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Database: UniProt
Entry: A0A3Q3BY55_HAPBU
LinkDB: A0A3Q3BY55_HAPBU
Original site: A0A3Q3BY55_HAPBU 
ID   A0A3Q3BY55_HAPBU        Unreviewed;       323 AA.
AC   A0A3Q3BY55;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=adenylate cyclase {ECO:0000256|ARBA:ARBA00012201};
DE            EC=4.6.1.1 {ECO:0000256|ARBA:ARBA00012201};
OS   Haplochromis burtoni (Burton's mouthbrooder) (Chromis burtoni).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Haplochromini; Haplochromis.
OX   NCBI_TaxID=8153 {ECO:0000313|Ensembl:ENSHBUP00000009051.1, ECO:0000313|Proteomes:UP000264840};
RN   [1] {ECO:0000313|Ensembl:ENSHBUP00000009051.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP = 3',5'-cyclic AMP + diphosphate; Xref=Rhea:RHEA:15389,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58165; EC=4.6.1.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001593};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   AlphaFoldDB; A0A3Q3BY55; -.
DR   Ensembl; ENSHBUT00000000903.1; ENSHBUP00000009051.1; ENSHBUG00000010620.1.
DR   GeneTree; ENSGT00940000167206; -.
DR   Proteomes; UP000264840; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004016; F:adenylate cyclase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; IPR032628; AC_N.
DR   InterPro; IPR029787; Nucleotide_cyclase.
DR   PANTHER; PTHR45627:SF15; ADENYLATE CYCLASE; 1.
DR   PANTHER; PTHR45627; ADENYLATE CYCLASE TYPE 1; 1.
DR   Pfam; PF16214; AC_N; 1.
DR   Pfam; PF00211; Guanylate_cyc; 1.
DR   SMART; SM00044; CYCc; 1.
DR   SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR   PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Reference proteome {ECO:0000313|Proteomes:UP000264840}.
FT   DOMAIN          84..211
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
SQ   SEQUENCE   323 AA;  37210 MW;  791FE82353EC5C92 CRC64;
     MYQSGLFIHY LTDHAQRQVF LETRRCIEGR LKLEQENQRQ DRLVLSILPR FVALEMIADM
     SAMEDDLNPQ EFHKIYIHQY KDVSILFADI KGFTLLSMNL SAQDLVRTLN ELFGRFDRLA
     EEHHCLRIKI LGDCYYCVSG VPEPQRAHAR YCVEMGLAMI NTIRYVQKQL NFDMDMRIGI
     HSGSVLCGVL GLQKWHFDVW SWDVGIANML EAGGIPGRIH ISRATLDCLE GTYKTEEGHG
     RDRNAFLRKY NIDTFLICTQ QDRDKVNHIK PPKVQKPIQT WSPDMPFKTV VDMNSVSAQI
     PNRKEGAEFG AFGQVVTNLN CII
//
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