ID A0A1M5WRJ4_BUTFI Unreviewed; 788 AA.
AC A0A1M5WRJ4;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=EAL domain, c-di-GMP-specific phosphodiesterase class I (Or its enzymatically inactive variant) {ECO:0000313|EMBL:SHH90255.1};
GN ORFNames=SAMN02745229_01138 {ECO:0000313|EMBL:SHH90255.1};
OS Butyrivibrio fibrisolvens DSM 3071.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Butyrivibrio.
OX NCBI_TaxID=1121131 {ECO:0000313|EMBL:SHH90255.1, ECO:0000313|Proteomes:UP000184278};
RN [1] {ECO:0000313|EMBL:SHH90255.1, ECO:0000313|Proteomes:UP000184278}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 3071 {ECO:0000313|EMBL:SHH90255.1,
RC ECO:0000313|Proteomes:UP000184278};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S51 family.
CC {ECO:0000256|ARBA:ARBA00006534}.
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DR EMBL; FQXK01000008; SHH90255.1; -; Genomic_DNA.
DR RefSeq; WP_073386181.1; NZ_FQXK01000008.1.
DR AlphaFoldDB; A0A1M5WRJ4; -.
DR STRING; 1121131.SAMN02745229_01138; -.
DR GeneID; 40456749; -.
DR OrthoDB; 9805474at2; -.
DR Proteomes; UP000184278; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd01948; EAL; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.20.20.450; EAL domain; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR001633; EAL_dom.
DR InterPro; IPR035919; EAL_sf.
DR InterPro; IPR000160; GGDEF_dom.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR InterPro; IPR005320; Peptidase_S51.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR PANTHER; PTHR33121; CYCLIC DI-GMP PHOSPHODIESTERASE PDEF; 1.
DR PANTHER; PTHR33121:SF84; SIGNALLING PROTEIN WITH EAL DOMAIN; 1.
DR Pfam; PF00563; EAL; 1.
DR Pfam; PF00990; GGDEF; 1.
DR Pfam; PF03575; Peptidase_S51; 1.
DR SMART; SM00052; EAL; 1.
DR SMART; SM00267; GGDEF; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF141868; EAL domain-like; 1.
DR SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR PROSITE; PS50883; EAL; 1.
DR PROSITE; PS50887; GGDEF; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022825};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 400..527
FT /note="GGDEF"
FT /evidence="ECO:0000259|PROSITE:PS50887"
FT DOMAIN 536..788
FT /note="EAL"
FT /evidence="ECO:0000259|PROSITE:PS50883"
SQ SEQUENCE 788 AA; 89998 MW; 871B4BD57A82741E CRC64;
MVLYLTSSFI PYQEPGSYQK MEPEECYGFF KDLKKEWPDS ANILFVPADP SKEKENECQI
KCVLDAFEST DLPVTEVKTL SESSGQALPG LIAWSDVIYL GGGHAPTQLA FMKRIGLKDA
LKDYKGIVIG LSAGSINCAY NAYLMPELEG EAKDPNYVRF SEGLDLTNIE IIPHAKCLKN
TTVDGLRCIE DIAIPDSFGS RFYLIEDGSY FKAKNGKTSF KGVGEVIEDG KISPLKQGAI
IPYMGVYEQP VIKTLLADGY DLVMSVNKKT NVCEMYYLDE KLWETFEGVK LKYTDVCFKL
AQKVVEEESE VLLEYMKIPF IMQEMRERGS FVRTIHIDTP RGRRAKNMRV REIPGYPDWI
LFSFFDITTS LDHDWMTDEY TRSGFLDRAR LFISEFSSAG NFSLVYTNVN GFKAVNELFG
DKNGDLVIFQ TRDALREYLK PVLMGRLESD HFVLITADEN LKEENLKTLC SQVFKIESKE
FNYEIRCGIY AIRNSNIDVT QLIAGAKLAE KNIKTGKGNL LYAYYDDVMK ENYVKQRFLL
ADFERALDEK EFEPYYQPIV DAKTGEIVSA EMLIRWRHKD FGMVSPGDFV PVIESEGKIS
YLDNFIVNRG MELIARRSFQ KKKNVPCAIN LSRVDFYDTF FIESIFKRVG DLSIDPSMIR
FEVTESAYAD LESKAMAYLN EMQEQGIKIL LDDYGSGMSS LSMLENFNFD IIKLDLGFIR
KIGINDKAES IIITTIGLAH MIGAKVTAEG VETEAQLKFL RDYDCDYIQG YYFYKPMPEK
DFEELLDK
//
