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Database: UniProt
Entry: A0A1Q7SJ46_9BACT
LinkDB: A0A1Q7SJ46_9BACT
Original site: A0A1Q7SJ46_9BACT 
ID   A0A1Q7SJ46_9BACT        Unreviewed;       441 AA.
AC   A0A1Q7SJ46;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   RecName: Full=Heparin-sulfate lyase N-terminal domain-containing protein {ECO:0000259|Pfam:PF16889};
GN   ORFNames=AUI33_04960 {ECO:0000313|EMBL:OLD76287.1};
OS   Ignavibacteria bacterium 13_1_40CM_2_61_4.
OC   Bacteria; Ignavibacteriota; Ignavibacteria.
OX   NCBI_TaxID=1805219 {ECO:0000313|EMBL:OLD76287.1, ECO:0000313|Proteomes:UP000186155};
RN   [1] {ECO:0000313|EMBL:OLD76287.1, ECO:0000313|Proteomes:UP000186155}
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   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
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:OLD76287.1}.
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DR   EMBL; MNHF01000482; OLD76287.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q7SJ46; -.
DR   Proteomes; UP000186155; Unassembled WGS sequence.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   Gene3D; 2.70.98.70; -; 1.
DR   Gene3D; 1.50.10.100; Chondroitin AC/alginate lyase; 1.
DR   InterPro; IPR008929; Chondroitin_lyas.
DR   InterPro; IPR012480; Hepar_II_III.
DR   InterPro; IPR031680; Hepar_II_III_N.
DR   PANTHER; PTHR39210; HEPARIN-SULFATE LYASE; 1.
DR   PANTHER; PTHR39210:SF1; HEPARIN-SULFATE LYASE; 1.
DR   Pfam; PF07940; Hepar_II_III; 1.
DR   Pfam; PF16889; Hepar_II_III_N; 1.
DR   SUPFAM; SSF48230; Chondroitin AC/alginate lyase; 1.
PE   4: Predicted;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          4..137
FT                   /note="Heparin-sulfate lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16889"
SQ   SEQUENCE   441 AA;  50564 MW;  6BCC58E75D8BE7B4 CRC64;
     MLLHARFILD NLESGPVRGN HYVSNLAGLY LCGLGLTEFR EAPRWREFAG EKLFSEMQRQ
     VTGDGLHYEA SLSYHAFVTE MFLFPALMES EKGGSFCRPY LEILEKMIEA VAILIRPDGT
     LPQVGDNDDG RFLMFSQYYR ARRDWRPLLA LGAYLFRRPQ WLALAGDAWV EGAWVLGEPF
     LRWRDSLRTL AAFPGFRCHA FPQGGIYQLG VGNIQMVVDA GCVGQRNNGS HAHNDTLAFD
     LYAFGREVLP DRGTGAYAPD LSLRNRFRST RSHNALQVDG EEINPFPDEP FRLIPADSPR
     VQRWRSGERY VYLRAEHVGY RRLPASVLHG RSILMDRLKG TFLIEDRLEG KGRHRFLASF
     HLAPGWSIVP GEHGWTARSQ EGDLILNLRW RHRPAGSRMQ VEDDLHSPSY GVTQNARTLR
     FEWESEVPCR LRYELTLLER K
//
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