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Database: UniProt
Entry: G5SVI1_9BACT
LinkDB: G5SVI1_9BACT
Original site: G5SVI1_9BACT 
ID   G5SVI1_9BACT            Unreviewed;       547 AA.
AC   G5SVI1;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   SubName: Full=GDSL-like protein {ECO:0000313|EMBL:EHG98836.1};
GN   ORFNames=HMPREF9441_03355 {ECO:0000313|EMBL:EHG98836.1};
OS   Paraprevotella clara YIT 11840.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Paraprevotella.
OX   NCBI_TaxID=762968 {ECO:0000313|EMBL:EHG98836.1, ECO:0000313|Proteomes:UP000003598};
RN   [1] {ECO:0000313|EMBL:EHG98836.1, ECO:0000313|Proteomes:UP000003598}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YIT 11840 {ECO:0000313|EMBL:EHG98836.1,
RC   ECO:0000313|Proteomes:UP000003598};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA   Chinwalla A., Mardis E.R., Wilson R.K.;
RL   Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the 'GDSL' lipolytic enzyme family.
CC       {ECO:0000256|ARBA:ARBA00008668}.
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:EHG98836.1}.
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DR   EMBL; AFFY01000054; EHG98836.1; -; Genomic_DNA.
DR   RefSeq; WP_008622480.1; NZ_JH376625.1.
DR   AlphaFoldDB; G5SVI1; -.
DR   STRING; 762968.HMPREF9441_03355; -.
DR   GeneID; 78584116; -.
DR   PATRIC; fig|762968.3.peg.2963; -.
DR   eggNOG; COG2755; Bacteria.
DR   HOGENOM; CLU_516489_0_0_10; -.
DR   OrthoDB; 9807041at2; -.
DR   Proteomes; UP000003598; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR   CDD; cd01821; Rhamnogalacturan_acetylesterase_like; 2.
DR   Gene3D; 3.40.50.1110; SGNH hydrolase; 2.
DR   InterPro; IPR037459; RhgT-like.
DR   InterPro; IPR013830; SGNH_hydro.
DR   InterPro; IPR036514; SGNH_hydro_sf.
DR   PANTHER; PTHR43695; PUTATIVE (AFU_ORTHOLOGUE AFUA_2G17250)-RELATED; 1.
DR   PANTHER; PTHR43695:SF1; RHAMNOGALACTURONAN ACETYLESTERASE; 1.
DR   Pfam; PF13472; Lipase_GDSL_2; 2.
DR   SUPFAM; SSF52266; SGNH hydrolase; 2.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..547
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003484719"
FT   DOMAIN          67..274
FT                   /note="SGNH hydrolase-type esterase"
FT                   /evidence="ECO:0000259|Pfam:PF13472"
FT   DOMAIN          322..526
FT                   /note="SGNH hydrolase-type esterase"
FT                   /evidence="ECO:0000259|Pfam:PF13472"
SQ   SEQUENCE   547 AA;  60986 MW;  6433513243ABF358 CRC64;
     MKKTCMLSAL LIGCGLCSTA QNPKDFRPME DVNHVTDLTL DSLEKANTAR PVPGSSRKGN
     HPVLFLVGNS TMRTGTKGNG DNGQWGWGYF AHEYFDADRL TVENHALGGT SSRTFYRKLW
     PDVKKGIRKG DYVIIELGHN DNGPFDSGRA RASIRGISPT DSLCVTIKET GEEEIVYSYG
     EYLRRFVREC KALGAHPILL SLTPRNAWDT KRPGHIARVD ETFGLWARQV AEEQGIPFVD
     LNEISASKYD RFSAWKVDYH FYRDRIHTSA FGARLNARSA AEGLAASTHP ALKALQACLT
     NLEPPAAQVK REKGKPVVFI TGDSTVKNED KAPDGMWGWG SQAGTIFDTD KITVANEAKA
     GRSTRTYLEE NRWERVYNAL QPGDFVLIQF GHNDIGDIGR GKARGVIACA QDTSHVYRVN
     KGDKVYNEVI YSFGWYLKKF IDDVREKGAT PILVSLTPRN EWPGGKIERR NDSYGKWYRE
     VVAQTAVEFV DLHNISADTL DRIGQEGAKA YYNRDHTHTS LKGAQLNAQS IAEGLRATDS
     PLARYLK
//
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