ID A0A177D5U0_ALTAL Unreviewed; 2111 AA.
AC A0A177D5U0;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=CC77DRAFT_1081013 {ECO:0000313|EMBL:OAG14868.1};
OS Alternaria alternata (Alternaria rot fungus) (Torula alternata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC Alternaria sect. Alternaria; Alternaria alternata complex.
OX NCBI_TaxID=5599 {ECO:0000313|EMBL:OAG14868.1, ECO:0000313|Proteomes:UP000077248};
RN [1] {ECO:0000313|EMBL:OAG14868.1, ECO:0000313|Proteomes:UP000077248}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lrK2f {ECO:0000313|EMBL:OAG14868.1,
RC ECO:0000313|Proteomes:UP000077248};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) 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}.
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DR EMBL; KV441497; OAG14868.1; -; Genomic_DNA.
DR RefSeq; XP_018380289.1; XM_018529329.1.
DR STRING; 5599.A0A177D5U0; -.
DR GeneID; 29114923; -.
DR KEGG; aalt:CC77DRAFT_1081013; -.
DR VEuPathDB; FungiDB:CC77DRAFT_1081013; -.
DR OMA; EIWWANK; -.
DR OrthoDB; 1698689at2759; -.
DR Proteomes; UP000077248; 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; PF00560; LRR_1; 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; 9.
DR SMART; SM00369; LRR_TYP; 11.
DR SMART; SM00332; PP2Cc; 1.
DR SMART; SM00314; RA; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
DR SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR SUPFAM; SSF81606; PP2C-like; 1.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
DR PROSITE; PS51450; LRR; 3.
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:UP000077248};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 601..692
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 1395..1671
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT DOMAIN 1732..1869
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 144..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 443..507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1078..1113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1126..1179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1489..1513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..196
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..268
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..309
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..324
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..380
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..415
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1087..1110
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2111 AA; 233833 MW; 45008507E6895627 CRC64;
MTRNETIGRH GSVESSWSSR SGDTIRPYGR AGSLRGTPVT VKTDKNLNSR VDRESEISPG
TVPPAPPPKD PSHKPRKPAN WDNPTTNALG HHRKQLAVLE TSGGRVPSIS RNPPTASSTN
SQVAPWASPP NGVNMANSVW SSFFNDSNED VSSSSPGFRP ATSTREDNMG FPMKDDRRPS
VASATTVSST GSKSSMGRGF HKRLQNVFGE DFPADDRQNS DTSLNTQQRN RGNSLSNTIG
SKQQSRPTSP TSSRPRTPQA SSEVTPWEFQ DSKDIPTPGE NGGRRSSEQH SAKSGRSHHK
LHVRLPGTGH RHKGSKEENK APDGRADISQ YQLRPTTSRD DSSYGVRSNQ PSALSSAFAS
KTSLLGRPSS PTPSSYSDMT RDERIAQRSP STSKTSHGFF ARLRGKDKDK SDRTLPQDNL
KNLVAAGTAS ATSLNPSINT ARLARPEASP QINMAKRQPA NNGVEAQGKE QRMRAPHHRL
PTFRKDKRPP ASENTGRDPN DTIASTAGND AVFFLDRNLD DMEGIVNPAS QQPPMTPPVG
EVPKQPPNLG EDISIPGPDD DGTAAWDAPD SWAVKRMKDE MDKLGDAEEA TTPSKEESDN
KTYCLRIFRV DSTFATLSAT LNTTVQEIIQ ILGKKTVLQD ELDNYHIVMR KHDTARQLES
NERPLLIQKR LLELAGYTDQ DRLEDVGRED NSYLCRFTFL PAKMSGYSSL ERDPGFSKMQ
KFSHIDLQGR NLITIPITLY QKATEIISLN LSRNLSLDVP RDFILACTNL REIKYTSNDA
RRLPPSLSLA SRLTMLDISN NRLQSLDRAE LYKLQSLQGL RLSNNGLTRL PRYFGEYRAL
RSLNLSSNSL SEFPDFLCEV RTLVDLDISF NSISSLPKIG QLTCLERLWA TNNKLTGSFP
STLSNLVNLR EIDVRFNALD SMDVMSQLPR LEYLMIGHNS ISAFEGYFPK IRVLHMNHNP
VTRFGLNQAT PSLSVLNLAS AKLAQLPEDL FGKLTGLTKL ILDKNHFTSI SNNIGKLYRL
EHLSVARNSL DVLPAEIGRL VELRYLDVRE NNLNKLPQEL WYARRLETLN VSSNVLEAFP
KPGASPPQVT NGDQSQVDGA STTATPGLAS SPSYEELGKL EDFQNRRPSQ ASGGLSVGAS
SASSQRKGSQ ASYNTASTRK PSVASRAPTE GTLTPVSRKD SSLSSRLVTT FAGSLRHVFL
ADNRLNDDVF DELCLLPELR IVNLAYNLIY DVPPRTIRRW QHLTELYLSG NDLTSLPAED
LEEVGSLKVL HINNNKFQVL PAELGKVAQL AVLDVASNSL KYNVSNWPYD WNWNWNHKLR
YLNLSGNKRL EIKPSGSYSG SGMSMREGRD LTDFSSLINL RVLGLMDVTM MVPSVPEQSE
DRRVRTAGSA VGTMAYGMAD SLGRNEHIST MDMVVPRFRS HDDEQLLGLF DAQPLAGGGA
KIAKYLYDHF KNRFANELER LQPTETPSDA LRRTYLGLNK ELATAASQGL DKNGLTAPST
QSRSSMPDLS DDDLTSGSVA TVLFLKEMEL YISNVGDAQA LLIRSEGGHK ILTRKHDPAE
PGERSRIREA GGFVSRQGKL NDVLEVSRAF GYVQMSPSVI ASPHILNLTL GDRDEMVLIA
SRELWDYLTP DFAVDVARSE RDDLMVAAQK LRDLAIAFGA TNKIMVMLLG VSDLKSKQRA
RYRTQSMSLI PAPGADPDFA ATRRRGKKGN LVGDSKLARL DNEVDAPTGE VSLVFTDIKN
STILWETYPI AMRSAIKMHN ELMRRQLRII GGYEVKTEGD AFMVAFRTVT SALLWCFTIQ
SQLLDVQWPQ EILNSVNGQE VVDPDGNVIF RGLSVRMGIH WGTPVCEVDP VTKRMDYFGP
MVNRASRISS VADGGQITVS SDFIAEIQRL LETHIEGDRK NSAGSEEAYS DDINSQMIRG
ELRSLSSQGF EVKDLGERRL KGLENPEYIY LMYPHSLASR LAVQRQTEQK PAEQQKEAVV
GQKMAGSQLT IDTEDVWNLW NISLRLEMLC SSLENPGCSE LKPPETALLE RMRSRGGEIT
DRFLINFVEH QISRIETCAS TLALRHMVRP FGAAPLLEQA CHMGDIFSEL EAKLKRLEEF
ERGAIEGMAP S
//
