ID M2RMI3_CERS8 Unreviewed; 1588 AA.
AC M2RMI3;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 28-JUN-2023, entry version 48.
DE SubName: Full=Histidine kinase {ECO:0000313|EMBL:EMD39682.1};
GN ORFNames=CERSUDRAFT_111992 {ECO:0000313|EMBL:EMD39682.1};
OS Ceriporiopsis subvermispora (strain B) (White-rot fungus) (Gelatoporia
OS subvermispora).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Gelatoporiaceae; Gelatoporia.
OX NCBI_TaxID=914234 {ECO:0000313|EMBL:EMD39682.1, ECO:0000313|Proteomes:UP000016930};
RN [1] {ECO:0000313|EMBL:EMD39682.1, ECO:0000313|Proteomes:UP000016930}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B {ECO:0000313|EMBL:EMD39682.1,
RC ECO:0000313|Proteomes:UP000016930};
RX PubMed=22434909; DOI=10.1073/pnas.1119912109;
RA Fernandez-Fueyo E., Ruiz-Duenas F.J., Ferreira P., Floudas D.,
RA Hibbett D.S., Canessa P., Larrondo L.F., James T.Y., Seelenfreund D.,
RA Lobos S., Polanco R., Tello M., Honda Y., Watanabe T., Watanabe T.,
RA Ryu J.S., Kubicek C.P., Schmoll M., Gaskell J., Hammel K.E., St John F.J.,
RA Vanden Wymelenberg A., Sabat G., Splinter BonDurant S., Syed K.,
RA Yadav J.S., Doddapaneni H., Subramanian V., Lavin J.L., Oguiza J.A.,
RA Perez G., Pisabarro A.G., Ramirez L., Santoyo F., Master E., Coutinho P.M.,
RA Henrissat B., Lombard V., Magnuson J.K., Kuees U., Hori C., Igarashi K.,
RA Samejima M., Held B.W., Barry K.W., LaButti K.M., Lapidus A.,
RA Lindquist E.A., Lucas S.M., Riley R., Salamov A.A., Hoffmeister D.,
RA Schwenk D., Hadar Y., Yarden O., de Vries R.P., Wiebenga A., Stenlid J.,
RA Eastwood D., Grigoriev I.V., Berka R.M., Blanchette R.A., Kersten P.,
RA Martinez A.T., Vicuna R., Cullen D.;
RT "Comparative genomics of Ceriporiopsis subvermispora and Phanerochaete
RT chrysosporium provide insight into selective ligninolysis.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:5458-5463(2012).
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; KB445793; EMD39682.1; -; Genomic_DNA.
DR STRING; 914234.M2RMI3; -.
DR HOGENOM; CLU_000445_50_4_1; -.
DR OrthoDB; 1770905at2759; -.
DR Proteomes; UP000016930; 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 GO; GO:0009881; F:photoreceptor activity; IEA:UniProtKB-KW.
DR GO; GO:0009584; P:detection of visible light; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; 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; 3.30.450.270; -; 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 Gene3D; 3.30.450.20; PAS domain; 2.
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; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013654; PAS_2.
DR InterPro; IPR016132; Phyto_chromo_attachment.
DR InterPro; IPR013515; Phytochrome_cen-reg.
DR InterPro; IPR043150; Phytochrome_PHY_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08446; PAS_2; 1.
DR Pfam; PF00360; PHY; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
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; 2.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50046; PHYTOCHROME_2; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chromophore {ECO:0000256|ARBA:ARBA00022991};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EMD39682.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Photoreceptor protein {ECO:0000256|ARBA:ARBA00022543};
KW Receptor {ECO:0000256|ARBA:ARBA00022543};
KW Reference proteome {ECO:0000313|Proteomes:UP000016930};
KW Sensory transduction {ECO:0000256|ARBA:ARBA00022606};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 697..859
FT /note="Phytochrome chromophore attachment site"
FT /evidence="ECO:0000259|PROSITE:PS50046"
FT DOMAIN 1070..1296
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1426..1555
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 41..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 533..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 638..661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1301..1329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1344..1372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1390..1418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..96
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..246
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..331
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1301..1328
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1344..1363
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1476
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1588 AA; 173599 MW; 2A46362E2A04F3D5 CRC64;
MTTEDDARQV KETPRTTQHT TPSVPTTSYV YPVRSLLSGV QAAAPTGQRQ GDSNYVRPTT
VPEGDIHAAS ASSANEGLSA GQGGSQPSAS VDNTSKRSAE FPRRPPNPRS GSEKDDVHSR
RRKHRHRTPN FRDFPQDENP LAPRTFTTSP SESPLRDSNT PSNSADMFFV AGPSGEPVIY
LPSRTSSESD EEPDYKPRRP TQISEVAAEG FSVVAPTASI LPGVLPRPPE LSRGSSPSNF
SQSGIVHLPP IGTRPSSSHG SRSVGSSARG RTSRISGECP VTSPAQSANS AQNDVEAMQL
SSDQASRPSS PLPSMSGSSS SMTGSSGSGV PHVTFRYQHV EDEDGHHLIV GREGELTKCE
DEPIRAPGAV QGFGILIAVE EDEETGNLVV RQVSENSTEL LGLSPKYLFA MDCFSQTLPD
NQADVLFDNI QYLSDPSLTP EEQAENLHVF MLSGWGEPGT ALVEDANQDE QRRRHWTVWC
AAHRPEMTAP PNTTGSGSAG IGRSPDYSLI ILEFELERDV FNPLYPSLIS EEASVRSGVS
SPSDASGSTS NSSGRTLVST TSGETDAMVT PSDSNSSPGS CDPSVIASIT ATSSSQSSSS
PYSLPGSDEW LPSAEDILES TTSRSKPLLA LERLRRTRQT LGEAPSSPVS AASGMDRGGS
RFRRSAARQR RGGGAVGMMD VFAVMAQINE QLGAAPDLET FLKVTAGVIK DLTQFHRVLV
YQFDELWNGQ VVAELVDWNQ THDLFRGLHF PAGDIPAQAR TLYALNKVRI LYDRGQPTAR
LVVRSKQDLE TPLDMTHCYL RAMSPIHLKY LENMGVRASM SVSIIAFGQL WGLVACHSYG
SQGMRVSFPV RQMLRLLSQS ISRNIERLSY AQRLHTRKLI NTMPSDQHPS GYIVSNADDL
LGLFDADYGV LVIGEGAKIL GPNFHGQEIL IVAEYLRLKQ FDTIQVSQAV TQDYPDLPLT
SGLEIIAGLL YVPLSAGGRD FIAFLRRGQP RQVNWAGRPY RDGEQKNLLE PRTSFRIWSE
TVAGRCRAWS DEHLETAGVL ALVYGKFIEV WRQKENALQT TKLTNILLSN ASHEVRTPLN
HIINYLELAL NGPLDVDTRE NLSQSHAASK SLLFTINDLL DLTRLESGNE TSFNELFDLH
KTIEDATLLY RNEAARRGLG FQLDVKTCPR MVVGDARKIH TVVANLTANA LKYTKEGSIS
IQCHTFEEPT GLRTAQNVAV EIIVSDTGCG IPSEKLESIF REFEQVETAP SRGNSPGLGL
GLAVVARIVE QLGGQLRVDS RLNEGSRFSF LIPFAMEISD THTGSASSSS RSSLLQTRHS
SNEGSRGDQI DNLVEALSFS HMSQQRYPSP GGLSQTTDPT SATHHDCGKV DIVGSGVPLR
PVKVDEYDLD LPLQRKPPQP AAPLPRRSPR GATNSVAEGS APSSLRILIV EDNDINRMIL
SKRLSLDGHT VVNTTNGQEG LELLESDWDF DCVLMDIQMP LLNGYEATER IRALEHKRKE
GCRLSHKLNG RLPIFAVSAS LYISQREELH RLGMDGWILK PIDFKRLRNI LKGVVDLKQR
EKDVYHVGSS WEQGGWLAKP LKVNEHQL
//
