ID A0A167DGD0_9HYPO Unreviewed; 1401 AA.
AC A0A167DGD0;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 28-JUN-2023, entry version 35.
DE SubName: Full=ATPase-like, ATP-binding domain protein {ECO:0000313|EMBL:OAA42359.1};
GN ORFNames=BBO_05022 {ECO:0000313|EMBL:OAA42359.1};
OS Beauveria brongniartii RCEF 3172.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria;
OC Beauveria brongniartii.
OX NCBI_TaxID=1081107 {ECO:0000313|EMBL:OAA42359.1, ECO:0000313|Proteomes:UP000076863};
RN [1] {ECO:0000313|EMBL:OAA42359.1, ECO:0000313|Proteomes:UP000076863}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 3172 {ECO:0000313|EMBL:OAA42359.1,
RC ECO:0000313|Proteomes:UP000076863};
RX PubMed=27071652; DOI=10.1093/gbe/evw082;
RA Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT "Divergent and convergent evolution of fungal pathogenicity.";
RL Genome Biol. Evol. 8:1374-1387(2016).
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:OAA42359.1}.
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DR EMBL; AZHA01000014; OAA42359.1; -; Genomic_DNA.
DR OrthoDB; 1770905at2759; -.
DR Proteomes; UP000076863; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0009881; F:photoreceptor activity; IEA:UniProtKB-KW.
DR GO; GO:0009584; P:detection of visible light; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.270; -; 1.
DR Gene3D; 3.30.450.40; -; 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; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013654; PAS_2.
DR InterPro; IPR016132; Phyto_chromo_attachment.
DR InterPro; IPR001294; Phytochrome.
DR InterPro; IPR013515; Phytochrome_cen-reg.
DR InterPro; IPR043150; Phytochrome_PHY_sf.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08446; PAS_2; 1.
DR Pfam; PF00360; PHY; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR01033; PHYTOCHROME.
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; SSF55781; GAF domain-like; 2.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50046; PHYTOCHROME_2; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000313|EMBL:OAA42359.1};
KW Chromophore {ECO:0000256|ARBA:ARBA00022991};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Photoreceptor protein {ECO:0000256|ARBA:ARBA00022543};
KW Receptor {ECO:0000256|ARBA:ARBA00022543};
KW Sensory transduction {ECO:0000256|ARBA:ARBA00022606};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 434..596
FT /note="Phytochrome chromophore attachment site"
FT /evidence="ECO:0000259|PROSITE:PS50046"
FT DOMAIN 810..1043
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1237..1368
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 79..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 363..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 985..1004
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1044..1117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1149..1229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..122
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1044..1062
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1082..1111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1149..1188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1200..1221
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1288
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1401 AA; 154344 MW; 7968433534CD5DAE CRC64;
MSSPQPHRPD ESQSQTATHN HPQRPCRPSS PTRDASHPPS DVSRDSATSP SVASESYISY
PSAVTEVSDL VFPIRSVVSV DKSSSRSDID DHASRTSNPG SMGTPVAQST PSRTITVDTG
PSSVPPSPSP MSPVGRGRSR ASVELNSSTH TDTTRFASLS TPIELDIAAS DAGSDAESGV
LGRPGLQAQT ELSSHISEAQ SSFDVPLVTT RFTHVETQEG HAIITGRDGV LQQCEDEPIH
SPGAVQSFGC LLAMQEETDG NFIVRYVSEN CKRFLGYSPR SLFRLTNFLD LLTDDQQDNL
LDHVDFIKDE DADPAINGPE ILSISIRHPK IGRSVKLWCA IHINAAHPDL IICEFELDDD
LDNPLRPPNE HTPDAPTDTL ESTPSKQALL EAAEIISKPL RILRSARKRR GEQGAMQVFD
ILSQVQEQLA SAPSLEVFLK ILVGIVKELT GFHRIMIYQF DSTFNGKVVT ELVDTSHTLD
LYKGLHFPAS DIPRQARELY KVNKVRLLYD RDQPTARIVC RSQQDLEVPL DMTHAYLRAM
SPIHVKYLGN MEVRSSMSIS INAFSELWGL IACHSYGERG MRVSFPVRKL CRLVGETASR
NIERLSYASR LQARKLINTS PTNKNPSGYI VASSDDLLSL FDAECGLLSI KDETKVMGNL
EHSQEALALL EYLRMRKLTS VLASQDVRLD FPDLRYPPGF HHIAGFLYVP LSVGGHDFIV
FFRKGQVKEV QWAGNPYEKN IRKGTAAYLE PRASFKVWNE TVIGKCREWD EEQVETASVL
CLVYGKFIEI WRQKEAAIQN TKLTRLLLAN SAHEVRTPLN AIINYLEIAL EGSLDSETRE
NLVRSHSASK SLIYVINDLL DLTKAEEGQN LIKDEVFDLR TCIEEATDPF KIDANRKGLC
YEVSQHDGLP KFVHGDTRQV RQALSNVTAN AVKHTQEGSV KISIQVTDLE EKQATIEFEV
IDTGSGMTSR QIDALFQDLE QVSATLSDSG DSPDPTYNSG SSRTLGLGLA VVGRTVRNMN
GQLRLTSEVG KGSRFTIQIP FQLPDSEIDS SEPGVSSGHN VRRASQRESK RPEGEITLVQ
RGSGSKVPTL RETSIGSDDC RSGSQRSRGS YESVKSDTDR LIDAIQTPLI GENKDTEYFT
LGRLSKGSTN LSTSLSGLSA GPASPKLTKQ GDLMSTSHTE SGSVSVKDSK TPIKAVKIPD
ESSSKTHTTR QDEKPVENRS QLGRPRNDSV AQEIPLRALI AEDDPINLKI VRKRLERAGH
MVTHAVNGED CAALFKSCAS TVDVIFMDMQ MPIVDGLTST KMIRSMEQEY QIEGHSDVAK
RNGRVPIIAV SASLVEGQRQ TYIDAGFDAW ILKPIDFKRL SVLMGGIHND LARNASVYVP
GQWEAGGWFS ARLPEEAHSS S
//
