ID A0A167IIJ1_CALVF Unreviewed; 1691 AA.
AC A0A167IIJ1;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 28-JUN-2023, entry version 32.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KZO92680.1};
GN ORFNames=CALVIDRAFT_519984 {ECO:0000313|EMBL:KZO92680.1};
OS Calocera viscosa (strain TUFC12733).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC Dacrymycetales; Dacrymycetaceae; Calocera.
OX NCBI_TaxID=1330018 {ECO:0000313|EMBL:KZO92680.1, ECO:0000313|Proteomes:UP000076738};
RN [1] {ECO:0000313|EMBL:KZO92680.1, ECO:0000313|Proteomes:UP000076738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TUFC12733 {ECO:0000313|EMBL:KZO92680.1,
RC ECO:0000313|Proteomes:UP000076738};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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DR EMBL; KV417308; KZO92680.1; -; Genomic_DNA.
DR STRING; 1330018.A0A167IIJ1; -.
DR OrthoDB; 1770905at2759; -.
DR Proteomes; UP000076738; 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:UP000076738};
KW Sensory transduction {ECO:0000256|ARBA:ARBA00022606};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 734..896
FT /note="Phytochrome chromophore attachment site"
FT /evidence="ECO:0000259|PROSITE:PS50046"
FT DOMAIN 1106..1333
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1516..1648
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 433..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 490..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 529..649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1336..1401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1669..1691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..24
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..214
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..315
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..452
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..511
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..602
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1338..1378
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1386..1401
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1673..1691
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1566
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1691 AA; 181877 MW; 14FAC6004C5B3448 CRC64;
MSSSSPARPP PSGQSPPQPL SPRARTPSPT SAHSPTGSGS YFGPAPSGSG PSGTSYVYPV
RSLLSNIQPA PEVDGYKSAT GTGSSYRGSR SGSGSDVDGE TRAQLQARSQ AAMHASRSVQ
GPDAPARERQ TFMYPRETPS ELSGPTPTDS SSSSSYFGQQ PQGTRMRSFS LPSPPTSDQD
QEKLPVPEEE DITPGPERPV TATDSERETL LPRPDSGTDD ALNTLFVSDA PASGPQSRVE
SESVDAPSGQ SMEGNAADSH RTPLSLAQTG IVRLPPSEPS TSGSRAGSRS TRSNQGSRPR
TDSLGPSSSL VSSGSGDGDG GGPLITARFE HKRTSGGHHV IVGREGVLTK CEDEPIRVPG
AVQGFGVLIA VAEDEETGNL VVRQVSENAT ELLGLSPEYL FSLTCFTQSL PPAQADILWD
NVQYLYELES DVEGSGTGSG TGSAGQDSPQ VFLLSGWGQP GSAFPEVAEM QPNPDPNQRR
EWTCWCAAHR PPAPRASGSG RSSSGTTSTS TMRQSLLILE FELERDTFNP LYPPFEQGDV
HLSGESSPGP GGSGSTTASR RSGRSAQSGS SGSSGGSRGS EGSGGSGVSA QSSLTERGDG
VADPTQSPSG YEAGPGGPST GLRTGAEDLP AQYRPSPEDV LESTTNRAKP LKALERMRRV
NRQVVARASG GAAAISSVAA GALESGRLAE GSISRSRRTG HAAHMPQPHN SGVSTMDVFA
LLSQVDDQWG RAPDLESFLK IVVGIIKDLT QFHRVLIYQF DESWNGQVVA ELVDWNQTHD
LYKGLHFPAG DIPAQARKLY AINKVRLLYD RSQLTARLVV RSKADLEPPL DMTHSYLRAM
SPIHIKYIAN MGVRASMSIS IMAFGQLWGL ITCHSYGQHG MRVSFPVRQM LRLMGDSISR
NIERLSYAQR LHTRKLISTL PTDQHPTGYI VSNAEDLLSL FDADFGILVI GEGAKILGPN
HSGQEVLIVA EYLRLKQFNI MQVSQAVTKD FPDLSLPSGM DVVAGLLYIP LSSGGRDFIA
FLRKGQLKEV HWAGKPFKEE GDADLEPRKS FKTWSETIAG RCRAWTDEQL ETAGVLALVY
GKFIEVWRQK ETAVKTTQLT NLLLSNASHE VRTPLNHIIN YLELALNGPL DTETRENLKL
THTASKSLLF TINDLLDLTR LESGNETSFN EPFDLPLTIQ EAVHLYRIEA ERRKLHFTID
TEDSPKIVLG DSRKIRTVVA NLTANAVKYT SEGTITVECR VFQEPAGLRD RRQIAVEIVV
GDTGCGIESS KLESIFREFE QVESSTPRPG EREGLGLGLA VVARIVEQLG GQLRVDSKVD
QGSRFSFLIP FALPSSDSRA GSAASDLNSR SGSASPSGSG GASSKGSKGS TIDSLVEALQ
SDPLNPIPRA GSNRSHRSMS NEKLPAVTAD AMRTPAADHA GQPGYFVESS RYPVRSVKVD
EFDLDKSVRQ PRTVEIPASP VLGSSGTRRS VVEARRRSLE YSKATVVPQP EPLTARSSAA
LRTRKESPTA GPVKLRILVV EDDPINRMIL HKRLVTDGHT VINTTNGQEA VEKVESDRDF
DCILMDIQMP ILNGFEASEK IREYESQNVL AQGTARPSTI LNGRIPIFAV SASLVEGARE
TLSERGMDGW ILKPIDYKRL GTLLRGISDH TQRAADVYRQ GHWEIGGWLE PPPGASPALP
TPVEKKKPSP K
//
