ID A0A135ULB7_9PEZI Unreviewed; 2177 AA.
AC A0A135ULB7;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=CSAL01_06807 {ECO:0000313|EMBL:KXH61200.1};
OS Colletotrichum salicis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum acutatum species complex.
OX NCBI_TaxID=1209931 {ECO:0000313|EMBL:KXH61200.1, ECO:0000313|Proteomes:UP000070121};
RN [1] {ECO:0000313|EMBL:KXH61200.1, ECO:0000313|Proteomes:UP000070121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 607.94 {ECO:0000313|EMBL:KXH61200.1,
RC ECO:0000313|Proteomes:UP000070121};
RA Baroncelli R., Thon M.R.;
RT "The genome sequence of Colletotrichum salicis CBS 607.94.";
RL Submitted (FEB-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 {ECO:0000256|ARBA:ARBA00003896}.
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-3 family.
CC {ECO:0000256|ARBA:ARBA00005381}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KXH61200.1}.
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DR EMBL; JFFI01001310; KXH61200.1; -; Genomic_DNA.
DR STRING; 1209931.A0A135ULB7; -.
DR OrthoDB; 1698689at2759; -.
DR Proteomes; UP000070121; 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; 2.
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; 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; 2.
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:UP000070121};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 660..751
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 1455..1731
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT DOMAIN 1794..1931
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT REGION 1..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 112..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 232..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 322..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 603..629
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1136..1246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..285
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..353
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..377
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..448
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..538
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1177..1195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1220..1234
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2177 AA; 241480 MW; C9B6068CE32D6832 CRC64;
MTRNEAGSRF SSLTSTSTDS TRSSATVRPS SNPIPATRKS SMRLKTEGNG NGSLADNDLS
PADPSASSTF ASAPRGALSP GTTKSNASSY RDHRLSDFAN YRRDLAVLET SGGRLPSIQH
NPPTATPSSN SQIAPWMSPS NGGATASTPQ SQLNTTFYND SSDNLSVASQ LSPGFRPPTN
RLAPQSSGSQ DSPDVAYFGD ERRPSLASIT TLSSQGSKTS IRRGGLQKLQ GFFGEEFPGR
DGSESSLHSS SGRDRSRSYS HSRPTRDRNY SNATDHARDR EASPSSSRPR TPVPAPEVVP
FLYQEADDIA RFGEAPVRDI LSGPDRERYM NNENPNNPQN PPKTSSSSRS GHSIVHLPGH
HHRHNRSIDD GRALRPTVSR EDSQASLQVQ QNPRERGGSA ATVMYGSNRS RAQSPTPSGG
YFSSRHGTVD GSTSPGGQQQ QQQQPQHHSK RNLLHRLRRN KDKDDGASRL RDLPGSTRSL
ATKPSRPEFA RPELSPSTFP LAFSGTEPGS DQDPRLAAYN QRNQTFNNRF PFSKSKGRQQ
RTLEPDEQIG PTDRQPGANN NLGSLGGIHL DTNLSDMDGI LTKPQPLTPM DSGVFSSIGD
AEKVEQPPPV PAKPDAVLGP NGSWNAPDSW AVRRNTEDTT YQAPDIDDIG SPPRPDEKMT
PYCIRIFRSD GTFATLSMAL DASVTDVISQ LIKKTYATDG LENYHIILKK HDLVRVLAAP
ERPLLMQKRL LQQIGYEERD RIEDVGREDN SYLCRFMFLS SRESDFHSVT NDLGLGRIQK
FNHVDLAGRN LITIPISLYS KASEIISLNL SRNLSLDLPR DFIQSCQNLR DIKFNNNEAR
RLPPSLGKAA KLTYLDVSNN RLEQLDHAEL NGLQGILKLN IANNRLKALP PYFGAYRALR
NLNISSNFLD KFPLFLCQVE TLIELDLSFN SISSLPNEIG RLRNLEKFVI TNNRLSNALP
DTFSELQGLR ELDIKYNAIT SIDIISLLPK LEILSADHNS ISQFIGSFDR IRSLKLNSNP
ITKFEINEPV LTLKMLNLSH CQLASIDETF NMMLNLERLV LDKNYFVSLP PLIGNLSKLE
HFSIANNNVA ELPPSIGCLT ELRVLDVRRN NIRKLPMELW WANKLETLNA SSNILENFPK
PGSRQPRPSG EEAQTPAAGT KANPMERIAQ SPLEESPDAS RRPSQNSSST LLSVGPSPVP
GGGDRKSSVV SVYGKGGRKT SVVSRSTSAG TVPPLPPSAT ARKDSSLSSR LYTTFAGSLR
NLYLAENKLD DEVFDQITML NELRVLNLSW NYINDMPQRS IKSWPQMVEL YLSGNELTTL
PADDLEDASL LQILHINGNK FTNLPADISR AKKLAVLDCG SNSLKYNICN VPYDWNWNLN
PNLRYLNLSG NKRLEIKQTT VGPTVTNRES LADFNRLSNL RVLGLMDVTL TQPTIPDQSE
DRRVRTSGSL AGHLPYGMAD TLGKNEHLST IDLVVPRYNS TETETLLGLF DGQALSSGGS
KIAKYLHENF GHIFGMELKG LKTRLNETPA DALRRAFLSL NKDLVTIAIQ HTEERSQKTH
RGSATPVVLS KEDLNSGGVA TVVYLQNTEL YVANVGDAQA MLIQTDGSHK ILTRKHDPAE
PSERQRIREA GGWVSRNGRL NDLLEVSRAF GYVDLMPAVQ AAPYVSNFTI REQDDIILIA
TREFWEYLDP ALVVDFARQE RGDLMRASQK LRDLAIAYGA TNKIMVMMMS VADLKRRVER
SRLHRGQSMS LYPSGVPEDL QQPMRRGKRN KADVLDSSLQ RLEAEIPAPT GNVSIAFTDI
KNSTTLWEMY PAAMRSAIKL HNEVMRRQLR RIGGYEVKTE GDAFMVSFPT ATSALLWCFA
VQMSLLDVNW PSEVINSVSC QALYDKDNAL IFKGLSVRMG IHFGEAVSEM DPVTRRMDYF
GPMVNKASRI SSVADGGQIT VSSDFISEIQ RCLENYQDTD RNGSTGSEDT FDDDQMGSAI
RKDLRSLSSQ GFEVKEMGEK KLKGLENPEV VYSLYPHALA GRIEHHQQHE QRTEVDKPAI
LQAGSELAFD TESIWALWRV SLRLEMLCSS LENVSGQGLQ PPETELLERM KHRGGEVTER
FLLNFMEHQV SRIETCVTSL SLRHIAFGSA PLQQLEDMRG PMSDILDQVA KQMAELARYK
ALYGELNDTE DDRSETE
//
