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Database: UniProt
Entry: V5IRM6_NEUCR
LinkDB: V5IRM6_NEUCR
Original site: V5IRM6_NEUCR 
ID   V5IRM6_NEUCR            Unreviewed;      1872 AA.
AC   V5IRM6;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 53.
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   Name=cr-1 {ECO:0000313|EMBL:ESA44141.1};
GN   Synonyms=nac {ECO:0000313|EMBL:ESA44141.1};
GN   ORFNames=NCU08377 {ECO:0000313|EMBL:ESA44141.1};
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 {ECO:0000313|EMBL:ESA44141.1, ECO:0000313|Proteomes:UP000001805};
RN   [1] {ECO:0000313|EMBL:ESA44141.1, ECO:0000313|Proteomes:UP000001805}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987
RC   {ECO:0000313|Proteomes:UP000001805};
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.,
RA   FitzHugh W., Ma L.J., Smirnov S., Purcell S., Rehman B., Elkins T.,
RA   Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D.,
RA   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 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., 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., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P., Glass L., Orbach M.J., Berglund J.A., Voelker R., Yarden O.,
RA   Plamann M., Seiler S., Dunlap J., Radford A., Aramayo R., Natvig D.O.,
RA   Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S.,
RA   Lander E.S., Nusbaum C., Birren B.;
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:0000256|ARBA:ARBA00003896}.
CC   -!- SIMILARITY: Belongs to the adenylyl cyclase class-3 family.
CC       {ECO:0000256|ARBA:ARBA00005381}.
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DR   EMBL; CM002236; ESA44141.1; -; Genomic_DNA.
DR   RefSeq; XP_011393196.1; XM_011394894.1.
DR   EnsemblFungi; ESA44141; ESA44141; NCU08377.
DR   GeneID; 3881413; -.
DR   VEuPathDB; FungiDB:NCU08377; -.
DR   OrthoDB; 1698689at2759; -.
DR   Proteomes; UP000001805; Chromosome 1, Linkage Group I.
DR   GO; GO:0004016; F:adenylate cyclase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
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; 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-like_dom_sf.
DR   InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR   InterPro; IPR000159; RA_dom.
DR   PANTHER; PTHR48051; -; 1.
DR   PANTHER; PTHR48051:SF1; NON-SPECIFIC SERINE/THREONINE PROTEIN KINASE-RELATED; 1.
DR   Pfam; PF08509; Ad_cyc_g-alpha; 1.
DR   Pfam; PF00211; Guanylate_cyc; 1.
DR   Pfam; PF13855; LRR_8; 3.
DR   Pfam; PF00481; PP2C; 1.
DR   SMART; SM00789; Ad_cyc_g-alpha; 1.
DR   SMART; SM00044; CYCc; 1.
DR   SMART; SM00364; LRR_BAC; 13.
DR   SMART; SM00365; LRR_SD22; 5.
DR   SMART; SM00369; LRR_TYP; 12.
DR   SMART; SM00332; PP2Cc; 1.
DR   SMART; SM00314; RA; 1.
DR   SUPFAM; SSF52058; L domain-like; 2.
DR   SUPFAM; SSF55073; Nucleotide cyclase; 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   cAMP biosynthesis {ECO:0000256|ARBA:ARBA00022998};
KW   Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001805};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          321..413
FT                   /note="Ras-associating"
FT                   /evidence="ECO:0000259|PROSITE:PS50200"
FT   DOMAIN          1124..1400
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51746"
FT   DOMAIN          1464..1601
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
FT   REGION          1..165
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          199..224
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          800..908
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1419..1439
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1844..1872
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        22..43
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        52..67
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        79..122
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        199..214
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        827..859
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        885..908
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1848..1864
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1872 AA;  208945 MW;  5848AD465166848B CRC64;
     MSADIARYGE APVRTSLTGP DRDRYIDSSQ NPPKTSSSAR SGHSIVHLPG HHKHNKSNED
     PRALKPSLSR EDSAASFARD FRNGSSSMMG TRSRAQSPAP SWTGTSRGLK ANSISDGTSS
     PAPSHKKGIL GRFRRHNKDK EDGSSLRSGS NHTLVHRPSR QDLTRAAEST YPASVYVSDP
     SEQREVPVRP GYVRQTTAPG FTTKLFTSKK SSSAKQPQDD MDEDIGPTDM HMGGGTVYHL
     DTNLNDMEGI LTKPQPMTPL DNSISMRRES EKMIVPITTD PEGAWAAPDS WAVRDNKKSL
     APQVNEDLCS RQPSEEKEKK SNYYIRVFRS DSTWTTLTLP LTATAEDVIM GVAKKTYLPP
     GAQDSYSLLI KKHDLFRVLN SAEQPLRIQK RLFQQIGYQE KDGIDEIGRE DNSYICRWVF
     LKEKEADMHL LSPDINFRNQ KLNHVDLSGR NLITIPVPLY RKAAEIVSLN LSRNLSLDVP
     RDFIQACTAL RDIKYNNNEA QALPKSFATA SKLTYLDVSN NRLQDLDHSE LSKLTGLLKL
     NLANNCLRSL PPTLGAYKSL RTLNISSNFL DVFPSFICEL ETIVDLDLSF NSINNLPDNL
     MKLRNLEKFV ITNNRLSGPI SESVRDLVSL RELDIRYNQI STIDVLSDLP RLEILSADHN
     QISKFSGSFE RLRSLKLNSN PIVKFEVKAP VPTLKILNLS NAQLASIDES IDNLMNLERL
     ILDSNYFVSL PNQIGNLKKL DHLSMANNHL GELPPEIGCL TELRTLDVHG NNMRKLPNEI
     WWANKLEHLN ASSNILTEFP KPASRAPQAP GEASPSPGAY PFPNANKNGL LSRTPSMDDL
     NGDASRRPSQ ASSTLLGVAV SPVPSGPDNR KSSMVSLYGK GGRKTSVVSR STTQSSTGVI
     TPSNGPRKDS SLSYRFTHTF SGSLKNLYLA DNQLDDDVFE ELKHLPELRV LNLSCNDLSD
     MPQGTIRSWP QLVELYLSGN ELTSLPAEDF LEEHCLLQTL HINGNKFINL PAEISRAKKL
     QVLDCSSNNL KYNVTNVPYD WNWNFNRDLR YLNLSGNKRL EIKNNYRQPQ SYRDDDFADT
     DFSKLTNLRV LGLMEVTHTL PNIPDQTEDR RVRTSEMKAG AYLPYGMADT LGKNEHLSLF
     DLVVPRLGSV ETDTLVALFD GKELSTGGSK IAKFLYEEFS RLFILELEKV KGKPNENPAD
     ALRRTFLSVN KLLMSLSNSA DERGLDSHPS RNYAHTVLTK EDLNSGCVAT VAYLSELKLY
     VANVGDVQGM LIQANGSFKM LTKKHDPADP VERSRIRNAG GWVSRNGRLN DVLNVSRAFG
     YTELLPAVQA APDITEHTID DKDETVLIAS KELWEHLRPE LIVDVARECR SDLMKASQKL
     RDLAIAYGST NKLLIMMIGV ANLKQRQAQQ FKGQLNATFS MPQDDPSHVP PSGNKRRKVR
     AEGPLDSNLM RLNAEVPPPT GQLSIVFTDI KNSTQLWENY PEAMRLAIKL HNEVMRRQLR
     MIGGFEVKTE GDAFMVSFPT ATSALLWCFA VQMKLLTVDW PPEVLSNSSC QPIYDRNNNL
     ITRGLSVRMG AHWGEPLAER DPVTRRMDYY GPMVNKASRI SAVADGGQIT ASSDFITEIH
     RCLETYKESV DVDEDSLEDD ATAKAIRAEL RALSSQGFEV KDMGEKKLKG LENPELVYSV
     YPHALVGRTE QHHAHTESTQ NQAALQPYGA LATPKPATMD PDSEIQFEPE TIWALWRVAL
     RLEMLCSTLE EPNARGLQAP ETELLERMKQ RAGEVTDHFL LNFMEHQISR IETCITSLAV
     RHIAIGSGPI TKLNDLRAPM NDVLSTLKEQ MDELARYKAK YGSLDQAETD DATDNNSSGD
     VDTLDGSDTE QE
//
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