ID A0A117SDA2_9FLAO Unreviewed; 923 AA.
AC A0A117SDA2;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Glycosyl hydrolase {ECO:0000313|EMBL:KUO65223.1};
GN ORFNames=APF83_02545 {ECO:0000313|EMBL:KUO65223.1};
OS Lutibacter sp. BRH_c52.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Lutibacter.
OX NCBI_TaxID=1734397 {ECO:0000313|EMBL:KUO65223.1, ECO:0000313|Proteomes:UP000054346};
RN [1] {ECO:0000313|EMBL:KUO65223.1, ECO:0000313|Proteomes:UP000054346}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRH_c52 {ECO:0000313|EMBL:KUO65223.1};
RA Bagnoud A., Chourey K., Hettich R.L., De Bruijn I., Andersson A.F.,
RA Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT "Microbial metabolic network in the subsurface.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 74 family.
CC {ECO:0000256|ARBA:ARBA00037986}.
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:KUO65223.1}.
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DR EMBL; LOEY01000064; KUO65223.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A117SDA2; -.
DR Proteomes; UP000054346; Unassembled WGS sequence.
DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR CDD; cd15482; Sialidase_non-viral; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 4.
DR InterPro; IPR036278; Sialidase_sf.
DR InterPro; IPR031778; Sortilin_N.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR43739; XYLOGLUCANASE (EUROFUNG); 1.
DR PANTHER; PTHR43739:SF2; XYLOGLUCANASE (EUROFUNG); 1.
DR Pfam; PF15902; Sortilin-Vps10; 1.
DR SUPFAM; SSF110296; Oligoxyloglucan reducing end-specific cellobiohydrolase; 1.
DR SUPFAM; SSF50939; Sialidases; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023326};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000313|EMBL:KUO65223.1};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..923
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007156305"
FT DOMAIN 118..244
FT /note="Sortilin N-terminal"
FT /evidence="ECO:0000259|Pfam:PF15902"
SQ SEQUENCE 923 AA; 102477 MW; 295D8F1BC4477C36 CRC64;
MKKLTTFFCF LFFFIGINAQ NSLVKNVPFT NIGPAIMSGR VVDIDVNPDQ PTEFNVAYAS
GGLWYTNNNG TSFTSVADNA PTQNMGDIAV DWNNGTIWIG TGESNSSRSS YSGIGMLKST
DKGKTWENVG LTDSHHIGRI IINKNNPEEV VVGAMGHLYS SNAERGIFKT SDGGKTWKNV
LFINENTGII DISASPTNAN ILYAASWERG RKAWDFDGDG ENSAIYKSSD AGSTWTKLTD
EKSGFPTGSG VGRIGLAAFN DAVVFALLDN QNRRPEVKKK AGEGLKKDDF KEMGVDEFLK
LDDEKLNAYL KDNNFDKKYT SKSVKSLVKK GKIKPSDLKT YLEDANFVLL NSEVIGAEVY
KSEDGGKTWE KTHDNYLDDV YSSYGYYFGI MAVNNSNENK IYIGGVPLLK SDDGGKTFTS
MDQENLHSDH QALWVNPKLN GHIVNGNDGG VNITYDDGKN WIKNNQPAVG QFYSVNVDNQ
KPYNVYGGLQ DNGVWVGPSN YKASKRWEAS GDYPYKSIGG GDGMQVQIDN RDHNIVYAGS
QFGYYFRVNV KTKERISIHP MHELGDSPYR YNWQTPILLS KHNQDILYMG ANKLLRSMNK
GETFEAISED LTTGGKKGNV PFGTITAISE SPFQFGYIYV GSDDGYVNIT TNSGGSWTRV
SDNLPQELWV SRVVASQHEK ELVYVALNGY RSDDFKPYIF LSENGGSTWK SIKGNLPNSP
VNVIKEDPED EAILYAGTDN GVYVSFDKGE NWQAFSNGLP KVAVHDLVIQ TDAKDLVIGT
HGRSIYKANI ASLQQYKTIK DKSITILEIP EVKHSPRWGT SWGAWSEVSE PKISIPFYVS
NEGTFDVIIT SDEDIELNRF SVPADKGFNF AEYDLSYSEK GKNAYLKKHK SAEIKSAKNG
SYYLLKGKYF VKIGKVKKAF EVK
//
