genomic_DNA.
DR VEuPathDB; FungiDB:FUN_000739; -.
DR VEuPathDB; FungiDB:GLOIN_2v1729848; -.
DR VEuPathDB; FungiDB:RhiirA1_424894; -.
DR OrthoDB; 1222064at2759; -.
DR Proteomes; UP000234323; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 8.
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; 1.20.120.1530; -; 5.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 1.10.8.500; HAMP domain in histidine kinase; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003660; HAMP_dom.
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; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF00672; HAMP; 5.
DR Pfam; PF18947; HAMP_2; 3.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 10.
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 SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 3.
DR PROSITE; PS50885; HAMP; 9.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000234323};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 232..284
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 324..376
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 416..468
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 508..560
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 600..652
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 692..744
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 784..836
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 876..928
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 968..1020
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 1042..1263
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1412..1530
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 115..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1461
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1555 AA; 169646 MW; 32C8D218B5894807 CRC64;
MTDVLGYVTD VLQNINDGNV EYCKTVRYQG QRNEQIEQFD SVLRKLLEKH IYLEEEVARY
QSLLNENDSV VIIKDSSLPA TNNEDCLQVK QSNETAILAP PSDKCQTNQI NSNHINNQIH
DSNSDSSPNT PPSLEHGDRV CLECLDQCTN VALAVTSGDF KKRVICPVAS GPMLTLRNAI
NTMVDKIDRV SIELIHVARE VGEEGKLGVQ SKSENLEGDF RDMMVHLNMM ASNHSKQVRD
IAEVCTAVAH GDLSKKITVE VKGETLVLKN TINTMVDQLN SFASEVTRVA HEVGTEGKLG
VQAQVQGVGG TWKLLTDNVN TMAANLTAQV RDIADVSKSV ARGDLSKKIT VDVKGEILDL
KNTINTMVDQ LQTFATEVTR VSLEVGTEGK LGGQANIKDV GGIWKDLTDN VNLMASNLTN
QVRDIATVCK AVACGDLSRK VTVPVQGEIL ELKVTINTMV EQLRMFAAEV TRVAREVGTE
GMLGGQAEVQ GVDGTWKILT DNVNTMAANL TAQVRDIANV SKAVARGDLS KKITVDVKGE
ILDLKNTINT MVDQLQTFAI EVTRVSLEVG TEGKLGGQAV VKDVGGTWKE LTDNVNIMAA
NLTTQVRSIA EVTTAVAKGD LSKKIIVDVK GEILDLKNTV NSMVEQLRTF AAEVTRVARE
VGTEGKLGGQ AVVKDVGGTW KELTDNVNTM AANLTAQVRD IANVSKAVAR GDLSKKITVD
VKGEIWDLKN TINTMVDQLQ TFATEVTRVS LEVGTEGKLG GQAVVKDVEG TWKVLTDNVN
IMAANLTTQV RSIAEVTTAV ACGDLSKKIS VDVKGEILEL KDTVNSMVDQ LRMFAAEVTR
VAREVGTEGI LGVQAHVKDV GGTWKELTDN VNTMASNLTA QVRDIANVCK SVACGDLSKK
ITVNVKGEIL DLKNTINTMV DQLSTFAAEV TRVAREVGTE GKLGVQAQVK DVKGTWKEIT
SNVNTMASNL TSQVRAFAQI SAAATDGDFT QYITVDASGE MDSLKTKINQ MVYNLRESIQ
KNTAAREAAE LANRSKSEFL ANMSHEIRTP MNGIIGMTTL TLETELTRQQ RENLMIVSTL
ANSLLTIIDD ILDISKIEAG RMTIEQIPFS LRSAVFGVLK TLAVKANQKK LDLIYDVDNG
IPDQLIGDPL RLRQVITNLI GNAIKFTTEG EVVLSVHTQL IEDDRVILEF CVSDTGIGIQ
EDKIDMIFDT FCQADGSTTR KYGGTGLGLS ISKRLVSLMG GDLWVKSVYG HGSEFYFTVK
VTLGTMSRET IEQKMNPWHG RHVLFIDTMH DKTGVVSIIE ELSLRPKIAC SVEEAALITA
SRKSDTPLFD TVIVDDLSIV ERLREITHLR YIPIVLLAPE IPNLNMKNCI DLGITSYSST
PSNLPDLMNA LLPALESHAA VPSDFARQQP LDILMAEDNI VNQKLAVKIL EKFGHRVEIV
SNGQLAVEAF KAKRYDLILM DVQMPIMGGF EATQKIREFE QETGGHVPII ALTAHAMIGD
REKCLFAGMD EYVTKPLRMN DLIATINKFP VKNPIEEISI PDGRNDTISA ISSKI
//
