ID A0A168QFK8_MUCCL Unreviewed; 1144 AA.
AC A0A168QFK8;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=HK_IA {ECO:0000313|EMBL:OAD09169.1};
GN ORFNames=MUCCIDRAFT_176325 {ECO:0000313|EMBL:OAD09169.1};
OS Mucor lusitanicus CBS 277.49.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX NCBI_TaxID=747725 {ECO:0000313|EMBL:OAD09169.1, ECO:0000313|Proteomes:UP000077051};
RN [1] {ECO:0000313|EMBL:OAD09169.1, ECO:0000313|Proteomes:UP000077051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 277.49 {ECO:0000313|EMBL:OAD09169.1,
RC ECO:0000313|Proteomes:UP000077051};
RG DOE Joint Genome Institute;
RA Corrochano L.M., Kuo A., Marcet-Houben M., Polaino S., Salamov A.,
RA Villalobos J.M., Alvarez M.I., Avalos J., Benito E.P., Benoit I.,
RA Burger G., Camino L.P., Canovas D., Cerda-Olmedo E., Cheng J.-F.,
RA Dominguez A., Elias M., Eslava A.P., Glaser F., Grimwood J., Gutierrez G.,
RA Heitman J., Henrissat B., Iturriaga E.A., Lang B.F., Lavin J.L., Lee S.,
RA Li W., Lindquist E., Lopez-Garcia S., Luque E.M., Marcos A.T., Martin J.,
RA Mccluskey K., Medina H.R., Miralles-Duran A., Miyazaki A., Munoz-Torres E.,
RA Oguiza J.A., Ohm R., Olmedo M., Orejas M., Ortiz-Castellanos L.,
RA Pisabarro A.G., Rodriguez-Romero J., Ruiz-Herrera J., Ruiz-Vazquez R.,
RA Sanz C., Schackwitz W., Schmutz J., Shahriari M., Shelest E.,
RA Silva-Franco F., Soanes D., Syed K., Tagua V.G., Talbot N.J., Thon M.,
RA De Vries R.P., Wiebenga A., Yadav J.S., Braun E.L., Baker S., Garre V.,
RA Horwitz B., Torres-Martinez S., Idnurm A., Herrera-Estrella A.,
RA Gabaldon T., Grigoriev I.V.;
RT "Expansion of signal transduction pathways in fungi by whole-genome
RT duplication.";
RL Submitted (JUN-2015) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OAD09169.1}.
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DR EMBL; AMYB01000001; OAD09169.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A168QFK8; -.
DR STRING; 747725.A0A168QFK8; -.
DR VEuPathDB; FungiDB:QYA_176325; -.
DR OrthoDB; 1222064at2759; -.
DR Proteomes; UP000077051; 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; 6.
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; -; 5.
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; 7.
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; 7.
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; 7.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:OAD09169.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000077051};
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..517
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 557..609
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 631..852
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1004..1124
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 1053
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1144 AA; 124946 MW; 4D66EB78A26107C5 CRC64;
MAANLTTQVR SIAEVTKAVA LGDLSKKIEV ETRGEILELK DIVNGMVDQL RIFASEVTRV
SKEVGTDGKL GGQASVPNVA GTWYELTDNV NIMAANLTTQ VRSIAEVTKA VASGDLSKKI
EVETRGEILD LKNTVNEMVD QLRVFASEVT RVAREVGTEG KLGGQARVPN VDGTWKDLTD
NVNTMATNLT NQVRSIAEVT KAVALGDLSK KIEVESGGEI LDLKNIVNSM VDQLRIFASE
VTRVAKEVGT EGKLGGQATV EGVAGTWMDL TDNVNTMAAN LTTQVRSIAQ VTKAVAKGDL
SKKIEVETRG EMLDLKDTIN DMVGQLRVFA SEVTRVSKEV GTEGKLGGQA VVQGVAGTWY
ELTDNVNIMA ANLTNQVRSI AEVTKAVASG DLSKKIEVET RGEILDLKNI VNSMVDQLRV
FASEVTRVAR EVGTEGKLGG QARVPNVDGT WKDLTDNVNT MATNLTNQVR SIAEVTKAVA
LGDLSKKIEI EVEVHGEIAE LKNTINTMVD QLSSFASEVT RVAKEVGTEG KLGVQAQVED
IEGLWRDITS NVNTMASNLT TQVRAFAQIS AAATENDFSR LITVEASGEM DSLKTKINQM
VGSLRDAIQK NRLAREAAEL ANRSKSEFLA NMSHEIRTPM NGIIGMTSLT LETELNRQQR
ENLMIVSSLA NSLLTIIDDI LDISKIEAGR MTIESIPFSL RSAVFSVLKT LAVKANQKKL
DLIYHVDQSI PDQLIGDPLR LRQVITNLIG NAVKFTTQGE VVLRTRAVRM QDSTVRLEFC
VSDTGIGIQE DKLNVIFDTF CQADGSTTRE YGGTGLGLSI SRHLVQLMGG DLWVESKYGR
GSEFYFTVNF FQFSLDQKEV IEKIRRYRNR RILFVDTMKD QTGAIDKVTM LGLKPYRVDS
IEEAAAISNA NSSKSKHAPF FDTVIIDKMA SAEKIREIVP LRYTPIVLIA PEVHLLNMKL
CIDLGITGYI NSPTTLADMA AVMLPALESH AALPSDASKT VPLEVLLAED NDVNQKLAVR
ILEKFGHHVK VVANGKLAVE AYESQTFDLI LMDVQMPVMG GFEATQRIRE IEHKMNNNSH
IPIIALTAHA MIGDREKCLQ AGMDEYVTKP LRFPELIAAI KKFAPQSAHM MVQGKSKAPA
IAKK
//
