ID A0A1Q7SUM0_9BACT Unreviewed; 1055 AA.
AC A0A1Q7SUM0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Glycosyl hydrolase {ECO:0000313|EMBL:OLD79969.1};
GN ORFNames=AUF67_14070 {ECO:0000313|EMBL:OLD79969.1};
OS Acidobacteria bacterium 13_1_20CM_58_21.
OC Bacteria; Acidobacteriota.
OX NCBI_TaxID=1803438 {ECO:0000313|EMBL:OLD79969.1, ECO:0000313|Proteomes:UP000186215};
RN [1] {ECO:0000313|EMBL:OLD79969.1, ECO:0000313|Proteomes:UP000186215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27843720;
RA Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA Banfield J.F.;
RT "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT heterotrophy are prevalent below the grass root zone.";
RL PeerJ 4:E2687-E2687(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:OLD79969.1}.
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DR EMBL; MNIJ01000203; OLD79969.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q7SUM0; -.
DR Proteomes; UP000186215; 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; 2.130.10.10; 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; 2.
DR SUPFAM; SSF110296; Oligoxyloglucan reducing end-specific cellobiohydrolase; 2.
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:OLD79969.1};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326}.
FT DOMAIN 92..215
FT /note="Sortilin N-terminal"
FT /evidence="ECO:0000259|Pfam:PF15902"
FT DOMAIN 250..356
FT /note="Sortilin N-terminal"
FT /evidence="ECO:0000259|Pfam:PF15902"
FT REGION 753..826
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 802..823
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1055 AA; 115122 MW; 8492C57A5A7C09D7 CRC64;
MQYRLIGPFR GGRVVAVSGV VGQDNVYYFG STAGGVWKTT DGGLNWKPIF DKTKDASPAI
GAIAVSESDP NVVYVGTGEA CIRGNIVGGN GVHKSIDAGK TWQFVGLADT HAIGRLAVNP
KNPDIAFVAA LGHPFADNEE RGIFRTQDGG KTWQKVLYKD AKTGGIDVVF DPSNSNILFA
ALWQARRTPW SLDSGGAGSG LYRSRDGGTT WKELKGHGLP EGILGRIGVT VSGANFNRVW
AVIEAEKGGI YRSDDGGDSW HLTTDDHRFR QRAWYYSHIF ADPKSEDTVY ILNTAMYRSN
DGGKTFSRIR APHGDNHALW IDPTNPKRLA NGNDGGATIS TDSGDSWTSV YNQPTAQFYH
VITDNRFPYY IYGAQQDNST VAIASASPKG AIDRPDWYDV GGGESGYIAP DPADPEIVYA
GSYGGEITRY DHRTGEEQAI NPWPVNPIGW SAGDVKHRFQ WTEPIAFSPH DPQTMYFAGE
VLFKTTDSGM SWTIISPDLT RNDKSKQVSS GGPITKDNTG VEVYDTIFSV VESPVQKALI
WAGTDDGLVQ LTRDGGGHWE NVTPKAMPDW GTVSMIEAST REAGTAYLAV ERHKLDDFAP
YVFKTTDFGK TWTKLVAGLP PNDFVHAVRV DPRRPSLLFA GTEQGVYVSF DDGAHWRPLQ
LNLPAAPVND LVIKNTDLVV ATHGRSFWVL DDIAPLEQYE DSIPQQEAHL FTPTSANHTV
FRGSFFAPSG NVGKNPPAGA VIDYWLKASL KKSDQAKPQA SGEGAPARTE TSPSTSSEAK
KTDTDEAPKI TMEILNSSGK VIRKYPKKEE PASDEEEDFF SRDRNAGGLP ADAGLNRFVW
DLRYEAATKV PHAPLWGGNT DGPEALPGAY QVRLTVLSKS YAAPLEIKAD PRLKIGQEDL
AKQFDLLLKI RDKVTETDDT IIQIRDLREQ IHTINKRLKS DPRAKAVADA GKTLDTAMTE
VEEALIQTKA KSGQDVLNFP VRLNNHLVAL SGVVGSADSA PTRQSYEVFD MLSKAVDEQL
AKWKAIVSTE VAAYNNLVKQ QEVPALMVTQ PEAGK
//