ID M2PD77_CERS8 Unreviewed; 1696 AA.
AC M2PD77;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Adenylate cyclase {ECO:0000256|ARBA:ARBA00021420};
DE EC=4.6.1.1 {ECO:0000256|ARBA:ARBA00012201};
DE AltName: Full=ATP pyrophosphate-lyase {ECO:0000256|ARBA:ARBA00032597};
DE AltName: Full=Adenylyl cyclase {ECO:0000256|ARBA:ARBA00032637};
GN ORFNames=CERSUDRAFT_87049 {ECO:0000313|EMBL:EMD33719.1};
OS Ceriporiopsis subvermispora (strain B) (White-rot fungus) (Gelatoporia
OS subvermispora).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Gelatoporiaceae; Gelatoporia.
OX NCBI_TaxID=914234 {ECO:0000313|EMBL:EMD33719.1, ECO:0000313|Proteomes:UP000016930};
RN [1] {ECO:0000313|EMBL:EMD33719.1, ECO:0000313|Proteomes:UP000016930}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B {ECO:0000313|EMBL:EMD33719.1,
RC ECO:0000313|Proteomes:UP000016930};
RX PubMed=22434909; DOI=10.1073/pnas.1119912109;
RA Fernandez-Fueyo E., Ruiz-Duenas F.J., Ferreira P., Floudas D.,
RA Hibbett D.S., Canessa P., Larrondo L.F., James T.Y., Seelenfreund D.,
RA Lobos S., Polanco R., Tello M., Honda Y., Watanabe T., Watanabe T.,
RA Ryu J.S., Kubicek C.P., Schmoll M., Gaskell J., Hammel K.E., St John F.J.,
RA Vanden Wymelenberg A., Sabat G., Splinter BonDurant S., Syed K.,
RA Yadav J.S., Doddapaneni H., Subramanian V., Lavin J.L., Oguiza J.A.,
RA Perez G., Pisabarro A.G., Ramirez L., Santoyo F., Master E., Coutinho P.M.,
RA Henrissat B., Lombard V., Magnuson J.K., Kuees U., Hori C., Igarashi K.,
RA Samejima M., Held B.W., Barry K.W., LaButti K.M., Lapidus A.,
RA Lindquist E.A., Lucas S.M., Riley R., Salamov A.A., Hoffmeister D.,
RA Schwenk D., Hadar Y., Yarden O., de Vries R.P., Wiebenga A., Stenlid J.,
RA Eastwood D., Grigoriev I.V., Berka R.M., Blanchette R.A., Kersten P.,
RA Martinez A.T., Vicuna R., Cullen D.;
RT "Comparative genomics of Ceriporiopsis subvermispora and Phanerochaete
RT chrysosporium provide insight into selective ligninolysis.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:5458-5463(2012).
CC -!- FUNCTION: Plays essential roles in regulation of cellular metabolism by
CC catalyzing the synthesis of a second messenger, cAMP.
CC {ECO:0000256|ARBA:ARBA00003896}.
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-3 family.
CC {ECO:0000256|ARBA:ARBA00005381}.
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DR EMBL; KB445805; EMD33719.1; -; Genomic_DNA.
DR STRING; 914234.M2PD77; -.
DR HOGENOM; CLU_000430_1_1_1; -.
DR OrthoDB; 1698689at2759; -.
DR Proteomes; UP000016930; Unassembled WGS sequence.
DR GO; GO:0004016; F:adenylate cyclase activity; IEA:UniProtKB-EC.
DR GO; GO:0006171; P:cAMP biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR CDD; cd07302; CHD; 1.
DR CDD; cd00143; PP2Cc; 1.
DR CDD; cd17214; RA_CYR1_like; 1.
DR Gene3D; 3.30.70.1230; Nucleotide cyclase; 1.
DR Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 3.
DR InterPro; IPR001054; A/G_cyclase.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR InterPro; IPR036457; PPM-type-like_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR InterPro; IPR000159; RA_dom.
DR PANTHER; PTHR48051; -; 1.
DR PANTHER; PTHR48051:SF45; LEUCINE-RICH REPEAT-CONTAINING PROTEIN 10B; 1.
DR Pfam; PF00211; Guanylate_cyc; 1.
DR Pfam; PF13516; LRR_6; 2.
DR Pfam; PF13855; LRR_8; 3.
DR Pfam; PF00481; PP2C; 1.
DR SMART; SM00044; CYCc; 1.
DR SMART; SM00364; LRR_BAC; 9.
DR SMART; SM00369; LRR_TYP; 8.
DR SMART; SM00332; PP2Cc; 1.
DR SUPFAM; SSF52058; L domain-like; 2.
DR SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR SUPFAM; SSF52075; Outer arm dynein light chain 1; 1.
DR SUPFAM; SSF81606; PP2C-like; 1.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
DR PROSITE; PS51450; LRR; 3.
DR PROSITE; PS51746; PPM_2; 1.
DR PROSITE; PS50200; RA; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW cAMP biosynthesis {ECO:0000256|ARBA:ARBA00022998};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000016930};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 285..376
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 1013..1289
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT DOMAIN 1345..1481
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT REGION 1..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 136..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1696 AA; 188790 MW; 8C208A8ECD6C30C6 CRC64;
MPSLGLSTTR LSDVGSEHTV SSNGGGSLRP LRQPSELRKP KSSLNIISNI IRKRSRSRLR
SETSLPPEEA PPLPSPDHFT TSFPSIQSPP TPVSRKEKLR GKKRTATAPP PTPPAAPQSV
RPIVDIKLDE MDGIIDFSAI PTGPADASPP SSAFDSQQSS SDVSSMHPTA GSSTIFINPF
GPSSGRKLAP GGNSYDNRKI SPKTRVPPQN GGKEGDEDSP SWAPPESWAV ETGGVEAEDP
DYSSSNDSEG VPAISPGMNG TRSRRKRPKK LSVIGEKPAA YSSKTKYKIR IHRADNTYHV
VSITLDVTVG ELTPQLNKKL LLDPERETHR LYLKERGRER VLAQTERPAD IVRRRLEQAG
YDVMDGLDLL GADDIHFLMK FVYKSNVLGM ADEEIKFDTF DLVDLTGRSL RTVPIVLYPN
ADGIVSLNLS RNPMLEIPLD FIQACSTLRE LRLSHMAMKK VPQSVRHCRS LHRLDISCNR
IADLDDAGLD YIPELRSLKV QNNRMEKLPW YFPRLRALKD LNISNNKFRR LPAVVSEITS
LVDLDISFNM IESLPEEIGQ LLSLERLIIV GNQVSKFPYE VSRLQKLRML DCRRNSISDI
SLVCMLPQVE QIFTDYNSIH ALELSFGPSL QLLDASNNDI TQLTLVPGPL GQPYKLTSLD
ISWAKLSSLD ELALAQLAAL QTLRVDHNSL KSLPDTIGSL TKLRHLSCSN NQLYALPTSI
GKLQRLEVLE AHNNDLAELP ETLWNCASLQ RINATSNLIS SWPLLSPQNT AVSSGSISVE
PVSTTTRLIY PERKGSSASS ITGRFVPPLA HSLEKLYLGE NQLTDVVLHP LALLKELRVL
NLSFNDIQEV PPTFFKSFIH LRELYLSGNN IRVIPVDDFH YLRKLDVLFL NGNKLQTLPS
ALGQLKNLAV LDVGSNELRY NIHNWEFDWN WNTNPTLRYL NLSGNKRLQI KPDKGHRLSR
DHAEPRARSD FSELKDLKIL GLMDVTTAMA ENIPDENETR RVRTSSTDVI GLAYGIADTL
GKTESINMLD LVQPQFRDKK NEAVFAMFGR PSHSGSNPSL NKFLHDKFLA VFQEELCKLK
QQKGEEVGDA LRRAFLRLNK NLHDHLYSAN GQRKMSHVST GTSAGIVHEM SRDRTGASAI
VLYLVDKRLY VANVGDSLAV ISRQGTAKML SRKHDPFERA ETSRIRAAEG WVSPKGFVND
EVDVSRSFGF YPLLPVVNAR PDVHVYDLSE MDEFVIIANI GLWKYVSPQT AVDIARSARS
DPMIAAQKLR DFVISYGAEG TTMIMVISVS DLFKKGQTRS RQQTMDSILD DETYHSIRRR
KKDDITNRGI SRLDVEVPPP TGHVALVFTD IRNSTHLWEV NPGMPTAMNL HNNLLRRQLR
FCGGYEVKTE GDAFMCSFPT VLSALWWCMS VQLQLLELSW PLEILECDDG KEIFDDSGKL
VARGLSVRMG IHCGQPVCEP DPITHRMDYF GPMVNRSARI NGSAAGGQIM CSAEVIREIN
ARIFETEPET EQSYLQPAQA IETVRRMEPV VIPLGETKLK GIEIPEMLSV VYPKGLEGRH
GLELPDAQPT VSGSRVHFSV EQMRELGLLC VRLEALTSGR IFRPLPVRKG STATPCPQPP
PDGYDPSAVI YGDPNLILPQ VTNASDADLM LLLDSLSQRI DNALAKLALD VAFRSSMGAD
AQEVMQQVMS ILYSPR
//
