ID A0A0D2AHN3_9EURO Unreviewed; 2086 AA.
AC A0A0D2AHN3;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 45.
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=PV07_10125 {ECO:0000313|EMBL:KIW24407.1};
OS Cladophialophora immunda.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=569365 {ECO:0000313|EMBL:KIW24407.1, ECO:0000313|Proteomes:UP000054466};
RN [1] {ECO:0000313|EMBL:KIW24407.1, ECO:0000313|Proteomes:UP000054466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 83496 {ECO:0000313|EMBL:KIW24407.1,
RC ECO:0000313|Proteomes:UP000054466};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Cladophialophora immunda CBS83496.";
RL Submitted (JAN-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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KN847045; KIW24407.1; -; Genomic_DNA.
DR RefSeq; XP_016244623.1; XM_016397432.1.
DR STRING; 569365.A0A0D2AHN3; -.
DR GeneID; 27349319; -.
DR VEuPathDB; FungiDB:PV07_10125; -.
DR OrthoDB; 1698689at2759; -.
DR Proteomes; UP000054466; 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; 10.
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; 5.
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:UP000054466};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 560..650
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 1349..1627
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT DOMAIN 1690..1827
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT REGION 74..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1038..1066
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1078..1129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1927..1951
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2067..2086
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..92
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..184
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..268
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..346
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..371
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 415..443
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..473
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1079..1129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2086 AA; 232215 MW; 3C3E7C8C3DA9C39C CRC64;
MVCSVELTWN LRSIQASTLP FLAMSRSNNE VAPWDTRPTQ PMPPKAMAIF GTGTNPNATG
RQQFPQPRAI HDIAPWDTQH PDDDDDIAPW ERDPQAHISG TRPLNSSYFN DSSGRDAPGS
SRRPDTARTN TSDSPEYDGD ARRPSIASAT TVSSTGSRSS TANGRFHKSL KGFFGEDPTD
SRKGSTADLA ESVPIASSSD KPSQRSGSVQ TQTTVDDRPK TPAPPPSSDV TPWAYQNFED
VSNFGSAPIR QEQQQQQLQP QHESLQPVAP ASTHRRGLLH RHTRSKEDPP KGQQTPASIP
KRPSTSRESS TSNLAFYRNT PPNSTPMSSS TTLTRNASPA PQSRKEPPTQ SEKRSIFSKL
TKSRKDKQSP QPEPIKTNVE VVRPPEEQKK GRIQSTKTTT SDLSDNKRDR ETSVASVDSA
STIKATDPSP KLDRTQTASS KASRFTRHGR HRGPSIQSDT SEKGKATSQQ APMQAGVFSL
DTNFDDMSDI ISQPPAPKTP GEAGIWTGKA SATPMSELSA PAWDAPDSWA VKGQEDEVLD
SLPEATEDGL PAIQEEDGIS YFMRVFRTDG TFATLSMSIN ATVAEVLQSL AKKSVLHDSI
DNYQLLMRKH QLSRQLGSGE RPVAMQKKLL YLAGYTERDR VEEVGREDNS YLIRFTFSHE
KQTGYGSGLD KDPAFNKMQK FSHVDLSGKS LVTIPIILYT KASEIISINL SRNLALKVPK
DFITACINLR EIKFTGNEAW RLPPSLAWAS RLTVLDVSNN RLEQLEHAEL HRLMGLVSLK
LANNKLSELP PSFSYFRQLR SLNLSSNNFT TFPENICSLK SLVDLDISFN KLSSLPKISQ
LTTLERLWVT NNDLKGPFNE TFASLINLKE IDARFNAITN IDNVTSLPNL EQLLVGHNNI
TTFKGSFPKL RVLVLDHCPI TSFELDQPVP TLSSLNIASA KLVEFKETMF DHMPNLQKLN
LDKNHLSNMS SQIGRLTKLE FLSMAKNPLN IVPPSIGNLA ELKFLNLREC NVKSLPPEIW
YCRKLETLNL SSNVLETFPK QNAAPPPSEP KDYTPTATPG LSTSPSFDDL GKLEDFQARR
PSQASSGMMS IGSSPGARKN SVVSLSAHRK QSVISRTNTE YSMSAATRKD SNISQARLHN
TFAGSLRYLY LADNRLEDDV FRELVLLPEL RVLNLSYNEL DDFPQGVLRR WPQLSELYLS
GNELTSLPSD DLEESSNLRI LHLNANRFQV LPAELCNVHK LSTLDVGSNS LKYNVSNWPY
DWNWNRNTNL KYLNFSANKR LEIKPAAHQN QSHFHSMNRN DTTDLTSFNT LKYLRVLGLM
DVTLLTNTIP DDNEDRRVRT SASVVGALMY GMADTLGKNE HLSTLDLLKP NFRGQDSEIL
IGMFDGQTMS SGGSRVAKYL HENFSAVFYD ELKKAESLKD TPIDALRRTF LAINKDMANF
ASSNFDTKEH RLANGHRGST VANILGPDDL SSGGVAAVLY INGQELHVAN VGDIEAILIQ
SNGQHRQLTR KHDPAEPGER ERIREAGGYV SRQGRLNDVL EVSRAFGYYS HMPSVIAAPH
TFKCQITESD ELIVVATKEF WDYVTVDVAV DAARAEKNDL MLAAQKLRDL AMAFGARDKI
MVMVLGISDL RKRGNHRFRG TSLSMAKEMG LDEGAIFPSS RKARRKGETL VGDSRLARLE
EPEPPVGDVA ICFTDIKNST ALWEILPVPM RSAIMMHNEL MRRQLRIIGG YEVKTEGDAF
MVSFPTVTSA LLWCFSCQSH LLELPWPQEI LETVHCQEKL DSEQNTIYRG LSVRMGMHWG
RPVCEQDPIT RRMDYFGPMV NKAARVSAVA DGGQITVSSD FIAEVQRTLE SYADDDRRDS
VGSEDTVNDD PLSVQIRREL RQLSSQGFEV KDLGEKKLKG LENPEYIYLM YPHSLASRLE
IPPGAEQKVQ LGGEGPATAD EKGQPGTLGK DSQLKDLQLD EVWKLWDIAL RLEMLCSCLE
APERAAGLHK PELSLLTRMK ERGGVQTDGF MMNLLEHQVT RVEACATTLQ LRHMYRPFQK
GVSLFDQAKP ISEVLHEIST ILAEVKEERN QIHTPDTGEE TDSESG
//
