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Database: UniProt
Entry: A0A1I0WW77_9BACL
LinkDB: A0A1I0WW77_9BACL
Original site: A0A1I0WW77_9BACL 
ID   A0A1I0WW77_9BACL        Unreviewed;      1770 AA.
AC   A0A1I0WW77;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Carbohydrate binding domain (Family 11) {ECO:0000313|EMBL:SFA92420.1};
GN   ORFNames=SAMN05216312_102271 {ECO:0000313|EMBL:SFA92420.1};
OS   Cohnella sp. OV330.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Cohnella.
OX   NCBI_TaxID=1855288 {ECO:0000313|EMBL:SFA92420.1, ECO:0000313|Proteomes:UP000198686};
RN   [1] {ECO:0000313|EMBL:SFA92420.1, ECO:0000313|Proteomes:UP000198686}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OV330 {ECO:0000313|EMBL:SFA92420.1,
RC   ECO:0000313|Proteomes:UP000198686};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
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DR   EMBL; FOKE01000002; SFA92420.1; -; Genomic_DNA.
DR   Proteomes; UP000198686; Unassembled WGS sequence.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0008810; F:cellulase activity; IEA:InterPro.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:InterPro.
DR   Gene3D; 2.70.98.70; -; 1.
DR   Gene3D; 1.50.10.100; Chondroitin AC/alginate lyase; 1.
DR   Gene3D; 2.60.120.430; Galactose-binding lectin; 2.
DR   InterPro; IPR008397; Alginate_lyase_dom.
DR   InterPro; IPR005087; CBM_fam11.
DR   InterPro; IPR008929; Chondroitin_lyas.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR012480; Hepar_II_III.
DR   InterPro; IPR001119; SLH_dom.
DR   PANTHER; PTHR39210; HEPARIN-SULFATE LYASE; 1.
DR   PANTHER; PTHR39210:SF1; HEPARIN-SULFATE LYASE; 1.
DR   Pfam; PF05426; Alginate_lyase; 1.
DR   Pfam; PF03425; CBM_11; 2.
DR   Pfam; PF13290; CHB_HEX_C_1; 1.
DR   Pfam; PF07940; Hepar_II_III; 1.
DR   Pfam; PF00395; SLH; 3.
DR   SUPFAM; SSF48230; Chondroitin AC/alginate lyase; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   PROSITE; PS51272; SLH; 3.
PE   4: Predicted;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198686};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..1770
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5039301020"
FT   DOMAIN          1582..1645
FT                   /note="SLH"
FT                   /evidence="ECO:0000259|PROSITE:PS51272"
FT   DOMAIN          1647..1707
FT                   /note="SLH"
FT                   /evidence="ECO:0000259|PROSITE:PS51272"
FT   DOMAIN          1708..1770
FT                   /note="SLH"
FT                   /evidence="ECO:0000259|PROSITE:PS51272"
FT   REGION          1412..1446
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1422..1442
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1770 AA;  189796 MW;  365C916553A10EA0 CRC64;
     MTLLTLKKKL AAAMAALLLV TSALAALPPN AAEAAGGGDS PLIVPYSQQL NAMDSTTNVA
     GDTVGTAGVA LVPNTDPAYI KEGTGSKKWL LAINVDAANP TAYIAGAALI YPKVAPSVDL
     NGYSTLKFWA YNVKARTGDQ ADKPIQLRFF MKGDSEYYYY RLPLDWTGWK EVEIPLSVVK
     TQTSSAGVKA WGPLDYVRLD QAGVSGTTLD PSLSMYLDDF RLTGTGEVYP AVADKPSGEY
     VNKATVTLSS ATKPSVLAGV YYKRVGVDAD FKRYAAPLVL TEDTTLAVKS SLAGTDSAEM
     TYNYTFVYRD FVENVTASPA AGTYAEPKTV ALRSATEGAE IYYKIEGVDA DFKPYTAPLL
     VDRSQTIKAK AEFEGKVSEE TSYAYDIDLS SSSSLQIGNT ETFAGWTNTI PAAEPAVMGG
     FSGRWLDPTA PIDVADVTNA PWQSNDQLEF WLYSDRVSNK KIYVIISTPD DANPGNEYFM
     SSFFVDWQGW KKIELPFNKF LNSNGGAKLA NIRKVILHPR WYDSDPVSSP DDKLYFDAMA
     LAKNAVEPSI RQIDKSALPG SEVHYAFSLK NIGGADTAYA LSLKTPMGAG YGTTFPATTA
     VVANGAETDV DVQATVPAAA QAGSTVKAVL NVHPLAGGKD TTIELNLKVG APRTATKQHP
     YVMVSQDQLA EAKAKIQSYG WARDYLAAIR LKADAWVDKT VYYPSKPGGE STLYVCGDTP
     LVFDYDKPNE HQCPTDGTWH TGDDLDAAWR FTAHTVNIEA ARNLALVYAL TGETKYAAKA
     KEILTHYAAL YPSYPLQPLN GRIYYQSLDE AVQIIELAHA YDLIEPSGLL TAAEKYDIEQ
     NLFAPSAKTL QGYDVGKSNW QTWHNAAIGT IGAILEDKTL MDFSVEGRSG FNFQMNNSVL
     SDGFWYEGAI GYHFYAQSAL LDHAQALLGM GYDLFANPNF KKMYDATLQY AFPDLGIING
     NDSGKYPTSL AAPGRVVPMD YEAVYAHYGD PVYGALLNKL YADKGRVRGG FIVPGNTASG
     IAGEQAVFYG AEVVPNGGSL SAESMNFNGL GHSVLRAGEG EDQLYALVDY GLHGGYHGHP
     DKLHLEIFGQ GERLAPDLGI PPYSNSMYES YYKKSFAHNT VLVDGDTQQI PTANGAETYE
     PTKLFLQSGP LGIMTNTSSK AYAGMNGYER TVAVTKDYLI DLFSVASDTE RQYDWVLHGM
     GDFSTDQAMT PFAGPLGTKD AYSFFRNGKS QTVAGQWEGA WKLPSGNGLK LFSLTAASDS
     PTRMIVGEAP GPGNATDVYT PTLVNRVQAK NAQFVSVLEP YAGESAIASV GKTDDGRVDV
     KLKDGREQVF YYKADAETAG ALQYYFVDGK EGTAALVRPT ASFADGVLDL ATGDAGAFDQ
     VTAVVYAPGA SKVRWKGKEI AFKSDNGFVM ASVQSEGEPE PSTSPSPTPT PAPTPTPIYV
     PTPSPAKQAE RQVQAGEAAS LSIGQEIVVS VPAGALNRMA TYKIVKLGDA ALIAQLLKEG
     DQAASPIYEI TKSESGTFGV PIQIRLTFDP SKIGEGQKPS IHYYDESKKQ WVEMGGTIDG
     NAVEVASDHL TKFAVLAVNA SPAASAFADT QGHWASADIQ AAAKAGIVKG YEDGTFKPNR
     SVTRAEFSVM LMNALQPEGQ AGAVTDFADR DQLFDWAAEA VAQAVKAGIL HGYDDRTLRP
     NAGLTRAQLA VMLAAALGNE PAADPSAPSG FADEARIPAW ASPAVRAVQA NGLMKGRTAG
     RFEPDGTVTR AEAATVVVRL IELMKAKARP
//
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