ID A0A2T5M599_9EURO Unreviewed; 1320 AA.
AC A0A2T5M599;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 13-SEP-2023, entry version 22.
DE RecName: Full=Phytochrome {ECO:0008006|Google:ProtNLM};
GN ORFNames=P175DRAFT_0552989 {ECO:0000313|EMBL:PTU23676.1};
OS Aspergillus ochraceoroseus IBT 24754.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=1392256 {ECO:0000313|EMBL:PTU23676.1, ECO:0000313|Proteomes:UP000244073};
RN [1] {ECO:0000313|EMBL:PTU23676.1, ECO:0000313|Proteomes:UP000244073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 24754 {ECO:0000313|EMBL:PTU23676.1,
RC ECO:0000313|Proteomes:UP000244073};
RX PubMed=29317534; DOI=10.1073/pnas.1715954115;
RA Kaerboelling I., Vesth T.C., Frisvad J.C., Nybo J.L., Theobald S., Kuo A.,
RA Bowyer P., Matsuda Y., Mondo S., Lyhne E.K., Kogle M.E., Clum A.,
RA Lipzen A., Salamov A., Ngan C.Y., Daum C., Chiniquy J., Barry K.,
RA LaButti K., Haridas S., Simmons B.A., Magnuson J.K., Mortensen U.H.,
RA Larsen T.O., Grigoriev I.V., Baker S.E., Andersen M.R.;
RT "Linking secondary metabolites to gene clusters through genome sequencing
RT of six diverse Aspergillus species.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:E753-E761(2018).
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:PTU23676.1}.
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DR EMBL; MSFN02000001; PTU23676.1; -; Genomic_DNA.
DR VEuPathDB; FungiDB:P175DRAFT_0552989; -.
DR OrthoDB; 1770905at2759; -.
DR Proteomes; UP000244073; 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 Sensory transduction {ECO:0000256|ARBA:ARBA00022606};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 390..552
FT /note="Phytochrome chromophore attachment site"
FT /evidence="ECO:0000259|PROSITE:PS50046"
FT DOMAIN 763..1004
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1163..1293
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 942..961
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1040..1094
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1106..1145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1040..1064
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1074..1088
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1214
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1320 AA; 145434 MW; 6642C47A5C5E61C7 CRC64;
MSSGANSPVA SQPRDEAHGP EYPSASHAQP GATEEQILVS TQDLGPGVTD RVFPVRSLVS
FDPSPPSDSQ SQSQTNPLSP AGTARQYSII DSETWNQIQS QSDTNTDSVS LSGEIRQTPD
DSCPTSQLVS EISSNPESNN ADATEALRPR YIPSSDDDHQ PRLVTTRFRH IVTSDGHAVV
TGRTVDSFKA CEDEPIHIPG AIQSFGALVA LREEADEKLS VRIASENSED ILGYSPSSLF
ALETFCEVLP EDQADLFLDH VDFVRDEGYD PSVDGPEVFI LTINQPVGHT VRVWCAIHVS
PSIDGLIVCE FELEDDQSNP FSTSGRASPT GPADTMGVHP TPEQLAGSTV NTSQPLRILR
RARRRKGEAA AMEVFSIVSQ IQEQLSRAEN METLMDITVG IVKELTGFHR VLVYQFDSEF
NGKVIAELVD PTMSIDLYKG LHFPAADIPK QARELYRINK VRLLYDRDQV TARLVCRTLK
DLETPLDMTH AYLRAMSPIH IKYLANMAVR SSMSISINGP SDLWGLISLH SYGSCGMRVS
FAIRKMCRLI GDTVSRNIER LSYASRLQAR KLINTVPTGA NPSGYIVASS DDLLRLFDAD
YGALCIREET KILAKSAHSQ EMLALVEFLK VRRFNSVVSS SHIVKDFRDL HYPPGFKDIS
GMLYVPLSTH GIDFIVFFRK GQLTEVKWGG NPYGKKFTDG HLEPRKSFQT WSETVLDQSR
EWTESEVDTA AVLCLVYGKF IKVWRQQEAV LESSNLTRLL LANSAHEVRT PLNAIVNYLE
IALEGALDTE TRDHLTKSYS ASKSLIYVIN DLLDLTNVEQ GQDLIKDESF DLRTTFTQAT
DMFNSEAARK KLNYTVLSHP GVPETVIGDQ RRVRQAMTNI ISNAIQHTSV GGVTVEIWSS
RDEVETEKAT VNIAVLDTGP GIPSDKLEAL FQELEQISAD DDSYYFDGSG PDSSDAASDS
REKNVLGLGL ALVARIVRNM HGQLSVRSEE GKGSRFQISL QFSVPKYSPQ SESNISHLAI
RTVDSATAFP SKEDIVLVGS TSSSQKGGSH GSVKNGTPSM QTEKREVNPK VVRRQNAEPQ
TSSDADEFRT GKCSPVASRE GVISSLASKL SETPSPLAIP QVAERERERD RASTQALDRP
LGSPPLSGAG CIPNFDPRMQ GLNVLVAEDD PINAKILQKR LGKTGCAVHL TVNGEEVARA
YRDNPRRWDV VLMDMQMPIL DGIDSTKRIR QFENESTGGQ VPTGGLIRRV PIFIVSASLL
EKDAQMYMDV GFNGWIMKPI NFARLNTLLA GLHSETARNN ATYQPGDWEN GGWFTPYTKS
//
