CYAA_NEUCR
ID CYAA_NEUCR Reviewed; 2300 AA.
AC Q01631; Q7RVM0; V5IQU1;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Adenylate cyclase;
DE EC=4.6.1.1 {ECO:0000269|PubMed:1680356};
DE AltName: Full=ATP pyrophosphate-lyase;
DE AltName: Full=Adenylyl cyclase;
DE AltName: Full=Crisp-1;
GN Name=cr-1; Synonyms=nac; ORFNames=NCU08377;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=1680356; DOI=10.1266/jjg.66.317;
RA Kore-Eda S., Murayama T., Uno I.;
RT "Isolation and characterization of the adenylate cyclase structural gene of
RT Neurospora crassa.";
RL Jpn. J. Genet. 66:317-334(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
CC -!- FUNCTION: Plays essential roles in regulation of cellular metabolism by
CC catalyzing the synthesis of a second messenger, cAMP.
CC {ECO:0000269|PubMed:1680356}.
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:0000269|PubMed:1680356};
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-4/guanylyl cyclase
CC family. {ECO:0000255|PROSITE-ProRule:PRU00099}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D00909; BAA00755.1; -; Genomic_DNA.
DR EMBL; CM002236; ESA44140.1; -; Genomic_DNA.
DR RefSeq; XP_011393197.1; XM_011394895.1.
DR AlphaFoldDB; Q01631; -.
DR SMR; Q01631; -.
DR STRING; 5141.EFNCRP00000006404; -.
DR EnsemblFungi; ESA44140; ESA44140; NCU08377.
DR GeneID; 3881413; -.
DR KEGG; ncr:NCU08377; -.
DR VEuPathDB; FungiDB:NCU08377; -.
DR HOGENOM; CLU_000430_4_0_1; -.
DR InParanoid; Q01631; -.
DR OMA; HDPAEPN; -.
DR Proteomes; UP000001805; Chromosome 1, Linkage Group I.
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:0000287; F:magnesium ion binding; IEA:InterPro.
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; IPR013716; Adenylate_cyclase_G-a-bd.
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; PF08509; Ad_cyc_g-alpha; 1.
DR Pfam; PF00211; Guanylate_cyc; 1.
DR Pfam; PF13855; LRR_8; 4.
DR Pfam; PF00481; PP2C; 1.
DR SMART; SM00789; Ad_cyc_g-alpha; 1.
DR SMART; SM00044; CYCc; 1.
DR SMART; SM00369; LRR_TYP; 12.
DR SMART; SM00332; PP2Cc; 1.
DR SMART; SM00314; RA; 1.
DR SUPFAM; SSF55073; SSF55073; 1.
DR SUPFAM; SSF81606; SSF81606; 1.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
DR PROSITE; PS51450; LRR; 17.
DR PROSITE; PS51746; PPM_2; 1.
DR PROSITE; PS50200; RA; 1.
PE 1: Evidence at protein level;
KW ATP-binding; cAMP biosynthesis; Leucine-rich repeat; Lyase; Magnesium;
KW Metal-binding; Nucleotide-binding; Reference proteome; Repeat.
FT CHAIN 1..2300
FT /note="Adenylate cyclase"
FT /id="PRO_0000195728"
FT DOMAIN 749..841
FT /note="Ras-associating"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00166"
FT REPEAT 867..890
FT /note="LRR 1"
FT REPEAT 892..914
FT /note="LRR 2"
FT REPEAT 915..938
FT /note="LRR 3"
FT REPEAT 939..961
FT /note="LRR 4"
FT REPEAT 962..986
FT /note="LRR 5"
FT REPEAT 988..1008
FT /note="LRR 6"
FT REPEAT 1009..1031
FT /note="LRR 7"
FT REPEAT 1033..1055
FT /note="LRR 8"
FT REPEAT 1056..1079
FT /note="LRR 9"
FT REPEAT 1081..1097
FT /note="LRR 10"
FT REPEAT 1098..1119
FT /note="LRR 11"
FT REPEAT 1120..1142
FT /note="LRR 12"
FT REPEAT 1143..1165
FT /note="LRR 13"
FT REPEAT 1166..1188
FT /note="LRR 14"
FT REPEAT 1189..1211
FT /note="LRR 15"
FT REPEAT 1213..1234
FT /note="LRR 16"
FT REPEAT 1349..1369
FT /note="LRR 17"
FT REPEAT 1373..1396
FT /note="LRR 18"
FT REPEAT 1398..1420
FT /note="LRR 19"
FT REPEAT 1422..1445
FT /note="LRR 20"
FT REPEAT 1447..1469
FT /note="LRR 21"
FT REPEAT 1474..1497
FT /note="LRR 22"
FT DOMAIN 1552..1828
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT DOMAIN 1892..2029
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT REGION 1..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 272..593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 631..652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1228..1336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1847..1867
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2272..2300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..171
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..288
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..326
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..379
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..471
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 480..495
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..550
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1255..1287
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1313..1336
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2276..2292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1897
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 1940
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT CONFLICT 968
FT /note="L -> V (in Ref. 1; BAA00755)"
FT /evidence="ECO:0000305"
FT CONFLICT 1121..1123
FT /note="TLK -> IPQ (in Ref. 1; BAA00755)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2300 AA; 254772 MW; 902301C768AC9A64 CRC64;
MTRNDGGSRY SSIDSAQSSI TAKPFPLTPT SSLGSSMTRP LSPSLQAGSS SSNGGHNVSR
SASQGARRPA PTRLKTDDGT QFASRSSRDF ESSQSQSQPS HTQTRSHSLS QATLQSCSQP
QLSLNSQQSQ SPSQYHSQQT PTQQQPQQQV SPTGGSRLTQ SPTTPSNASI REHRMSELGG
YRREMAAMLD TTGGALSRTS SHSQQQPQQP QQQQQQQQQQ QGHAAGSVSG TFSNLSQYAP
YLGGNNGGGM SMGSFLNDST DNLSVISQLS PGIRPMTARP SQASAGSMEF PDSAYYDDER
RPSIASITTT ASSQGSRTSK TRGGLQKLQQ FFGDRDDWPG RDSSEISLPQ PSHSGPMSTG
KEHRSHSYSL PGSGRSHRDR NYSNATDHHP STFGSVSTVG GRDRDASPVP SRPRTPVPAP
EVVPFLYQEA DDIARYGEAP VRTSLTGPDR DRYIDSSQNP PKTSSSARSG HSIVHLPGHH
KHNKSNEDPR ALKPSLSRED SAASFARDFR NGSSSMMGTR SRAQSPAPSW TGTSRGLKAN
SISDGTSSPA PSHKKGILGR FRRHNKDKED GSSLRSGSNH TLVHRPSRQD LTRAAESTYP
ASVYVSDPSE QREVPVRPGY VRQTTAPGFT TKLFTSKKSS SAKQPQDDMD EDIGPTDMHM
GGGTVYHLDT NLNDMEGILT KPQPMTPLDN SISMRRESEK MIVPITTDPE GAWAAPDSWA
VRDNKKSLAP QVNEDLCSRQ PSEEKEKKSN YYIRVFRSDS TWTTLTLPLT ATAEDVIMGV
AKKTYLPPGA QDSYSLLIKK HDLFRVLNSA EQPLRIQKRL FQQIGYQEKD GIDEIGREDN
SYICRWVFLK EKEADMHLLS PDINFRNQKL NHVDLSGRNL ITIPVPLYRK AAEIVSLNLS
RNLSLDVPRD FIQACTALRD IKYNNNEAQA LPKSFATASK LTYLDVSNNR LQDLDHSELS
KLTGLLKLNL ANNCLRSLPP TLGAYKSLRT LNISSNFLDV FPSFICELET IVDLDLSFNS
INNLPDNLMK LRNLEKFVIT NNRLSGPISE SVRDLVSLRE LDIRYNQIST IDVLSDLPRL
EILSADHNQI SKFSGSFERL RSLKLNSNPI VKFEVKAPVP TLKILNLSNA QLASIDESID
NLMNLERLIL DSNYFVSLPN QIGNLKKLDH LSMANNHLGE LPPEIGCLTE LRTLDVHGNN
MRKLPNEIWW ANKLEHLNAS SNILTEFPKP ASRAPQAPGE ASPSPGAYPF PNANKNGLLS
RTPSMDDLNG DASRRPSQAS STLLGVAVSP VPSGPDNRKS SMVSLYGKGG RKTSVVSRST
TQSSTGVITP SNGPRKDSSL SYRFTHTFSG SLKNLYLADN QLDDDVFEEL KHLPELRVLN
LSCNDLSDMP QGTIRSWPQL VELYLSGNEL TSLPAEDFLE EHCLLQTLHI NGNKFINLPA
EISRAKKLQV LDCSSNNLKY NVTNVPYDWN WNFNRDLRYL NLSGNKRLEI KNNYRQPQSY
RDDDFADTDF SKLTNLRVLG LMEVTHTLPN IPDQTEDRRV RTSEMKAGAY LPYGMADTLG
KNEHLSLFDL VVPRLGSVET DTLVALFDGK ELSTGGSKIA KFLYEEFSRL FILELEKVKG
KPNENPADAL RRTFLSVNKL LMSLSNSADE RGLDSHPSRN YAHTVLTKED LNSGCVATVA
YLSELKLYVA NVGDVQGMLI QANGSFKMLT KKHDPADPVE RSRIRNAGGW VSRNGRLNDV
LNVSRAFGYT ELLPAVQAAP DITEHTIDDK DETVLIASKE LWEHLRPELI VDVARECRSD
LMKASQKLRD LAIAYGSTNK LLIMMIGVAN LKQRQAQQFK GQLNATFSMP QDDPSHVPPS
GNKRRKVRAE GPLDSNLMRL NAEVPPPTGQ LSIVFTDIKN STQLWENYPE AMRLAIKLHN
EVMRRQLRMI GGFEVKTEGD AFMVSFPTAT SALLWCFAVQ MKLLTVDWPP EVLSNSSCQP
IYDRNNNLIT RGLSVRMGAH WGEPLAERDP VTRRMDYYGP MVNKASRISA VADGGQITAS
SDFITEIHRC LETYKESVDV DEDSLEDDAT AKAIRAELRA LSSQGFEVKD MGEKKLKGLE
NPELVYSVYP HALVGRTEQH HAHTESTQNQ AALQPYGALA TPKPATMDPD SEIQFEPETI
WALWRVALRL EMLCSTLEEP NARGLQAPET ELLERMKQRA GEVTDHFLLN FMEHQISRIE
TCITSLAVRH IAIGSGPITK LNDLRAPMND VLSTLKEQMD ELARYKAKYG SLDQAETDDA
TDNNSSGDVD TLDGSDTEQE
