ID A3LSN1_PICST Unreviewed; 1749 AA.
AC A3LSN1;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 2.
DT 27-MAR-2024, entry version 104.
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 Name=CDC35 {ECO:0000313|EMBL:ABN65930.2};
GN ORFNames=PICST_67440 {ECO:0000313|EMBL:ABN65930.2};
OS Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS Y-11545) (Yeast) (Pichia stipitis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX NCBI_TaxID=322104 {ECO:0000313|EMBL:ABN65930.2, ECO:0000313|Proteomes:UP000002258};
RN [1] {ECO:0000313|EMBL:ABN65930.2, ECO:0000313|Proteomes:UP000002258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545
RC {ECO:0000313|Proteomes:UP000002258};
RX PubMed=17334359; DOI=10.1038/nbt1290;
RA Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.S.,
RA Passoth V., Richardson P.M.;
RT "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT yeast Pichia stipitis.";
RL Nat. Biotechnol. 25:319-326(2007).
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; CP000497; ABN65930.2; -; Genomic_DNA.
DR RefSeq; XP_001383959.2; XM_001383922.1.
DR STRING; 322104.A3LSN1; -.
DR GeneID; 4837824; -.
DR KEGG; pic:PICST_67440; -.
DR eggNOG; KOG0618; Eukaryota.
DR HOGENOM; CLU_000430_4_1_1; -.
DR InParanoid; A3LSN1; -.
DR OMA; EIWWANK; -.
DR OrthoDB; 1698689at2759; -.
DR Proteomes; UP000002258; Chromosome 3.
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; IPR048580; CYAA_C.
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; PF21187; CYAA_C; 1.
DR Pfam; PF00211; Guanylate_cyc; 1.
DR Pfam; PF13855; LRR_8; 3.
DR Pfam; PF00481; PP2C; 1.
DR SMART; SM00789; Ad_cyc_g-alpha; 1.
DR SMART; SM00044; CYCc; 1.
DR SMART; SM00364; LRR_BAC; 9.
DR SMART; SM00365; LRR_SD22; 5.
DR SMART; SM00369; LRR_TYP; 14.
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; 4.
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, ECO:0000313|EMBL:ABN65930.2};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000002258};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 349..439
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 1035..1311
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT DOMAIN 1368..1505
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT REGION 1..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 126..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 174..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 216..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..83
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..160
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1749 AA; 195555 MW; 07612C34E1C573DD CRC64;
MSFLRRDKSK NNLNASAIQN STAYDIDRPL SPTANLTTNR SPLLRKNTDT YSPRSSIVSL
PSEGPPSDVA DSGNDSVSSL KDNYRGFHAN RRPKAIANIP PLSQPIKPRF KKKSGSLLGK
LIYSSRKDSD SSAHSGETTK SEPITEHDRK SASSDTADTV SKHKFRMPSI SLEHHHHHHH
HPHHPSLEPK ESDSDSAKVV GTTFDLDMNL DEMHGIIKSP EDPRNKSSFS DSSTNAAEAI
HDGRGNIATQ KSHISGPAGP VPESKAVWKA PDSWDVQLDQ NMNPIRTIDL ALSDSDDTDE
KEVNDDIHNH LDVERQEFRR MSDLPVLYGT RQSSHIIQGE LDSKTGKPPN HIVRVFREDN
TFTTILCSLE TTTAELLAIA QRKFFLESIS NYQISVYIGN CVKVLEPFEK PLKIQLGLLL
LSGYTDNDNL KIIGREDLSY LCKFVVENIN LRNLTHEEET MLSRDYVDVN IAGLNLKNIP
IIFHQHTYEI EKLNVADNPS IYIPLDFIQS CNNLISINFS KNGCSKFPLN FLEAKKLTHL
DMEKNFLDDL PSKFSHLKNL THLKLNSNQL TTLPKSFSRL KNLEVLNLSS NYFSVYPESI
SELSNLKDLD MSYNDLASLP ESINKLTNLS KLNLCTNKLS KSLPDYFAKM TALKRLDIRY
NLLSNVDVLG SLPNLEVAYF SKNNVSAFVD QMENMRLLHF DRNPITSLHF DNMLQYLTIV
DLSKAKITSI PDEFITKIPN IEKFVLDKNH LVTLPNELGN LQKLASLSVF GNNLSSLPST
IGKLSSLQIL DIHSNNLQSL PDDIWLLKSL SVLNVSSNIL SSFPKPPISV AKRVSSTNRL
LVLTLADNRL GDDCFESISF LVSLKSLNLS YNDILEIPEG AMRRLTRLTE VYLSGNEIAT
LPADDLENLK ALKLLFVNNN KLVSLPAELS KLTNLQHLDV GSNQLKYNIS NWPYDWSWHW
NKNLKYLNFS GNKRFEIKSS HVKNQETGEF FDSLLVLKNL KVLGLIDVTL TTTAVPDQST
EMRIRTTSSE LDNIGYGVSD SMGLREFVSS RDVFIQKFRG NENEVLICTF DGKRGAPNQG
HRVSSLAKNL FVSHFTHELE KVKSDEEIND ALRRTFLSLN KEINGILAAK KCNSFAATPQ
MLKEAVDLNL ADDGRAGCSV TVIYIKDKKL YTANCGDTAA ILSRNNGDHV LLTNRHDPTS
RSEFERIRAS GGYVSGDGAL DGDLPVARGV GFFNYLPHTH SGPDISSISL TAADDMIVVA
NKIMWDYISY ELAVDILRQE KDDPMLAAQK LRDYAICYGA TDKIAVIVIT LGEQKSNRSK
FGSNGLYNNL GRESDVIAKK RRDRVATTGD SSLRRLDDEI EPPVGELALV FTDIKNSTLL
WDAYPVPMRS AIKTHNSIMR RQLRIVGGYE VKTEGDAFMV SFPSPTSALL WCFNVQQNLL
TADWPSEILE TDQCCEVTDG KGQVIFRGLS VRMGIHWGSP VCETDVVTGR MDYFGPMVNR
ASRISAVADG GQIAVSSDFL DEFDALHKIH EEISEGKMTL FDAYQGNPRA GEIIEREIAS
IEDNGYHYFK LGERKLKGLE TPEPITLVYT SKLKIRFEIF EKRMSQNQEF NLSTRVVGAL
PVDSIYGLRT ISLRLENICS GLNGGSFVNE GFSNSSGVIS EKMNTTFKEG DLIALLNHIV
TRIESCVTTL YLRQQMSIAH GEEGVLDIKS GKSLNMVMDD VALLVRAYRE MLKIGGRGEE
KHGYIENLG
//
