ID A0A0L6VBM3_9BASI Unreviewed; 2067 AA.
AC A0A0L6VBM3;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, 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=VP01_197g6 {ECO:0000313|EMBL:KNZ58191.1};
OS Puccinia sorghi.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX NCBI_TaxID=27349 {ECO:0000313|EMBL:KNZ58191.1, ECO:0000313|Proteomes:UP000037035};
RN [1] {ECO:0000313|EMBL:KNZ58191.1, ECO:0000313|Proteomes:UP000037035}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RO10H11247 {ECO:0000313|EMBL:KNZ58191.1,
RC ECO:0000313|Proteomes:UP000037035};
RA Rochi L., Burguener G., Darino M., Turjanski A., Kreff E., Dieguez M.J.,
RA Sacco F.;
RT "Next Generation Sequencing and Analysis of the Genome of Puccinia sorghi L
RT Schw, the Causal Agent of Maize Common Rust.";
RL Submitted (AUG-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:KNZ58191.1}.
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DR EMBL; LAVV01006814; KNZ58191.1; -; Genomic_DNA.
DR STRING; 27349.A0A0L6VBM3; -.
DR VEuPathDB; FungiDB:VP01_197g6; -.
DR OrthoDB; 1698689at2759; -.
DR Proteomes; UP000037035; Unassembled WGS sequence.
DR GO; GO:0004016; F:adenylate cyclase activity; IEA:UniProtKB-EC.
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; 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; PTHR45752; LEUCINE-RICH REPEAT-CONTAINING; 1.
DR PANTHER; PTHR45752:SF149; LEUCINE-RICH REPEAT-CONTAINING PROTEIN 39; 1.
DR Pfam; PF00211; Guanylate_cyc; 1.
DR Pfam; PF13855; LRR_8; 2.
DR Pfam; PF00481; PP2C; 1.
DR SMART; SM00044; CYCc; 1.
DR SMART; SM00364; LRR_BAC; 6.
DR SMART; SM00369; LRR_TYP; 6.
DR SMART; SM00332; PP2Cc; 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; 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:UP000037035};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 702..805
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 1330..1604
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT DOMAIN 1665..1791
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT REGION 1..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 186..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 334..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 431..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 510..565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 630..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1097..1135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..255
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..646
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 663..679
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1119..1135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2067 AA; 224657 MW; BA4E8F9CC3949734 CRC64;
MDSPNHSKHS PPSPSRAHHP SILRATTTQN PFIPTHPTKP YSSLNQSSIS SHVNPSRHRR
TEDSSQPRLR QFSSQSSLNF ASSSSNTSPQ PLQFTIAPIP GSSFNQDQYT PTPFQSPNTP
QISTNPSGSS VTSSATKKRG FFGMLRRKAS RGDINASDDL SYATRSFPEE LSFPNSKIKD
LTGVTDQEWQ AQQQQPQQQS TVTPTTTSTT SKKQRIRKLT GGSGLSSKEK AHKADQNIQQ
PPISSLGSTN SFTHSNRLMS ANQGEVITLD TNLDEMDGII NRDHAAMQVR RTSSFSGAPS
FFGSPSHLNN SEIQGVGGGT VFADPFNPGR TLGSPNCVPR NTGFHEPGAG SNTGPTDSSV
HHYPSLPRSH RSIRSLGGSS SRDFIPVDSR RRESQNSQKS LTGMSLHANL NDPDFGPPAH
ATNRSLFPAT TLAQSSPSRK PPAHHYGGGL NQVGPNPTPV ATTGLGIGAA MVSAVNGTIS
AFGAGKSVSN APSLNSLAGA NTAAGWTAPE SWAVNPMDGN DSADTDVDGS EEEDGLVVSD
FYPPHPDNHD GPSDPGGAPS GAGRYAFQTN GSFSGVSGTT VFSQTGTSFS GSLYSSTTIG
SSGANTALMI PPINRLGSID ESVKSTGFGT PVMNGANASS SRRPSEAGGM SIMDGSEGSG
HGCRPTPGSN VSGSTVNGKM GGATRAGPAD GSKSLTLFIC MPKWTIRISR ADGSFATLSC
PLMYTAAEIC HQLGRKLFNQ KPPAGYKLYM KERGLERVIA PNEKPLVFQR RRLEQAGYTM
LDRLDDVGRL DYSYLMKFLY KEESLTVVAT DEDFHEHYEF VDLQARSIQA IPIVLFNHAA
LLISLNLSKN PKLDIPLDFI QLCTSLQELK LCHMAMKRVQ PSIRQCHSLM RLDISNNRIV
DLEHARLDDL PELMALRAHN NRLWTLPDYF RDFRSLSLLN ISNNKFESLP SVICEIKSLV
DLDISFNMIN SLPNEIGQLA NLQRFVFLAN PISTIPSTFS GLSELRELDC RRCLLGDIAI
FSDLPHLKKL LCENNAATIL DGRFNSLQEL NAGHNSITRL LLVGTGATLV SLNVSYAKIS
SLGQEFFDAL EFPMPPAASA NDPPGQNADD HKPQVKPSLP NLKPSNGSSS AHNRSLPPLA
RSLQELFMGD NGLGDNVFGP ISLLSELRVL NLSFNELYEI PPLTLSKCES LEELYLSGNS
LTSLPGEDIE NLSNLKTFFL NGNKLQTLPA ELGKLKHLES LDVSSNLLKY NVTNWPYDWN
WQYLNLSGNK RLEIKPAAGA QQDAVAAAKR KNLSNFNALR RLRVLGLMDV TLTTPSVPDE
SEDRRVRVTQ SEVSSMGYGI ADSMGREDYT VVGLDMVVSR FRNKDDESLF GLFDAHSKTP
FGGGKLAKFL HDSFSTTLAG ELRRLKENES VTEALRRAFL NTNRDYGNMV TSQFETRRKG
SNVGLQRSDR PSITAANCGV DAKCGASAVV MYVAKKTIYV ANVGDALAVV AKREIERIRS
AEAWVSQKGL VEDEVEVSRS FGYFHVHPAI NARPSIQTLD LSEDDEFIII ANAGLWSHMT
YQAAVDVARA QNKKADPMGA AQKLRDLALS YGAESNLMVM VIALGDLFKA KRRLTYRGAG
GAHIDEELYG ATRVATRRGQ MLDAPGEKYL TLLDREVAPP TGMVALVFTD IRNSTSLWET
NPGMQSAMRM HNQLLRRQLR AIGGYEVKTE GDAFMVSFPS VTSALLWCFT VQLELLREDW
PQEILDAEDG KEIYDSNGML CYRGLSVRMG IHWGNPHCEA DPITRRMDYF GPMSFMRIIR
TARISGEAKG GEITASLDVI EIVKTLCFDQ NDGKEGNDPL AQESDAILDP ATRRDVASIR
KMGFGVSEIG EKRLKGLEMP EFISLIYPRS LAGRLNNQGA SLGGPDSKVD EVYEPTPRML
DVNHIKQLVT LVVRLEAVSA AAVHAPLSFS PSSASTTNKL TGSNVDVSGE ERAATIGNSN
KRPKSKLLNG HLLTYPIRSE STDEELAAIL ENQVIRIENV LSSLELRSLG PIYDVLLALG
DAVKVQPNVL LHALEAFGLA SNAAGLF
//
