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PHT1B_ORYSJ
ID   PHT1B_ORYSJ             Reviewed;         921 AA.
AC   Q2RBR1; A0A0P0XXT5;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 2.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Phototropin-1B;
DE            EC=2.7.11.1;
GN   Name=PHOT1B; OrderedLocusNames=Os11g0102200, LOC_Os11g01140;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16188032; DOI=10.1186/1741-7007-3-20;
RG   The rice chromosomes 11 and 12 sequencing consortia;
RT   "The sequence of rice chromosomes 11 and 12, rich in disease resistance
RT   genes and recent gene duplications.";
RL   BMC Biol. 3:20-20(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [5]
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=12068117; DOI=10.1104/pp.002410;
RA   Kasahara M., Swartz T.E., Olney M.A., Onodera A., Mochizuki N.,
RA   Fukuzawa H., Asamizu E., Tabata S., Kanegae H., Takano M., Christie J.M.,
RA   Nagatani A., Briggs W.R.;
RT   "Photochemical properties of the flavin mononucleotide-binding domains of
RT   the phototropins from Arabidopsis, rice, and Chlamydomonas reinhardtii.";
RL   Plant Physiol. 129:762-773(2002).
CC   -!- FUNCTION: Protein kinase that acts as a blue light photoreceptor in a
CC       signal-transduction pathway for phototropic responses. Regulates a wide
CC       range of physiological activities in plants that maximize the
CC       efficiency of photosynthesis, such as chloroplast relocations, stomata
CC       opening, and leaf expansion (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1;
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250};
CC       Note=Binds 2 FMN per subunit. {ECO:0000250};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Absorption:
CC         Abs(max)=450 nm {ECO:0000269|PubMed:12068117};
CC         Note=Exhibits a smaller absorbance peak at 350 nm. The broad
CC         fluorescence emission spectrum peaks at 490 nm.;
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- DOMAIN: The PAS (PER-ARNT-SIM) domains are required for the binding of
CC       FMN chromophores. {ECO:0000250}.
CC   -!- PTM: Autophosphorylated in response to blue light irradiation.
CC       {ECO:0000250}.
CC   -!- PTM: 2 molecules of FMN bind covalently to cysteines after exposure to
CC       blue light and are reversed in the dark. {ECO:0000250}.
CC   -!- MISCELLANEOUS: Undergoes a photocycle characterized by fluorescence and
CC       absorption changes induced by blue light.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR   EMBL; DP000010; ABA91098.2; -; Genomic_DNA.
DR   EMBL; AP008217; BAF27360.1; -; Genomic_DNA.
DR   EMBL; AP014967; BAT12271.1; -; Genomic_DNA.
DR   RefSeq; XP_015617473.1; XM_015761987.1.
DR   AlphaFoldDB; Q2RBR1; -.
DR   SMR; Q2RBR1; -.
DR   STRING; 4530.OS11T0102200-00; -.
DR   PaxDb; Q2RBR1; -.
DR   PRIDE; Q2RBR1; -.
DR   EnsemblPlants; Os11t0102200-00; Os11t0102200-00; Os11g0102200.
DR   GeneID; 4349531; -.
DR   Gramene; Os11t0102200-00; Os11t0102200-00; Os11g0102200.
DR   KEGG; osa:4349531; -.
DR   eggNOG; ENOG502QPPH; Eukaryota.
DR   HOGENOM; CLU_006321_1_0_1; -.
DR   InParanoid; Q2RBR1; -.
DR   OMA; VQPKPHR; -.
DR   OrthoDB; 529293at2759; -.
DR   Proteomes; UP000000763; Chromosome 11.
DR   Proteomes; UP000059680; Chromosome 11.
DR   Genevisible; Q2RBR1; OS.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0009882; F:blue light photoreceptor activity; IDA:UniProtKB.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR   GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR   CDD; cd00130; PAS; 2.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF13426; PAS_9; 2.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00086; PAC; 2.
DR   SMART; SM00091; PAS; 2.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF55785; SSF55785; 2.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   TIGRFAMs; TIGR00229; sensory_box; 2.
DR   PROSITE; PS50113; PAC; 2.
DR   PROSITE; PS50112; PAS; 2.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Chromophore; Flavoprotein; FMN; Kinase; Nucleotide-binding;
KW   Photoreceptor protein; Receptor; Reference proteome; Repeat;
KW   Sensory transduction; Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..921
FT                   /note="Phototropin-1B"
FT                   /id="PRO_0000395003"
FT   DOMAIN          123..197
FT                   /note="PAS 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT   DOMAIN          197..251
FT                   /note="PAC 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00141"
FT   DOMAIN          400..473
FT                   /note="PAS 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT   DOMAIN          474..528
FT                   /note="PAC 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00141"
FT   DOMAIN          594..881
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          87..118
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          286..345
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          366..391
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        34..50
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        88..118
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        286..315
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        322..344
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        719
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         172..177
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         190
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         205
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         215
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         236
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         449..454
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         467
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         482
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         492
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         513
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         600..608
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         623
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         173
FT                   /note="S-4a-FMN cysteine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         450
FT                   /note="S-4a-FMN cysteine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   921 AA;  103437 MW;  1DF66056E4A213EC CRC64;
     MASKGTEGGH GGVERKEQQQ QRGYQLPRDS RGSLEVFNPS SASSFRTAAA APKSASPFLA
     IPDREEDNVV AQQRAAEWGL VLQTDHHTGL PQGVSARPSS GSARTSSEDN PQQQQSAAAI
     PRVSEELRAA LSVFQQTFVV SDATHPNHPI MYASAGFFNM TGYTSKEVVG RNCRFLQGSG
     TDPHEIDKIR QSLANGSNYC GRILNYKKDG TPFWNLLTIA PIKDEDGRLL KFIGMQVEVS
     KYTEGKKDTV VRPNGLSESL IKYDARQKDH ARSSVSELLL ALKNPRSLSE SSNNTLKRKS
     QESLSMSMSE VPSKRSSESG SRRNSRSGTR SSLQKINEVP DQVNRTRKSG LRAFMGFLGM
     GHGSVEKNML KPRDEDPLID SDDERPESFE DEFRRKEMRR GIDLATTLER IEKNFVITDP
     RLPDNPIIFA SDSFLQLTEY NREEILGRNC RFLQGPETDR ATVRKIRDAI DNQAEVTVQL
     INYTKSGKKF WNLFHLQPMR DQKGDVQYFI GVQLDGTEHV QDDAAKEGVV LVKKTADNID
     EAAKELPDAN LRPKDLWANH SKVVLPNPHM KDTASWRAIQ KVLESGESIG LKHFRPVKPL
     GSGDTGSVHL VELLNTGEYF AMKAMDKSIM LNRNKVHRAT AERQILDLLD HPFLPTLYAS
     FQTKTHICLI TDYCPGGELF VLLDNQPLKV LHEDAVRFYA AEVVVALEYL HCQGIIYRDL
     KPENILLHRD GHISLTDFDL SCLTSCRPQV FLPEDADEKK GRKNGSYPIF FAEPMRASNS
     FVGTEEYIAP EIITGAGHTS AVDWWALGIL LYEMLYGYTP FRGKTRQRTF ANILHKDIRF
     PASISVSLAA RQLMYRLLHR DPANRLGSYE GANEIKGHPF FRGINWPLIR ATAPPKLEIP
     LFSKDDMEKK GLVTNNRTDM F
 
 
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