ID A0A0P6X646_9CHLR Unreviewed; 791 AA.
AC A0A0P6X646;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=EAL domain-containing protein {ECO:0000259|PROSITE:PS50883};
GN ORFNames=ADN01_15070 {ECO:0000313|EMBL:KPL78509.1};
OS Levilinea saccharolytica.
OC Bacteria; Chloroflexota; Anaerolineae; Anaerolineales; Anaerolineaceae;
OC Levilinea.
OX NCBI_TaxID=229921 {ECO:0000313|EMBL:KPL78509.1, ECO:0000313|Proteomes:UP000050501};
RN [1] {ECO:0000313|EMBL:KPL78509.1, ECO:0000313|Proteomes:UP000050501}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIBI-1 {ECO:0000313|EMBL:KPL78509.1,
RC ECO:0000313|Proteomes:UP000050501};
RA Hemp J., Ward L.M., Pace L.A., Fischer W.W.;
RT "Genome sequence of Levilinea saccharolytica DSM 16555.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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:KPL78509.1}.
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DR EMBL; LGCM01000055; KPL78509.1; -; Genomic_DNA.
DR RefSeq; WP_062418804.1; NZ_LGCM01000055.1.
DR AlphaFoldDB; A0A0P6X646; -.
DR STRING; 229921.ADN01_15070; -.
DR OrthoDB; 3178064at2; -.
DR Proteomes; UP000050501; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008233; F:peptidase activity; IEA:InterPro.
DR GO; GO:0006465; P:signal peptide processing; IEA:InterPro.
DR CDD; cd01948; EAL; 1.
DR CDD; cd06462; Peptidase_S24_S26; 1.
DR Gene3D; 3.20.20.450; EAL domain; 1.
DR Gene3D; 2.10.109.10; Umud Fragment, subunit A; 1.
DR InterPro; IPR001633; EAL_dom.
DR InterPro; IPR035919; EAL_sf.
DR InterPro; IPR036286; LexA/Signal_pep-like_sf.
DR InterPro; IPR015927; Peptidase_S24_S26A/B/C.
DR InterPro; IPR001733; Peptidase_S26B.
DR NCBIfam; TIGR02228; sigpep_I_arch; 1.
DR PANTHER; PTHR33121; CYCLIC DI-GMP PHOSPHODIESTERASE PDEF; 1.
DR PANTHER; PTHR33121:SF71; CYCLIC DI-GMP PHOSPHODIESTERASE PDEF; 1.
DR Pfam; PF00563; EAL; 1.
DR Pfam; PF00717; Peptidase_S24; 1.
DR PRINTS; PR00728; SIGNALPTASE.
DR SMART; SM00052; EAL; 1.
DR SUPFAM; SSF141868; EAL domain-like; 1.
DR SUPFAM; SSF51306; LexA/Signal peptidase; 1.
DR PROSITE; PS50883; EAL; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000050501};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..28
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 135..153
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 186..205
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 414..434
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 524..776
FT /note="EAL"
FT /evidence="ECO:0000259|PROSITE:PS50883"
SQ SEQUENCE 791 AA; 87924 MW; 0101EC2481906897 CRC64;
MLRSFLLRPA VMGSALMVVI TAALWGIFAP MPFGGRTTYV IVNGNSMEPG FHKGDLVLLR
PAQQYTVGEI VMYRYPGLGP VIHRIVRQNG TRFVLKGDNN GWEDSYEPET SEIAGTFWLH
IPRVGIAFGW LREPWAAAAV AGGTIFVLGV LMLKLPEPRG KRETPFWWKG WTRSASYWLA
RWQEPYFMVM YILAAAGIVL GLFAFTRPAL RQVADNLPYQ QTGYYVYYAD LPVNLYDNRR
LESGDAIYPQ LNCQVNVLFH YQLLSAAEFA GGGSYALQAR VRDAAGWHRS FPLGEAANFS
GGDFQAQQVL DVCAAQRLIT EMEEMTGVQR PQYYLDITPN VQVAGTLGGR IIKTDFAPAL
SFVVEDQQVF LNTTAVPGAD VLRPSAAGLL EGSRLEANTL DISRVRIPVN TARGLAVLLV
VLSLVGLAVP VVMLQQAEKK EEKLRAHLVA GPKLVEAAGS LLAFGDRTVE VRQLEDLTRL
AEKAGSVVFF HEDPPWATYL VRENGVSYYY RTLSAANRDS APEVGNWGED LVRALRNDEL
VLFYQPSVSM QDGQISQVEA FLRWQHPERG FLMPMQFLPW AEKSGLVQFI DEWVLNTGCL
QLRRWQDQGY LNLPLAINIS SYELRQEGLA KLVETVLKRH ELSAEMLRVE IDESDLSLQP
AILDNMRQLK AMGVGISITA PRGESLEAVH SLLDVDQVKF GRNMVQQVLA TESNSQSARQ
WIHQAHQRHI KVVAMGVETQ EQYGFFQLSA CDEAQGFFIS PPMPAEDLTR ALKAGPDFKN
PALGNGSGGA A
//