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Database: UniProt
Entry: A0A2S2FGG2_9GAMM
LinkDB: A0A2S2FGG2_9GAMM
Original site: A0A2S2FGG2_9GAMM 
ID   A0A2S2FGG2_9GAMM        Unreviewed;       952 AA.
AC   A0A2S2FGG2;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=EAL domain-containing protein {ECO:0000313|EMBL:AWL29412.1};
GN   ORFNames=DJ533_12925 {ECO:0000313|EMBL:AWL29412.1};
OS   Acinetobacter defluvii.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=1871111 {ECO:0000313|EMBL:AWL29412.1, ECO:0000313|Proteomes:UP000245977};
RN   [1] {ECO:0000313|Proteomes:UP000245977}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WCHA30 {ECO:0000313|Proteomes:UP000245977};
RA   Hu Y., Qin J., Feng Y., Zong Z.;
RT   "The complete genome of Acinetobacter defluvii strain WCHAD010030.";
RL   Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP029397; AWL29412.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S2FGG2; -.
DR   STRING; 1871111.GCA_001704615_01901; -.
DR   KEGG; adv:DJ533_12925; -.
DR   OrthoDB; 9804951at2; -.
DR   Proteomes; UP000245977; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   CDD; cd01948; EAL; 1.
DR   CDD; cd01949; GGDEF; 1.
DR   CDD; cd00130; PAS; 1.
DR   Gene3D; 3.30.70.270; -; 1.
DR   Gene3D; 3.20.20.450; EAL domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 2.
DR   InterPro; IPR001633; EAL_dom.
DR   InterPro; IPR035919; EAL_sf.
DR   InterPro; IPR000160; GGDEF_dom.
DR   InterPro; IPR029787; Nucleotide_cyclase.
DR   InterPro; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013655; PAS_fold_3.
DR   InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR   NCBIfam; TIGR00254; GGDEF; 1.
DR   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR44757:SF2; CYCLIC DI-GMP PHOSPHODIESTERASE PDER; 1.
DR   PANTHER; PTHR44757; DIGUANYLATE CYCLASE DGCP; 1.
DR   Pfam; PF00563; EAL; 1.
DR   Pfam; PF00990; GGDEF; 1.
DR   Pfam; PF08447; PAS_3; 1.
DR   Pfam; PF13426; PAS_9; 1.
DR   SMART; SM00052; EAL; 1.
DR   SMART; SM00267; GGDEF; 1.
DR   SMART; SM00086; PAC; 2.
DR   SMART; SM00091; PAS; 2.
DR   SUPFAM; SSF141868; EAL domain-like; 1.
DR   SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR   PROSITE; PS50883; EAL; 1.
DR   PROSITE; PS50887; GGDEF; 1.
DR   PROSITE; PS50113; PAC; 1.
DR   PROSITE; PS50112; PAS; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        25..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        49..69
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        89..109
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        121..140
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        147..166
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        172..190
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          391..464
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          466..518
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          550..683
FT                   /note="GGDEF"
FT                   /evidence="ECO:0000259|PROSITE:PS50887"
FT   DOMAIN          692..945
FT                   /note="EAL"
FT                   /evidence="ECO:0000259|PROSITE:PS50883"
SQ   SEQUENCE   952 AA;  111093 MW;  7A21F6E50B050E5F CRC64;
     MVIDVQDELL YASQIKSAAV LLQRFLIWLF VIILYDVFVY YIYFKNFSFS FNLWFATTSI
     ICTISWLLIK SILVSPYHNV FNLDALCQFI CLIIGCSFGF GIFTLQHYVL IDTPDITSTH
     LLILSSILIC LVSISALTYL TSRFRYFLFL FIPATIPCLF YKFLSVSPLS HYYQFSFNFI
     LIFILLAGYI THKLHHKLGL ITFERSKLLL QAKQQTFDNN QLQNKLKHEI EKSIHIKNEL
     LLNNQLLEQK VKERTYDIKQ INDRLENHQA NLAFAHETAG INSWLWNIEK RTIEIFDTKN
     KILFNHIDEY HLQIDSLIHP DDLENYQHLM RQHLRGRTER FEAKYRIKRN DQWCWIQDTG
     KVIARHPISF KPIRMVGIHR DIQKEKSDQE QLKLAANVFE QVAQGVFVLD NNLCYLEVNP
     YFEKLIGYHQ SDLLGKHLFD ITVNNKKEII EEHFDITKKL VAEREYDAEL QIEFLTGKHL
     TLWLHINAIT DEKNKIINYV GIITDLTERR KQEQRVSYLE NYDLLTDLPN RFYFNLQLHH
     YLTDPNNILQ NLAVIRINID RFRSFNEFAS TQAGDILLQK IAQRLRQACP DALLISYLNN
     DDYAMIYNYG QNKKTIHQTA KSILKAFESP FMIHNNEHFI SISIGIALYP EHGRQVDTLN
     SHAEQALAEA KSLGGNTAYL YSNKNARLIQ QNINLEGDLR QALKNKELLV YYQPKICTQT
     EKIYGFEALI RWQHPKLGLI TPDLFLPIAE ESSLITEIGR FVLFETCKQI RIWQDLNFDY
     LRVSVNIVAQ QIHRGELIQD IDQALNMYKI SGDMLELEIT ESSLIAKSDN VLNLLQQIKQ
     RHISISLDDF GTGYSSLAYL TNYPIDTLKI DKIFISKIEQ EKDQAIVSAI IAMGKAMGMS
     VIAEGVETIE QINFLKKHGC HILQGYYYSK PLTAQECLDY LTKFKLASVY RV
//
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