TCSA_EMENI
ID TCSA_EMENI Reviewed; 682 AA.
AC Q9P896; C8VGY4; Q5B2D4;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 2.
DT 25-MAY-2022, entry version 130.
DE RecName: Full=Two-component system protein A;
DE EC=2.7.13.3;
GN Name=tcsA {ECO:0000312|EMBL:CAB93498.1}; ORFNames=AN5296;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1] {ECO:0000312|EMBL:CAB93498.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=biA1;
RX PubMed=10905426; DOI=10.1007/s002940000123;
RA Appleyard V.M.C.L., McPheat W.L., Stark M.J.R.;
RT "A novel 'two-component' protein containing histidine kinase and response
RT regulator domains required for sporulation in Aspergillus nidulans.";
RL Curr. Genet. 37:364-372(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
CC -!- FUNCTION: May be part of a two-component regulatory system required for
CC formation of conidia on certain growth media.
CC {ECO:0000269|PubMed:10905426, ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- PTM: Activation probably requires a transfer of a phosphate group
CC between a His in the histidine kinase domain and an Asp of the response
CC regulatory domain. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB93498.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AJ271843; CAB93498.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AACD01000093; EAA62456.1; -; Genomic_DNA.
DR EMBL; BN001305; CBF82150.1; -; Genomic_DNA.
DR RefSeq; XP_662900.1; XM_657808.1.
DR AlphaFoldDB; Q9P896; -.
DR SMR; Q9P896; -.
DR STRING; 162425.CADANIAP00003803; -.
DR PRIDE; Q9P896; -.
DR EnsemblFungi; CBF82150; CBF82150; ANIA_05296.
DR EnsemblFungi; EAA62456; EAA62456; AN5296.2.
DR GeneID; 2871585; -.
DR KEGG; ani:AN5296.2; -.
DR VEuPathDB; FungiDB:AN5296; -.
DR eggNOG; KOG0519; Eukaryota.
DR HOGENOM; CLU_000445_114_15_1; -.
DR InParanoid; Q9P896; -.
DR OMA; RLCHAAY; -.
DR OrthoDB; 27870at2759; -.
DR Proteomes; UP000000560; Chromosome V.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; NAS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000156; F:phosphorelay response regulator activity; ISA:AspGD.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0004673; F:protein histidine kinase activity; ISA:AspGD.
DR GO; GO:0030437; P:ascospore formation; IMP:UniProtKB.
DR GO; GO:0048315; P:conidium formation; IMP:AspGD.
DR GO; GO:0000160; P:phosphorelay signal transduction system; ISA:AspGD.
DR GO; GO:0075306; P:regulation of conidium formation; IMP:AspGD.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
DR Gene3D; 3.30.565.10; -; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 1.
DR SMART; SM00091; PAS; 2.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF47384; SSF47384; 1.
DR SUPFAM; SSF52172; SSF52172; 1.
DR SUPFAM; SSF55785; SSF55785; 2.
DR SUPFAM; SSF55874; SSF55874; 1.
DR TIGRFAMs; TIGR00229; sensory_box; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 3: Inferred from homology;
KW ATP-binding; Conidiation; Cytoplasm; Kinase; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Repeat; Sporulation; Transferase;
KW Two-component regulatory system.
FT CHAIN 1..682
FT /note="Two-component system protein A"
FT /id="PRO_0000081411"
FT DOMAIN 45..105
FT /note="PAS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 166..239
FT /note="PAS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 241..292
FT /note="PAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00141"
FT DOMAIN 307..530
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT DOMAIN 563..680
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT REGION 11..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 310
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 615
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT CONFLICT 217..219
FT /note="LYS -> SIV (in Ref. 1; CAB93498)"
FT /evidence="ECO:0000305"
FT CONFLICT 319..320
FT /note="MQ -> IE (in Ref. 1; CAB93498)"
FT /evidence="ECO:0000305"
FT CONFLICT 336..338
FT /note="REH -> GD (in Ref. 1; CAB93498)"
FT /evidence="ECO:0000305"
FT CONFLICT 364..367
FT /note="SGSF -> IRLL (in Ref. 1; CAB93498)"
FT /evidence="ECO:0000305"
FT CONFLICT 406..411
FT /note="PTRMRG -> HAHAW (in Ref. 1; CAB93498)"
FT /evidence="ECO:0000305"
FT CONFLICT 472..479
FT /note="TLFTPFSR -> HSLHPLLA (in Ref. 1; CAB93498)"
FT /evidence="ECO:0000305"
FT CONFLICT 547..553
FT /note="VPTEVAS -> YPRSCF (in Ref. 1; CAB93498)"
FT /evidence="ECO:0000305"
FT CONFLICT 576..584
FT /note="VMLKLLHTI -> RYVEAPTYQF (in Ref. 1; CAB93498)"
FT /evidence="ECO:0000305"
FT CONFLICT 682
FT /note="T -> RSPQSQHGYWTETRRYAFICMSWRQERYHGKSIYAAYRDL (in
FT Ref. 1; CAB93498)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 682 AA; 75316 MW; 29D37B021170964D CRC64;
MLLNGQISAL SLDDNDNGQQ HQDEVQAKHQ DQGHTCPSRP SVPSLSRIYR CTPVPTIVLD
ASMVIIEVSN SHVALFGKPR DSLLHTSISD VSPECIPVPN IPILYGALRA ACSTREIQVV
EHVVVGEKIA HNLRVTPVYE DETLLFVVLE VENLRAEVIN NQHAYMNETY KILVDTVKDY
AIFMLDPTGH IATWNAGAGV LKGYKAEEII GKHFSILYSP ADRDNGKPAR ALDVCLREGR
IEDEGWRYRR DGSRFWANVL ITPIYQFGQH VGFVKVTRDL TERKEAEACM IAAFEESSRL
KTDFLANISH EIRTPMNGMQ IALTMLTDTG LSEEQREHAN IVQDSMSLLL QIVNDVLDYS
KLSSGSFSLH ADMLDIREIV GAVVRNCRSS LQEGVELDTE ISPKLPTRMR GDPLRYRQVL
QNLVGNAVKF TEKGSIHVKI TSSTDEEDSD SSVVRTEVTD TGIGVPDSAI NTLFTPFSRF
ANSAARKYQG TGLGLSICKS LAELMDGSVG YSPNPNASGS VFWFTAKMGG RSVTPPSKSP
SVSGSPVPTE VASEMRSIAP RKHVLLVEDN IVNHTVMLKL LHTIGFQRID GAWNGAEAVR
MVRQKPLSYD IILMDVSMPV LDGLAATEQI RDMGLTMPII AITGNAMKGD AETYIAQGMD
DCICKPVHRD QLLRVLWKWF GT
