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Database: UniProt
Entry: Q2JLM7_SYNJB
LinkDB: Q2JLM7_SYNJB
Original site: Q2JLM7_SYNJB 
ID   Q2JLM7_SYNJB            Unreviewed;       766 AA.
AC   Q2JLM7;
DT   07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   07-MAR-2006, sequence version 1.
DT   27-MAR-2024, entry version 80.
DE   SubName: Full=GDSL-like lipase/acylhydrolase domain protein {ECO:0000313|EMBL:ABD02380.1};
GN   OrderedLocusNames=CYB_1412 {ECO:0000313|EMBL:ABD02380.1};
OS   Synechococcus sp. (strain JA-2-3B'a(2-13)) (Cyanobacteria bacterium
OS   Yellowstone B-Prime).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=321332 {ECO:0000313|EMBL:ABD02380.1, ECO:0000313|Proteomes:UP000001938};
RN   [1] {ECO:0000313|EMBL:ABD02380.1, ECO:0000313|Proteomes:UP000001938}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JA-2-3B'a(2-13) {ECO:0000313|Proteomes:UP000001938};
RX   PubMed=18059494; DOI=10.1038/ismej.2007.46;
RA   Bhaya D., Grossman A.R., Steunou A.S., Khuri N., Cohan F.M., Hamamura N.,
RA   Melendrez M.C., Bateson M.M., Ward D.M., Heidelberg J.F.;
RT   "Population level functional diversity in a microbial community revealed by
RT   comparative genomic and metagenomic analyses.";
RL   ISME J. 1:703-713(2007).
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DR   EMBL; CP000240; ABD02380.1; -; Genomic_DNA.
DR   RefSeq; WP_011433028.1; NC_007776.1.
DR   AlphaFoldDB; Q2JLM7; -.
DR   STRING; 321332.CYB_1412; -.
DR   CAZy; CBM20; Carbohydrate-Binding Module Family 20.
DR   KEGG; cyb:CYB_1412; -.
DR   eggNOG; COG2755; Bacteria.
DR   HOGENOM; CLU_365126_0_0_3; -.
DR   OrthoDB; 9805159at2; -.
DR   Proteomes; UP000001938; Chromosome.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:2001070; F:starch binding; IEA:InterPro.
DR   CDD; cd05467; CBM20; 1.
DR   CDD; cd00229; SGNH_hydrolase; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 3.40.50.1110; SGNH hydrolase; 1.
DR   InterPro; IPR013784; Carb-bd-like_fold.
DR   InterPro; IPR002044; CBM_fam20.
DR   InterPro; IPR014903; DUF1796.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013830; SGNH_hydro.
DR   InterPro; IPR036514; SGNH_hydro_sf.
DR   PANTHER; PTHR30383; THIOESTERASE 1/PROTEASE 1/LYSOPHOSPHOLIPASE L1; 1.
DR   PANTHER; PTHR30383:SF5; THIOESTERASE 1_PROTEASE 1_LYSOPHOSPHOLIPASE L1; 1.
DR   Pfam; PF00686; CBM_20; 1.
DR   Pfam; PF08795; DUF1796; 1.
DR   Pfam; PF13472; Lipase_GDSL_2; 1.
DR   SMART; SM01065; CBM_2; 1.
DR   SUPFAM; SSF52266; SGNH hydrolase; 1.
DR   SUPFAM; SSF49452; Starch-binding domain-like; 1.
DR   PROSITE; PS51166; CBM20; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:ABD02380.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001938}.
FT   DOMAIN          1..119
FT                   /note="CBM20"
FT                   /evidence="ECO:0000259|PROSITE:PS51166"
SQ   SEQUENCE   766 AA;  86270 MW;  7CA17EA68C38979F CRC64;
     MYRFQVRAIT QPGERIALVG SSAKLGSWDP CHCIWLQTDP AHYPLWWVEL PLSPADGTPG
     PLLPYSGCSK EIPRVEYRYL RVQAGGEVIW ESTAVNRWVP LEPEPLPAVL IVEDGEFGQI
     PAYPYGYFAD PIPEVEPENP QGLKVVILGS SVALGCSAWL LRGWAWLLQK ALQERYGHQV
     RNLSQLGANV SRTLLRFEQA VIPEHPDVVI VALSLGNEGL ASALPQHRRA LQRRFENGLQ
     RLIQRIQDIG ALPVLGGVYP HANYGPEQHL LLQETQQRML SWGCPVFNWL PHLEDGQSRW
     KPDLAFDPAH PNSKGHQVMF EAIDLSLLDP GQVSSARRKL AQPVGERVVF ADEHGFWVTA
     ETGKNQFRIV NITPYPYTIT PTWQPLQAAF QKAGLQPGLY IGKSDERLGD ATLYSLSVQE
     DGSVQTTLSI PADADLVFSP VAQFFSSESV ETIFEDGSLI LLKLSGSSEG SSDPMPRLCV
     INQSSHEYNI HPMWKEVRAA LKAMPAGVYE DPSHREALFR TLMIGEGGLE SRVKAAPGSV
     MLLEYTCKLS DIHRFAIVPL GDRCAVRMLL YKLEYDGPAF PFDLTRTSNL ADVADMIHNE
     FQGMWDPQYL HYSPEDRRIY HSKWTGLSFG HEVEEGEDPL QNMHPIHERM RTRYTARAKR
     FMYVLEKADK VLFVRTGGCR REAVVDLMDK LAAKRRGKPF LLLIVSPQSS DEFAGIPNVI
     HYEMELNPDR MCADPEHWKY CTGVMRDILH SLGVSTRNLF WCPPQL
//
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