ID A0A167N7R6_CALVF Unreviewed; 2812 AA.
AC A0A167N7R6;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=CALVIDRAFT_88561 {ECO:0000313|EMBL:KZO97433.1};
OS Calocera viscosa (strain TUFC12733).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC Dacrymycetales; Dacrymycetaceae; Calocera.
OX NCBI_TaxID=1330018 {ECO:0000313|EMBL:KZO97433.1, ECO:0000313|Proteomes:UP000076738};
RN [1] {ECO:0000313|EMBL:KZO97433.1, ECO:0000313|Proteomes:UP000076738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TUFC12733 {ECO:0000313|EMBL:KZO97433.1,
RC ECO:0000313|Proteomes:UP000076738};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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};
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DR EMBL; KV417280; KZO97433.1; -; Genomic_DNA.
DR STRING; 1330018.A0A167N7R6; -.
DR OrthoDB; 1222064at2759; -.
DR Proteomes; UP000076738; 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; 24.
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; -; 14.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 1.10.8.500; HAMP domain in histidine kinase; 2.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 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; 16.
DR Pfam; PF18947; HAMP_2; 8.
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; 25.
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; 14.
DR PROSITE; PS50885; HAMP; 25.
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:UP000076738};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 3..55
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 95..147
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 187..239
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 279..331
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 371..423
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 463..515
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 555..607
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 647..699
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 739..791
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 831..883
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 923..975
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 1015..1067
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 1107..1159
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 1199..1251
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 1291..1343
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 1383..1435
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 1475..1527
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 1567..1619
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 1659..1711
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 1751..1803
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 1843..1895
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 1935..1987
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 2028..2080
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 2120..2172
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 2212..2264
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 2286..2515
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 2658..2782
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 2791..2812
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 765..792
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 2712
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 2812 AA; 300978 MW; 15D7AC004A1009BD CRC64;
MANNLTVQVR AIADVTTAVA KGDLSRFIKV EAQGEVLQLS ETVNTMIVRL AAFASEVTRV
ASEVGTHGKL GGQAEVADVE GTWAELTANV NRMAQNLTQQ VRSISDVTIA VAKGDLSKEI
QVEAEGEIET LKDTINGMVR NLRAFASEVT SLAMDVGTRG ILGGQAKVDD VEGCWAELTA
NVNKMADNLT SQVRSIADVT KAVAAGDLTK KIAVDAQGEI EQLKDTINSM VDQLGTFAKE
VTTLALDVGT HGVLGGQAKV EGVQGTWADL TTNVNRMAEN LTNQVRSIAA VTTAVAKGNL
TEKINVDAQG EINSLKITVN SMVDQLNTFA REVTRVALEV GTEGKLGGQA EVAGVQGTWA
DLTTNVNKMA ENLTSQVRSI ADVTKAVAAG DLTKKIDVVA QGEIQQLKDT INSMVDQLST
FAKEVTSLAQ DVGTYGRLGG QAQVEGVQGT WADLTTNVNR MAQNLTQQVR SIAAVTTAVA
KGNLTEKITV DASGEIEQLK KTINSMVDQL STFASEVTRV ALDVGTYGQL GGQAKVEGVE
GTWADLTTNV NRMAENLTNQ VRSITTVTTA VADGDLSKHI NVDAQGEILG LKIIINRMVD
QLSTFASEVT RVALDVGTEG SLGGQAKVEG VKGTWADLTT NVNRMADNLT IQVRAIADVT
RAVAAGDLTK KIEVDAKGEI LGLKKTINSM VEQLNTFASE VTRVALEVGT EGKLGGQATV
AGVEGTWADL TTNVNRMADN LTNQVRSIAD VTKAVAAGDL TKKINVDAKG EIQELKETIN
SMVEQLNTFA SEVTRVALEV GTYGRLGGQA TVEGVQGTWA DLTRNVNSMA DNLTNQVRSI
AAVTTAVARG DLTKKISVSA MGEIEGLKNT VNSMVDQLNT FASEVSRVAL EVGTQGKLGG
QARVLGVEGT WEELTNNVNR MADNLTIQVR SIANVTKSVA RGDLTKTIDV STEGEIDDLK
RTINGMVRNL SLFAAEVTKV ALEVGTKGQL GGQANVQDVE GVWADLTDNV NRMAQNLTVQ
VRSIATVTTA VAKGDLTKTI EVSAEGEIEQ LKDTVNSMVR NLSTFASEVT SLARSVGTQG
ILGQRANVHG VEGIWASLTE NVNSMADNLT TQVRSISNVT KAIACGDLST FIEVQAHGEI
LELKNTINSM VSQLSLFASE VTRVALDVGT EGKLGGQAKV EGVQGTWADL TTNVNRMADN
LTNQVRSIAD VTKAVAAGDL TKSIQVDAKG EILDLKNTVN SMVEQLNAFG SEVTRVANEV
GTQGKLGGQA IVAGVEGIWA DLTDNVNKMA DNLTNQVRNI ASVTKGIAEG DLTRYIEVPA
QGEILGLKET VNNMVSGLSH MAGELSRVAL EVGTMGVLGG QAIIQNMPGT WGVLVINVNN
MANNLTSNVR SIAAVTKAVA EGDLTQMTNV HAQGEIGQLS ETINTMVTQL NTFAKEVTRV
ALDVGTHGKL GGQAKVAGVS GIWADLTFNV NRMADNLTVQ VRSISEVTKA VAAGDLARTI
EVQAQGEILE LKDTVNTMIR RLNTFASEVT RVALEVGTQG ILGGQAHVQD VEGVWADLTD
NVNRMADNLT YQVRSISNVT KAVAAGDLTS YIEVEAQGEI EELKSTVNTM IRRLNTFASE
VTRVALEVGT EGKLGGQAQV QDVEGVWADL TDNVNRMADN LTGQVRSISR VTKAVASGDL
SQSIDVQAQG EIEELKDTVN TMIRRLNTFA SEVTRVALEV GTEGKLGGQA QVQDVEGVWA
DLTDNVNRMA ENLTSQVRSI SRVTKAVASG DLSQSIDVQA QGEIEELKDT VNTMIRRLNT
FGSEVTRVAL EVGTQGKLGG QATVQDVEGV WAELTSNVNR MADNLTDQVR SISRVTKAVA
AGDLTSYIEV EAQGEIEDLK STVNTMIRRL NKFASEVTRV AYEVGTKGVL GGQAQVDDVE
GVWAALTTSV NSMAENLTLQ VRSISSVTKA VSMGDITKLV DVDVRGEMSD LKETVNSMVH
QLDFIVNEVS RVALQVGIEG NLGGQAMVGP LVQGKWKVLT DNVNLMAHNL TNQVRSIALV
TTAVAQGDLS KRIEIDAQGE ILDLKDTVNG MCDSLETFGS EVTRIARLVG TEGKLGVQAE
VYNVAGIWKD LTDNVNGMAK NLTEQVRDIA RATKAVSIGN LTTKVEIQAE GEIFQLVQTI
NGMIDQLATW AGEVQRVARE VGTEGRLGVN ASIHDVEGTW REITISVNTM ANNLTTQVRG
FAQIASAATD GDFTKFVTVE ASGEMDSLKS KINHMIRDLR DSIQRNTMAK EAAESANRSK
SEFLANMSHE IRTPMNGIIG MTSLCLESGE LTRSNKDNLQ IVHSLAQSLL FIIDDILDIS
KIEAGRMTIE YITFSIRHLV FQALKGLSVR AQQGKVDLTY DVDNDIPDQI VGDMFRLRQV
LVNLVGNAIK FTPASEEHPG KVTVSVGWIP NDTTNTDIKL RFSVKDTGIG IAPDKVNVIF
DTFSQADGST TRKFGGTGLG LSISKRLVLL MGGDLWVESV ENRGSTFYFT IMARLTPGNA
DAETMQKIAL YENRPVLWLN TGRNGDNVTR LLQDLKFNVR VAHSVEEVPQ DDTRYDAIMI
DKVGLVDVVR QQENLKESPF VILDGAAAHL DLQWCVGNSV QSHLPWADSV PTLAGALLPA
LEYVSGEPLT GDRAVPYDIL LAEDNVVNQK VAVKILEKLG HRLEVVDNGK KALDAVQAKA
KAGRQYDLVL MDVSMPFMGG IEATEMIRQW EADNGVQRVP IVALTAHAML GDRERCIQAG
MDEYVPKPLK RPDLISSMTK AVRISQRKQH QAYTAHSTQT YTAHSTGVPT VP
//
