CYAA_USTMA
ID CYAA_USTMA Reviewed; 2493 AA.
AC P49606; A0A0D1E2W9; Q4P3T1;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Adenylate cyclase;
DE EC=4.6.1.1;
DE AltName: Full=ATP pyrophosphate-lyase;
DE AltName: Full=Adenylyl cyclase;
GN Name=UAC1; Synonyms=REM1; ORFNames=UMAG_05232;
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=518;
RX PubMed=7995519; DOI=10.1101/gad.8.23.2805;
RA Gold S., Duncan G., Barrett K., Kronstad J.W.;
RT "cAMP regulates morphogenesis in the fungal pathogen Ustilago maydis.";
RL Genes Dev. 8:2805-2816(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021;
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021;
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays essential roles in regulation of cellular metabolism by
CC catalyzing the synthesis of a second messenger, cAMP.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-3 family.
CC {ECO:0000305}.
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DR EMBL; L33918; AAA57469.1; -; Genomic_DNA.
DR EMBL; CM003143; KIS70161.1; -; Genomic_DNA.
DR PIR; A55481; A55481.
DR RefSeq; XP_011388269.1; XM_011389967.1.
DR AlphaFoldDB; P49606; -.
DR SMR; P49606; -.
DR STRING; 5270.UM05232P0; -.
DR EnsemblFungi; KIS70161; KIS70161; UMAG_05232.
DR GeneID; 23565179; -.
DR KEGG; uma:UMAG_05232; -.
DR VEuPathDB; FungiDB:UMAG_05232; -.
DR eggNOG; KOG0618; Eukaryota.
DR HOGENOM; CLU_000430_0_0_1; -.
DR InParanoid; P49606; -.
DR OMA; CESLAHI; -.
DR OrthoDB; 19317at2759; -.
DR PHI-base; PHI:22; -.
DR Proteomes; UP000000561; Chromosome 4.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0004016; F:adenylate cyclase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IEA:InterPro.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IBA:GO_Central.
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 Gene3D; 3.30.70.1230; -; 1.
DR Gene3D; 3.60.40.10; -; 1.
DR Gene3D; 3.80.10.10; -; 4.
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_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase_dom.
DR InterPro; IPR000159; RA_dom.
DR Pfam; PF00211; Guanylate_cyc; 1.
DR Pfam; PF13855; LRR_8; 3.
DR Pfam; PF00481; PP2C; 1.
DR SMART; SM00044; CYCc; 1.
DR SMART; SM00369; LRR_TYP; 12.
DR SMART; SM00332; PP2Cc; 1.
DR SUPFAM; SSF55073; SSF55073; 1.
DR SUPFAM; SSF81606; SSF81606; 1.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
DR PROSITE; PS51450; LRR; 18.
DR PROSITE; PS51746; PPM_2; 1.
DR PROSITE; PS50200; RA; 1.
PE 3: Inferred from homology;
KW ATP-binding; cAMP biosynthesis; Leucine-rich repeat; Lyase; Magnesium;
KW Metal-binding; Nucleotide-binding; Reference proteome; Repeat.
FT CHAIN 1..2493
FT /note="Adenylate cyclase"
FT /id="PRO_0000195730"
FT DOMAIN 970..1072
FT /note="Ras-associating"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00166"
FT REPEAT 1086..1107
FT /note="LRR 1"
FT REPEAT 1110..1132
FT /note="LRR 2"
FT REPEAT 1134..1155
FT /note="LRR 3"
FT REPEAT 1157..1178
FT /note="LRR 4"
FT REPEAT 1181..1202
FT /note="LRR 5"
FT REPEAT 1204..1225
FT /note="LRR 6"
FT REPEAT 1227..1248
FT /note="LRR 7"
FT REPEAT 1250..1271
FT /note="LRR 8"
FT REPEAT 1273..1294
FT /note="LRR 9"
FT REPEAT 1295..1316
FT /note="LRR 10"
FT REPEAT 1317..1336
FT /note="LRR 11"
FT REPEAT 1339..1360
FT /note="LRR 12"
FT REPEAT 1363..1385
FT /note="LRR 13"
FT REPEAT 1386..1407
FT /note="LRR 14"
FT REPEAT 1409..1430
FT /note="LRR 15"
FT REPEAT 1432..1453
FT /note="LRR 16"
FT REPEAT 1511..1534
FT /note="LRR 17"
FT REPEAT 1535..1556
FT /note="LRR 18"
FT REPEAT 1559..1580
FT /note="LRR 19"
FT REPEAT 1583..1605
FT /note="LRR 20"
FT REPEAT 1606..1628
FT /note="LRR 21"
FT REPEAT 1635..1654
FT /note="LRR 22"
FT DOMAIN 1710..2000
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT DOMAIN 2058..2194
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT REGION 1..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 99..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 197..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 355..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 475..565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 616..660
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 753..832
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 854..882
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 904..967
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2220..2241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2354..2378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2467..2493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..85
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..284
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..325
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 355..369
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..660
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 778..804
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 854..874
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 912..941
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2467..2483
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 2063
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 2105
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 2493 AA; 271983 MW; 106A872C3C1C5BF8 CRC64;
MLFTMQFTTR STVASPEQQH QHQQRSISYS DIELGLERIS SRDSNGSSNF THRAYPPPLS
QQYDDTSTNS FHSSQPDITA SSSTLSSRLV SANYSRPRFE HAHTQPPTPD QDRSSSGSGS
GSGSRSYFPA NSHSDSLPGP STHSISPSFD EDELRQIMSH IPANQATSSS DGDVGKAVQS
ANHQDISPFL FQSENAAPFS SSHSNRTSVN PSAASTASPS TSAATRTRPR GGTNASQYNT
LDTSFGSIDR PGLSSSRSQY SLRPQTPPSA STSTSTLNGS KDTHASAVKK TRNPFGFLKK
KSSAHSNASS NHPTRHDIGS VSSLSSRYGP NAAANVNPMR PPAWLDNHCT LANSNSPSSA
SLRSHYHQPP ASSNPPPWQN PLVSRADSTP SAMSLEDEVE AEHHLKKDPR KRIKGVRHHL
AKTTKPGEDA DSARDPAFAA QSQSIEQEVE LSLDMNFDQL DDFVDTNAAR QRLQGSITES
ASPSEHRSPN GSEAGVYRSP SPSQTPIAER QTSVTSTVES PSHASEASLA PSGSLRTPSR
TTASTSTSSA STVLSDRLPS QVNMLPRNSV PRLSLAEMQN YQSLRKLSNN LIDMSQTQNP
SAMGASYRRG SIAAAQAPVD APQLGVAPRT DSELSDRKDS VVSTHSMRSN HSGISPKTSY
ANLPSVIQER QKPATALPSA ANWTSSITRD KTANGHADHA YQFPPATEYQ SNLLLSVRKS
SASSGQEPSS SWMAPDSWAV QPDKMRDYLR DDNVGEEEDD DDDQHQARAA LATDGKRRGS
SSGISSTHAS SMFRTSSTDP FKKTASLAGS RRGTDDSVDP LTALPPLPGS KSVDEAAANK
VDVLQQTNNL AQSALVQQQS QSQNHHQPSP NVRPTSRGGA GAHMFASAGA SAAAAAAGKL
GLHRPSKHRM NARPNTAGSV GATRPSTTTL GSTLSAEDDT SINGSIRRDG HPLKRSATAN
TNNATGTLPR NHFIRVYKTD GTFATLSCSL VSTANEVQTI LARKSLTTES AAYRLFVRDK
GSERPLGISD KPSQLQRRRL IQAGYTENDG LEDMGRDDLS YLLRFVFRPD SVPTFDSESI
GHSEHTFQHL DLHSRNLEMV PIFLYKHADW IVSLDLSGNP MSDLPLDFVQ LCSSLRTLRL
SNLALKRIPQ SVRHSETLTH LDVSNNRIVE LAHVSLDLIP ELMSLKVQNN RLFDLPSYFS
SISTLRNLNI SNNRFEEFPK VICDVPSLVD LDVSFNSITE LPAEIANLIN LERFILAGNE
LEKLPDSMSE LVSLRTIDLR RNKVQDVSSL LGLPRLQNIQ AESNNIKSFE ATLGPQLTQV
ELGRNPLSKV RIAALTTCDL TSLDLSSTNM TRLEEGLFPQ LPALVKLTLD GNQLVVLPDT
LGDLKRLEML SCSNNLLATL PESIGDLKAL KELLVHNNNL KTLPQTLWLC ESLAHINLSS
NLLESFPAVP DIRTDASVGD AAAAAGTSAV IAARKGSTSS SLTHRSNTGG ANGNINLSTP
SEVFVAPLSL SLQKLRLGDN RLGDDVFSVL SELTSLEVLN LSFNEIFEIP DFSLQTLTKL
RELYISGNQL STIPSDDLVV LQELRILHLN CNKLTTLPTE LGKLKKLANL DVGNNVLKYN
IANWHYDWNW NMNPELRYLN LSGNTRLEIK TKLSDMGFTR KSNISDFSRL TSLRMLGLMD
VTMPLHSNAT PDESDNRRVR TSLSQVNGMA YGIADALGKH DNLSVIDLVI PTFRKDEGEC
IFGLFDGRGH GAHVGSRIAH HLAEWSGHRL SWEFQKHQNE MTAEPVSVPD ALRRAFLRLQ
KDYADALIND GSRKLSEAHA EAAADVTRSS APAIAAASNK HDWRAGASAI LAYVVDHTLY
IANAGDALAV MSRNGGTAHL ISNKHEPFDR AEIERIRSAE GWVSLRGYVN DMLDVSRSFG
YFHLFPIVNA APAVTTVQLT DSDEFVIIAN RTLWQYVSYQ TAVDIARTQR NDPMIAAQKL
RDFAISYGAE ESIMVMVISV GDLFYRSDQR NGGGLNFASY KNSDAIQKAG RRFREELPGD
RTLARLDREV APPIGQVALV FTDIKNSTSL WETNNGMQTA MRLHNYLLRR QLRTIGGYEV
KTEGDAFMVS FPSVSAALLW CFTVQQQLLQ EDWPREILDS EDGKEVYDQS GELIHRGLSV
RMGIHWGRPV CEADPITRRM DYFGPMVNRA ARISGAADGG QILASKDVIK ELQGLLGTFD
ESSTAGGAGG EGENLEKTEE ELDEDAFRLL NPNVSRDVVL LRRMGFGLSQ LGERRLKGLE
TPEMLWLVYP KQLAGRLEQA KTDDAPDAPT AQVYEPTVQL LDIEDVKQVG MLCLRLEYLS
NSTVCPGIFA AKDEADRSQP STPLDDNGRN PIDGHGTAVP LLSHQARRKG VEAMLTMHPE
LLIYSIRDDA TDEELAGILD QLTTRIQNAV SSLMLNMLRD KTANGTKELG VDPGVLELLM
GLLSQPPPRA STSALSLPSP RTSPRNRLLE LVP
