ID   U5W7E0_9ACTN            Unreviewed;       993 AA.
AC   U5W7E0;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   SubName: Full=Glycoside hydrolase family protein {ECO:0000313|EMBL:AGZ45093.1};
GN   ORFNames=AFR_34175 {ECO:0000313|EMBL:AGZ45093.1};
OS   Actinoplanes friuliensis DSM 7358.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Actinoplanes.
OX   NCBI_TaxID=1246995 {ECO:0000313|EMBL:AGZ45093.1, ECO:0000313|Proteomes:UP000017746};
RN   [1] {ECO:0000313|EMBL:AGZ45093.1, ECO:0000313|Proteomes:UP000017746}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 7358 {ECO:0000313|EMBL:AGZ45093.1,
RC   ECO:0000313|Proteomes:UP000017746};
RX   PubMed=24637369; DOI=10.1016/j.jbiotec.2014.03.011;
RA   Ruckert C., Szczepanowski R., Albersmeier A., Goesmann A., Fischer N.,
RA   Steinkamper A., Puhler A., Biener R., Schwartz D., Kalinowski J.;
RT   "Complete genome sequence of the actinobacterium Actinoplanes friuliensis
RT   HAG 010964, producer of the lipopeptide antibiotic friulimycin.";
RL   J. Biotechnol. 178:41-42(2014).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family.
CC       {ECO:0000256|ARBA:ARBA00007806, ECO:0000256|RuleBase:RU361185}.
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DR   EMBL; CP006272; AGZ45093.1; -; Genomic_DNA.
DR   RefSeq; WP_023561430.1; NC_022657.1.
DR   AlphaFoldDB; U5W7E0; -.
DR   STRING; 1246995.AFR_34175; -.
DR   KEGG; afs:AFR_34175; -.
DR   PATRIC; fig|1246995.3.peg.6915; -.
DR   eggNOG; COG1501; Bacteria.
DR   HOGENOM; CLU_301041_0_0_11; -.
DR   OrthoDB; 176168at2; -.
DR   Proteomes; UP000017746; Chromosome.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd04082; CBM35_pectate_lyase-like; 1.
DR   CDD; cd14752; GH31_N; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1760; glycosyl hydrolase (family 31); 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 2.
DR   InterPro; IPR005084; CMB_fam6.
DR   InterPro; IPR033403; DUF5110.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR048395; Glyco_hydro_31_C.
DR   InterPro; IPR025887; Glyco_hydro_31_N_dom.
DR   InterPro; IPR000322; Glyco_hydro_31_TIM.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR006311; TAT_signal.
DR   PANTHER; PTHR22762; ALPHA-GLUCOSIDASE; 1.
DR   PANTHER; PTHR22762:SF54; BCDNA.GH04962; 1.
DR   Pfam; PF03422; CBM_6; 1.
DR   Pfam; PF17137; DUF5110; 1.
DR   Pfam; PF13802; Gal_mutarotas_2; 1.
DR   Pfam; PF01055; Glyco_hydro_31_2nd; 1.
DR   Pfam; PF21365; Glyco_hydro_31_3rd; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR   PROSITE; PS51175; CBM6; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|RuleBase:RU361185};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361185};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017746};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..993
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004666149"
FT   DOMAIN          869..993
FT                   /note="CBM6"
FT                   /evidence="ECO:0000259|PROSITE:PS51175"
SQ   SEQUENCE   993 AA;  107517 MW;  F82AA7573EAE85D2 CRC64;
     MQPSRRSFLK VAGLAVGVPA LPLGRALADE TLTDYGSHVV DSRSLTVTSS TGQQLRITAY
     GGHVVRVRAV RNGEVFFADN RYEMVDPASH SGMGGTLQVT ESGDAFTITT APADGVRVVL
     RKSPLRVEFS SRNDNAALVR EDTTHSVSWG GTVVRQTFTP PAAGERFVKA GHGLYGRAPK
     VDRTGDIVSH NYGLQSSHVD QAPAIVPMYL SSRGYAVFFN TTFDTTFNFG NGGTYEFSAD
     GHGASGARPQ LDYFLIKGPE FPKLLDRYTQ LTGRPRFPRL GMFGLQLSDK NFPAVSDQSW
     WTSRITALRD AGFPLDVQVH DNRWRAGTGA WGGSWFEFSP ERWPDPAAFK RWADEHGILT
     TLDYNRNNSN EMAGWVGGPP PGYSFRPADL AGVADNDAVP DWSNPATRAW AWNVFWTKAF
     NPALGFPGDA LWIDEPDEMG PIPYDALAAN GQRWSELRNA FFLYCQKAAG QEGWDPATAG
     HIGHTRRPWI FTRGATAGQQ RYGHLWTGDI NSDYTEMQEQ IRGMQNAGLG GFPFANIDAG
     GFFGAVISDG LYRNWVAAWA STSPIWRPHS NGDTGAQGLA ASRWPIDQGT ASRTEFLRYA
     RVRYTLLPYL YTIAHTAHAT GVPMARAMVI DHQHNPMAYT HDLQYLWGPS IIVMPVTTDT
     DGAVQRVWLP AGDTWYDFWS DAQNVGSDST EKRYVTSTGE IIMYVRAGSI LPKYRYAQST
     AFLDKSQLEL EVYTGQDGSF TLYEDDGVTE EFRISNAAAT TGLTYTHAAL RVVVAHPAGT
     YRGAPAARRY VVRLHGLTAP IGMRVGAGAN LPAFTGESAA ILNGSGQVWN AARRILTVVT
     PMINVSAGGG VAATVEPSGA AFPAPSRQVV YEAEDATRSG ATLASQHNGY TGNGYADFTN
     ATGDHVEWTV PVAAGGVQPL GFRYANGGTT DRPLRISVND TIVAAHLSCP PTGSWKTWRT
     ATVTVSLPAG TAVRIRATTT GASGANLDSL SVG
//