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Database: UniProt
Entry: B4WU25_SYNS7
LinkDB: B4WU25_SYNS7
Original site: B4WU25_SYNS7 
ID   B4WU25_SYNS7            Unreviewed;       876 AA.
AC   B4WU25;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   SubName: Full=Globin domain protein {ECO:0000313|EMBL:EDX83240.1};
GN   ORFNames=S7335_420 {ECO:0000313|EMBL:EDX83240.1};
OS   Synechococcus sp. (strain ATCC 29403 / PCC 7335).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=91464 {ECO:0000313|EMBL:EDX83240.1, ECO:0000313|Proteomes:UP000005766};
RN   [1] {ECO:0000313|EMBL:EDX83240.1, ECO:0000313|Proteomes:UP000005766}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29403 / PCC 7335 {ECO:0000313|Proteomes:UP000005766};
RA   Tandeau de Marsac N., Ferriera S., Johnson J., Kravitz S., Beeson K.,
RA   Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the adenylyl cyclase class-3 family.
CC       {ECO:0000256|ARBA:ARBA00005381}.
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DR   EMBL; DS989905; EDX83240.1; -; Genomic_DNA.
DR   RefSeq; WP_006458143.1; NZ_DS989905.1.
DR   AlphaFoldDB; B4WU25; -.
DR   STRING; 91464.S7335_420; -.
DR   eggNOG; COG1017; Bacteria.
DR   eggNOG; COG2114; Bacteria.
DR   eggNOG; COG5000; Bacteria.
DR   HOGENOM; CLU_015967_0_0_3; -.
DR   OrthoDB; 315417at2; -.
DR   Proteomes; UP000005766; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004016; F:adenylate cyclase activity; IEA:UniProt.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0019825; F:oxygen binding; IEA:InterPro.
DR   GO; GO:0009190; P:cyclic nucleotide biosynthetic process; IEA:InterPro.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   CDD; cd07302; CHD; 1.
DR   CDD; cd06225; HAMP; 1.
DR   CDD; cd12131; HGbI-like; 1.
DR   Gene3D; 1.10.490.10; Globins; 1.
DR   Gene3D; 1.10.8.500; HAMP domain in histidine kinase; 1.
DR   Gene3D; 3.30.70.1230; Nucleotide cyclase; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 1.
DR   InterPro; IPR001054; A/G_cyclase.
DR   InterPro; IPR000971; Globin.
DR   InterPro; IPR009050; Globin-like_sf.
DR   InterPro; IPR012292; Globin/Proto.
DR   InterPro; IPR003660; HAMP_dom.
DR   InterPro; IPR029787; Nucleotide_cyclase.
DR   PANTHER; PTHR45655; GUANYLATE CYCLASE SOLUBLE SUBUNIT BETA-2; 1.
DR   PANTHER; PTHR45655:SF13; SOLUBLE GUANYLATE CYCLASE GCY-35-RELATED; 1.
DR   Pfam; PF00042; Globin; 1.
DR   Pfam; PF00211; Guanylate_cyc; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   SMART; SM00044; CYCc; 1.
DR   SMART; SM00304; HAMP; 1.
DR   SUPFAM; SSF46458; Globin-like; 1.
DR   SUPFAM; SSF158472; HAMP domain-like; 1.
DR   SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR   PROSITE; PS01033; GLOBIN; 1.
DR   PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
DR   PROSITE; PS50885; HAMP; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005766};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        17..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        423..444
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          445..497
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          537..664
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
FT   DOMAIN          713..844
FT                   /note="Globin family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS01033"
SQ   SEQUENCE   876 AA;  97607 MW;  BBC97548C1092741 CRC64;
     MKVQIPLIHQ LTFKSKLILL TLFASISSVI VIAILSIGLS RRGLRQAAFS QLNVLRSEQA
     EQVQNYFQQL QSHTLTLSAN RAIVVAMVEF NKEFRRLDRQ FIPTEWDEPL KRYYEANYFP
     RLSDITGSEP RFGSYRPSGQ AARYLQHYYL SQNDYLDAEK NQLITADDDS EYSRYHSEFH
     PLLNDIAQQF GYADLYLINQ KTGDIVYSVN KRPDYGTNLE TGAYRDSSLA DLVATVRESS
     ARGEVAIADF APYEPASGVP SLFIASPIYN GPYVVGILAI RLETDQISQL MTETLTEDTP
     STSLDSYLVG ADGSLRSEPQ FFRDSLSKDD IQSYTRRLRR QGVSDETLAA ITRLESPVLL
     QPVKAAAAQS AIGGATDTER LQDYRGVSVL SAYAPLEIEG LDWAVISQID TAEAFATLTH
     LELAILVASI LLITAFTFLA MAAATMTIQP VRQLNEWADR VVDGDFEAEI DLDLEDEIGQ
     LTDTLQIMVT SLSHQVATLD QKMAQNEVLL TNLVPPAIAK RLKRGETIIA DQIRQITVIY
     ANIVGISELS QTLSPEEVTA LLTKLMQAFD DVGEQHGMER QNTPSVDYMA ICGLTTARLD
     HTKRTVDFAL EMLKIINLPE FGQSFALGLR LAVHTGPVTA GVVGTKRFGY SVWGESIYLV
     TRLYAHAALN SVVLTEAAYQ QIAETYTCVA AGAVAIEKFG RVETWILATR EKLAVRQVEL
     VQRSFAKVEP ISEQVGKLFY EHLFETRPDF KPLFSSTDME TQQRKLMMTL ATAVEGLRHP
     EEIISKVQAL GRSHQGYGVK AEDYEAIGAT LLWTLKEKLG DDFTPEVKRA WEVAFQFLSK
     IMINAAAQIE SDTQAGTELE TEPTTELEIE LKGIEV
//
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