ID A0A1Z5TFR0_HORWE Unreviewed; 2178 AA.
AC A0A1Z5TFR0;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=BTJ68_05342 {ECO:0000313|EMBL:OTA34837.1};
OS Hortaea werneckii EXF-2000.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Hortaea.
OX NCBI_TaxID=1157616 {ECO:0000313|EMBL:OTA34837.1, ECO:0000313|Proteomes:UP000194280};
RN [1] {ECO:0000313|EMBL:OTA34837.1, ECO:0000313|Proteomes:UP000194280}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-2000 {ECO:0000313|EMBL:OTA34837.1,
RC ECO:0000313|Proteomes:UP000194280};
RA Sinha S., Flibotte S., Neira M., Lenassi M., Gostincar C., Stajich J.E.,
RA Nislow C.E.;
RT "The recent genome duplication of the halophilic yeast Hortaea werneckii:
RT insights from long-read sequencing.";
RL Submitted (JAN-2017) 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:OTA34837.1}.
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DR EMBL; MUNK01000053; OTA34837.1; -; Genomic_DNA.
DR STRING; 1157616.A0A1Z5TFR0; -.
DR VEuPathDB; FungiDB:BTJ68_05342; -.
DR InParanoid; A0A1Z5TFR0; -.
DR OrthoDB; 1698689at2759; -.
DR Proteomes; UP000194280; 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:SF1; ZGC:77287; 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; 11.
DR SMART; SM00365; LRR_SD22; 8.
DR SMART; SM00369; LRR_TYP; 12.
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; SSF52075; Outer arm dynein light chain 1; 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:UP000194280};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 650..741
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 1462..1740
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT DOMAIN 1801..1938
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT REGION 1..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1147..1167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1180..1250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1556..1581
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..256
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..293
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..324
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..451
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..476
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..528
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1181..1250
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2178 AA; 240300 MW; A768591F4ACE059F CRC64;
MTLRNKRSKE GTGQHDGGGQ QQQQQQPLYQ QPQYQQQQRS TQPHEGRQGS AESSGAESWR
SNSTVRGHLG GSLGDGGGAG GSSGGGGRKG SLKEGRGTAV TVNTENTKNK RLQLDRKDSE
VSPGTVVAGK QAPASNARGT IAPWEQDEAP SPGSQPSEFR NDFTIHHGQG NAPSINRHPP
SASLQWDGRS GGNERPMPNS IFSSSFYDDS NENLGQVSPG YAPPNGMGFP GDGDDRRPSI
ASATTVSSSG SKSSFGNKYK KKLHGFFGED PYNSGQQDNG STSRHNSEAS SMKGGILPSF
APGASRARNN SMNDAMGRSG PPSPSSSRPR TPVAPGPSSE VTPWVFQDQD RNASETQIAE
QSNGRPSRSH RLHLPGHRHN RSTEEKPSIS HGYPLRPATS RDQSFSTLRR DREPSSAMSS
TLNLRARATS PTPSAHSSLG GQVQNQRSPR DGGPAPNKRS LFDRVTGRHK NEKASGEGLH
TSASMTSLPM NNSLVNKSRN ETKSVSRPSK GTMRTDTANG NVSGQQKPSR IPFKGRKGDT
AADVRQLTKD PNAAGPGEGD ALWHLDTDMS HMEGIVDHRQ PPMTPPNNDI YTGWPGEQPT
TKQPNQGVED TGEWNAPDSW AVRRVTDENQ GRLMELDDEG NVPRDEDPGP MYFMRIFRAD
STFAVISASL NTTAAELISM MAKKTFLQDE LDNYQIVMRK QDASRQLESG ERPLVMQKKL
LEMAGYKESD RLEDLGREDH GYLCRFTFLP AKMSGYSSLE RDPGFNKMQR FNHIDLSGRN
LITIPITLYQ KATEIITLNL SRNLKLDIPK DFIQSCTSLR EIKYTSNEAW RLPPSLSLAQ
RLTMLDISNN RLEQLEHADL WKLNGLVSLK LSNNKLSSVP PYFSQYHALR SLNLSSNSLT
EFPDALRQLT TLVDLDVSFN SISSLGDLGT LSNLERLWAT NNKLSGPFDR SFSHLINLKE
IDARFNAISN IDVVSQLPKL EILMLGHNSI SQFEGSFARL KVLFLNHNPV TNFDLNAPVP
TLSVLNLASA KLSRLPDAVF MKMGGLTKLT ISKNHFVSLS PHFGLLSKLE YLSIAKNELS
RLPTEIGRLT ELRYLDVREN NLSILPPEIW YAKRLETLNV SSNVLADFPK PATAPLPPLP
ADVGFAAGGM TPAKEGSGPL GTSPDFEELG KLEDFQMRRP SQASGMLSVS SSPGGSASRK
GSVVSYNSST GKSGPGALPR NASTASSVNT TGTATPTGPT GPQGQGIRKD STLSSRLATT
FSTSLRHLFL ADNRLEDDVF NELVLLPELR ILNLSYNQLY DIPPRTIRRW THLTELYLSG
NDLTSLPSED LEESSSLKVL HLNNNKFQVL PAELGKVQKL AILDVGSNVL KYNVSNWPYD
WNWNWNHQLR YLNLSGNKRL EIKPSAQSLN ARDSRDLTGF SSLVNLRVLG LMDVTLTIPS
VPDQAPDRRV RTAGSTIGNT MPYGMADTLG RNEHLSTLDM VVPRFRGHED ETLVGLFDGQ
SLSSGGSRVA KYLHEKFKHH FIEELEKLGN DETPVDAMRR TYLGLNKELS TAATQALDAR
EHPSSALVHR PSVSGPELGE DDLNSGSVAT VIYLQGMQLY MSNVGDAQAL LIQSEGGHRV
MTRKHDPAET TERARIREAG GFVSRQGKLN DQLDVSRAFG YVQLSPCVVA APHVCKVDIK
ESDEMILLAS RELWDYLTPD FAVDVARQER GDLMRAAQKL RDLAIAFGAT GKIMVMMIGV
SDLRKREKAR FRTHSMSMNP SGGPDDFFTT VSKGKRRRDA VGDQRLARLD QEVDAPTGEV
TLVFTDIKNS TILWETYPEA MQSAIKMHNE VMRRHLRIIG GYEVKTEGDA FMVAFPTVTS
ALLWSFTIQT QLLEVQWPQE ILNSVHGEEM QDADGNVIFR GLSVRMGVHW GRPVCEIDPV
TKRMDYFGPM VNRAARIEGV ADGGQICVSS DFIQEVQRML ESHIESDRSG STGSEDTLSD
DMMTQAIRRE LRSLSSQGFE VKDLGQRTLK GLENPEYIYL MYPHSLASRL VVQQQKAEAE
ARSKDEHQAT KTRNSELTID TENVWDLWNV SLRLEMLCSS LESTGITSLK PPETALLERM
KSRGGEVTDR FLLNFVEHQI SRIETCITTL AVRNMMRPFK HGMLKQACPM SDILTDLTSQ
LDELKMYREA AEMDMAPS
//
