ID A0A074X7T8_9PEZI Unreviewed; 1207 AA.
AC A0A074X7T8;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KEQ70661.1};
GN ORFNames=M436DRAFT_52873 {ECO:0000313|EMBL:KEQ70661.1};
OS Aureobasidium namibiae CBS 147.97.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043004 {ECO:0000313|EMBL:KEQ70661.1, ECO:0000313|Proteomes:UP000027730};
RN [1] {ECO:0000313|EMBL:KEQ70661.1, ECO:0000313|Proteomes:UP000027730}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 147.97 {ECO:0000313|EMBL:KEQ70661.1,
RC ECO:0000313|Proteomes:UP000027730};
RX PubMed=24984952;
RA Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT "Genome sequencing of four Aureobasidium pullulans varieties:
RT biotechnological potential, stress tolerance, and description of new
RT species.";
RL BMC Genomics 15:549-549(2014).
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DR EMBL; KL584716; KEQ70661.1; -; Genomic_DNA.
DR RefSeq; XP_013424823.1; XM_013569369.1.
DR AlphaFoldDB; A0A074X7T8; -.
DR STRING; 1043004.A0A074X7T8; -.
DR GeneID; 25411670; -.
DR HOGENOM; CLU_002763_0_0_1; -.
DR OrthoDB; 12386at2759; -.
DR Proteomes; UP000027730; 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 CDD; cd00082; HisKA; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal 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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43719:SF11; HISTIDINE KINASE/RESPONSE REGULATOR, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR43719; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF01590; GAF; 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; SSF55781; GAF domain-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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000027730};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 540..818
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1073..1201
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 266..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 342..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 416..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..284
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1130
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1207 AA; 133197 MW; 0302F936EDC5035A CRC64;
MAPKQAKQHK ARERALTLQE REMHRFYQPW LDAQGTSANV AEHVQDLAAV DDFAINTLSE
QGFRPLASRD TTLTAFAQLA ALRLNVRRAM VSLIDSKHQY VLAEATRTLS LVDDTRHAEG
DALWLGTTSL AREDAVCQCA FTRQYTVEDE NGHAVTSIAA VMPDCRLDDD FKDKPYVLSE
PGVRFYAGVP IRSRSGHNIG VYAVSHDEPR EPLTYDELRF MQDIAVTVMN HLEWARDRVD
RYKGERIVRG MADFIEGAPS VRAMSKEMDN TDQPATTANG SAPASQPREA KADNLSKLLD
RASRILREST LAEGVVFFGP SSGSGHAKAS LRSVMAARDK LSGTDDESAR HLSVDSVDVE
NSTDSDANHI HASKILGLSL ANKKDSSLFH DTTLDVLTLE NYFKLYPNGK SLHFSEAGSG
LSSEDDSASE SQKSAGEEPK AAPETASQKV IGKKKKMRMS HQILLKNLPG VKNVIFLPLW
DYIEEKMVAG CFLWTSSTGR MMNLDDDLSY LRAFGNTIMS EVSRMNALKD DRAKTTFIAS
MSHELRSPLH GILGSVEFLQ ETATDAYQAG LVNSISTCGK TLLDTLDHVL DYAKINKLGR
ARMKKNAKSN RLASATDSPS ESLSISAEID LGLVVEEVVE AVCAGHAFKK MHTGDLKSRE
GPVITMSRHS SSSKVSTADG GNIHEGEVAV LLDVSPRACW LVRTQPGALR RIIMNLLGNA
LKYTPRGWVA VSLRAQESTQ SHKMDVVFRV VDSGKGMSED FQKNRLFTPF SQEDEFMPGT
GLGLSIVRQI IDSLGGTIDV KSVQNVGTEI EVRLSLALAQ HSDTPDEELT AVIAKTRGLR
LALLDPNGEK ERDRNDNISR LDTTLSEVCW GWFEMEVTKA DSLKDVDADM YMYTEPPSVE
YLLEHHSVNK TSNEGGRGKE VPLIIVCLNA SEAVEITSNH IKALSDLGRI VEVVSQPCGP
RKLAKILAQC TRRMEETFHR PMKPDRQPQP QGFPHRSRLE DMGAATMLGL PSMTLPRLNT
SEERSESIRA REFIRNTPTE LPPSTAVAFP NIDRDEGNAR EPQGQAQAAS VPHVLLVDDN
SINLQLLVMF MKKHKMPYQE ATNGQEALDK YIEFGSGDPN KPHLDFILMD ISMPVMNGLE
ATRRIREFEI EQGIEKKATI IALTGLASAE AQADAESSGV DIYMAKPVKF QALRPLLITK
KPEKKAE
//