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Database: UniProt
Entry: B4PWP1_DROYA
LinkDB: B4PWP1_DROYA
Original site: B4PWP1_DROYA 
ID   B4PWP1_DROYA            Unreviewed;      1489 AA.
AC   B4PWP1;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 2.
DT   27-MAR-2024, entry version 81.
DE   RecName: Full=adenylate cyclase {ECO:0000256|ARBA:ARBA00012201};
DE            EC=4.6.1.1 {ECO:0000256|ARBA:ARBA00012201};
DE   Flags: Fragment;
GN   Name=Dyak\GE16042 {ECO:0000313|EMBL:EDX01787.2};
GN   ORFNames=Dyak_GE16042 {ECO:0000313|EMBL:EDX01787.2};
OS   Drosophila yakuba (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7245 {ECO:0000313|EMBL:EDX01787.2, ECO:0000313|Proteomes:UP000002282};
RN   [1] {ECO:0000313|EMBL:EDX01787.2, ECO:0000313|Proteomes:UP000002282}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tai18E2 / Tucson 14021-0261.01
RC   {ECO:0000313|Proteomes:UP000002282};
RX   PubMed=17994087; DOI=10.1038/nature06341;
RG   Drosophila 12 genomes consortium;
RA   Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B., Markow T.A.,
RA   Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., Pollard D.A., Sackton T.B.,
RA   Larracuente A.M., Singh N.D., Abad J.P., Abt D.N., Adryan B., Aguade M.,
RA   Akashi H., Anderson W.W., Aquadro C.F., Ardell D.H., Arguello R.,
RA   Artieri C.G., Barbash D.A., Barker D., Barsanti P., Batterham P.,
RA   Batzoglou S., Begun D., Bhutkar A., Blanco E., Bosak S.A., Bradley R.K.,
RA   Brand A.D., Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C.,
RA   Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S.,
RA   Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A.,
RA   Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A., Daub J.,
RA   David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., Edwards K.,
RA   Eickbush T., Evans J.D., Filipski A., Findeiss S., Freyhult E., Fulton L.,
RA   Fulton R., Garcia A.C., Gardiner A., Garfield D.A., Garvin B.E., Gibson G.,
RA   Gilbert D., Gnerre S., Godfrey J., Good R., Gotea V., Gravely B.,
RA   Greenberg A.J., Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A.,
RA   Haerty W., Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V.,
RA   Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A., Hubisz M.J.,
RA   Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., Jeck W.R.,
RA   Johnson J., Jones C.D., Jordan W.C., Karpen G.H., Kataoka E.,
RA   Keightley P.D., Kheradpour P., Kirkness E.F., Koerich L.B., Kristiansen K.,
RA   Kudrna D., Kulathinal R.J., Kumar S., Kwok R., Lander E., Langley C.H.,
RA   Lapoint R., Lazzaro B.P., Lee S.J., Levesque L., Li R., Lin C.F., Lin M.F.,
RA   Lindblad-Toh K., Llopart A., Long M., Low L., Lozovsky E., Lu J., Luo M.,
RA   Machado C.A., Makalowski W., Marzo M., Matsuda M., Matzkin L.,
RA   McAllister B., McBride C.S., McKernan B., McKernan K., Mendez-Lago M.,
RA   Minx P., Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E.,
RA   Negre B., Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L.,
RA   Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S., Pesole G.,
RA   Phillippy A.M., Ponting C.P., Pop M., Porcelli D., Powell J.R.,
RA   Prohaska S., Pruitt K., Puig M., Quesneville H., Ram K.R., Rand D.,
RA   Rasmussen M.D., Reed L.K., Reenan R., Reily A., Remington K.A.,
RA   Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., Rohde C., Rozas J.,
RA   Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., Sanchez-Gracia A.,
RA   Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., Schlenke T.,
RA   Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., Sisneros N.B.,
RA   Smith C.D., Smith T.F., Spieth J., Stage D.E., Stark A., Stephan W.,
RA   Strausberg R.L., Strempel S., Sturgill D., Sutton G., Sutton G.G., Tao W.,
RA   Teichmann S., Tobari Y.N., Tomimura Y., Tsolas J.M., Valente V.L.,
RA   Venter E., Venter J.C., Vicario S., Vieira F.G., Vilella A.J.,
RA   Villasante A., Walenz B., Wang J., Wasserman M., Watts T., Wilson D.,
RA   Wilson R.K., Wing R.A., Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G.,
RA   Yamamoto D., Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E.,
RA   Zhang P., Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA   Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA   Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA   Bayul T., Berlin A., Bessette D., Bloom T., Blye J., Boguslavskiy L.,
RA   Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA   Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA   D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA   Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA   Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA   Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA   Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA   Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA   Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA   Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA   Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA   Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA   McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA   Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA   Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA   Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA   Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA   Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA   Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA   Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA   Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA   Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA   Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA   Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA   Chin C., Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.;
RT   "Evolution of genes and genomes on the Drosophila phylogeny.";
RL   Nature 450:203-218(2007).
RN   [2] {ECO:0000313|EMBL:EDX01787.2, ECO:0000313|Proteomes:UP000002282}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tai18E2 / Tucson 14021-0261.01
RC   {ECO:0000313|Proteomes:UP000002282};
RX   PubMed=17550304; DOI=10.1371/journal.pbio.0050152;
RA   Ranz J.M., Maurin D., Chan Y.S., von Grotthuss M., Hillier L.W., Roote J.,
RA   Ashburner M., Bergman C.M.;
RT   "Principles of genome evolution in the Drosophila melanogaster species
RT   group.";
RL   PLoS Biol. 5:E152-E152(2007).
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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; CM000162; EDX01787.2; -; Genomic_DNA.
DR   RefSeq; XP_002100679.2; XM_002100643.2.
DR   SMR; B4PWP1; -.
DR   EnsemblMetazoa; FBtr0262560; FBpp0261052; FBgn0233593.
DR   GeneID; 6524839; -.
DR   KEGG; dya:Dyak_GE16042; -.
DR   eggNOG; KOG3618; Eukaryota.
DR   HOGENOM; CLU_001072_12_1_1; -.
DR   OrthoDB; 3686360at2759; -.
DR   Proteomes; UP000002282; Chromosome X.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004016; F:adenylate cyclase activity; IEA:RHEA.
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; 2.
DR   InterPro; IPR001054; A/G_cyclase.
DR   InterPro; IPR029787; Nucleotide_cyclase.
DR   PANTHER; PTHR45627; ADENYLATE CYCLASE TYPE 1; 1.
DR   PANTHER; PTHR45627:SF8; ADENYLATE CYCLASE TYPE 9; 1.
DR   Pfam; PF00211; Guanylate_cyc; 2.
DR   SMART; SM00044; CYCc; 1.
DR   SUPFAM; SSF55073; Nucleotide cyclase; 2.
DR   PROSITE; PS50125; GUANYLATE_CYCLASE_2; 2.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:EDX01787.2};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        97..115
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        127..146
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        158..176
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        265..288
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1140..1159
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1216..1238
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1250..1269
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1276..1296
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1324..1342
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          375..502
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
FT   DOMAIN          1404..1489
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
FT   REGION          661..692
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          721..745
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          843..966
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1172..1199
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        672..688
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        726..745
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        843..864
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        882..926
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        940..966
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1180..1195
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1489
FT                   /evidence="ECO:0000313|EMBL:EDX01787.2"
SQ   SEQUENCE   1489 AA;  164344 MW;  EBFC242BE9E3826D CRC64;
     MSESRRQSVS SRAMPPGVLV NDSRANSTDD IQIALAPHIQ TYLSQTGRRH SCCSVMLPVA
     FERAAAKSWL DPKFDSPVLE EQYQASVFPH IRMRYRFTLS YILLCSLMWC LYFVVDGGSE
     DFWRPISSSF SMLSLVTIMA LCFTHWDLYR EHRTVTSALT ALLLCGASLA FLTYTGRAFS
     PLGHFAICLE IVLLIYTALP MPLWLGASTA ISYSIAFEMV SHMVIGCSAI HGGPMHGGAG
     EAAGSAGSAG GSGVEANGDP SNRILILRIM AHLSVHLVGV HVLIMNLVRM RGTFMKVGQN
     LLVRRQLEME KQLKEKMIHS VMPPKVADML LNEGGPSGLD ASGLPPESHY MRPRASNDVK
     SLFRPFHMHS MENVSILFAD IVGFTRMSST KTAEQLVEIL NDLFERFDDL CSLSGCEKIS
     TLGDCYYCVS GCPEPRADHA ICCVEMGLGM IDAMRCFDAQ RHEGVKMRVG VHTGTVLCGI
     VGTRRVKFDV WSNDVSLANK MESSGKPEQV HISQETSSFL GDAYYLEEGE EVFGHRTYFV
     VGRRRDFTRT NSLSPSMPAN ATGSSLLLPG AHGASLSQSA TNVSVVQPNV PPASPVGQLS
     SSLNPSPVLS MRPRLTSLSM KMRKKSQNRD RDVERGIIHP AAAGVPPVIV VRERPKIIIT
     TKSLPGSLDS DEQPPVSPPL PPPANPPATE TRSKIKLKVW KIPRFLKRFE DLTNRSSCGS
     ISSAAQLEKE REREREKEEL HHQNQLNPEE TLAFMDNQMQ NGNGCGYQQL PVLVESNHRT
     QTLDIPAARP VLHHAATSTA LASSVLRSPE AGVSGGGGCC SPGQFSMYDD IIDVRSYISQ
     SRSDISPFGR SGSYRSQCGR QSTGGVNGAG GAAGVGTEGR AGTSQAAPQV EQSPLPRPRA
     STLATGRPTP NSLEPGTSST SPCCLPAPGN SGGCGGIYPP THSRQSSICP SATSRKDSGI
     KSNSRRSSIQ QQIYALNQTA ISQHRVSGYF TSSTSSISNL GEVQGLGLPL AVQPPPPLLM
     PACSSQMADP LAACLQQLRK QSDLQLIRCV RDNARSQRSY LVKPPLRKFS LYFKSRQLER
     DFRSKAHRFG AENETEGPPT LATPRYNTYI DIFVGIAVYL CISVSLFLMT QNTVSPSFRL
     WVTLFSCFTG IQVFALFLFT RQMCRRQSGS NVSNRFRSKS TTSEDLEREE RGGGPGGTPH
     FESCADRIFE AISSWYPWHI CLAVLMAMPV LLIIANFLLL DLEQLEAFEY HYGFLIFVCI
     VHFCNFTQLN CWVRNVLAFL AALCFIGIAV SQLMVYSHNR SDQQQDQDQE ASNFIQEIKW
     FQDYHVEIYL DLLLILVLVW FLNREFEIGY RLTFYGNAVA NQDKVRVQNM KNQADMLLHN
     IIPKHVAEHL KNTAKYSENH HNIAIIFASI VNFNEMYDES YLGGKEFLRV LNELIGDFDE
     LLSRPEFRAV EKIKTIGSTF MAASGLDPSH RGTGNEHIHP LIEFSIAKQ
//
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