ID A0A177BY78_9PLEO Unreviewed; 1368 AA.
AC A0A177BY78;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 13-SEP-2023, entry version 32.
DE RecName: Full=Cyanobacterial phytochrome B {ECO:0008006|Google:ProtNLM};
GN ORFNames=CC84DRAFT_1102986 {ECO:0000313|EMBL:OAF99900.1};
OS Paraphaeosphaeria sporulosa.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Didymosphaeriaceae;
OC Paraphaeosphaeria.
OX NCBI_TaxID=1460663 {ECO:0000313|EMBL:OAF99900.1, ECO:0000313|Proteomes:UP000077069};
RN [1] {ECO:0000313|EMBL:OAF99900.1, ECO:0000313|Proteomes:UP000077069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP3s5-JAC2a {ECO:0000313|EMBL:OAF99900.1,
RC ECO:0000313|Proteomes:UP000077069};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KV441560; OAF99900.1; -; Genomic_DNA.
DR RefSeq; XP_018030266.1; XM_018174992.1.
DR STRING; 1460663.A0A177BY78; -.
DR GeneID; 28758478; -.
DR InParanoid; A0A177BY78; -.
DR OrthoDB; 1770905at2759; -.
DR Proteomes; UP000077069; 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; IPR001294; Phytochrome.
DR InterPro; IPR013515; Phytochrome_cen-reg.
DR InterPro; IPR043150; Phytochrome_PHY_sf.
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; PR01033; PHYTOCHROME.
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|PROSITE-ProRule:PRU00169};
KW Photoreceptor protein {ECO:0000256|ARBA:ARBA00022543};
KW Receptor {ECO:0000256|ARBA:ARBA00022543};
KW Reference proteome {ECO:0000313|Proteomes:UP000077069};
KW Sensory transduction {ECO:0000256|ARBA:ARBA00022606};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 383..545
FT /note="Phytochrome chromophore attachment site"
FT /evidence="ECO:0000259|PROSITE:PS50046"
FT DOMAIN 759..998
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1139..1269
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1001..1131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1295..1368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..96
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..127
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..347
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1025..1056
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1318..1368
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1190
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1368 AA; 151306 MW; A12FD82646ED2403 CRC64;
MGTLSPTATD RVFPIRSVVS VDPHPTPTQR GQPDYFHQHA RPYEGRVPAD GRRQSQSSTA
SQTSQPSQRG PPPTQPTSRQ TSANRGSASA TRNETSRKLP PPLPAQLFND FGSESAHGNS
MSRSPSLKPE HPHSADAASI RSAVSSLGDM GNLVTHRFKH VVTEGGHAVI TGRDGATLQR
CEDEPIHIPG AVQGFGLLIA LQEDPGGSGS LPVRIVSENA KRILGRSPQE LFALESFTDI
LSEEQADNLL DHIDFIKDED ADVQTNGPEV FTLSIKFPNA RRSRKLWCAM HINDTNPGLI
ICEFELEDDD VYPLVPSNEM TPELPEDTLQ SNPTAEEFQE STETGSRPLR VLRSARKRKG
EAAAMEVFNI MSQVQEQLAA APSLEKFLKV LVGVVKELTG FHRVMIYQFD QSFNGRVVTE
LVDPRATKDL YKGLSFPASD IPKQARELYK INKVRMLYDR DLETARLVCR SAEDLETPLD
LTHSYLRAMS PIHLKYLANM AVRSSMSISI NAFGELWGLI ACHSYGGRGM RVSFPIRKMC
RLVGDSASRN IERLSYASRL QARKLINTVP TQHNPSGYII ASSDDLLKLF DADFGLLSIR
DETKILGHLD NSQEALALLE YFRMRRISSV LTSTDVSQDF PDLRYAPGFQ VIAGMLIVPL
SVGGTDFIVF FRKGQLREVK WAGNPYEKFI KAGTEGYLEP RKSFKTWSET VVGKCRDWTE
EEVETAAVLC LVYGKFIEVW RQKEAALQSS QLTRLLLANS AHEVRTPLNA IINYLEIALE
GSLDSETREN LSRSHSASKS LIYVINDLLD LTKTEEGGPL IKGESFDLRA TLTEATNMFV
GDAKRKNISY DVVEHPGLPQ HCIGDQRRVR QAISNITANA IQNTTQGGVK VEMYVAARRS
NTQVDVEVAV TDSGVGMSSK KLDQLFNDLE QVQSEPAAML EDALIPSTEQ LLEQSEKTTL
GLGLAVVARI IKNMEGQLRL KSEEGKGSRF VIQFPFELPD SEPQVPAVGS SEGSITPLPG
TSRPRGERSA STKSVRPTLS KRNSIDNAIA SSPRRTRSRS LEQDAQVVIP PHLRSMDVRS
PGEEPITSSR TSLKAIRMPD DLGSPIDPRP RSGSVLGEVS DEPEKISTGS KELSSKHLRV
LVAEDDPVNS RIVQKRLEKL GHEVYLTVNG EECAGAYCDK PQDFDVVLMD MQMPIVDGLT
STKMIRSFEK THKNIYSPRA ALNGRVPIIA VSASLIEKNR EKYMDAGFDA WILKPISFPR
LNELMAASVD RSIRESCLYQ SGEWERGGWF HFEESSADEV STEPAGEPLI DDPSEGMGKA
NQDSDDRQAG DESDRISDEQ NRLLHAQEQE RKSLGLDDEA APEHGDSV
//
