ID A0A074VR49_9PEZI Unreviewed; 1216 AA.
AC A0A074VR49;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KEQ63235.1};
DE Flags: Fragment;
GN ORFNames=M437DRAFT_34626 {ECO:0000313|EMBL:KEQ63235.1};
OS Aureobasidium melanogenum CBS 110374.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043003 {ECO:0000313|EMBL:KEQ63235.1, ECO:0000313|Proteomes:UP000030672};
RN [1] {ECO:0000313|EMBL:KEQ63235.1, ECO:0000313|Proteomes:UP000030672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 110374 {ECO:0000313|EMBL:KEQ63235.1,
RC ECO:0000313|Proteomes:UP000030672};
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; KL584832; KEQ63235.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A074VR49; -.
DR STRING; 1043003.A0A074VR49; -.
DR HOGENOM; CLU_002763_0_0_1; -.
DR OrthoDB; 12386at2759; -.
DR Proteomes; UP000030672; 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 G7-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:UP000030672};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 555..833
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1090..1216
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 236..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 356..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 432..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..253
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..282
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..456
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1147
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KEQ63235.1"
FT NON_TER 1216
FT /evidence="ECO:0000313|EMBL:KEQ63235.1"
SQ SEQUENCE 1216 AA; 134045 MW; 0C7DE8CF6CE3F00E CRC64;
RFYQPWLDAQ GTSANVASHV QDLADVDDFA INTLSDKGFR PLASRDTTLT AFAQLAALRL
NVRRAMVSLI DSKHQYILAE ATKTLSLVDD TRHAEGDALW LGTTSLARED AVCQCSFTRQ
YTVQDDDGHT ITATAAVMPD CRLDPDYKDK PYVIQEPGVR FYAGVPIKSR SGHNIGVYAV
SHDAPREPLT YDELRFMQDI AVAVMDHLEW ARDRVDRYKG ERIVRGMADF IEGAPSMRAM
KKESDKEEDH SAMVVNNPDP TPQVDIDLKE DTVKRQSPKR ADSSRSVNRP SLESRSQSFI
RRREPKTDSL SKLLDRASRI LRESTLAEGV VFFGPSGNNP SKPTLRSAMA ARDRMSGTDD
ESTRHLAVDS PDVENSTDSD VATYPVRTSK ILGLSLVNKK DSSLFHDTAL DVLTLENYFK
LYPNGKSLHF SEAGSGLSSE DDSASDGLSA SDRSRSHPKS TSQKVIGKKK KIRMSHQQLL
ENLPGVKNVI FLPLWDYVEE KMVAGCFLWT SSTGRMMNLD DDLSYLRAFG NTIMSEVARM
NALKDDRAKT TFIASMSHEL RSPLHGILGS VEFLQETAAD AYQSGLINSI STCGKTLLDT
LDHVLDYAKI NKLGRNRMKK DARSNRLASA TDSPSESLSI SAEIDLGLVV EEVVEAVCAG
HAFKKMHTGE LKSHDGPVVT MSRHSSASKV PAADGGNIHD GEVAVLLDVS PRASWVVRTQ
PGALRRIIMN LLGNALKYTP KGWVAVSLRA QESAHPHKMD VVFRVVDSGK GMSEDFQKNR
LFVPFSQEDT FQPGTGLGLS IVRQIVDSLG GTIDIKSVQN VGTEVDVRLS LAIAEPSASN
SPNNEIASVA AKTKGLRLCL LDPNGEKERD QNDNISRLDT TLSEVCWGWF EMEVTRASSL
QDADADLYMY TEPPSVEYLL EHHSVNQNRT GGGRGKEVPL IIVCLNASEA VGITSNHIKA
LSDLGRIVEI ISQPCGPRKL AKVLGQCVRR MEETFNRPMV PDRQPKPEGL PHRSRLEDVG
AASILGLPSV TLPRLNTYEE KTESVKAREL IRNADVEIPP STAVSFPTIN REEGNARETP
SQTESGSIPH VLLVDDNPIN LQLLVMFMKK HKLPYQEAVN GQEALDKYIE FGSGDPNKPR
FDFVLMDISM PIMNGLESTR RIREFEVEQG FEKKATIIAL TGLASAEAQA DAESSGVDIY
MAKPVKFQAL RPLLVS
//