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Database: UniProt
Entry: A0A1L9QXR0_9CYAN
LinkDB: A0A1L9QXR0_9CYAN
Original site: A0A1L9QXR0_9CYAN 
ID   A0A1L9QXR0_9CYAN        Unreviewed;      1930 AA.
AC   A0A1L9QXR0;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Histidine kinase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=BI308_00310 {ECO:0000313|EMBL:OJJ27454.1};
OS   Roseofilum reptotaenium AO1-A.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Desertifilales; Desertifilaceae;
OC   Roseofilum.
OX   NCBI_TaxID=1925591 {ECO:0000313|EMBL:OJJ27454.1, ECO:0000313|Proteomes:UP000183940};
RN   [1] {ECO:0000313|EMBL:OJJ27454.1, ECO:0000313|Proteomes:UP000183940}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AO1-A {ECO:0000313|EMBL:OJJ27454.1};
RA   Buerger P., Wood-Charlson E.M., Weynberg K.D., Willis B., Van Oppen M.J.;
RT   "CRISPR-Cas defence system in Roseofilum reptotaenium: evidence of a
RT   bacteriophage-cyanobacterium arms race in the coral black band disease.";
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the phytochrome
CC       family. {ECO:0000256|ARBA:ARBA00006402}.
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:OJJ27454.1}.
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DR   EMBL; MLAW01000001; OJJ27454.1; -; Genomic_DNA.
DR   STRING; 1925591.BI308_00310; -.
DR   Proteomes; UP000183940; Unassembled WGS sequence.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00130; PAS; 7.
DR   Gene3D; 3.30.450.40; -; 3.
DR   Gene3D; 3.10.580.10; CBS-domain; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 8.
DR   InterPro; IPR000644; CBS_dom.
DR   InterPro; IPR046342; CBS_dom_sf.
DR   InterPro; IPR003018; GAF.
DR   InterPro; IPR029016; GAF-like_dom_sf.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013656; PAS_4.
DR   InterPro; IPR013655; PAS_fold_3.
DR   InterPro; IPR016132; Phyto_chromo_attachment.
DR   InterPro; IPR011495; Sig_transdc_His_kin_sub2_dim/P.
DR   NCBIfam; TIGR00229; sensory_box; 7.
DR   PANTHER; PTHR41523:SF7; ETHYLENE RESPONSE SENSOR PROTEIN; 1.
DR   PANTHER; PTHR41523; TWO-COMPONENT SYSTEM SENSOR PROTEIN; 1.
DR   Pfam; PF00571; CBS; 1.
DR   Pfam; PF01590; GAF; 3.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF07568; HisKA_2; 1.
DR   Pfam; PF08447; PAS_3; 4.
DR   Pfam; PF08448; PAS_4; 2.
DR   Pfam; PF13426; PAS_9; 2.
DR   SMART; SM00065; GAF; 3.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00086; PAC; 6.
DR   SMART; SM00091; PAS; 8.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF54631; CBS-domain pair; 1.
DR   SUPFAM; SSF55781; GAF domain-like; 3.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 8.
DR   PROSITE; PS51371; CBS; 1.
DR   PROSITE; PS50113; PAC; 6.
DR   PROSITE; PS50112; PAS; 7.
DR   PROSITE; PS50046; PHYTOCHROME_2; 2.
PE   3: Inferred from homology;
KW   CBS domain {ECO:0000256|PROSITE-ProRule:PRU00703};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000183940};
KW   Virulence {ECO:0000256|ARBA:ARBA00023026}.
FT   DOMAIN          17..76
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
FT   DOMAIN          163..299
FT                   /note="Phytochrome chromophore attachment site"
FT                   /evidence="ECO:0000259|PROSITE:PS50046"
FT   DOMAIN          330..401
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          625..695
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          698..745
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          746..816
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          819..871
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          929..964
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          966..1018
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          1019..1093
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          1098..1151
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          1148..1221
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          1224..1276
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          1296..1432
FT                   /note="Phytochrome chromophore attachment site"
FT                   /evidence="ECO:0000259|PROSITE:PS50046"
FT   DOMAIN          1463..1537
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          1539..1591
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   COILED          862..893
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1930 AA;  222744 MW;  A1A393BBCDC32CF8 CRC64;
     MSFASVSFQL PSLESVLDRH PVVVSPDLSV EEAIAFWNRE SPYPYLVVSQ NQQVLGMITV
     SDYHQIRTHW QKWRSVSVER VMTPQGCSLT WQPDLDLLAV TKLMVEEQIE YLPILNLQQN
     IMGVVCAHDL QKSLQDLDAI SVYYGLAQLQ AIHKKSDDRH NIGFQTLLDR TVTEIHQGLK
     CDRVLIYRFE PDGGGTVIAE SVYPLCKSLL GIKIKDSHFG EDLFKAYING RTQVTHDIES
     GGLTPCHVEF LRQIQVKANL VVPILQENHL WGLLTAQQAI APRYWSRNDE AFLKQQADQL
     AICLKQSLPF QDLPTQLREH QWMHYTLEQE KNFTHAILSA VDALVVVVNQ QGEIIYFNNA
     CQRLSGVLEQ QAQGQRFWEF LIPVAEQPQI KHVIGQALQG ESTGAYQCHW VIQGSKKRRI
     EWSNQIFHDR GIVTHAIITG IDLSRRQEAQ IQLRFRDRQQ QTLTYLSQYA ITATDLQSLM
     NEIVQQVAKT LSVDYVEILE LLPNQAAFQM QAAHGFTSCY HHDLHHSIEQ PTLGATKNTQ
     PGYTLSCGQS VIVDDLQIET RFRGAALHNN RRIISSITTI IPGVKQPFGV LGVHSREHRH
     FNPDEVQFLE AIAHLLASFL EQHRLTEELN QFFNLSLDLF CIITFDGSFK RINPRFQGLL
     GYSSHQLQSR SLFDFIHPDD LAATQAQVQQ LASRVPTVNF EHRYRCQDGS YRWIAWTAMP
     TDESYFYAVG RDITERREIE IALKESRKRY VTLATASPVG IFQTDNQGLC LYVNQCWCDM
     TDLSAQEAMM EGWLQTLHPE DSERVFQEWN KAVEEYRPFS SEYRFKHRDG SVVWVMGQAV
     ADVDEEGKIV GYVGSITDIS DRKQAEEALK YLNQTLEDQV AQRTADLETA NEALCYAEER
     FRIALKNAPI TVFNQDVDLR YTWIYNPTLG YTAEAVIGKS DRDLFAPEDA QKLERIKQQA
     LDSQSSVREE VMLTDRGNLK CYDITVDPLS NLENQVIGIT CAVLDITHRK KAELALQENE
     RFIQRIADAS PNILYIYDLE QHKTVYSNKN IALVLGYTPH EVQEMGNIVC EDFLHPEDRP
     KLAQWYQELM NANNTDIWEL EYRMLDRNGE SHWFVSRDTI FTRNAEGKPM QLLGAASDIT
     ERKEVEEQLR LSERAIAASS NGIVIIDAQQ PDFPVISVNP AFERVTGYCA QDIIGKNCRI
     LQGTDREQEG LETIRKALKN EESCTVVLRN YRKDGSLFWN RTTISPIHDD QGILTHYLGI
     QNNITEIKVA EERLLAKVKR EELFGMITQR IRESLDLQEI LRTTVQEVKQ LLLSDRVLVY
     RILPNYTGQV IAEAVNPGWT GTLDKKFPEE TFPRECYDQY LAGKTYAISD VTQTDIRPCL
     VEFLQEFQVK SKIVVPIIQN NLLWGLLIVH QCDRVRDWKE EEIELLKQIA SQLAIAIQQS
     EFYQQLQREL KERIVAETAL LMSQERIQYL LSSSPGILYS LRANDSLELT FVSDNAYDVI
     GYELLEMFEE NFWWTHLHPE DQVKISQHGL KRLFDQGFYS HEYRFLHKDG RYIWIYDKLN
     LVRDEEGNPL EIIGYWIDIT DRKRIEQKLQ ETTSRLTSLI SNLQLGVLVK DEHHKVALIN
     QTFCHLFKTT NCSEQLIGQE WGNIGDEFSH LFDRPEEISQ HHQDIVAHNK IVTNQEIKLA
     DGRILEQNYV PILIDSIDRG HLWMYRDISD RKQAESRLVT SLQEKEILLK EIHHRVKNNL
     LVVSNLLEFQ ADYVSDPTLI KVLEDSRNRI YSMALIHEKL YRSMTLDTIN FGEYLQDLVL
     NLFESYNVED NKVKFYLDIE PVLLNIETAH PCGLIVNELL SNTLKHAFPE EKIGKVEVIM
     YQKDNNQIVV KVADNGIGFP EDLDFRKVDS LGMELVCTLT EQLEGEITLF RDHGTTFELR
     FSELKYRQRV
//
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