ID A0A1G0XR63_9BACT Unreviewed; 1103 AA.
AC A0A1G0XR63;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Right handed beta helix domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=A2X48_17600 {ECO:0000313|EMBL:OGV36078.1};
OS Lentisphaerae bacterium GWF2_49_21.
OC Bacteria; Lentisphaerota.
OX NCBI_TaxID=1798573 {ECO:0000313|EMBL:OGV36078.1, ECO:0000313|Proteomes:UP000178513};
RN [1] {ECO:0000313|EMBL:OGV36078.1, ECO:0000313|Proteomes:UP000178513}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the polysaccharide lyase 9 family.
CC {ECO:0000256|ARBA:ARBA00038263}.
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:OGV36078.1}.
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DR EMBL; MHBH01000084; OGV36078.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G0XR63; -.
DR STRING; 1798573.A2X48_17600; -.
DR Proteomes; UP000178513; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0016052; P:carbohydrate catabolic process; IEA:InterPro.
DR Gene3D; 2.60.40.1190; -; 2.
DR Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 2.
DR InterPro; IPR039448; Beta_helix.
DR InterPro; IPR010502; Carb-bd_dom_fam9.
DR InterPro; IPR006626; PbH1.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR PANTHER; PTHR40088; PECTATE LYASE (EUROFUNG); 1.
DR PANTHER; PTHR40088:SF1; PECTATE LYASE PEL9; 1.
DR Pfam; PF13229; Beta_helix; 1.
DR Pfam; PF06452; CBM9_1; 2.
DR SMART; SM00710; PbH1; 6.
DR SUPFAM; SSF49344; CBD9-like; 2.
DR SUPFAM; SSF51126; Pectin lyase-like; 1.
PE 3: Inferred from homology;
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1103
FT /note="Right handed beta helix domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009569608"
FT DOMAIN 256..417
FT /note="Right handed beta helix"
FT /evidence="ECO:0000259|Pfam:PF13229"
FT DOMAIN 772..832
FT /note="Carbohydrate-binding"
FT /evidence="ECO:0000259|Pfam:PF06452"
FT DOMAIN 1022..1103
FT /note="Carbohydrate-binding"
FT /evidence="ECO:0000259|Pfam:PF06452"
SQ SEQUENCE 1103 AA; 121201 MW; A6387AFC524185D3 CRC64;
MIFKKLISIA MAAMVSASGF AAEYYVSQQA GAADENPGTL EKPWASLDKA GKEAKAGDTV
HIQAGTYRSN LQIMNSGTKE APISFIGEGK VIITGANKIS GFSKEEKLWV KRPWGHVFKW
HWGDESTYPE VANENSPFMS AARMENVFMY GVPMQWVPKK EDLAPGRFFW NGSTEGKGEL
IIHPPEGLDD PEKAGIEIPL RGAVLCGPWG TFPRGMSEVR GGGKKFEDAA KYKNCEYIIL
KNLTFGYTCE GFVGAGAVIS GDNWTVENCI FEYMNAGGLW VGGDYAKVKN CIFRYNGKYG
LGTKFHLDGA LIEDCISHNN NRKFYKIAWD AGGMKLHHTK NTTVRRLTTA FNFGAALWFD
IECEGNTIED CTSFGNEGLG LFYEVSDTGK FRNNVSFGNG VGIMYAHSAH GDMQDNVIIG
CSSGLVIGGD REKYKGVNNK FQKNILFEIR GNNLGWKSSK TPNSKDLSSK NMLTENLYAS
VNGSTSFEFG SLLPDLKTFE AEYKNASGNV QVKGLENIDT AARSRIDTAF QRIIKCLNTL
RPELKLSEEK VHLKSVWKLG GKGSVDGFWL ETAGGPLLMM SVYGEDTISL SCDKKDGVVL
WNFPHLGANT REDLKGNGFM VTGKTRKKFA IMTGLPRDAG PSKEIFQVAS LQQGKPKNDF
REGEEFTANI SITNPLKSAA SFTVQGPGLD NQQFQLGPGE KKSVDVPQKA VGGKDQLVYV
LKSDILGVPL EQSIHLKVTR MALAKKCPEG EFSTVQNIII DSAQQRNANV WDEQTGKTWQ
GKSDLSGTAS VGWNEKNLTV MAKVTDNKVV RSSRGVQGAD GLELFLDCRG ETSFHSSKYA
DGVLHLKIAA PLKDSWEPLP LDTEKALVKN GNFKKGITEW FVPKDAKAKE VQEAASNYAR
IEGNSIIQQD IPLEPQWGKI KVSCRARYEN IVPGDKSWHT GRLVVEFKDK AGAHAGEYPD
MITFKGTSKE WAAQSMEYDI PADTVKFRLQ AGMWNVKSGT LEIDDIVVVP VADRSGKKID
LSQQEGISVT GRTVAGGYEV KVVVALERFK ELKPQSGTVI GFDIGLNDSD VDDSKALQSQ
LFWQDARGTN AYDASKFGFI RLE
//
