ID A0A1C1CYK8_9EURO Unreviewed; 2060 AA.
AC A0A1C1CYK8;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
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=CLCR_09421 {ECO:0000313|EMBL:OCT53627.1};
OS Cladophialophora carrionii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=86049 {ECO:0000313|EMBL:OCT53627.1, ECO:0000313|Proteomes:UP000094526};
RN [1] {ECO:0000313|Proteomes:UP000094526}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSF {ECO:0000313|Proteomes:UP000094526};
RA Teixeira M.M., Souza R.C., Almeida L.G., Vicente V.A., de Hoog S.,
RA Bocca A.L., de Almeida S.R., Vasconcelos A.T., Felipe M.S.;
RL Submitted (JUL-2015) 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:OCT53627.1}.
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DR EMBL; LGRB01000008; OCT53627.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C1CYK8; -.
DR STRING; 86049.A0A1C1CYK8; -.
DR VEuPathDB; FungiDB:CLCR_09421; -.
DR VEuPathDB; FungiDB:G647_00578; -.
DR eggNOG; KOG0618; Eukaryota.
DR Proteomes; UP000094526; 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; PF13855; LRR_8; 3.
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; 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; 6.
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:UP000094526};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 538..628
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 1327..1605
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT DOMAIN 1668..1805
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT REGION 1..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1017..1103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1900..1919
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2035..2060
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..90
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..143
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..255
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..324
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..352
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..420
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..455
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1057..1103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2060 AA; 228759 MW; 1F6D5A4903E19FBF CRC64;
MAPSNSDIAP WDTRSSQSTP MPPKAMAIFG TNADSGSASR KHLPRPIQAS EIAPWETRLA
HDDDIAPWER DPQAQISGSR SMNQSYFPDS IGRYDGQAAS RRPDTARTNI SDSPDYDGDA
RRPSIASATT VSSTGSRSSA ANGRFHKSLK GFFGEDPTDS RKGSTANLPE QLPPPNSSEK
PAQRSGSTQT QNTVEDRPKT PAPPPSSDVT PWAYQNFEDV SNFGSAPIRQ EQQEQQQPQN
DTLVPSSSAS SQRHGLFRHR YTRSKEDPPK GQAAPTSMPK RPSTSRESST SNLGFYRNTP
QATTPMSSST ALARNASPAP SSRKETSTKS EKRGLFSKFT KSHKDKHSPQ PEPTKTNVEP
VRLPEEPKKP RAMSNKTAAS DADNKRDRET SVASVDSAST IKASDPSPKL DRTQTASSKS
SRFHRTRHRG PSIQSETSDK GRSTSGHQGP PQAGIFSLDT NLDDISDIVS QPAAPKTPGE
AGIWAGKAAA TPMSELSAPA WDAPDSWAVK GQEDEVLDSL PEATDDGLPA IQEEDGISYF
MRVFRTDGTF ATLSMSINAT VGEVLQSLAK KSVLHDSIDN YQLVMRKHQL SRQLGSGERP
VAMQKKLLYL AGYTERDHVE DVGREDNSYL IRFTFSHEKQ TGYGSGLDKD PAFNKMQKFS
HVDLSGKSLV TIPIILYTKA SEIISINLSR NLALKVPKDF ITACINLREI KFTGNEVWRL
PPSLAWASRL TVLDVSNNRL EQLEHAELHR LMGLVSLKLA NNKLSQLPPN FSYFRQLRSL
NLSSNNFTTF PENICSLKSL VDLDISFNKL SSLPKIAQLT TLERLWVTNN DLKGPFNESF
RSLVNLKEID ARFNAITNID NITNLPNLEQ VLVGHNSITT FKGSFPKLRV LVLDHCPITS
FELDQPVPTL SSLNIASAKL VEFKETMFDY MPNLQKLNLD KNHLSNMSSQ IGRLTKLEFL
SMAKNPLNIV PPSIGNLGEL KFLNLRECNV KSLPPEIWYC RKLETLNLSS NVLETFPKQN
AAPPPNDLRD FTPTATPGMS TSPSFDDLGK LEDFQARRPS QASSGMMSIG SSPGGRKNSV
ASLSAHRKQS VISRTNTEYS MSTATRKDSN ISAARLHNTF AGSLRYLYLA DNRLEDDVFR
ELVLLPELRV LNLSYNELDD FPQGALRRWP QLSELYLSGN ELTSLPSDDL EESSNLRILH
LNANRFQVLP AELCNVHKLS TLDVGSNSLK YNVSNWPYDW NWNRNTNLKY LNFSANKRLE
IKPATHQNQN HFHAVNRDET TDLTSFNTLK YLRVLGLMDV TLLTNTIPDD NEDRRVRTSA
SLVGALMYGM ADTLGKNEHL ATLDLLKPNF RGQESEILIA MFDGQTMSSG GSRVAKYLHE
NFSAVFYEEL KKAENLKDTP IDALRRTFLA INKDMANFAS SGFDTKEHRL ANGHRGSTVA
NILGPDDLSS GGTATVLYVN GQELHVANVG DIEAILISSN GQHRQLTRKH DPAEAGERER
IREAGGYVSR QGRLNDVLEV SRAFGYYSHM PSVIAAPHTC NYQITESDEI IVIATKEFWD
YVTVDVAVDA ARAEKNDLML AAQKLRDLAM AFGARDKIMV MVLGISDLRK RGNHRFRGTS
LSMAKELGLD EGAIFPSSRK ARRKGETLVG DSRLARLEEP EPPVGDVAIC FTDIKNSTAL
WELLPVPMRS AIMMHNELMR RQLRIIGGYE VKTEGDAFMV SFPTVTSALL WCFSCQSHLL
ELPWPQEILE TAHCQEKLDS DQNTIYRGLS VRMGIHWGRP VCEQDPITRR MDYFGPMVNK
AARVSAVADG GQITVSSDFI AEVQRTLESY ADDDRRDSVG SEDTVNDDPL SVQIRRELRQ
LSSQGFEVKD LGEKKLKGLE NPEYIYLMYP TTLASRLGIS PGIESKTQPG GEPGTLGEDS
QLKDLQLDQV WKLWDIALRL EMLCSCLEAP ERAAGLHKPE LSLLTRMKER GGVQTDAFMV
NLLEHQVTRV EACATTLQLR HMYQPFQKGV SLFEQAKPIG EILSEVANLL AEVKAERSEI
KTPETSEESS EGESSEEDDE
//
