ID A0A0D2CSV2_9EURO Unreviewed; 2422 AA.
AC A0A0D2CSV2;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KIW53092.1};
GN ORFNames=PV05_08690 {ECO:0000313|EMBL:KIW53092.1};
OS Exophiala xenobiotica.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=348802 {ECO:0000313|EMBL:KIW53092.1, ECO:0000313|Proteomes:UP000054342};
RN [1] {ECO:0000313|EMBL:KIW53092.1, ECO:0000313|Proteomes:UP000054342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 118157 {ECO:0000313|EMBL:KIW53092.1,
RC ECO:0000313|Proteomes:UP000054342};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala xenobiotica CBS118157.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KN847321; KIW53092.1; -; Genomic_DNA.
DR RefSeq; XP_013313676.1; XM_013458222.1.
DR STRING; 348802.A0A0D2CSV2; -.
DR GeneID; 25330598; -.
DR HOGENOM; CLU_001037_0_0_1; -.
DR OrthoDB; 1222064at2759; -.
DR Proteomes; UP000054342; 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; IPR027417; P-loop_NTPase.
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 SMART; SM00220; S_TKc; 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; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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:UP000054342};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 89..389
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 2150..2273
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 60..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 435..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2278..2422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..79
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..465
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..506
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2319..2364
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2396..2422
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2204
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 2422 AA; 269323 MW; D8F22964FF514157 CRC64;
MDDILGEDLP LPPARLYERL SQVPNYTWDR SFRPFHTSYD HWHVYGILHN PDVGNHRSSL
STLTSLSAPS GSSKSSPKLD THRPSLRHHH WSSMSGASTD SENTSSRDEP EATWQPVVAR
ISTHVVRLER EFQYNQWIMK ECDPDCLHTI RPIEIFKLPT TPGDEQPMIC CVYEAPGKNY
LREVIDFGPA FYGIHDVRQN SDGSPGERIP LQAFLDFAIG ASEALELLHH GAKIVHGEIR
GDSFHWNRET GSVKIANGGN GPRAFENILS SEGWATLSRE IGVKNKLQFI APEQTGRLPA
DPDSRTDIYG LGVLFWILLT GQPAFDADTP IDIIQKVLTH RLPLVTAIRM DIPDVISHII
ARMTQKQMDE RYHSVSGLKY DLLQIQKFLG EGDLGKIRNY KVGQRDVSSF FILPSKQFGR
HSEIERINKI IEKAHKRHSS TGTRHSPSQQ GLLNAASNSS ISDSRADVVE PGEGSDSSSS
FGFRESRSNS TTIGLDGPSF TPAFGSKTNL LGKRAPGPRG GLLDSVSDRD SNLSGGVQST
PEGLPGMMTR RRNSHKYKRR TKTEVITILG PTGVGKTALI KAIQPSIRRH GYFALGRFDR
ARPSPFEPMI KVMASLFRQI FSEKDVNTPY HEHLRAHVTP FWPVLSSMLD LPATLLDVTV
LSKKLLTKGD ATTQSFNTEI TTVDNGNKTA NGLTNHGAWD ANDFLRGPAN TKSIRLINTY
MDVLRTICTG KLICLCLDDL QAAEGESIDL LMHIIKAKVP VVLLLSSRTE DGQIPECTAK
ILDLDSTNKI ELGNLREKHV FEYVAATMSQ SVENVIPLAA VVYAKSEGNP FLVKDILQAC
YQRECLWYDW KASGWQFDLD KIFDEFSSDG SCSDNEYLSR RLQELAPAAR SILAWASLIG
STFSFKLIQQ IMSGDYFYSS GRDQAHDATC PKRAKLFNLS ESDCVNGLQQ LVNMYIITPG
QTDDEFRWTH ARYLKAANEM RECQNTTKMH FIIAQTMMTY LSQCKYNLYP LARHICLSAD
IIKERVPTRM RYRDVLWRGA QKALETGAQP TGLWYYKNAL KLLQDDKWNS DNPDVFYDET
LQLHVNSAEI MYLQREVEEA LALLEETFEH ARCSADKTRS YILKGRILSF KGQFLPAFDA
QRQCLAELGL PMPEKSWEEC DIEFKRLEFR LRELNKEELL SRPLSEDKTV IALGTVLSEA
LGALYWSDAL RWYQLNLAYI TAVLDRGTFV QAGLGFTMLG AAAIGRFKDI ELGLFYGEIA
QDYFTLFDDP WTRGRGWTLF TLFIGHFQTP VRNLLPILDN ALEYSLSSGD RFVSILNIGV
MALSRFWAGQ DLSEVEAFCN YGPEEFDSWE NDRRGGTLLT VTRQVSRALQ GKTGIHDVNT
VLNDEHHDSQ RWLAECDKYA ANARRPRDIY QAVSLLAYHI LGYHEYVVEI GSELLGTTLD
ELWSNRPACG ARFALGLSLM TIAREKPEEE RSPYVEKAKI LKRDIDQWGK ANDVNYFAWS
HMLEAAIADV TGKYSVIISN LEAAVDHCQV HGFALEEALA IEMQAEFLLA RGAKRAGKVM
IQEAITAWNR INASGKAKQL SDKHEWLIKT ATTSRTMEAA TQTEDLHLPM SEEAQAQIKR
DYTSAWVSPK TAITTQAPPD VPGLGLDILD LTSILEFSRV ISSELQINNL LSKMISVILE
SVGGQAEFCA IVIDSEDQGW CVAASADHET GVKTYPDGIP FSEVDDQAAQ QITHYLLRTK
ETVFVQNVLE DDRFSNVGDA YLARNPHGRS IIAIPIIQAD HLMGVIHLEG RPNAFTQRNM
IVLNLLTNQV AISLGNALLY RKVRKVSASN ASMVESQKRA LVAAREAEAK AKKAEAEAMH
NVKLKEEAAK AKSIFLANVS HELRTPLNGV IGMSELLKGT PLSKDQEQYA DSIRVCADTL
LTVINDILDF SKLEAGKMQM FAVPLNLKET ITEVVRALAY TNQEHGLQTI EDLQIDDGLV
LGDPVRLHQI FMNLLSNAYK FTPKGSVTVR ARKNAETRDR VKITCSVADT GIGITKEQLA
RLFQPFSQAD SSTARSYGGS GLGLSICKAM IENVLGGKIW IESTPGVGTT VSFTLNYQKA
PKDSSVQNDM KIAAKDPDPM ANWSQAASPD TEQKNASFCD LTRVPREELR VCIAEDNQIN
RKIAISFVKK IGLSCEAYED GKQAYDALKA KSKEGKPFHL VLMDVQMPVL DGYEATKAIR
ADSDPNVSQV LIIAMTASAI RGDREKCLEA GMNDYLAKPV RQTALKAMLD DYLNNPKLAA
TNNSPTVATP SDKANGLVGE DASKPTKTLV NGDLPSSTGE KPKARRPFGR VMKKVDTSVA
EEKGESKTTD SRPSGKRETD ELGKVTNENV LPKDQVLVEI SAVDGNGELN GPKRESGDSG
ETSVLTQSAL PLNGRAQEGE ST
//
