ID A0A2T2NFV2_CORCC Unreviewed; 2119 AA.
AC A0A2T2NFV2;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=BS50DRAFT_636524 {ECO:0000313|EMBL:PSN64321.1};
OS Corynespora cassiicola Philippines.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Corynesporascaceae; Corynespora.
OX NCBI_TaxID=1448308 {ECO:0000313|EMBL:PSN64321.1, ECO:0000313|Proteomes:UP000240883};
RN [1] {ECO:0000313|EMBL:PSN64321.1, ECO:0000313|Proteomes:UP000240883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Philippines {ECO:0000313|EMBL:PSN64321.1,
RC ECO:0000313|Proteomes:UP000240883};
RX PubMed=29551995; DOI=10.3389/fmicb.2018.00276;
RA Lopez D., Ribeiro S., Label P., Fumanal B., Venisse J.S., Kohler A.,
RA de Oliveira R.R., Labutti K., Lipzen A., Lail K., Bauer D., Ohm R.A.,
RA Barry K.W., Spatafora J., Grigoriev I.V., Martin F.M., Pujade-Renaud V.;
RT "Genome-Wide Analysis of Corynespora cassiicola Leaf Fall Disease Putative
RT Effectors.";
RL Front. Microbiol. 9:276-276(2018).
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; KZ678138; PSN64321.1; -; Genomic_DNA.
DR STRING; 1448308.A0A2T2NFV2; -.
DR Proteomes; UP000240883; 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; 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:SF43; LEUCINE-RICH REPEAT-CONTAINING PROTEIN 47-LIKE PROTEIN; 1.
DR Pfam; PF08509; Ad_cyc_g-alpha; 1.
DR Pfam; PF00211; Guanylate_cyc; 1.
DR Pfam; PF00560; LRR_1; 1.
DR Pfam; PF13855; LRR_8; 2.
DR Pfam; PF00481; PP2C; 1.
DR Pfam; PF00788; RA; 1.
DR SMART; SM00044; CYCc; 1.
DR SMART; SM00364; LRR_BAC; 8.
DR SMART; SM00365; LRR_SD22; 4.
DR SMART; SM00369; LRR_TYP; 11.
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; 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; 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:UP000240883};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 601..692
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 1403..1679
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT DOMAIN 1740..1877
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT REGION 1..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 147..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 525..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1077..1119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1132..1188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1691..1722
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..270
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..344
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..402
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..420
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..442
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..478
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1088..1111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1133..1188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1708..1722
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2119 AA; 235427 MW; B615B44BA44352C4 CRC64;
MTRNEAGNRH ASIESSTSWR SSDTVRPFRA ARGTPVTVKT SKDHNYPIEK ESEISPGTVP
PIPPPKDPAH KPRKNSNWDS PQANDFRDYR KQLAVLETSG SRIPSISRNP PTATSPTPPW
ASSGTNGSAM PSSVWGSFYN DSDENLAQLS PGFARPGSGK DEAMAFAGDD RRPSVASATT
ISSSGSKSSI SRGGFHKKLQ GFFGEEFPGD SRQNSDTSLP TPYAVETQSN RGVTRNRTNS
LNHTLGSSLN SRPGSPVNSR PRTPAPSSEV TPWEFQDFKD APAPPPGENG RPSSEQHSTK
SGKGPHKLRL PGHRSNRSKD DIKTSDARTE ISQPYPLRPV TSREDSSYSV RREQPYPSAL
SVALNSRANL MPRPSSPTPS SFSEMSRDAS ASSPSTSKKI SILDRFRGNR KDKSDRSYPD
HLRNANANAS QVSLQPSVKS ANFPRPEPSP GTFAKKPSID SQKDRHNKGK DGRPQHRRLG
PLGRSRQPPQ MQDQPVGRDP NEVDPATFET GNLWSLDTDL SHMEGIVHPQ PQQPPMTPPT
GEAPTTTWPG EEVGPEIKED ANGAWDAPDS WAVKRLGDEN MPRHGEFDEA AVTPKEEESS
KTYCVRIFRV DSTFATLSAT LNTSVSEIIQ ILGKKTLLQD ELDNYHIVMR KHDTSRQLDS
HERPLLIQKR LLEQAGYTDA DRLEEVGRED NSYLCRFTFL PAKMSGYSSL EKDPGFSKMQ
KFSHIDLQGR NLITIPITLY QKATEIISLN LSRNLSLDIP KDFVQACTNL REIKYTSNDA
RRLPPSLGLA TRLTMLDISN NRLQQLDHAD LYKLQSLHGL RLSNNRLTQL PAYFGQYRAL
RSLNLSSNSL HEFPDFLCEV RTLVDLDISF NSISSLPRIG QLTCLERLWA TNNKLSGSFP
SSLSNLVNLR EIDVRFNALT SMDVMSRLPR LEYLMIGHNS ISAFEGSFPK IRVLHMNHNP
VTRFDIRQPV PTLSALNLAS AKLAQLPEEL FQNTSGLTKL ILDKNHFSSL SSNIGRLYRL
EHLSVARNTL DDLPAEIGRL SELRYLDVRE NNLGRLPPEI WYARRLETLN VSSNVLDGFP
KPTAPPPQNT MNGDAANSSM DAATPLSTPG LGPSPSYEEL GKLEDFANRR PSQASAGYLS
SSGPSPATSQ RKGSMASYNT ASTSNTRKQS MQSRAPTEGT LTPVTRKDSS LSNRMVTTFA
GSLRHLFLAD NRLTDDVFDE LCLLPELRIV NLSYNLIYDI PPRTLRRWQH LTELYLSGND
LTSLPAEDLE EVSSLKVLHI NSNKFQVLPA ELGKVAKLAI LDVASNSLKY NVSNWPYDWN
WNWNHNLKYL NLSGNKRLEI KPTGAFSGGG AAMREGRDLT DFTSLINLRV LGLMDVTLMV
PSVPEQTEDR RVRTSGSAVG TMAYGMADSL GRNEHISTMD MVIPRFRSHD DEQILGLFDG
QPLASSGSKI AKYLYDNFKN RFADELDRLR PQETPEDALR RTYLGLNKEL ATVATQALDK
NNMTIPSTQS RGAVPDLSDD DLNSGSVATV LYLKEMELYI SNVGDAQALL IRSEGGHRML
TRKHDPAEAG ERARIREAGG FVSRQGKLND VLEVSRAFGY VQMSPSVIAA PHILNLTLGD
TDEMILMASR ELWDYLTPDF AVDVARSARD DLMRAAQKLR DLAIAFGATN KIMVMLIGVS
DLKSKQRARF RTHSMSMGPS GSPDDYPWNR RGNKRNRNLP NDSKLARLDN EVDAPTGDVS
LVFTDIKNST LLWETYPIAM RSAIKMHNEL MRRQLRIIGG YEVKTEGDAF MVAFPTVTSA
LLWCFTIQSQ LLDVPWPQEI LSSVNGQEVV DPDGNVIFRG LSVRMGIHWG TPVCEVDPVT
KRMDYFGPMV NRASRISSVA DGGQITVSSD FIAEIQRLLE THIEGDRSNS AGSEEQLGED
AMSQAIRQEL RSLSSQGFEV KDLGERRLKG LENPEYIYLM YPHSLASRLA VQRQLEQQKQ
PQATAAQAGQ KMPGSELTID TETVWDLWNV SLRLEMLCST LENPGSVELK PPETALLERM
KNRGGEITDR FLINFVEHQI SRIETCATTL ALRHMVRPFG SCPILEQACP MSDIISELQA
QLAELQQYKD EAASQMVSA
//
