ID A0A316UA52_9BASI Unreviewed; 1428 AA.
AC A0A316UA52;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=BCV69DRAFT_152360 {ECO:0000313|EMBL:PWN21694.1};
OS Pseudomicrostroma glucosiphilum.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Exobasidiomycetes; Microstromatales; Microstromatales incertae sedis;
OC Pseudomicrostroma.
OX NCBI_TaxID=1684307 {ECO:0000313|EMBL:PWN21694.1, ECO:0000313|Proteomes:UP000245942};
RN [1] {ECO:0000313|EMBL:PWN21694.1, ECO:0000313|Proteomes:UP000245942}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 4718 {ECO:0000313|EMBL:PWN21694.1,
RC ECO:0000313|Proteomes:UP000245942};
RX PubMed=29771364; DOI=10.1093/molbev/msy072;
RA Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA Spatafora J.W., Aime M.C.;
RT "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT clade Ustilaginomycotina.";
RL Mol. Biol. Evol. 0:0-0(2018).
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 EMBL; KZ819324; PWN21694.1; -; Genomic_DNA.
DR STRING; 1684307.A0A316UA52; -.
DR OrthoDB; 1222064at2759; -.
DR Proteomes; UP000245942; 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; 5.
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; -; 3.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 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; 3.
DR Pfam; PF18947; HAMP_2; 2.
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; 7.
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; 2.
DR PROSITE; PS50885; HAMP; 7.
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:UP000245942};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 291..344
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 384..436
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 476..528
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 568..620
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 660..712
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 752..804
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 844..896
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 918..1141
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1286..1405
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 71..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 183..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1335
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1428 AA; 154642 MW; 0D6AB0B84FADC4DD CRC64;
MAAATAATLG APSNGRDQSL LSSSISSVSS GSSSSTLSRT TRSPLPDLAS LPTNFIDHLL
LITQTLVHST PPPSLKSTYA AESSSSDYNG STSATNGHDR SNSAVSASSV SSTSSSSTAL
PSHPSGAANA SQGSSEATVT LPLPRFHYEG GDKRTDQIEA DIGRLVERLW RSENQLQAIA
RADPAAYERS LSPSSGVLPS SPASRSPILQ GSSAVSVKDT SRRASLTSFP YPISQDHPQS
SSYPLSYPLA MGTDGPMILT PEQPDAGPES VIRAIERNAE ETGLSAEEEL RLLKAQVQDI
ARVCKAVAFG DLSQHILVPV QGPVMVELKD IINQMVDRLS NFATEVTRVS LEVGTEGKLG
GQVEVEGVEG RWKELKDVVN RLAANLTSQV RGVALVTKAV ARGDLSKKID VEADGEVLDL
KLTINVMVDQ LRKFADEVTR VSREVGSRGQ LGGQANVPGV QGVWEELTIN VNRMCLNLTE
QVRGVALVTT AVAKGDLTKT IDIEAEGEMA ELKDTVNRMV HQLRIFASEV VRMSMEVGTY
GKLGGQAHVP NVEGTWKDLT ENVNKMADNL TSQVREIARV TKCVAEGVLT EFIEVDVKGE
ILELKLTVNN MVRQLRCLSD EIIRVSVEVG TQGKLGGQAN VEDVKGQWQV LTEQVNMMAS
NLTTQVRSIA TVTTAVAKGD LSKTINVEVS GEFLDLKLTV NNMVESLRTF STEVTRVAKE
VGTEGKLGGR ATVLNVGGTW KDLTDSVNTM AANLTLQVRT IAHATTAVAR GDLSQKVTIE
VRGEILDLVD TINNMIDQLS FFASEVTRVA REVGTEGKLG TQAQKKDIRG KWGEITDNVN
IMANNLTSQV RAFAQITAAA TDGDFSRFVT VEASGEMDSL KTKINQMVYS LRDSIQKNTA
AREAAELANR SKSEFLANMS HEIRTPMNGI IGMTALTLET ELSRSQRENL VTVSSLASNL
LAIIDDILDI SKIEAGRMNV EEVPYSLRGI VFSVLKTLSV RATQKKLNLM YEVAPDVPDP
LVGDALRLKQ IITNLIGNAV KFTDAGGRVA LKCTLAKMIS PSEAMLEFCA SDSGIGIKQD
KLDVIFDTFC QADGSTTRKY GGTGLGLSIS RRLVNLMGGD LWVRSNFGHG SDFFFTMVVK
IDDLGKDQVL DKMQTFAGRN IFYLDTLRDS TGVEKMLIEL GLQPFTVHSI EEAFQKSKAM
PRIDAIIADS LTVVEDLRTV EHLRYIPINL VSPSMLTLNL TYCLDHGISS YINTPTTPAD
LSYALWASLE SSAAIISEGN KEEVYDILLC EDNRVNIVIA RRMLEREGHK VQTVSDGKQA
VEAVMARRYD VVLMDVSMPV MSGIEATKSI RIFEEETKAG RTPIIALTAH AMKGDKERCL
ASGMDDYCSK PLRKLDLLTA IRQATMNRRK GGGDGRVVVY PRPQPMVQ
//
