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Database: UniProt
Entry: A0A074X7T8_9PEZI
LinkDB: A0A074X7T8_9PEZI
Original site: A0A074X7T8_9PEZI 
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
//
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