ID S3CXM7_GLAL2 Unreviewed; 2170 AA.
AC S3CXM7;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 52.
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=GLAREA_00849 {ECO:0000313|EMBL:EPE29689.1};
OS Glarea lozoyensis (strain ATCC 20868 / MF5171).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Helotiaceae; Glarea.
OX NCBI_TaxID=1116229 {ECO:0000313|EMBL:EPE29689.1, ECO:0000313|Proteomes:UP000016922};
RN [1] {ECO:0000313|EMBL:EPE29689.1, ECO:0000313|Proteomes:UP000016922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 20868 / MF5171 {ECO:0000313|Proteomes:UP000016922};
RX PubMed=23688303; DOI=10.1186/1471-2164-14-339;
RA Chen L., Yue Q., Zhang X., Xiang M., Wang C., Li S., Che Y.,
RA Ortiz-Lopez F.J., Bills G.F., Liu X., An Z.;
RT "Genomics-driven discovery of the pneumocandin biosynthetic gene cluster in
RT the fungus Glarea lozoyensis.";
RL BMC Genomics 14:339-339(2013).
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; KE145367; EPE29689.1; -; Genomic_DNA.
DR RefSeq; XP_008083798.1; XM_008085607.1.
DR STRING; 1116229.S3CXM7; -.
DR GeneID; 19459907; -.
DR KEGG; glz:GLAREA_00849; -.
DR eggNOG; KOG0618; Eukaryota.
DR HOGENOM; CLU_000430_4_0_1; -.
DR OMA; EIWWANK; -.
DR OrthoDB; 1698689at2759; -.
DR Proteomes; UP000016922; Unassembled WGS sequence.
DR GO; GO:0004016; F:adenylate cyclase activity; IEA:UniProtKB-EC.
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; 3.
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; ZGC:77287; 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; 9.
DR SMART; SM00365; LRR_SD22; 5.
DR SMART; SM00369; LRR_TYP; 10.
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; 4.
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:UP000016922};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 618..709
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 1419..1697
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT DOMAIN 1759..1896
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT REGION 1..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1098..1175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2145..2170
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 54..83
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..102
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..177
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..213
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..239
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..257
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..352
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..414
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..504
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1112..1154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2170 AA; 238758 MW; 452CF787B238FB9E CRC64;
MTRKSDAASR LSSQTSSSTD SHTTIRPSTS LFRGPPRRGA PMQVKIDGRN SSRVEPDPQV
SPTSTAPQSA ISPSSTSPNV SPRDHRLSDF GNYRRDLACL ETDRGRIPQI QHNPPTAMGS
PGQIAPWMSS SSGGNTPSGT FGTSFYNDSS DNLSQASQLS PPFRPGTGFT GYTNASDSPA
DADFGDERRP SVASVTTASS TGSKSSITRT GIHKQLKTFF GEDYNEKDAS STSLPSHGKE
RSHSFARSHR ERNLSSATEA TQRDASPVPS RPRTPVPSSD VVPFLYQDSQ DISKYGEAPV
RENLSGPDRD RYIDNPQPPP KPSSSSRSHG VHLPGHSHRH NRSNDDSRNL RPSISRGDSG
FSERYRDRAP SSMGVAMGNA SNTSLAKRPA SPTPSGNSNW SGSTAKTPHN DGSSSPPGHA
KRGLLSRLRK HKDKDGPSKL SHLPGSVKSL ATPSKHGHEK TNGSSEFVQW NRDGSISHSE
LNLPRTDNGQ FGRPPTSSST KRPKLGFSRK TRRGATDESQ GPFDAGSNLP QESLFNLDSD
LSNMEGILAK PPPLTPLDNN IFAGTFEDEM KVETPDGSAL GWDAPDSWAV KKVEDNNMAR
LDEIDEAGIP DRIDEKATPY CIRIFRVDGT FATLSTPLNA SVTDIMVQLG KKTYMTDSLE
NYQIVMKKHD LQRILSAGER PVVIQKKLLQ QAGYEEQDRI EEIGREDNSY LCRFSFVPAR
ESGYATVGND PGVSRVQKYS HVDLSGKNLI TIPIALYSKA SEIISLNLSR NLSLDLPKDF
IQSCQNLRDI KFINNEAWKL PPGLSRASRL TILDVSNNRL EELENAELSR LSGLISLKLA
NNRLRSLPAY FGGFKTLRTL NVSSNFLETF PPFLCQLEGL VDIDLSFNGI SSLPDDVGKL
KNLERFVITN NRLYGELPAN FAELKNLREI DIRYNALTSI DVIATLPKVE QISADHNSVS
VCESSFTKIR ILRLNSNPVT RFEIKNSVPT LTTLILSNAK LAQIPDASFD RMPNLVKLVL
DKNHFVSLTS HIGKLSKLEH FSIAMNALNV VPPEIGCLTE LRLLDLRQNN LKKLPMELWW
ANKLETLNVS SNVLENFPKP ASRAPQVPGN ATPDRAATQT SGTPGQNNSN SSLDDLGPLE
NFGQQQQRRP SQGGLLSVGG SPIPGSADRK GSVVSLYGKG GRKTSVVSRS ASTDTIGTLT
PSARKDSTIS SRLVNTFAGS LRNLIMAENQ LDDDVFDEIK YLSELRILNL SYNDLNDIPS
QSIRCWPQLV ELYLSGNELT SLPSDDFEEF SLLQVLHING NKFQTLPAEL GKAHRLAVLD
CGSNSLKYNV SNWPYDWNWN WNTNLKYLNL SGNKRLEIKP SLPNGSSSAR DGRDLTDFSA
LGNLRILGLM DVTLTIERIP DQTEDRRVRT SGSLAGQLAY GMADTLGKND HLSLIDMVVP
RFQSNENETL LGMFDGQSLS NAGSKIAKYL HENFGHTLQE EMKKLNLNST PKENPGDALR
RTFLSLNKDL ATAATQHTQD RSISSHRGSA APAVLSQADL RSGGVATVMF LQGSELYVAN
VGDAQAMLIH SEGSHRILTS KHYPAEFHER QRIRDAGGWV SRQGKLNDIL DVSRAFGYVQ
LIPAVQAAPY VTHVTVKEQD EMILIASKEL WEYLSPELVV DIARNERDDL MRAAQKLRDL
AMAFGATNKI MVMMIGVSDL KKRANIRPHR VQSMSLNPGA IVDDGYAPAK RVKRKGNGVG
DSVLNRLDTE IAAPEGEVGI VFTDIKSSTL LWETYPEAMR AAIRLHNDLL RRQLRIIGGY
EVKTEGDAFM VSFPTATSAL LWAFAVQSAL LEVPWPSEIL TSILGQEIYD TDSNLIFKGL
SVRMGIHWGR PVCEMDPVTK RMDYFGPMVN RTSRISNVAD GGQITVSADF ISEIQRCLET
YSESDRNGST GSEEEYGNDL VAAAIRRELR SLSSQGFEVK DIGERKLKGL ENPEYIYLMY
PHSLSGRIQY QQQLLQNEKA AAAAGEQPAS LSQKTKLSID TDTVWALWAV SLRLEMLCSS
LEGDKGKTSA LQAPETAVLE RMKQKGGEVT DRFLVNFMNH QVSRIETCIS AISTRHLAMG
KGPLHSLNQL RAPMGDVLSG LEAQLQLLQQ YQKAYGPLNT EVKPATKRNL PRETSNHYFK
SSHETSATKS
//
