ID A0A2H3E2J6_ARMGA Unreviewed; 1533 AA.
AC A0A2H3E2J6;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Phytochrome {ECO:0008006|Google:ProtNLM};
GN ORFNames=ARMGADRAFT_1162720 {ECO:0000313|EMBL:PBK97922.1};
OS Armillaria gallica (Bulbous honey fungus) (Armillaria bulbosa).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Physalacriaceae; Armillaria.
OX NCBI_TaxID=47427 {ECO:0000313|EMBL:PBK97922.1, ECO:0000313|Proteomes:UP000217790};
RN [1] {ECO:0000313|Proteomes:UP000217790}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ar21-2 {ECO:0000313|Proteomes:UP000217790};
RX PubMed=29085064; DOI=10.1038/s41559-017-0347-8;
RA Sipos G., Prasanna A.N., Walter M.C., O'Connor E., Balint B., Krizsan K.,
RA Kiss B., Hess J., Varga T., Slot J., Riley R., Boka B., Rigling D.,
RA Barry K., Lee J., Mihaltcheva S., LaButti K., Lipzen A., Waldron R.,
RA Moloney N.M., Sperisen C., Kredics L., Vagvoelgyi C., Patrignani A.,
RA Fitzpatrick D., Nagy I., Doyle S., Anderson J.B., Grigoriev I.V.,
RA Gueldener U., Muensterkoetter M., Nagy L.G.;
RT "Genome expansion and lineage-specific genetic innovations in the forest
RT pathogenic fungi Armillaria.";
RL Nat. Ecol. Evol. 1:1931-1941(2017).
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DR EMBL; KZ293649; PBK97922.1; -; Genomic_DNA.
DR STRING; 47427.A0A2H3E2J6; -.
DR InParanoid; A0A2H3E2J6; -.
DR OMA; WVMKPIN; -.
DR OrthoDB; 1770905at2759; -.
DR Proteomes; UP000217790; 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; 1.
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};
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:UP000217790};
KW Sensory transduction {ECO:0000256|ARBA:ARBA00022606};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 631..793
FT /note="Phytochrome chromophore attachment site"
FT /evidence="ECO:0000259|PROSITE:PS50046"
FT DOMAIN 1006..1233
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1373..1503
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 70..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 213..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 455..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1239..1311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..198
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..269
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 466..517
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..534
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1239..1297
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1423
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1533 AA; 166336 MW; 892542EEE570285C CRC64;
MYGDDRDHDN PPQRHISPSK SFVYPVKSLL TGIQPAQEHT GGVSRTVVSS IGAPPSPEFS
KWIAGEVVRA HDTTTNPDKP AYDPNEAPFL SNVSPRRSHS MATASPSHSA FAGRRSAKKN
QSISGTSPHF PIESELPSPA NFSPRFPSGS SSAGAKPSSS LPSSTSSGLA EFHSCQSPAM
PAQDAFASTS TSLAPEAVPS PFNPSELGLV HLGPISTSSH SSTSGALHSG RIDSCTPDAS
GRFNSSDLSA TDNTCPSASP EDSADKQLSS EEPLFTVRFQ AMQDEHGHHV VLGREGKLTR
CEDEPIRTPG AVQGFGVLIV VDEKDDVLVV RQVSENSTQL LGLSPRYLFS LDCFTDTLPE
SQADLLWNNV QFLSEPGSQP PDDGHDPPHI FRISGWGAPG TAKDPPVVVA SDGASSEDRC
LWTCWCAMHR PPSATGPNSK LFVMEFELEV DVLNPLYPPQ PEATNPASPG QNTSDFDSDS
ITAGEASNDG MGRTSLGTGD MTSSLPSSRS HPGDQPPELH TSPQPSPPSL PPLGANSLNA
PAVMSSLSGL DGDDTWIPSA ADIMESTMSV SKPLPALERL RRLGRIAASE PTSAKSKSRR
GKKAIIPGGS DMMDVLAVMA QINEQLGDPP DLETFLKVVV GIIKDLTQFH RVLVYQFDER
WNGQVVAELV DWKITHDLYK GLHFPAADIP AQARQLYTTN QVRILYDRGQ ATARIVVRSK
EDLEQPLDMT HCHLRAMSPI HIKYLGNMGV RASMSVSIMA FGTLWGLVAC HSYGARGMRV
SLPTREMLKL LSQSISRNIE RLSYAQRLHT RKLINTMASE NHPTGYIVSD FDSLLSLFDA
DFGILVIGDG AKILGPNANE HGQEILIMTE YLRLKQYGTI QVSQEVTTDY PDLKISTGLD
VVAGLMYVPL SSGGKDFIAF LRKGQPRDVH WAGKPFKGDG SKAMLEPRKS FKIWSETVAG
RCRAWTDEQL ETAGVLALVY GKFIEVWRQK ESALQTTKIT NLLLSNASHE VRTPLNHIIN
YLEMALNGAL DSETRDNLSQ SHSASKNLLF TINDLLDLTR LESGNETSFN QLFNLPAAVE
EAIGPYRSEA QRQSIDFILD VSECPKEVIG DARKIQTVVQ NLTANALKYT AEGSITVCCV
STQEPVGLRN SQQTAVEIVV ADTGCGIQQE KLENIFREFE QVESLEPKTS ADAGVGLGLA
VVARIVEQLG GQLRVDSRVK QGSRFSFLIP LSFHTGAVNP LSSSSQTSSS ESLRIRSRPP
SINSNNEIDS LVEAISSNHM GPKSSSPKSS PSLEDQRNID DFPNIPAPKR SEGTFEVVGS
QVPVRPIKMD ENISTPSANL RLGTVALKSA HGSRVATSAK LGPSQKCAPS KLRVLIVEDN
ILNQKLLAKR LKLDGHTVVN TMNGQEGLDI MRADRDFDCV LMDLSMPILN GFEATEQIRA
VEAKSPASAL RLSHRLNGRI PIFAVSASLF EQQRDKLSKC GMDGWILKPI DFKRLGVILS
GVTDVGQRQR DLYRPGCNWE SGGWLREHLP LDS
//
