ID   PCYAB_EUGLO             Reviewed;         860 AA.
AC   Q76L33;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Photoactivated adenylate cyclase subunit beta;
DE            EC=4.6.1.1;
DE   AltName: Full=Photoactivated adenylyl cyclase subunit beta;
GN   Name=pacB {ECO:0000303|PubMed:14630964};
OS   Euglena longa (Euglenophycean alga) (Astasia longa).
OC   Eukaryota; Discoba; Euglenozoa; Euglenida; Spirocuta; Euglenophyceae;
OC   Euglenales; Euglenaceae; Euglena.
OX   NCBI_TaxID=3037;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:BAD04849.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX   PubMed=14630964; DOI=10.1104/pp.103.034223;
RA   Ntefidou M., Iseki M., Watanabe M., Lebert M., Haeder D.-P.;
RT   "Photoactivated adenylyl cyclase controls phototaxis in the flagellate
RT   Euglena gracilis.";
RL   Plant Physiol. 133:1517-1521(2003).
RN   [2] {ECO:0000305}
RP   SUBCELLULAR LOCATION.
RX   PubMed=16121285; DOI=10.1039/b502002f;
RA   Ntefidou M., Haeder D.-P.;
RT   "Photoactivated adenylyl cyclase (PAC) genes in the flagellate Euglena
RT   gracilis mutant strains.";
RL   Photochem. Photobiol. Sci. 4:732-739(2005).
CC   -!- FUNCTION: Acts as a photoreceptor for the step-up photophobic response.
CC       {ECO:0000269|PubMed:14630964}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP = 3',5'-cyclic AMP + diphosphate; Xref=Rhea:RHEA:15389,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58165; EC=4.6.1.1;
CC         Evidence={ECO:0000250|UniProtKB:Q8S9F1};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:Q8S9F1};
CC   -!- SUBUNIT: Heterotetramer of two alpha and two beta subunits.
CC       {ECO:0000250|UniProtKB:Q8S9F1}.
CC   -!- SUBCELLULAR LOCATION: Cell projection, cilium, flagellum
CC       {ECO:0000269|PubMed:16121285}.
CC   -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC       family. {ECO:0000255|PROSITE-ProRule:PRU00099}.
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DR   EMBL; AB085170; BAD04849.1; -; mRNA.
DR   AlphaFoldDB; Q76L33; -.
DR   SMR; Q76L33; -.
DR   GO; GO:0031514; C:motile cilium; IDA:UniProtKB.
DR   GO; GO:0004016; F:adenylate cyclase activity; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0009882; F:blue light photoreceptor activity; IEA:InterPro.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0009881; F:photoreceptor activity; IDA:UniProtKB.
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; 2.
DR   Gene3D; 3.30.70.1230; -; 2.
DR   InterPro; IPR001054; A/G_cyclase.
DR   InterPro; IPR036046; Acylphosphatase-like_dom_sf.
DR   InterPro; IPR007024; BLUF_domain.
DR   InterPro; IPR029787; Nucleotide_cyclase.
DR   Pfam; PF04940; BLUF; 2.
DR   Pfam; PF00211; Guanylate_cyc; 2.
DR   SMART; SM01034; BLUF; 2.
DR   SUPFAM; SSF54975; SSF54975; 2.
DR   SUPFAM; SSF55073; SSF55073; 2.
DR   PROSITE; PS50925; BLUF; 2.
DR   PROSITE; PS50125; GUANYLATE_CYCLASE_2; 2.
PE   2: Evidence at transcript level;
KW   ATP-binding; cAMP biosynthesis; Cell projection; Chromophore; Cilium; FAD;
KW   Flagellum; Flavoprotein; Lyase; Nucleotide-binding; Photoreceptor protein;
KW   Receptor; Repeat; Sensory transduction.
FT   CHAIN           1..860
FT                   /note="Photoactivated adenylate cyclase subunit beta"
FT                   /id="PRO_0000233947"
FT   DOMAIN          56..149
FT                   /note="BLUF 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00030"
FT   DOMAIN          205..333
FT                   /note="Guanylate cyclase 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT   DOMAIN          471..563
FT                   /note="BLUF 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00030"
FT   DOMAIN          619..748
FT                   /note="Guanylate cyclase 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT   REGION          420..443
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          819..860
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        819..848
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   860 AA;  94375 MW;  2FFD4DDDD239B39D CRC64;
     MYILVWKRGQ QIKTFHTLDE AANFKAASNI DEAQMFSITV APAISASGGS NEATNLRRLM
     YLSKSTNPEE CNPQFLAEMA RVATLRNREI GVSGFLMYSS PFFFQVIEGT DEDLDFLFAK
     ISADPRHERC IVLANGPCTG RMYGDWHMKD SHIDSITTHP AMKTILYQIA RSFSSMWSYL
     PKSAGNMLLL GKDPAAQPPE PMSVVVTFIY LVEFGSILSN PNLTEQAAEV LSTFVDVCVK
     NVEGSGGNIA KFITGICMAY WPINRTEDAL NAIQQISEDL AQLRSQQAPG SAISLMYSQA
     GVHYGRAMLC NAGSRKSDFT LLGDCINTTS RIATLAKKLK TPLLFSFEVR CLLGDEMREE
     VEGAGMHQVK GRDKPVVVYQ FPGPELDVEM VRQKIEHFTP GRFRCQMPVV EYESLPISQR
     PPIFDDTPKG KPRPRTPGYG GRQRSDSLVD RLIMIAKLAG PSISATGDST LTTLTYISQA
     TRPMSRLDLS AIMRTATRRN AQLSITGTLL YVNGLFVQTL EGPKDAMVNL YLKIRQDPRH
     TDVVTVHMAP IQERAYPAEW TLTSATEEML ATFPPLQDVL SQLAKSFTSL ETYVPSTVVR
     YLTAGNNPRN LMPVSCGVVM LATDICSFTS LTEKSSLTEV WMICNTFIDA CTSAICQEGG
     EVIKLIGDCV TAYFPGNGAD SAVAAAQELF TFCRQLREAF VDVLDVRGCV SCGVGLDYGQ
     VVMAQCGSLG LTEYVVAGAV SARVMEVESI TREVGYAIVI TEPVADRLSP QLRDHGIIPT
     PQAIEGLPCY GIAGEEFELD VDSIKRGIKA LHAARSGEKP LALEPEEAKQ DYRVSPGRMR
     HGDSGRRSNS AQGKRSTQVR