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Database: UniProt
Entry: PBLFB_EUGGR
LinkDB: PBLFB_EUGGR
Original site: PBLFB_EUGGR 
ID   PBLFB_EUGGR             Reviewed;         859 AA.
AC   P84741; Q2P9M6;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2006, sequence version 1.
DT   22-FEB-2023, entry version 66.
DE   RecName: Full=Photoactivated adenylate cyclase subunit beta-like protein FB;
GN   Name=pacB {ECO:0000312|EMBL:CAJ57398.1};
OS   Euglena gracilis.
OC   Eukaryota; Discoba; Euglenozoa; Euglenida; Spirocuta; Euglenophyceae;
OC   Euglenales; Euglenaceae; Euglena.
OX   NCBI_TaxID=3039;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:CAJ57398.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RC   STRAIN=FB {ECO:0000269|PubMed:16121285};
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   -!- 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}. Note=Paraxonemal body. And paraxonemal
CC       bodies (PABs).
CC   -!- MISCELLANEOUS: The FB strain is deficient in phototaxis. It is not
CC       known if this is due to defective adenylate cyclase activity or
CC       defective BLUF domains in this protein. In wild-type E.gracilis,
CC       photoactivated adenylate cyclase is found in the paraxonemal bodies
CC       (PABs). PABs are not visible in all cells in this strain, and are
CC       smaller than in wild-type.
CC   -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC       family. {ECO:0000255|PROSITE-ProRule:PRU00099}.
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DR   EMBL; AM181339; CAJ57398.1; -; mRNA.
DR   AlphaFoldDB; P84741; -.
DR   SMR; P84741; -.
DR   GO; GO:0031514; C:motile cilium; IDA:UniProtKB.
DR   GO; GO:0009882; F:blue light photoreceptor activity; IEA:InterPro.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0009190; P:cyclic nucleotide biosynthetic process; IEA:InterPro.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   CDD; cd07302; CHD; 2.
DR   Gene3D; 3.30.70.100; -; 2.
DR   Gene3D; 3.30.70.1230; Nucleotide cyclase; 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; Acylphosphatase/BLUF domain-like; 2.
DR   SUPFAM; SSF55073; Nucleotide cyclase; 2.
DR   PROSITE; PS50925; BLUF; 2.
DR   PROSITE; PS50125; GUANYLATE_CYCLASE_2; 2.
PE   2: Evidence at transcript level;
KW   Cell projection; Cilium; Flagellum; Repeat.
FT   CHAIN           1..859
FT                   /note="Photoactivated adenylate cyclase subunit beta-like
FT                   protein FB"
FT                   /id="PRO_0000195724"
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          414..449
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          813..859
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        813..847
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   859 AA;  94248 MW;  F7C4D688610C8EF6 CRC64;
     MYILVWKKGQ QIKTFHTLDE AAQFKAASNI DEAQMFSVTV APAISASGGS NEATNLRRLM
     YLSKSTNPEE CNPQFLAEMA RVATIRNREI GVSGFLMYSS PFSFQVIEGT DEDLDFLFAK
     ISADPRHERC IVLANGPCTG RMYGDWHMKD SHMDSITTHP AMKTILYQIA RSFSSMWSYL
     PKSAGNMLLL GKDPAAQPPE PMSVVVTFIY LVEFGSILSN PNLTDQAAEV LSTFVDVCVK
     NVEGSGGNIA KFITGICMAY WPINRTEEAL TAIQQISEDL AQLRSQQAPG SAVSLMYSQA
     GVHYGRPMLC NAGRRKSDFT LLGDCINTTS RIATLAKKFK TPLLFSQEVR CLLRDEMREE
     IVGAGMHQVK GRDKPVVVYQ FPGPELDVEM VRQKIEQFTP GRFRCQMPVV EYEGLPNSQR
     PPIFDDTPKA NRRPRTPGYG GRQRSDSQVD RPIMIAKLAG PSVSATGDTT LTTLTYISQA
     TRPMSRQDLS AIMRTATRRN AQQSITGTLL HVNGLFVQTL EGPKDAVANL YLRVRQDPRQ
     TDVTTVHMAP LQERVYPSEW TLTSATAEML ATFPPLQDVL AQLAKSFTSL ETYVPSTVVR
     HLTAGNNPRN LMPVSCGVVM LATDICSFTS LTEKSSLTEV WMICNTFIDA CTSAICQDGR
     EVIKLIGDCV TAYSPGNNAD SAVAAAQELF TFCRQLREAF VDVLDVRGCV SCGVGLEYGQ
     VVMAQCGSMG LTEYVVAGAV SARVMEVEAI TREVGYAIVV TEPVADRLSP QLRDHGIVPT
     PQAIEGLPCY GIAGEEFELD VDSIKRGIKA LHAARSGEKP LTEPEAAKPD FRVSPGRVRH
     GDSGRRSNSA QGKRSIQVR
//
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