ID A0A0A7K1W2_9FLAO Unreviewed; 803 AA.
AC A0A0A7K1W2;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Glycosyl hydrolase family 3 {ECO:0000313|EMBL:AIZ40111.1};
GN ORFNames=M666_00010 {ECO:0000313|EMBL:AIZ40111.1};
OS Cellulophaga baltica 18.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Cellulophaga.
OX NCBI_TaxID=1348584 {ECO:0000313|EMBL:AIZ40111.1, ECO:0000313|Proteomes:UP000030786};
RN [1] {ECO:0000313|EMBL:AIZ40111.1, ECO:0000313|Proteomes:UP000030786}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=18 {ECO:0000313|EMBL:AIZ40111.1,
RC ECO:0000313|Proteomes:UP000030786};
RX PubMed=24428166; DOI=10.1111/1462-2920.12391;
RA Holmfeldt K., Howard-Varona C., Solonenko N., Sullivan M.B.;
RT "Contrasting genomic patterns and infection strategies of two co-existing
RT Bacteroidetes podovirus genera.";
RL Environ. Microbiol. 16:2501-2513(2014).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP009976; AIZ40111.1; -; Genomic_DNA.
DR RefSeq; WP_029445485.1; NZ_CP009976.1.
DR AlphaFoldDB; A0A0A7K1W2; -.
DR STRING; 1348584.M666_00010; -.
DR GeneID; 78059125; -.
DR KEGG; cbat:M666_00010; -.
DR HOGENOM; CLU_004542_5_1_10; -.
DR OrthoDB; 9805821at2; -.
DR Proteomes; UP000030786; Chromosome.
DR GO; GO:0009044; F:xylan 1,4-beta-xylosidase activity; IEA:InterPro.
DR GO; GO:0045493; P:xylan catabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.1700; Glycoside hydrolase family 3 C-terminal domain; 1.
DR Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR044993; BXL.
DR InterPro; IPR026891; Fn3-like.
DR InterPro; IPR002772; Glyco_hydro_3_C.
DR InterPro; IPR036881; Glyco_hydro_3_C_sf.
DR InterPro; IPR001764; Glyco_hydro_3_N.
DR InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR42721:SF3; BETA-D-XYLOSIDASE 5-RELATED; 1.
DR PANTHER; PTHR42721; SUGAR HYDROLASE-RELATED; 1.
DR Pfam; PF14310; Fn3-like; 1.
DR Pfam; PF00933; Glyco_hydro_3; 1.
DR Pfam; PF01915; Glyco_hydro_3_C; 1.
DR PRINTS; PR00133; GLHYDRLASE3.
DR SMART; SM01217; Fn3_like; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AIZ40111.1};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 721..790
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 803 AA; 89384 MW; 81D2AAC7D84AA9C8 CRC64;
MKYTSIVFIA SSILLLSLST KKEQPKIYHK GWIDFNKNGI MDVYENPKAT IDARVANLVS
LMNVEEKTCQ MATLYGFSRV LADELPTENW KNEIWKDGIA NIDEHLNTIW NQPKTQTPYS
FPYSTHAEAI NKVQKWFIEE TRMGIPVDFT NEGVHGLCHK KATPLPAPIG IGSTWNKDLV
YKAGTIVGRE AKALGYTNIY APILDVARDP RWGRVLECYG EEPFHIAEMG KQMTLGLQSQ
NVASTLKHFA VYSIPKGARD GDARTDPHVA PREMHQLHLY PFKRVIEEAS PMGVMSSYND
YDGVPITASH YFLTELLREK YGFDGYVVSD SEAVEYVFEK HHVAEDYKEG VRQVVEAGLN
VRTTFRTPES FIEPLRALIQ EGKIAMKTID LRVSEVLKVK FQLGLFDQPY VENPKASDDL
VHTKADEEFS KQINRESLVL LKNENNTLPL DISKLKNILV TGPLADEVNF TYSRYGPAEN
PSTSVYQGIK KYAAGKATVT YQKGCDVVDA NWPESEIIPM PLSEDEEASI AAAVEKAKQS
DVIIAVVGED DKRVGETMSR TSLGLPGRQF ELVQALYATG KPVILVLING QPLTINWENK
FIPAILEAWF PSTAAGEVIA ETLFGEYNPG GKLSVTFPKS VGQIPLNFPF KPGSQAGQPS
SGPNGSGNTR VLGALYPFGY GLSYTSFEYS NIIVHQKSKQ SQGEIKVSCV IKNTGSVAGD
EVVQLYIKDK VSSVTTYESQ LRGFERIHLK PGESKKVNFT LEPDDLAILD KNMNFKVEPG
AFEINIGASS VDIRLKEEFE IIN
//