ID A0A162Q929_MUCCL Unreviewed; 1347 AA.
AC A0A162Q929;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
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};
DE Flags: Fragment;
GN ORFNames=MUCCIDRAFT_126456 {ECO:0000313|EMBL:OAC99959.1};
OS Mucor lusitanicus CBS 277.49.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX NCBI_TaxID=747725 {ECO:0000313|EMBL:OAC99959.1, ECO:0000313|Proteomes:UP000077051};
RN [1] {ECO:0000313|EMBL:OAC99959.1, ECO:0000313|Proteomes:UP000077051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 277.49 {ECO:0000313|EMBL:OAC99959.1,
RC ECO:0000313|Proteomes:UP000077051};
RG DOE Joint Genome Institute;
RA Corrochano L.M., Kuo A., Marcet-Houben M., Polaino S., Salamov A.,
RA Villalobos J.M., Alvarez M.I., Avalos J., Benito E.P., Benoit I.,
RA Burger G., Camino L.P., Canovas D., Cerda-Olmedo E., Cheng J.-F.,
RA Dominguez A., Elias M., Eslava A.P., Glaser F., Grimwood J., Gutierrez G.,
RA Heitman J., Henrissat B., Iturriaga E.A., Lang B.F., Lavin J.L., Lee S.,
RA Li W., Lindquist E., Lopez-Garcia S., Luque E.M., Marcos A.T., Martin J.,
RA Mccluskey K., Medina H.R., Miralles-Duran A., Miyazaki A., Munoz-Torres E.,
RA Oguiza J.A., Ohm R., Olmedo M., Orejas M., Ortiz-Castellanos L.,
RA Pisabarro A.G., Rodriguez-Romero J., Ruiz-Herrera J., Ruiz-Vazquez R.,
RA Sanz C., Schackwitz W., Schmutz J., Shahriari M., Shelest E.,
RA Silva-Franco F., Soanes D., Syed K., Tagua V.G., Talbot N.J., Thon M.,
RA De Vries R.P., Wiebenga A., Yadav J.S., Braun E.L., Baker S., Garre V.,
RA Horwitz B., Torres-Martinez S., Idnurm A., Herrera-Estrella A.,
RA Gabaldon T., Grigoriev I.V.;
RT "Expansion of signal transduction pathways in fungi by whole-genome
RT duplication.";
RL Submitted (JUN-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:OAC99959.1}.
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DR EMBL; AMYB01000007; OAC99959.1; -; Genomic_DNA.
DR STRING; 747725.A0A162Q929; -.
DR VEuPathDB; FungiDB:QYA_126456; -.
DR OrthoDB; 1698689at2759; -.
DR Proteomes; UP000077051; Unassembled WGS sequence.
DR GO; GO:0004016; F:adenylate cyclase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; 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 InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR48051; -; 1.
DR PANTHER; PTHR48051:SF1; NON-SPECIFIC SERINE/THREONINE PROTEIN KINASE-RELATED; 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; 10.
DR SMART; SM00369; LRR_TYP; 10.
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; SSF52075; Outer arm dynein light chain 1; 1.
DR SUPFAM; SSF81606; PP2C-like; 1.
DR SUPFAM; SSF54236; Ubiquitin-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 cAMP biosynthesis {ECO:0000256|ARBA:ARBA00022998};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Reference proteome {ECO:0000313|Proteomes:UP000077051};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 45..142
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 799..1052
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT DOMAIN 1121..1257
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OAC99959.1"
FT NON_TER 1347
FT /evidence="ECO:0000313|EMBL:OAC99959.1"
SQ SEQUENCE 1347 AA; 151090 MW; FBBAF3B850B80901 CRC64;
WAPPDSWGVQ PPSIMSASTN MLEEDHADFE DYQIDVQEKW DVPKKNANIK IYRPDKTYNT
LHVPLNSTTL EILKKLATKF FMSDMTKFNL VMKRHNIERI LGLTERPLQI QKLLQEQMGY
MDQDKIDDST YLVRFQMMPN IAQPVQEDKD FGQHVDLQSR SLATIPIYLY KHASRIVSLD
ISKNLHIEIP LDFIQMCTSL KQLWLANNEY LALPPSTQHI ASLEHLNISG NRLRDLDHAN
LHEITGLRTL RAINNKLESI PDTFATCFDH LTTLFISNNS FTKFPMVICD ILTLAYLDIS
FNKIQMFPEE IGQLTNLVGL FAIANRITGA LPASFVHLTK LQELDIRQNL ITDLDVVSHL
PRLEILLVDY NSTSIVNFEI KSLKQLKMYK NHLTQFNLTS GPGGGTCLTE LNLSCCKLSS
LPEDLFNNTQ GLERLVLDSN TLNSIPSSIG ALQRLVKLSI QNNNLETLPA EIGKLSELKA
LDAQKNNLKS LPKEIWLCSS LQTLNCSSNL LDSFPEPLST ITPCSTPLTN KKAGDDLSDM
TLICDEDDDM MMNIIPPALN AGQGVVKRLD HLLDYNSMTR STSRATFVSS NSPRNHPPPL
SLSLRQLFLG DNRFTDDIWS PLSLFLELRT LNLSFNDLYE VPPDGLCHQH LYELYLSGNQ
LTSLPADDIE RLQYMRVLAV NGNKLQTLPA EIGKLRKLLV LDVGNNVLKY NIANWPYDWN
WNWNLGLKYL NLSGNKRLEI QKTHPDPNNP KDKDLSDFSA LTRLRMLGLM DITILGVSVP
EEFHDRRVRT SPSEVNSMSY GVADWLGPSD HLSTWDLVMP RFRSKEDECI FALFDGSKHP
KSGCRLTKQL NDTLTAQFTK ELASIKSDDT IVSAVRRVFL GLEQSLGTSP YIVDKDSGAS
AVLCYISGTK LYVANVGDAL AVISRNNGQA FEITQKHIPL NPSEVSRIRA AGGHVSNSGL
LNNELHVSRS FGHFHLVPVV NCNPFVSTID LTENDEFVIM ASRGLWDKMT YQTAVDIART
QKDDLMAAAQ KLRDFAITYG ATDNLMVMVI GVGDLFDKRE KRYRGNRGNN MGPGRGGVGA
DAGAEDGLLV KSKRRGKEEV PGDSTLARLE REVAPPVSQL ALVFTDIKSS TQFWETQPEN
MRSAIKIHDA IMRRTLRSVG GYEVKTEGDA FMVCFKNITA ALLWCFTVQL QLLEADWPAG
ILDTEEGREI EKDGIVIYKG LSVRMGIHWG SPVFERNPIT QRMDYFGPVV NKASRICNAA
DGGQICVSSD VIAALRNFPS MFDQDAELQT NTSTEVDAFS GTFPVSRDLL QLKQLGFHVV
ELGERRLKGL ETPETLSLVY SKQLLAR
//