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Database: UniProt
Entry: A0A0P8BQX4_9CYAN
LinkDB: A0A0P8BQX4_9CYAN
Original site: A0A0P8BQX4_9CYAN 
ID   A0A0P8BQX4_9CYAN        Unreviewed;      1210 AA.
AC   A0A0P8BQX4;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Methyl-accepting chemotaxis protein PixJ {ECO:0000313|EMBL:KPQ36383.1};
GN   Name=pixJ {ECO:0000313|EMBL:KPQ36383.1};
GN   ORFNames=HLUCCA11_05850 {ECO:0000313|EMBL:KPQ36383.1};
OS   Phormidesmis priestleyi Ana.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae;
OC   Phormidesmis.
OX   NCBI_TaxID=1666911 {ECO:0000313|EMBL:KPQ36383.1, ECO:0000313|Proteomes:UP000050465};
RN   [1] {ECO:0000313|EMBL:KPQ36383.1, ECO:0000313|Proteomes:UP000050465}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ana {ECO:0000313|EMBL:KPQ36383.1};
RA   Nelson W.C., Romine M.F., Lindemann S.R.;
RT   "Identification and resolution of microdiversity through metagenomic
RT   sequencing of parallel consortia.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC       family. {ECO:0000256|ARBA:ARBA00029447}.
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:KPQ36383.1}.
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DR   EMBL; LJZR01000006; KPQ36383.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0P8BQX4; -.
DR   STRING; 1666911.HLUCCA11_05850; -.
DR   PATRIC; fig|1666911.3.peg.5090; -.
DR   Proteomes; UP000050465; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR   CDD; cd06225; HAMP; 2.
DR   CDD; cd11386; MCP_signal; 1.
DR   Gene3D; 3.30.450.40; -; 2.
DR   Gene3D; 1.10.8.500; HAMP domain in histidine kinase; 1.
DR   Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR   InterPro; IPR003018; GAF.
DR   InterPro; IPR029016; GAF-like_dom_sf.
DR   InterPro; IPR003660; HAMP_dom.
DR   InterPro; IPR004089; MCPsignal_dom.
DR   InterPro; IPR016132; Phyto_chromo_attachment.
DR   PANTHER; PTHR32089; METHYL-ACCEPTING CHEMOTAXIS PROTEIN MCPB; 1.
DR   PANTHER; PTHR32089:SF119; METHYL-ACCEPTING CHEMOTAXIS PROTEIN TLPQ; 1.
DR   Pfam; PF01590; GAF; 2.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF00015; MCPsignal; 1.
DR   SMART; SM00065; GAF; 2.
DR   SMART; SM00304; HAMP; 2.
DR   SMART; SM00283; MA; 1.
DR   SUPFAM; SSF55781; GAF domain-like; 2.
DR   SUPFAM; SSF158472; HAMP domain-like; 1.
DR   SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 1.
DR   PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
DR   PROSITE; PS50885; HAMP; 2.
DR   PROSITE; PS50046; PHYTOCHROME_2; 2.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|PROSITE-
KW   ProRule:PRU00284}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        124..146
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        433..453
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          455..507
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          538..674
FT                   /note="Phytochrome chromophore attachment site"
FT                   /evidence="ECO:0000259|PROSITE:PS50046"
FT   DOMAIN          710..846
FT                   /note="Phytochrome chromophore attachment site"
FT                   /evidence="ECO:0000259|PROSITE:PS50046"
FT   DOMAIN          879..930
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          935..1171
FT                   /note="Methyl-accepting transducer"
FT                   /evidence="ECO:0000259|PROSITE:PS50111"
FT   REGION          1..92
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        15..38
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        58..92
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1210 AA;  130245 MW;  79A620C7B17F6973 CRC64;
     MTTDVRPPYP PDANENAVNG NTPASLDAAN NGNGVTPQLS IPEEEEAVLS AAPDKTAPDK
     TAPDRTAPDR TAPDKTASDK EYRGVQYNRD SGERYAPEKI EITPNSRSGL FQSFHDLPVA
     DKQLAGLLTS KILSVAGVIG LSLLLLSLNG RRQLFEQAVS ELSATANDLS SAATSGPLLT
     DDALIEAAEY YLNTEVVDAG LAAEAREVLR ATLIAGELEY VSLVGTDTRV IASGGPERQG
     NVFNLDDLVA TALKNGQPET ATSLVTVQAL QQLGVEAPEY ADEAALVRFG VTPVFAGSNV
     EDNAVARGEV IGALVIGDIL DGNSASVVSA LNQFPQGYSA IYRQDPSQGF ARVAVGEIGQ
     SSAEPDVAQQ QFLIDAVSIP VGEVVSERFA GPQGDRFMVA ATPLVDGRGE PVAVVLRGLS
     EDSMRERLSQ NSWLIIGAAM LALLVDVIIA KLLGRSIVKP MRNLQVATEK FASGDRSARA
     VVFARDEVGR VASAFNELAA SVSSSESSLR FQSKTQTEAA RRSQLLSEFT SQIRQTLDVD
     SIMGTAVDRV RAIFDADRVL VYRFNADYSG GDVTAESVGK GWSRAKGEYL EDPMLPKSMA
     RFKTGLISSV EDVDQADLTE CHCRLLKELD VKANMVGPII VGEDLIGLLC VHQCDGPRHW
     DSEELSMMQQ LTTQVGYALA QSRLMQSQKQ AVRREQQLTS LVTSIRETSD RDQIFRLVTR
     QVKLAIESSR VIVYTFDEHW NGTIVAESVD PQWPLALGAQ ITDPCFADSY IEQYTTGRVK
     ATSDIYNAGL TPCHLSQLEP FKVRANLVAP IVVDNRLLGL LIAHECTGPR NWSEVTINFI
     QRAATQLGYA LEQADAVNQK EQALAQNERL FEERVKREGL VQDQLAELLS EVEAAADGNL
     TVRAEVKPGE IGTAADFFNV IVENLRQIVT QVKQSATQVN DSLGQNERAI RQLADEALQQ
     AEQTTLTLDS VSEMTASIHQ VAQQAQEAAA VARSASETAT IGEEAMDLTV SNILAMRQTV
     GQTAKKVKRL GESSQQITKA VLLINQIAQQ TNLLAINAGI EAARAGEAGQ GFAAVAEEVG
     ELATRSASAT EEIERIVDTI QRETNDVVEA IEQSTAQVVE STRRVEDAKS SLNQILAGSQ
     RMDELAGMIS EATGSQVETS TTVSTLMAEI AQLSKRTSES SKQVAEALRQ TVAVAQNLQS
     QVETFVVEEG
//
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