ID   A0A813P3U9_9BILA        Unreviewed;      1011 AA.
AC   A0A813P3U9;
DT   29-SEP-2021, integrated into UniProtKB/TrEMBL.
DT   29-SEP-2021, sequence version 1.
DT   28-JAN-2026, entry version 15.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CAF0744636.1};
GN   ORFNames=QVE165_LOCUS1121 {ECO:0000313|EMBL:CAF0744636.1};
OS   Adineta steineri.
OC   Eukaryota; Metazoa; Spiralia; Gnathifera; Rotifera; Eurotatoria;
OC   Bdelloidea; Adinetida; Adinetidae; Adineta.
OX   NCBI_TaxID=433720 {ECO:0000313|EMBL:CAF0744636.1, ECO:0000313|Proteomes:UP000663832};
RN   [1] {ECO:0000313|EMBL:CAF0744636.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Nowell W R.;
RL   Submitted (FEB-2021) 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:CAF0744636.1}.
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DR   EMBL; CAJNOM010000003; CAF0744636.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A813P3U9; -.
DR   OrthoDB; 9972949at2759; -.
DR   Proteomes; UP000663832; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0016837; F:carbon-oxygen lyase activity, acting on polysaccharides; IEA:UniProtKB-ARBA.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0006027; P:glycosaminoglycan catabolic process; IEA:InterPro.
DR   Gene3D; 2.70.98.10; -; 1.
DR   Gene3D; 1.50.10.100; Chondroitin AC/alginate lyase; 1.
DR   Gene3D; 2.60.120.430; Galactose-binding lectin; 1.
DR   Gene3D; 2.60.220.10; Polysaccharide lyase family 8-like, C-terminal; 1.
DR   InterPro; IPR039174; Chondroitin_ABC_lyase.
DR   InterPro; IPR008929; Chondroitin_lyas.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR014718; GH-type_carb-bd.
DR   InterPro; IPR011071; Lyase_8-like_C.
DR   InterPro; IPR003159; Lyase_8_central_dom.
DR   InterPro; IPR015177; Lyase_catalyt.
DR   InterPro; IPR015176; Lyase_N.
DR   PANTHER; PTHR37322; -; 1.
DR   PANTHER; PTHR37322:SF3; CHONDROITIN SULFATE ABC EXOLYASE; 1.
DR   Pfam; PF02278; Lyase_8; 1.
DR   Pfam; PF09093; Lyase_catalyt; 1.
DR   Pfam; PF09092; Lyase_N; 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:0000256|ARBA:ARBA00023239};
KW   Reference proteome {ECO:0000313|Proteomes:UP000663832}.
FT   DOMAIN          9..150
FT                   /note="Lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF09092"
FT   DOMAIN          279..494
FT                   /note="Lyase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF09093"
FT   DOMAIN          564..771
FT                   /note="Polysaccharide lyase family 8 central"
FT                   /evidence="ECO:0000259|Pfam:PF02278"
SQ   SEQUENCE   1011 AA;  117315 MW;  D0F8C96210BD6FA7 CRC64;
     MNDDLKYWHA TDGEITLSTE RFKHGTSSLK WEWSSSAAAL TYTNPEAFHS LKWANNKCFA
     FWLFNSQESN IDENNPQQPL YIEFLSEKDN KPIAHLWYHV NFYGWRPIGI RYGLLSQFKT
     NLTRIHGIRF TSPSNVSNGV YFINGINFDY THTVGPKADY QQPWATPENI KRLTDDPSKW
     LFNSKNIFYN RPWLEEQKIN VTDDDIDKLK TRWLKTIPYG TWSPTTKPET FQKLQELAEV
     YGIKSDTISN VPLGKGGFYS PTNALDIQPF LLGPLKRTAT TYQCHRHSQT FESEEGQNVW
     ILLQQLCDYL LEQGWAEGNL NVEGHLDIGY EIRYFPMCLV YIRDQLNENP RLQSMITSGI
     WIMYGNLLTE QQTSTMGTDI IHNYLTNVVR LIVCISDQDE LIRRIIAFRY LLDYSFENRI
     HEPLALDGTV HHHWMCHFEY ASYSLPDILN LVSDMNDTSF QFSDNIRRIL RRCIHTLNFC
     LIENDKIPPN LSGRAGKFVT CNGINMTKKC VCICDRDHTY DPFVAGMLVD MCPKTDKSII
     PYINDGVDPV PLEGHLTLNS TAASIHRRQN FFACIVGMGK NRRGLEIYGW LSDTNNYGEY
     VRNCSIFIAP ADNQGIIKYS NAGCAYPGWQ WSHWPGTTCL LKPRSELFEG YCNLTAKNWL
     AGGTSIANKD GMFSNDFFVW DVAFRRSVYC FDNRITVLTS NIKLLQQQKR PVITTLFQSN
     FSNLEKLEQT PFILNNEEEI SEFPYENTIE NHDLHSITDH RNLTYYLHPN ENSNESFRIV
     LKRSEQEMIY CNPYYLIDSK QNPIVDIKTK KFQEPKFEDN EKYFKTTKDK YGLGYIEHLN
     VDDSTSSFVY TILIGHELSN EWMEEFSHPS KDPWSTEELT DLPPSIILSK SDDTHIFYDR
     NTDTTCYTCY SKERLEVNIG LVRSFGQPCM SMVRGRGPGS ITISIATTDF MLNETMWMLL
     KGKWNNAQLI SDDENGCVHV RSELVDDENT KITIWQRIYM PVEFHIAQMV D
//