ID A0A0S7Z8L5_9BACT Unreviewed; 1095 AA.
AC A0A0S7Z8L5;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Glycosyl hydrolase {ECO:0000313|EMBL:KPJ83287.1};
GN ORFNames=AMS19_04930 {ECO:0000313|EMBL:KPJ83287.1};
OS Gemmatimonas sp. SG8_23.
OC Bacteria; Gemmatimonadota; Gemmatimonadetes; Gemmatimonadales;
OC Gemmatimonadaceae; Gemmatimonas.
OX NCBI_TaxID=1703356 {ECO:0000313|EMBL:KPJ83287.1, ECO:0000313|Proteomes:UP000051174};
RN [1] {ECO:0000313|EMBL:KPJ83287.1, ECO:0000313|Proteomes:UP000051174}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_23 {ECO:0000313|EMBL:KPJ83287.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(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:KPJ83287.1}.
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DR EMBL; LJNO01000052; KPJ83287.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S7Z8L5; -.
DR PATRIC; fig|1703356.3.peg.2306; -.
DR Proteomes; UP000051174; 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; 2.
DR Gene3D; 2.60.40.4070; -; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 5.
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; SSF50939; Sialidases; 2.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023326};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000313|EMBL:KPJ83287.1};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..1095
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006641299"
FT DOMAIN 133..257
FT /note="Sortilin N-terminal"
FT /evidence="ECO:0000259|Pfam:PF15902"
SQ SEQUENCE 1095 AA; 118969 MW; 7F3E00F6B04E57E7 CRC64;
MLKSTLASAR TTLALLIALA PLWAVATTEA GAQVSVADAL GALALREVGP AVAGGRIADI
AVHPTNRSTW YVAVGSGGVW KTTNAGTTWT PIFDDQPSYS IGSVAIDPGS PDVVWVGTGE
NVSGRHVAWG TGLYRSRDGG RTWQNVGLAA SEHIGKILVH PEDGNTVLVA AEGPLWSSGG
DRGVFLTRDG GETWSNVLSI NEDTGVTDLE FDPSDPDVVY AAAYQRRRHI WGLMSGGEHS
GIWKSTDGGA TWRELSTGLP RGDMGKIGLA VTPADPNLVY ATIEANDEER GFYRSTDKGE
SWEKRNRYIS GGTGPHYYQE IEASPTEPDI VIQMDVFFQI TRDGGATFSN LGTGREKHSD
NHALWIDPDD TRHMLAGTDA GLYETFDRGD TWRHFPNMPI SQFYKVAVSN NEPFYEILGG
AQDLGTLWGP ARTTNVEGVR NSDWYFPMGA DGYGVQIDPT DPDILYLMTQ QGNLYRTHRR
SEESIQIQPQ PAPGDPPERW NWDSPIIISP HDSNRLYFAS QRLWRSDDRG DSWTVISQDL
TTNTNRYELP YFGRVWSVDA MHDNGAMSKY ATLTTISESP VTEGLLYTGS DDGLIHVSED
AGATWTRAAD LPGVPERAFI NKVEADVHTS GALFALADAH KVGDYTPYLF RSTDNGRSWT
SIRGDLPSGV IGWAIQQDHV EPDLLFLAGE NAIYVSMNGG QNWYPLSAGA PTIAFRDLKL
HRRDDDVVGA TFGRGFYVLD DYSPLREIAN GALESAGGVM PVRDAWWYVP SVPNQAVGRP
TLGSTAYAAP NPDFGATFTY LLPSVPQRPS EARAETELAL RDGGQSAPFP GYDALRAEAA
ERGPSVWLEV SDASGTPVRR VEGTARAGVH RVTWDLRRPA PDPIDLSVPA FRPPWASDPV
GPLVAPGAYS VQLLLVTSEG VSEIGAARSF ELEPVPTAPP GTDFVVVAEF QHRTSELSRR
SGAASRELGR VREQLRAMRE ALVRTPAADP ALRGRMDAID NELDALSLRL QRDPIRGSLN
ESTVPTISNR IGNVVGGHWS TRMEPTLTQR RNIEIAEGDL IGLEQDLAAL IDGELAAVEQ
ALIAAGAPWT PGRRR
//
