ID   PCYAA_EUGLO             Reviewed;        1019 AA.
AC   Q76L34;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Photoactivated adenylate cyclase subunit alpha;
DE            EC=4.6.1.1;
DE   AltName: Full=Photoactivated adenylyl cyclase subunit alpha;
GN   Name=pacA {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:BAD04848.1}
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:Q8S9F2};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:Q8S9F2};
CC   -!- SUBUNIT: Heterotetramer of two alpha and two beta subunits.
CC       {ECO:0000250|UniProtKB:Q8S9F2}.
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; AB085169; BAD04848.1; -; mRNA.
DR   AlphaFoldDB; Q76L34; -.
DR   SMR; Q76L34; -.
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   Gene3D; 3.80.10.10; -; 1.
DR   InterPro; IPR001054; A/G_cyclase.
DR   InterPro; IPR036046; Acylphosphatase-like_dom_sf.
DR   InterPro; IPR007024; BLUF_domain.
DR   InterPro; IPR032675; LRR_dom_sf.
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..1019
FT                   /note="Photoactivated adenylate cyclase subunit alpha"
FT                   /id="PRO_0000233946"
FT   DOMAIN          55..148
FT                   /note="BLUF 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00030"
FT   DOMAIN          204..332
FT                   /note="Guanylate cyclase 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT   DOMAIN          467..559
FT                   /note="BLUF 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00030"
FT   DOMAIN          615..744
FT                   /note="Guanylate cyclase 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT   REGION          822..859
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        842..858
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1019 AA;  112078 MW;  69F402B6002414A7 CRC64;
     MYILVWKEGQ QIKTFQDLEE CGQFQIASNI TDGQIFSVSV TPTMSKGGET GETQLRRLMY
     LSASTEPEKC NAEYLADMAH VATLRNKQIG VSGFLLYSSP FFFQVIEGTD EDLDFLFAKI
     SSDPRHERCI VLANGPCTGR MYGEWHMKDS HIDNITKHPA IKTILFQIAR SFSSMWSYLP
     KNAANMLLLG KNPNKQAPEP MSVVVTFIYL VEFSSILAHP GLTEQCADIL AAFVDACVRN
     VEGTGGQVAK FITGICMAYW PINRAEDALV GLQQLSEDLA ELRSQQPPGS ALSLIYSRCG
     VHYGRALLCN AGFRKADFTL LGDCINTASR ITSLSVKLKV PLLLSFEVRC LLGDEMREEL
     ESAGLHKVKG RDKPVQVYQF NAPELDSAVV RTKIEQFNPG RYRALCPVKP YDSLHPAQRP
     PIFDDTPRDS QPKVNQMQRR DSLVDRLSMI AKLAFPSSMM VGGESQLITL TYISQAAHPM
     SRLDLSSIQR VSFSRNESSN ITGSLLYVNG LFVQTLEGPK SAVVSLYLKI RQDKRHKDVV
     AVFMAPIEER VYGSPLDMTA ATEEMLATFP PLQDVLSQLA KSFISLETYV PSTVVRYLTA
     GNNPRNLQPV SVEVVMLATD ICSFTPLSER CSLTEVWTIC NTFIDACTSA ICNEGGEVIK
     LIGDCVTAYF PPTAADNAVH ACQEIVSFCA QLRDAFRDVL DCRSVVACGV GLDFGQVIMA
     QCGSLGMTEF VVAGEVSARV MEVEALTREA GRAIVITEPV ADRLSPKLRD TGIVPCQEGV
     DGVPCYGILG VEWELDVAII KKNIYGFHEA RAQAALKKVD DGTNAPGRGA PAAGVPSSPK
     ARALGRTSSV SSYTPDLNET LDPRMAESVF NDLCNQRGDA PNNSIAAKLR QAANDDRLDL
     GRMLQGPHEL MPVLQAIKQL TNLRMLNMSD NFVDDNNVGE LAESCIPMRS LQVLDLSNNP
     GLTKVIALKR LIKHNTQIRE ILLNGTRIAP MEQRKLQSSM NVNRMCASTD SKSSHKYDH