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Database: UniProt
Entry: A0A239KLP7_9ACTN
LinkDB: A0A239KLP7_9ACTN
Original site: A0A239KLP7_9ACTN 
ID   A0A239KLP7_9ACTN        Unreviewed;      1001 AA.
AC   A0A239KLP7;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   SubName: Full=Alpha-glucuronidase {ECO:0000313|EMBL:SNT19081.1};
GN   ORFNames=SAMN05421812_103632 {ECO:0000313|EMBL:SNT19081.1};
OS   Asanoa hainanensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Asanoa.
OX   NCBI_TaxID=560556 {ECO:0000313|EMBL:SNT19081.1, ECO:0000313|Proteomes:UP000198362};
RN   [1] {ECO:0000313|EMBL:SNT19081.1, ECO:0000313|Proteomes:UP000198362}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.5593 {ECO:0000313|EMBL:SNT19081.1,
RC   ECO:0000313|Proteomes:UP000198362};
RA   Kim H.J., Triplett B.A.;
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FZPH01000003; SNT19081.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A239KLP7; -.
DR   Proteomes; UP000198362; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0046559; F:alpha-glucuronidase activity; IEA:InterPro.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:InterPro.
DR   InterPro; IPR011099; Glyco_hydro_67_C.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF07477; Glyco_hydro_67C; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198362};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        727..750
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        771..791
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        797..817
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        824..842
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        862..881
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        893..914
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          500..554
FT                   /note="Glycosyl hydrolase family 67 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF07477"
FT   REGION          971..1001
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1001 AA;  106500 MW;  C8294E8AED8DD857 CRC64;
     MRWVVGAAVA VLLAAGAVVA YGVDGALGLS YSAADVPVER VAEAGPAPLA APPAIAAIRV
     PDDPLVTRAA GVVADALEAR GRPRPKIGGT GPAQLTARIA ALPGARSLES FRLTSAAGGI
     TVTGVTAAGT AAGLYAVADR IRSGAAITGD TVTAPRLGLR LTDAGSVGRE AAPDETDYSL
     NTDVVGSALL PDAPWVDRAA AERIGAQFRA FVDHSLSQGY NGIVIPGFLE YVTFEGVGVY
     DDGDDHIGRN EALVAAFAPI FRYAADSGMK VYFLTDMLAL SPPLERFLAR TTGGLDATDP
     RLWAVYQAGL AELFERMPFA GGLMIRIGEG GAVYRQQGWD YESRLAVTTP EAVRAMLTAL
     LATAGQGGRD IIFRSWTVGV GAVGDLHTNP ASYDEVLGTI DDPHLVVSTK YPAGDFYSHL
     PLNPTLTRGN QRRIVEFQSR REFEGFGSLP NDLTALHQQA LRTFLAANPR VEGSWTWTQD
     GGPLRAGPTS LYLRAGFWQL YDLNTYAAAR LAWRPDTPAE EITRDWVRQT FSTDPATERA
     ITGMLARSRA AVTKGLYIGP YADKQVKALG LEPPPMMWIF EWDIVTGDSA ALDSIYAVSR
     DRLDEAIAGG DRAVALAVEM RDLVAATDPA TYRDPALRQR LTDTLDFQVD LFETLAAYRT
     TVLRHAQWLD TGDGTARQQW QAARAVYETR KAGHLARYGG DRDLPAYQFT AADLGTDRAD
     RDPAMAWLAR VLLALVLLVV ALGAANRNAA CRALWLGATR PWGLGRPPDR ATAASVVAIA
     AVALVASRLV YTWFAAPAHL VLVLTAWLVF ALIARALTDN RTWAVIGGVI LLRTALLLGA
     LAVRGPGHYW FEFWTAPTAR AVYITVAFAG FGWLFVAVTL AQPGTRRRRA VGNTLVAGGG
     TLAVLAAGIA ALGLERALTI WNDQLALLPW GLSRILGITV YLGIPTNLPL VALAAGVVTA
     AAGAAVRWSA ATDGGARPDG RSASNTGRQS RLRRRSVART S
//
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