ID L8GBS5_PSED2 Unreviewed; 1330 AA.
AC L8GBS5;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=GMDG_04802 {ECO:0000313|EMBL:ELR10527.1};
OS Pseudogymnoascus destructans (strain ATCC MYA-4855 / 20631-21) (Bat
OS white-nose syndrome fungus) (Geomyces destructans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=658429 {ECO:0000313|EMBL:ELR10527.1, ECO:0000313|Proteomes:UP000011064};
RN [1] {ECO:0000313|Proteomes:UP000011064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4855 / 20631-21 {ECO:0000313|Proteomes:UP000011064};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C.A., Blehert D.S., Lorch J.M., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E.,
RA Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The genome sequence of Geomyces destructans 20631-21.";
RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GL573260; ELR10527.1; -; Genomic_DNA.
DR RefSeq; XP_012743228.1; XM_012887774.1.
DR STRING; 658429.L8GBS5; -.
DR VEuPathDB; FungiDB:GMDG_04802; -.
DR HOGENOM; CLU_000445_3_2_1; -.
DR InParanoid; L8GBS5; -.
DR OrthoDB; 1222064at2759; -.
DR Proteomes; UP000011064; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 5.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 1.20.120.1530; -; 3.
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; IPR003660; HAMP_dom.
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; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF00672; HAMP; 3.
DR Pfam; PF18947; HAMP_2; 2.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 6.
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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 2.
DR PROSITE; PS50885; HAMP; 6.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000011064};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 198..253
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 293..345
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 385..437
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 477..529
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 569..621
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 661..713
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 735..959
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1109..1228
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 75..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1235..1330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 161..206
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 85..102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1239..1253
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1158
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1330 AA; 145114 MW; 7A8F71FEA302CC7B CRC64;
MTDDAALAAA TAYIQSLATS STGLSALKAS RKDADTNGIE EIHLPGSSTT AKHALERELT
SLAKRVRLLE SNVAASKDHL PDTPNDSIDS SPANDIIPTA STSAAREKIV STLLASRESP
AGQSTVTYTK LSSEQLEALR EHVDHQSGQL ESQKLELASV NAQLLRQKQL QEKALKAVEV
ERVNALEREL KKHQQANEAF QKALREIGEI VTAVARGDLS KKVQIHSVEM DPEITTFKRT
INTMMDQLQV FSSEVSRVAR EVGTEGMLGG QAQISGVDGT WKELTKNVNV MAQNLTDQVR
EIAAVTTAVA HGDLTQKIER PAQGEILQLQ QTINTMVDQL RTFAAEVTRV ARDVGTEGIL
GGQAEIEGVK GMWNTLTVNV NAMANNLTTQ VRDIAMVTTA VAKGDLTQKV QAECKGEIFE
LKSTINSMVD QLQQFAREVT KIAREVGTEG RLGGQATVHD VEGTWRDLTE NVNGMAMNLT
TQVREIAKVT TAVAKGDLTK KITVEVRGEI LDLKITINTM VDKLSIFAFE VSKVAREVGT
DGTLGGQAKV ENVEGKWKDL TENVNTMASN LTSQVRGIST VTQAIANGDM SQKIEVEAAG
EILVLRETIN NMVDRLSIFS NEIQRVAKDV GVDGKMGGQA DVAGIGGRWK EITTDVNTMA
MNLTAQVRAF GDITNAATDG DFTKLITVEA SGEMDELKRK INQMVFNLRE SIQRNTAARE
AAEMANRTKS EFLANMSHEI RTPMNGIIGM TQLTLDTDLT QYQREMLNIV HNLANSLLTI
IDDILDLSKI EANRMVMEEI PYSVRSIVFN ALKTLAVKAN EKFLDLTYRV DSSVPDHVVG
DSFRLRQVIL NLVGNAIKFT ENGEVSLTIR KADQDNCEHN EYAIEFSVSD TGIGIQADKL
DLIFDTFQQA DGSMTRKFGG TGLGLSISKR LVNLMRGDVW VKSTYGKGSS FFFTCTVRLA
TSDISFIEKA LKPYQGHQVL FIDKGETGHG KEIISMLSQI GLEPVVVESD SHTDLMQAGR
PANHPSNYDV VIVDSIETGR RLRSIDEFKY IPIVLLAPVV HVSLKSSLDL GITSYMTTPC
QTIDLGNGMI PALENRAMPS LADNTKSFDI LLAEDNVVNQ RLAVKILEKY HHVVTVVGNG
LEALEAIKLK RYDCILMDVQ MPIMGGFEAT AKIREYEYNI GTTRTPIIAL TAHAMLGDRE
KCIQAQMDEY LSKPLKQNHL IQTILKCATL GGQLLEKGRE PRQSTKEERP TKIGPPVKAP
QPLSPLSPAA KKRAELKSGG KGNIPDENGS KTARPQGASP SPGPGKGEAG SPTKEQDDPL
ARLLMRAHGS
//
