ID   A0A0G1D471_9BACT        Unreviewed;       363 AA.
AC   A0A0G1D471;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Sortilin N-terminal domain-containing protein {ECO:0000259|Pfam:PF15902};
GN   ORFNames=UV67_C0002G0004 {ECO:0000313|EMBL:KKS92514.1};
OS   Parcubacteria group bacterium GW2011_GWC1_43_12.
OC   Bacteria.
OX   NCBI_TaxID=1618909 {ECO:0000313|EMBL:KKS92514.1, ECO:0000313|Proteomes:UP000034170};
RN   [1] {ECO:0000313|EMBL:KKS92514.1, ECO:0000313|Proteomes:UP000034170}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
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:KKS92514.1}.
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DR   EMBL; LCFJ01000002; KKS92514.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1D471; -.
DR   STRING; 1618909.UV67_C0002G0004; -.
DR   Proteomes; UP000034170; 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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023326};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00023295};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326}.
FT   DOMAIN          137..239
FT                   /note="Sortilin N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF15902"
SQ   SEQUENCE   363 AA;  40542 MW;  C8E1F25A4DF4B56B CRC64;
     MKIKFVHNKS IYSFAFPIIF FAALAAFSLS CGFSRDGGIF KTFNRGETWE HKIKAANNQT
     ISTANVLRIE IDPGDSKIIY LGTKGNSLIK TMDGGELWYS ASAGNLDKRA DIFDIAIDPK
     NSANVFLAGY QNGLGMFLRS NDAGKNWEQT YQTARELYAV LTVEIDPFES SAVYMGTAEG
     GFFSSSDYGK NWKAIKWFDD AVSDLKINPI DPRIMYLSTF NSGVFKSNDK GQTWQKLEES
     DGFWESKDIE TLVMDKNNPD TLYTGSRRGF LKSYNGGQTW QKLNIIIPPE SLTVQAIALD
     LLNPSFIYYA AGNVVYRSQD YGQTWAYNSI QTGGLINVLT IDHKDSNILY AGISREPTFG
     LGY
//