ID A0A448Z4R0_9STRA Unreviewed; 1044 AA.
AC A0A448Z4R0;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:VEU37018.1};
GN ORFNames=PSNMU_V1.4_AUG-EV-PASAV3_0037970
GN {ECO:0000313|EMBL:VEU37018.1};
OS Pseudo-nitzschia multistriata.
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC Bacillariophyceae; Bacillariophycidae; Bacillariales; Bacillariaceae;
OC Pseudo-nitzschia.
OX NCBI_TaxID=183589 {ECO:0000313|EMBL:VEU37018.1, ECO:0000313|Proteomes:UP000291116};
RN [1] {ECO:0000313|EMBL:VEU37018.1, ECO:0000313|Proteomes:UP000291116}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B856 {ECO:0000313|EMBL:VEU37018.1,
RC ECO:0000313|Proteomes:UP000291116};
RA Ferrante I. M.;
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CAACVS010000113; VEU37018.1; -; Genomic_DNA.
DR Proteomes; UP000291116; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00156; REC; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.450.350; CHASE domain; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR006189; CHASE_dom.
DR InterPro; IPR042240; CHASE_sf.
DR InterPro; IPR011006; CheY-like_superfamily.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF03924; CHASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM01079; CHASE; 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 PROSITE; PS50839; CHASE; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000291116};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 68..91
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 447..470
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 235..313
FT /note="CHASE"
FT /evidence="ECO:0000259|PROSITE:PS50839"
FT DOMAIN 646..857
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 923..1040
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 39..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 540..605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 884..914
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..57
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..555
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..575
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 895..913
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 974
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT UNSURE 29
FT /note="D or N"
FT /evidence="ECO:0000313|EMBL:VEU37018.1"
SQ SEQUENCE 1044 AA; 116859 MW; 4EAA2558ECCC11F0 CRC64;
MRKKTASTVS TTTYDDLATI STYTSAGRDR EWXKFVHRGS NRKWSRGQQQ EHQRRRNRGN
RNNTRSSIAG LAGIIVVFGL IAGVVFAMIF LRAENRSRRN EFESGASVTV AKIGDSFDEY
ADVASLIHGR CRHRPRFNAT SFEHNQTSYT EYYNAWSESF RRDFRELYEY IDASGLEFKA
MQFDPNISAL ERPNAESEAG AFYGEHYPEV DYTGFRGFNG DATSLEPRWR NQSFYFPIHY
MEPIRGNEAA IDLDYYSSES RIRAVNALFR TKRPSLTDRL SLVKHEGQVS RCSSGNDDTS
YSGPSFGXVL MHPGVRLSED DETSWPRDFS SIVLCISDLM KRAAIHQNQK VSVYIHDLSH
PXEIDPVFMG AARLDCNSTY SSDENRNHHD GTAMVQXASS FHLLEEVSLY DLDCDDDISC
YQKTISIANR KWTVTVLNEE GPDRIQMVVV AMIGLFVFAA FVGLAVWVVA NDRRNRVYAK
LKSRAAAERN ALVLENANKA AQTERELNDF LAHEVRNPLA AAMAATQFLR TELDRRSRSX
RGIGDHFHDA NTDAEXNMDI DMGEDSDDDD DXDGEEQRNA GVASFSVEKD IDEDENDCSG
AADDNDGLVS SLTRAALHSS GRTEXSPRLV QAREDIRVVD HALHFINDLL RNMLDMNRAA
SKKLKVKFAP ADLLQDVLQP IAGMLHRGGE NIGGGNGVNS KVRIIVDCPE NIIVNTDVLR
LKQVILNLSR NSVKFIDEGF IRLRAEVLER DGDDDLSIDL SSNDFDIEAN TMKSLDSTVK
IYVEDSGSGI PIEKQENLFN KYQESLDLLG QGTGIGLHLC KTLIDLMDGE ISLDPTYCSG
IPGYPGARFV IDLRSSPIGS SVFTPYVDGV RICENDDECI ENDTGGDTEC KKVDTSETTN
TNQKQNQDKG SATTLPELPK HLKVLFIDDD RILRKLFART MKTVAPEWTI REAANGETAI
LLXEEEEFDL IFCDMYMASV EKQLLGTETV AELRANGITS RICGLSANDK ETEFLEAGSD
AFLFKPIPCG KKALRETLQQ VLYG
//
