ID A0A0C1R3S1_9CYAN Unreviewed; 894 AA.
AC A0A0C1R3S1;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE SubName: Full=PAS domain-containing protein {ECO:0000313|EMBL:KAF3889660.1};
GN ORFNames=DA73_0237600 {ECO:0000313|EMBL:KIE06945.1}, DA73_0400032450
GN {ECO:0000313|EMBL:KAF3889660.1};
OS Tolypothrix bouteillei VB521301.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Tolypothrichaceae;
OC Tolypothrix.
OX NCBI_TaxID=1479485 {ECO:0000313|EMBL:KIE06945.1};
RN [1] {ECO:0000313|EMBL:KIE06945.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=VB521301 {ECO:0000313|EMBL:KIE06945.1};
RX PubMed=25700407;
RA Chandrababunaidu M.M., Singh D., Sen D., Bhan S., Das S., Gupta A.,
RA Adhikary S.P., Tripathy S.;
RT "Draft Genome Sequence of Tolypothrix boutellei Strain VB521301.";
RL Genome Announc. 3:e00001-15(2015).
RN [2] {ECO:0000313|EMBL:KAF3889660.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=VB521301 {ECO:0000313|EMBL:KAF3889660.1};
RA Sarangi A.N., Mukherjee M., Ghosh S., Singh D., Das A., Kant S., Prusty A.,
RA Tripathy S.;
RT "Improved Assembly of Tolypothrix boutellei genome.";
RL Submitted (NOV-2019) 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:KIE06945.1}.
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DR EMBL; JHEG04000001; KAF3889660.1; -; Genomic_DNA.
DR EMBL; JHEG02000059; KIE06945.1; -; Genomic_DNA.
DR RefSeq; WP_050046606.1; NZ_JHEG04000001.1.
DR AlphaFoldDB; A0A0C1R3S1; -.
DR STRING; 1479485.DA73_0237600; -.
DR OrthoDB; 419276at2; -.
DR Proteomes; UP000029738; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR004089; MCPsignal_dom.
DR InterPro; IPR005330; MHYT_dom.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR016132; Phyto_chromo_attachment.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR32089:SF92; LYSOZYME-LIKE PROTEIN-RELATED; 1.
DR PANTHER; PTHR32089; METHYL-ACCEPTING CHEMOTAXIS PROTEIN MCPB; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF00015; MCPsignal; 1.
DR Pfam; PF03707; MHYT; 2.
DR Pfam; PF13426; PAS_9; 1.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00283; MA; 1.
DR SMART; SM00086; PAC; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50924; MHYT; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50046; PHYTOCHROME_2; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|PROSITE-ProRule:PRU00244};
KW Reference proteome {ECO:0000313|Proteomes:UP000029738};
KW Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|PROSITE-
KW ProRule:PRU00284}; Transmembrane {ECO:0000256|PROSITE-ProRule:PRU00244};
KW Transmembrane helix {ECO:0000256|PROSITE-ProRule:PRU00244}.
FT TRANSMEM 6..28
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00244"
FT TRANSMEM 40..66
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00244"
FT TRANSMEM 78..96
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00244"
FT TRANSMEM 103..124
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00244"
FT TRANSMEM 139..161
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00244"
FT TRANSMEM 173..196
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00244"
FT TRANSMEM 216..239
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00244"
FT DOMAIN 5..197
FT /note="MHYT"
FT /evidence="ECO:0000259|PROSITE:PS50924"
FT DOMAIN 275..410
FT /note="Phytochrome chromophore attachment site"
FT /evidence="ECO:0000259|PROSITE:PS50046"
FT DOMAIN 436..503
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 504..558
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 561..612
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 617..853
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
FT COILED 549..580
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 894 AA; 97729 MW; 8A16B5089EE35C76 CRC64;
MNGTYNQNLV ALSIAIAVFA SYTGLNLAGH MSAVSKKVRI AWLIGGAIAI GIGIWSMHFV
AMLALYLPTP ISYDLGKVLF SILPAILASG AALFLVSCPI LGFGRLLIGG VLMGLGIACM
HYTGMGAMQM AVNTQYDPLW FAGSLIIAVA ASITALWLGF YTRKTKAGSF IKISSAIAMG
IAISGMHYTG MAGASFTPNK LAQTVSFVQD VQTDDTLLGI CLGLATFIIL GFTLLTSLVD
RHLYTQTKIL KQQQADALRS QQFTDMTLRI RRWLSLDDVL NTAVNEIRQA LDIDRVIIYR
FKPDWSGTIV AESVTRTWMR TIGKTLNDPM NEHCRELYKN GRVRATNNIY EAGFTDCHRE
ILENLQVKAN VVAPIVINDA LVGLLCAHQC SGFRKWQQSE VDLFGQLAIQ VSIAIEHANL
LHELRQAQEV LWLRDRAIAA ASNAIIITDA RQSDNPIIFC NTAFENITGY SSQEVMGRNC
RFLQGRDTDP ATVGEIRNAL QQRRDCQVII KNYRKDGTPF WNQLTVSPVK DASGQVSHFI
GVQADITERM QAQQELESSK ETLQRQVVEL LNDVQEAAKG DLTVRAEITP GEIGVIADFF
NLIIESLQQI VISVKNTARQ VNVSVGDNSE AMHELADEAL QQAEEINYIL ESLDSMALSI
QDVADNAHKA TEMARSASTT AKAGRNAMEH TVNNIMNLRL TISETAKKVK RLGEASQEIT
KVVSMINQIA LQTNVLSINT SIEAAKVGVE GQAFTVVAEE IGGLALRASQ ATKDIEQIVD
NIQLEARAAI KAVEQGLTQV VDGTECVQDA KLQLGEILDV SCQIDNLLHS ISNTTVSQAA
TSQAVVCLMK QIADSSLRTS DLSRQVSTSL LQTVEMAQEF QASVGVFKTE RVRR
//
