ID   A0A2V5JXD4_9BACL        Unreviewed;      1037 AA.
AC   A0A2V5JXD4;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   SubName: Full=Hyaluronate lyase {ECO:0000313|EMBL:PYI51515.1};
GN   ORFNames=DLM86_24135 {ECO:0000313|EMBL:PYI51515.1};
OS   Paenibacillus flagellatus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=2211139 {ECO:0000313|EMBL:PYI51515.1, ECO:0000313|Proteomes:UP000247476};
RN   [1] {ECO:0000313|EMBL:PYI51515.1, ECO:0000313|Proteomes:UP000247476}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DXL2 {ECO:0000313|EMBL:PYI51515.1,
RC   ECO:0000313|Proteomes:UP000247476};
RA   Dai X.;
RT   "Paenibacillus flagellatus sp. nov., isolated from selenium mineral soil.";
RL   Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the polysaccharide lyase 8 family.
CC       {ECO:0000256|ARBA:ARBA00006699}.
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:PYI51515.1}.
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DR   EMBL; QJVJ01000012; PYI51515.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2V5JXD4; -.
DR   OrthoDB; 6636047at2; -.
DR   Proteomes; UP000247476; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0042806; F:fucose binding; IEA:UniProt.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:1901575; P:organic substance catabolic process; IEA:UniProt.
DR   GO; GO:0010185; P:regulation of cellular defense response; IEA:UniProt.
DR   GO; GO:0001868; P:regulation of complement activation, lectin pathway; IEA:UniProt.
DR   CDD; cd01083; GAG_Lyase; 1.
DR   Gene3D; 2.70.98.10; -; 1.
DR   Gene3D; 1.50.10.100; Chondroitin AC/alginate lyase; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 2.60.220.10; Polysaccharide lyase family 8-like, C-terminal; 1.
DR   InterPro; IPR018905; A-galactase_NEW3.
DR   InterPro; IPR008929; Chondroitin_lyas.
DR   InterPro; IPR000421; FA58C.
DR   InterPro; IPR006585; FTP1.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR014718; GH-type_carb-bd.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR038970; Lyase_8.
DR   InterPro; IPR011071; Lyase_8-like_C.
DR   InterPro; IPR012970; Lyase_8_alpha_N.
DR   InterPro; IPR004103; Lyase_8_C.
DR   InterPro; IPR003159; Lyase_8_central_dom.
DR   PANTHER; PTHR38481; HYALURONATE LYASE; 1.
DR   PANTHER; PTHR38481:SF1; HYALURONATE LYASE; 1.
DR   Pfam; PF00754; F5_F8_type_C; 1.
DR   Pfam; PF02278; Lyase_8; 1.
DR   Pfam; PF02884; Lyase_8_C; 1.
DR   Pfam; PF08124; Lyase_8_N; 1.
DR   Pfam; PF10633; NPCBM_assoc; 1.
DR   SMART; SM00607; FTP; 1.
DR   SUPFAM; SSF48230; Chondroitin AC/alginate lyase; 1.
DR   SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF49863; Hyaluronate lyase-like, C-terminal domain; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000313|EMBL:PYI51515.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000247476}.
FT   DOMAIN          890..1036
FT                   /note="Fucolectin tachylectin-4 pentraxin-1"
FT                   /evidence="ECO:0000259|SMART:SM00607"
SQ   SEQUENCE   1037 AA;  113911 MW;  15D0CFE00694366C CRC64;
     MRKMLLLLIV FAIAIPVLYG SAVSAADEYD ALRLKWRDYL TGGTEVDPSD PDYAKAIERI
     ARSVTNAEGT GVWDRMNKAP DRGYLWSDLT STTNSAQVSS HYTRLKEMAL AFATPGSPLF
     GDERLKNDIV GGLDWTYANR YNERKSEYNN WWDWEIGSPM LLADTMTLMY DHLSATQIAD
     YVRAIDKFCP DPTKRTNLSN FEETGANRLD KALIVVLRGI VTKSAAKIEQ GRDAMSQVFP
     YVTKDDGFYR DGSFVFHDNL AYTGSYGSVL LGDIAKLLYL LTGSSWQVTD PNLDNAFRWV
     TDSFEPLVYR GVMMDMVNGR SISRKDRSMW GPISTIAWMA EFAPPDRAAE YKRIVKGWLT
     ANPWLPSLYE KSGLSAIRMV KSILNDPAVQ PKGSLIMSKP FAAMDRYVHL RPGFGFGISM
     SSARIANFES GTENLKGWYT GDGMTYLYNS DIDQFFDGFW PTVDAMRLPG TTSDGATRRH
     LRTTSKTWVG GSSIDGLYGT AGMDLDPDNS TLGGKKSWFL FDDEIVALGA GLTSTDNRRV
     ETIVENRMIA GDNAFTVNGE AMPSELGWSE TMESVSWAHL AGSRPGADIG YYFPDRPTVN
     GLREQRTGSW SDINTLMNPT EPITRNYLSL SLDHGTNPSG ESYSYVLLPN RDAASTGSYG
     ADPDVGVLSN TERLQAVRER KLGVTGLNFW QDGTYDFVRS YQPASVMIKE DGDELTVAVS
     DPTMLQEKLT IELGKSAVSV LSADETVAVT RKAPYIRLDI DTAGSLGRTH TVKLRINPAS
     RNHLPDVNRV TVDIAESRLY RGDSANVAVT VTNLGERTPG GTLELRLPDG WTANGPLRYP
     IRSLGPDESA TVTATVYVPS NAAYARHRIT AVQKTGNATF EGSDAVDVVK RNVAAGKPAS
     QSSTAFGGVP ERAVDGNTNG AYSAGSVSHT APEAQPYWQT DLGADYLVDE IVLWNRTDCC
     SNRLSQYYVF VSDRPFESAS LADTLRQPDV WSTYESGTAG RPTAIEVGRT GRYVRVQLSG
     TNPLSLAEVQ VISSGNP
//