ID A0A072PKB3_9EURO Unreviewed; 2052 AA.
AC A0A072PKB3;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
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=A1O9_05131 {ECO:0000313|EMBL:KEF60281.1};
OS Exophiala aquamarina CBS 119918.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=1182545 {ECO:0000313|EMBL:KEF60281.1, ECO:0000313|Proteomes:UP000027920};
RN [1] {ECO:0000313|EMBL:KEF60281.1, ECO:0000313|Proteomes:UP000027920}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 119918 {ECO:0000313|EMBL:KEF60281.1,
RC ECO:0000313|Proteomes:UP000027920};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala aquamarina CBS 119918.";
RL Submitted (MAR-2013) 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:KEF60281.1}.
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DR EMBL; AMGV01000003; KEF60281.1; -; Genomic_DNA.
DR RefSeq; XP_013262871.1; XM_013407417.1.
DR STRING; 1182545.A0A072PKB3; -.
DR GeneID; 25280058; -.
DR VEuPathDB; FungiDB:A1O9_05131; -.
DR HOGENOM; CLU_000430_4_0_1; -.
DR OrthoDB; 1698689at2759; -.
DR Proteomes; UP000027920; 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; IPR025875; Leu-rich_rpt_4.
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; PF12799; LRR_4; 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; 7.
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:UP000027920};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 507..597
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 1297..1575
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT DOMAIN 1636..1773
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT REGION 1..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 986..1014
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1027..1078
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2026..2052
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..289
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..360
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..390
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1030..1047
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1059..1078
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2052 AA; 228143 MW; 2933A2231FBB30DD CRC64;
MAIFGSPANP PARQQAQQRN AAADIAPWDL RPPNDDEIAP WERGPQAQIT GIRPFNQSYF
NDATPREAQP SVRPDTAKTN ISDSPDFDAD ARRPSIASAT TISSTGSRGS AVNGRFHKSL
KGFFGEDPTD SRKGSTANLP DQVQPNLFAE KPPQRSGSVQ TQNTAEERPK TPAPPPSSEV
TPWAYQNFED VSNFGSAPIR QPPQNESVAP NNSSSAPLHR RGLLHRHTRS KEDPPKGQQA
TSAIPKRPST SRESSTSNLG HFRGTPQTST PMSSSTALPR NTSPGPGSRK EASAPTEKRS
IFSKLKHRHH KEKQPPQPEP LRTAIEPVSP PEELKKPRSH SNRANTSDSQ DNKRDRETSV
ASVDSASTIK ASDSSPKVDR TYTAQSTKSS RFGRHGRHRG PSFQQEPLER KTTATQAPMQ
AGVFNLDTNF DDMSDIIAQP QVPKTPVDPG IFTGSKIAQT PASEISAPAW DAPDSWAVKG
QEDEVLDALP EANEDGLPAI QEEDGISYFM RVFRSDGTFA TLSMSINATV GEVLQSLAKK
SVLHDSIDNY QLLMRKHQLS RQLGGSERPV AMQKKLLQLA GYTDRDRIED IGREDNSYLI
RFTFSHEKQT GYGSGLDNDP AFNKMQKFSH VDLQGKSLVT IPIILYTKAS EIISINLSRN
IALRVPKDFV TACINLREIK FTGNEVWRLP PSLAWATRLT VLDVSNNRLE QLEHAELHRL
MGLGSLKLAN NKLTALPANF AHFRQLRSLN LSSNNFTTFP EHICALKSLV DLDISFNKLS
SLPKISQLIT LERLWVTNND LKGPFNESFK SLVNLKEIDA RFNGITDIDS VAQLPNLEQL
LVGHNNITTF KGCFQKLRVL VLDHCPITSF ELEQSVPTLT SLNIASAKLV EFKESLFDFC
PNLQKLNLDK NHLSSMSSQI GRLSKLEFLS MAKNPLNLIP PSIGNLVELK FLNLRECNIK
SLPPEIWYCR KLETLNVSSN VLETFPKQNA APPPNDARDL TPATTPGLST SPSFEELGKL
EDFQARRPSQ ASAGMMSIGS SPGGGRKNSV ASIPGHRKAS VISRTNTEYS MSPATRKDSN
ISQARLQNTF GGSLRYLYLA DNRLEDDVFR ELVLLPELRV LNLSYNELDD FPQGVLRRWT
QLSELYLSGN ELTSLPSDDL EENSNLRVLH LNVNRFQVLP AELCNVHKLA TLDVGSNSLK
YNVSNWPYDW NWNRNTNLKY LNFSANKRLE IKPAAHQNQS QFNSMSGEQT TDLTSFNTLK
YLRVLGLMDV TLLTNTIPDD NEDRRVRTSA SLVGALMYGM ADTLGKNEHL STLDLLKPNF
RGHDAEILIG LFDGQSMSSG GSRVAKYLHE NFPAMFYDEL KRSEATKDTP VDALRRTFLS
LNKDMANFAS SNFDTKEHRL ANGHRGSTVA NILGPDDLTS GGVATVMYLN GTELHVANVG
DAEAILIQSN GQHRELTRKH DPAEHRERER IREAGGYVSR QGKLNDALEV SRAFGYYSHM
PCVIAAPHTF NCGLTESDEL IVVATKEFWD YVTVDLAVDV ARAEKTDLML AAQKLRDLAM
AYGARDKIMV MVLGISDLRK RGSHRFRGTS LSMAKELGLD EGTIFPTRKK RRDQTLVGDS
RLARLEEPEA PIGEVAICFT DIKNSTALWE ILPVPMRSAI MMHNELMRRQ LRIIGGYEVK
TEGDAFMVSF PTVTSALLWC FSCQSHLLEQ NWPTEILETV HCQEKLDADQ NRIYRGLSVR
MGLHWGRPVC EQDPITRRMD YFGPMVNKAA RVSAVADGGQ ISVSTDFIAE IQRTLEAYAD
DDRRDSVGSE DTVNDDPLAN QIRRELRQLS SQGFEVKDLG EKKLKGLENP EYLYLMYPHS
LAGRLTIPPG AENKVQLGGD TPNANEEKSG PGALGKNTRL NLELDEVWKL WDIALRLEML
CSCLETPDRA AGLQKPELSL LTRMKERGGV QTDSFMMNLL EHQVTRVESC VTTLQLRHML
QPFQKGTPLV DQAAPIAGLL SQISELLRQA NRLKVGGQAA QVEEIDQYEI VDEDVDESDD
DAESAVEDTD SD
//
