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Database: UniProt
Entry: A0A1J4T3W8_9BACT
LinkDB: A0A1J4T3W8_9BACT
Original site: A0A1J4T3W8_9BACT 
ID   A0A1J4T3W8_9BACT        Unreviewed;       357 AA.
AC   A0A1J4T3W8;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=Sortilin N-terminal domain-containing protein {ECO:0000259|Pfam:PF15902};
GN   ORFNames=AUJ27_04075 {ECO:0000313|EMBL:OIO06490.1};
OS   Candidatus Falkowbacteria bacterium CG1_02_37_44.
OC   Bacteria; Candidatus Falkowbacteria.
OX   NCBI_TaxID=1805146 {ECO:0000313|EMBL:OIO06490.1, ECO:0000313|Proteomes:UP000183192};
RN   [1] {ECO:0000313|EMBL:OIO06490.1, ECO:0000313|Proteomes:UP000183192}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CG1_02_37_44 {ECO:0000313|EMBL:OIO06490.1};
RX   PubMed=27112493;
RA   Probst A.J., Castelle C.J., Singh A., Brown C.T., Anantharaman K.,
RA   Sharon I., Hug L.A., Burstein D., Emerson J.B., Thomas B.C., Banfield J.F.;
RT   "Genomic resolution of a cold subsurface aquifer community provides
RT   metabolic insights for novel microbes adapted to high CO concentrations.";
RL   Environ. Microbiol. 0:0-0(2016).
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:OIO06490.1}.
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DR   EMBL; MNUU01000077; OIO06490.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1J4T3W8; -.
DR   STRING; 1805146.AUJ27_04075; -.
DR   Proteomes; UP000183192; 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; 3.
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};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..357
FT                   /note="Sortilin N-terminal domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012904734"
FT   DOMAIN          133..251
FT                   /note="Sortilin N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF15902"
SQ   SEQUENCE   357 AA;  39337 MW;  1ED352C014E8A408 CRC64;
     MIYKKTNFIL LVMLLASALV ITGCSVKFNT NKNEGNNGGI YWSNSKGDIW QQKVLIPTTS
     GLPNSIGGVS VNDLVMDPSD NKALYLASFD NGLIYTYDGA GTWQIAKNLG QRTINAVAID
     PNSKCIIYAT TGNEVYKSTD CNRTWTRVYI DNNSTTAVSA VAVDHFDSAI IYIGTSRGEI
     IKSFDRGDTW QTLSSFKNKI NKIIISPHDS RNLFVYIQGL GLERSSDGGN NWESLKENLK
     NFKNSANIND IIVSENTSGL IFLAAGGGLL KSSDNGNNWE EIKLITPSDS IINAMAVNPQ
     NTQEIYYVTN TTFYRSLDGG ENWKTIKMPT SAIGWKLLID PKEPNIIYLG IKLPPKK
//
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