ID   A0A1Y4CSC2_9BACT        Unreviewed;       624 AA.
AC   A0A1Y4CSC2;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Right handed beta helix domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=B5F77_13880 {ECO:0000313|EMBL:OUO49923.1};
OS   Parabacteroides sp. An277.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae;
OC   Parabacteroides.
OX   NCBI_TaxID=1965619 {ECO:0000313|EMBL:OUO49923.1, ECO:0000313|Proteomes:UP000196154};
RN   [1] {ECO:0000313|Proteomes:UP000196154}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=An277 {ECO:0000313|Proteomes:UP000196154};
RA   Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA   Rychlik I.;
RT   "Function of individual gut microbiota members based on whole genome
RT   sequencing of pure cultures obtained from chicken caecum.";
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal, non-reducing alpha-D-galactose
CC         residues in alpha-D-galactosides, including galactose
CC         oligosaccharides, galactomannans and galactolipids.; EC=3.2.1.22;
CC         Evidence={ECO:0000256|ARBA:ARBA00001255};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal, non-reducing branched (1->3)-alpha-D-
CC         galactosidic residues, producing free D-galactose.; EC=3.2.1.n1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001271};
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:OUO49923.1}.
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DR   EMBL; NFJB01000046; OUO49923.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y4CSC2; -.
DR   OrthoDB; 9767990at2; -.
DR   Proteomes; UP000196154; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004557; F:alpha-galactosidase activity; IEA:UniProtKB-EC.
DR   Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 2.
DR   InterPro; IPR039448; Beta_helix.
DR   InterPro; IPR011459; DUF1565.
DR   InterPro; IPR049169; Glyco_hydro_120_ins.
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; PF07602; DUF1565; 1.
DR   Pfam; PF21258; Glyco_hydro_120_ins; 1.
DR   SMART; SM00710; PbH1; 5.
DR   SUPFAM; SSF51126; Pectin lyase-like; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000196154};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..624
FT                   /note="Right handed beta helix domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012327992"
FT   DOMAIN          27..65
FT                   /note="DUF1565"
FT                   /evidence="ECO:0000259|Pfam:PF07602"
FT   DOMAIN          98..206
FT                   /note="Glycoside hydrolase 120 insertion"
FT                   /evidence="ECO:0000259|Pfam:PF21258"
FT   DOMAIN          257..443
FT                   /note="Right handed beta helix"
FT                   /evidence="ECO:0000259|Pfam:PF13229"
SQ   SEQUENCE   624 AA;  70200 MW;  EC48A3BD4647A2F4 CRC64;
     MRKNVIYWMY FLLPTLLSAT EYHVSPSGND AGTGLSDNPF RTINHAAQIA LPGDTVTVHA
     GTYREWVNPL NGGESDWKRI LYRAAEGERV ELKGSELVTG WKKEKNGVWK VVLPNRFFGD
     YNPFNDKLYG DWLWSENTYH TADVYLNDVS LYEVTSLEKV FTPDTIRSIR DPQGSTQCWF
     AQVDAEQTTI YANFGEANPN KETVEVSVRP TCFYPTREGL NYITIQGFHV SQAATQWAAP
     TAEQVGMIAT HWCKGWIIED NVIKNSRSNG ITLGKERSSG HNLECNDKRL DGTLHYIEVI
     FNVLRRGWSK ENIGSHIVRN NVISDCEQTG ICGSMGGAFS EIYGNHIYNI LVKQQFGGAE
     MAGIKLHGAI DTYIHNNRIH KTGNYGIWLD WMAQGAHVSS NLFYDNATSD LFFEVDHGPY
     IVDNNIALSA YSVHENTDGG AYLHNLFGGS IGRYDDARYT PYHLNHSTEI KGFRTITEGD
     HRFYNNVFVG GTNEKQQYGL IMFDASQWPI YAEDNLFYNG AKPMTGKEQG KVTESINPNL
     RIEETADAVY LVSDVDWQTL LAGKGKGIDA ARLGITKLTG FRFEHTDGTP YVLRMDYFGK
     ERAAQSPAIG PLENIPSSNR LKVW
//