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Database: UniProt
Entry: I4W558_9GAMM
LinkDB: I4W558_9GAMM
Original site: I4W558_9GAMM 
ID   I4W558_9GAMM            Unreviewed;       520 AA.
AC   I4W558;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Carbohydrate-binding family V/XII {ECO:0000313|EMBL:EIL94599.1};
GN   ORFNames=UU5_11515 {ECO:0000313|EMBL:EIL94599.1};
OS   Rhodanobacter sp. 115.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Rhodanobacteraceae; Rhodanobacter.
OX   NCBI_TaxID=1162282 {ECO:0000313|EMBL:EIL94599.1, ECO:0000313|Proteomes:UP000004557};
RN   [1] {ECO:0000313|EMBL:EIL94599.1, ECO:0000313|Proteomes:UP000004557}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=115 {ECO:0000313|EMBL:EIL94599.1,
RC   ECO:0000313|Proteomes:UP000004557};
RX   PubMed=22843592; DOI=10.1128/JB.00871-12;
RA   Kostka J.E., Green S.J., Rishishwar L., Prakash O., Katz L.S.,
RA   Marino-Ramirez L., Jordan I.K., Munk C., Ivanova N., Mikhailova N.,
RA   Watson D.B., Brown S.D., Palumbo A.V., Brooks S.C.;
RT   "Genome sequences for six rhodanobacter strains, isolated from soils and
RT   the terrestrial subsurface, with variable denitrification capabilities.";
RL   J. Bacteriol. 194:4461-4462(2012).
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:EIL94599.1}.
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DR   EMBL; AJXS01000275; EIL94599.1; -; Genomic_DNA.
DR   RefSeq; WP_008213105.1; NZ_AJXS01000275.1.
DR   AlphaFoldDB; I4W558; -.
DR   PATRIC; fig|1162282.3.peg.2194; -.
DR   OrthoDB; 6018988at2; -.
DR   Proteomes; UP000004557; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
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:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd12215; ChiC_BD; 2.
DR   Gene3D; 2.10.10.20; Carbohydrate-binding module superfamily 5/12; 2.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR003610; CBM_fam5/12.
DR   InterPro; IPR036573; CBM_sf_5/12.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR42976; BIFUNCTIONAL CHITINASE/LYSOZYME-RELATED; 1.
DR   PANTHER; PTHR42976:SF1; GH18 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF02839; CBM_5_12; 2.
DR   SMART; SM00495; ChtBD3; 2.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51055; Carbohydrate binding domain; 2.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..40
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           41..520
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003696846"
FT   DOMAIN          49..98
FT                   /note="Chitin-binding type-3"
FT                   /evidence="ECO:0000259|SMART:SM00495"
FT   DOMAIN          129..178
FT                   /note="Chitin-binding type-3"
FT                   /evidence="ECO:0000259|SMART:SM00495"
FT   REGION          82..132
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          152..212
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        82..106
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        107..123
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        152..186
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        187..211
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   520 AA;  52699 MW;  B29292B165F1A849 CRC64;
     MHAKRSEKWS RLALGTLSGA IGTALSVSLL AMAPVQTAHA GVAAEQACAA SWNSTTAYSG
     GATVSENGVN YLANWWTQGN DPATSNGATG SGQPWTSQGA CGGGSPSPTP TPTPTPTPTP
     TPSPSGSCDA AWNATTAYNG GATVSENGEN YKANWWTQGN DPATSSGASG SGQPWTPIGS
     CSGGSPSPTP TPTPTPTPTP TPTPTPTPSP SGLLFSPYKD VTINANWNTD GMQTAVTGTV
     MPVVGSGSLV STVEPNLGAI TLAFATGECG SENWGGIPAA GFASANIPAL DSAGVDYVVS
     TGGQAGVFSC SSESGMAQFL SRYMSPHMVG VDFDIEGGQS AATITNLVAS VAYAETLYPN
     LRYSFTLQTL AASDGSYGGL NTLGNSVMQA IKAANLQNYT INLMVMDYGS TGPGLCVVVG
     GSCDMGQSAI QAVTNLEHTY GVPASKIELT PDLGINDTSS EVFTLSNVDT IVNYAKANGL
     AGLHFWSLDR DNSSGPGATG DGISGPPLQY TNRFLHDLGR
//
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