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Database: UniProt
Entry: A0A1H4LZK1_9BACL
LinkDB: A0A1H4LZK1_9BACL
Original site: A0A1H4LZK1_9BACL 
ID   A0A1H4LZK1_9BACL        Unreviewed;       584 AA.
AC   A0A1H4LZK1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   SubName: Full=Adenylate cyclase {ECO:0000313|EMBL:SEB76199.1};
GN   ORFNames=SAMN05443246_1822 {ECO:0000313|EMBL:SEB76199.1};
OS   Paenibacillus sp. GP183.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1882751 {ECO:0000313|EMBL:SEB76199.1, ECO:0000313|Proteomes:UP000199177};
RN   [1] {ECO:0000313|EMBL:SEB76199.1, ECO:0000313|Proteomes:UP000199177}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GP183 {ECO:0000313|EMBL:SEB76199.1,
RC   ECO:0000313|Proteomes:UP000199177};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FNSW01000001; SEB76199.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H4LZK1; -.
DR   STRING; 1882751.SAMN05443246_1822; -.
DR   Proteomes; UP000199177; 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:0009190; P:cyclic nucleotide biosynthetic process; IEA:InterPro.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   CDD; cd07302; CHD; 1.
DR   Gene3D; 3.30.70.1230; Nucleotide cyclase; 1.
DR   InterPro; IPR001054; A/G_cyclase.
DR   InterPro; IPR007890; CHASE2.
DR   InterPro; IPR029787; Nucleotide_cyclase.
DR   PANTHER; PTHR43081:SF16; ADENYLATE CYCLASE, TERMINAL-DIFFERENTIATION SPECIFIC; 1.
DR   PANTHER; PTHR43081; ADENYLATE CYCLASE, TERMINAL-DIFFERENTIATION SPECIFIC-RELATED; 1.
DR   Pfam; PF05226; CHASE2; 1.
DR   Pfam; PF00211; Guanylate_cyc; 1.
DR   SMART; SM01080; CHASE2; 1.
DR   SMART; SM00044; CYCc; 1.
DR   SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR   PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199177};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..584
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5038664156"
FT   TRANSMEM        283..301
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        308..327
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        339..358
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          399..531
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
SQ   SEQUENCE   584 AA;  65178 MW;  5C36F63271EAE4FE CRC64;
     MVLLCSLLFL SGALSTISNS LFDFNMKNGM SHAPAGDILL VTIDTESLQK LGPYPWDRKL
     YSDLIQKLED GGAKAIAFDI ELYTQSNNPA SDALVSAISK KYNNIIFPSH ADLEGTISRS
     TIVQKGKLIH TDKIVTPLAD FKTVPAHINA VFDPDGVIRR TWLQIDTPQG VYSSFALKLA
     EMAGADIKPF LNAQPTGDRP KTETLIKYDA VQKDFENVSY HKVLEGTVPS KIFKDRIVLV
     GYTAPGSDQG ITPIENHMNL VYAHANILNQ ILAGELITFT SDMWLFLIMI LLALIAGYFT
     WRLKSSIWSV VLVFLIVIVL LVAQYYLYVN NTLIFDATYP LTAVILAYLV NIAIKTYFET
     KNKNFITKQF GRYISPELVK EIASNDREIE LGGINKELSI LFLDIRGFTT LSEKLQPAEV
     VDFLNTMFNL ITEKALENHG TIDKFIGDAA MILFNAPLDV PNHEYYAVKT AYDIQRGMED
     VRNRIKEKYN VVVSVGIGIN TGEVVVGNIG SYLRVDYTAI GDNVNIAARI ESNTTAHQIL
     VSESTYDRTK EHFEYNFAGE KMMKGKTVAL KLFEVTELKS PLSN
//
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