ID W2RJ33_9EURO Unreviewed; 2432 AA.
AC W2RJ33;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ETN36497.1};
GN ORFNames=HMPREF1541_08775 {ECO:0000313|EMBL:ETN36497.1};
OS Cyphellophora europaea CBS 101466.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Cyphellophoraceae; Cyphellophora.
OX NCBI_TaxID=1220924 {ECO:0000313|EMBL:ETN36497.1, ECO:0000313|Proteomes:UP000030752};
RN [1] {ECO:0000313|EMBL:ETN36497.1, ECO:0000313|Proteomes:UP000030752}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101466 {ECO:0000313|EMBL:ETN36497.1,
RC ECO:0000313|Proteomes:UP000030752};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Phialophora europaea CBS 101466.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KB822725; ETN36497.1; -; Genomic_DNA.
DR RefSeq; XP_008721315.1; XM_008723093.1.
DR STRING; 1220924.W2RJ33; -.
DR GeneID; 19976114; -.
DR VEuPathDB; FungiDB:HMPREF1541_08775; -.
DR eggNOG; KOG0519; Eukaryota.
DR HOGENOM; CLU_001037_0_0_1; -.
DR InParanoid; W2RJ33; -.
DR OrthoDB; 1222064at2759; -.
DR Proteomes; UP000030752; 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 CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR041664; AAA_16.
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; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR43047:SF46; HISTIDINE KINASE_RESPONSE REGULATOR, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G12550)-RELATED; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF13191; AAA_16; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 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; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
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}; Reference proteome {ECO:0000313|Proteomes:UP000030752};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 63..383
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1878..2099
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 2153..2276
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 58..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 528..556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2283..2432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..548
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2284..2326
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2361..2379
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2380..2395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2207
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 2432 AA; 271016 MW; 14A8F3BE263DA4D3 CRC64;
MDDNILGEDL PLPPTRLFER LAHVPNYTWD QSFAPFHSTY DHWHVFGILH NPDVDGPTTS
SSFLTSRSTR SGSARGSPKV DHRPSLRHTH WSSISGTSES SDFSSSKEEP DMIWIPVVAR
ISTHMLKLER EYNFYKSIIK QDDPDCIHIG RPIDIFRLPT TPGDAHSMIV CVYEAPGINH
LREITDFGPA FFGLQSRKKS VNPENSGQID LASFLDFAIG TCECLELLHH GAKTVHGEIR
QDTFHWSKEA NVVKLMNCGS GPRSFENLLS SEGWATLSKE LGVKNKLQFI APEQTGRLPA
EPDSRTDIYS LGVLFWTILT GQPAFNADTP IDIVQKVLSS RLPLASSIRI DIPDVISRII
AKMTQKQMDA RYHSISGLKY DLTQVQMALG EGDQEKVATY KIGEHDVSSF FILPSKQFGR
NSDHERIVKI IDKVYKRQSQ SAIRSGPNTH LLLSNTSNSS VSEERLDVDI ADTDSSSSYS
LRETRSNSTT VGLETAPYAM SGAFKDHRHF QGVGRGIAEA RTNSLDVSDR DSSFSGGFSQ
QSDSLGTMSR RRNSHKWKAK GKTDVISVLG AQGVGKSLLV KSVQPHIRRH GYFAMARFDR
ARPTPFEPLI KVMSSLFRQI FSERDVSTSY HEHLRSHVRP LWNVLHSVLD LPESLLDTTA
PSKKIMLATG NSDLGTPSIK TEETRPATAA SSNANVTGVR DANDFLRGPA STKSIRFMHT
YVDVLRLMSS GKVICLCLDD FHATDNDSLE LVLHIIKSKI PVVFLLASRA DQEGVPESAR
KVMEQDASYR LELTNLKEKH VFEYVAETMS QPVETVLPLA AVVFEKSRGN PFLVREILQL
CYQRDCLWYD WRSSGWQFDL DKIFTEMSSA DSPGTLDDTF ITKKMQLLSP APRAILAWAS
LIGASFSFRL VQEILTGQYF YSSGRDQGHD FTCPKTFQQW NLTESECIDG LQKLMNMYMI
VPGDSDDEFR FTHSRVLRAA NDMRECQNTT KMHFIITQAM MSYLSECRYN LYPLARHICL
CADIIKERIP NRIRYRDVLW RGAQKAVESG AKSTALWYYQ TSIALLQNDK WNADNPDVFY
DESLQLCVNT SEILYALKKD DEALEMLMET FTNARCDADR TRSYILKGRI YSRKGQYDVA
FAKLKECLAG LGLPLPDKSW TELDIDFKKL EYKFRNLDRA ALVRRPLSEA KADIALGTVL
SDMLGAAYWF DSKLWYQIVI NFIDIVVERG NIVQAGVGFT MLAAASIGRF KDFQLAMLYG
ETAQDYFTAY DDVWTRGRGW TLYTLFVGHF RTPIRNLLPV LENALEYSMA SEDRFISILN
VGAMALTRLW AGQDVAEIEA FCSYGPEEWD DWELDMRGGA ILLATRQTVR ALQGKTKVNN
VDTMLDDDSF KKSTWMETVK QHASNPHRPS DLFDAITISV YFMYEQIDYV VETGRRLIST
TLDDLWSNRP CAAVRFYLCM ALMCKAWDMP DMADRLPLLE EARTLKAWID NWGSAYDVNY
LAWSHLMASA IACAARDFPN IINNIEIAID HCQVHGFALE EAIAVEMQAE FLLERGAKRA
GKVMIQEAMA AYNRISAVGK AKFLAERHEW LLKTATTTRA VDMGVQTMDV ADFVGNEEQS
KREYTKNWVE PKQVNGSPHD VSGLGLDILD LTSILEFSRI ISSELQINSL LSKMVSVILE
SVGGQAEFCA IVIDSEEQGW CVAASADHDT GVKTYPDGIP FSEVDDQAAQ QITHYVLRTK
ETVFLQNVLE DDRFSNVGEP YLARNPGGRA IITIPIVQAE HLMGVIHLEG RPHAFTQRNH
VVLNLLTNQV AISLGNALLY RKVRKVSASN ASMVESQKRA LVAAREAEAK AKKAEAEAMH
NVKLKEEAAK AKSIFLANVS HELRTPLNGV IGMSELLKGT PLGKDQEGYA DSIRVCADTL
LTVINDILDF SKLEAGKMQM FTVPLNLKET ITEVVRALAY TNQEHGLNTV EDLQIDDNLV
LGDPVRLHQI FMNLLSNAYK FTPHGSVTIR ARKVAETGQK VKITCSVADT GIGISEEQLA
RLFQPFSQAD SSTARSYGGS GLGLSICKAM IENVLGGKIW IESTPGVGTT VSFTLTFRKA
PKDSAVPDMK IAAKDPDPMA NWSQAASPAG VDENKDPMPA HLDLSRIPKE DLRVCIAEDN
AINRKIAISF VNKIGLKCEA YEDGKLAYEA LQRKSKEGEP FHLVLMDVQM PVLDGYEATK
AIRKDSDPNV NKVLIIAMTA SAIRGDREKC LEAGMNDYLA KPVRQNVLKS MLDEYMTDTQ
AARTAAADGG TTTKVTPGDK ASGQSGQEQA KQQEAQGKQA VNGVEAASLS SRRPIKKHRD
HSHLSETTNM VSSGSPPSGK RETDELGKIS REQLSEKPRS MTHENLQQAL SQLDGNANGA
VEGEGGNKNN GGAVQLDGEQ RAETNGERPT SG
//
