ID   A9AWC8_HERA2            Unreviewed;       942 AA.
AC   A9AWC8;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   02-SEP-2026, entry version 93.
DE   SubName: Full=Cellulose-binding family II {ECO:0000313|EMBL:ABX04778.1};
GN   OrderedLocusNames=Haur_2138 {ECO:0000313|EMBL:ABX04778.1};
OS   Herpetosiphon aurantiacus (strain ATCC 23779 / DSM 785 / 114-95).
OC   Bacteria; Bacillati; Chloroflexota; Chloroflexia; Herpetosiphonales;
OC   Herpetosiphonaceae; Herpetosiphon.
OX   NCBI_TaxID=316274 {ECO:0000313|EMBL:ABX04778.1, ECO:0000313|Proteomes:UP000000787};
RN   [1] {ECO:0000313|EMBL:ABX04778.1, ECO:0000313|Proteomes:UP000000787}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23779 / DSM 785 / 114-95
RC   {ECO:0000313|Proteomes:UP000000787};
RX   PubMed=22675585; DOI=10.4056/sigs.2194987;
RA   Kiss H., Nett M., Domin N., Martin K., Maresca J.A., Copeland A.,
RA   Lapidus A., Lucas S., Berry K.W., Glavina Del Rio T., Dalin E., Tice H.,
RA   Pitluck S., Richardson P., Bruce D., Goodwin L., Han C., Detter J.C.,
RA   Schmutz J., Brettin T., Land M., Hauser L., Kyrpides N.C., Ivanova N.,
RA   Goker M., Woyke T., Klenk H.P., Bryant D.A.;
RT   "Complete genome sequence of the filamentous gliding predatory bacterium
RT   Herpetosiphon aurantiacus type strain (114-95(T)).";
RL   Stand. Genomic Sci. 5:356-370(2011).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 74 family.
CC       {ECO:0000256|ARBA:ARBA00037986}.
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DR   EMBL; CP000875; ABX04778.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9AWC8; -.
DR   STRING; 316274.Haur_2138; -.
DR   KEGG; hau:Haur_2138; -.
DR   eggNOG; COG4447; Bacteria.
DR   eggNOG; COG5297; Bacteria.
DR   HOGENOM; CLU_004180_1_0_0; -.
DR   InParanoid; A9AWC8; -.
DR   BioCyc; HAUR316274:GHYA-2166-MONOMER; -.
DR   Proteomes; UP000000787; Chromosome.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0030247; F:polysaccharide binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0010411; P:xyloglucan metabolic process; IEA:TreeGrafter.
DR   CDD; cd15482; Sialidase_non-viral; 1.
DR   FunFam; 2.130.10.10:FF:000534; Xyloglucanase Xgh74A; 1.
DR   FunFam; 2.130.10.10:FF:000545; Xyloglucanase Xgh74A; 1.
DR   Gene3D; 2.60.40.290; -; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR   InterPro; IPR001919; CBD2.
DR   InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR   InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR052025; Xyloglucanase_GH74.
DR   PANTHER; PTHR43739:SF2; OLIGOXYLOGLUCAN-REDUCING END-SPECIFIC XYLOGLUCANASE-RELATED; 1.
DR   PANTHER; PTHR43739; XYLOGLUCANASE (EUROFUNG); 1.
DR   Pfam; PF00553; CBM_2; 1.
DR   SMART; SM00637; CBD_II; 1.
DR   SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR   SUPFAM; SSF110296; Oligoxyloglucan reducing end-specific cellobiohydrolase; 2.
DR   PROSITE; PS51173; CBM2; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Cellulose degradation {ECO:0000256|ARBA:ARBA00023001};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000787};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..942
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002734377"
FT   DOMAIN          831..941
FT                   /note="CBM2"
FT                   /evidence="ECO:0000259|PROSITE:PS51173"
FT   REGION          756..830
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        756..797
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        798..815
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        818..830
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   942 AA;  99325 MW;  6DF745AC032C738F CRC64;
     MRMLKMAAAV VVLFAGVIQA MVAVPQSRAA STQPYNWSNV EIVGGGFVPG IIYNPTERDL
     VYARTDIGGA YRWNPTTKRW IPLTDWIGAT DWNWTGIDSL ATDPVDPNRL YLAAGTYTND
     WTSANGAILR STNKGNSWAR TDLPFKLGGN MPGRSMGERL AIDPNKNSVL YLGTRGQGLW
     RSTDYGATWA QVTSFPAIGN YTDPYFNDRI GVVWVTFDPR TGTSGSASQT IYVGVADTTT
     SIYRSTDGGA TWAALPGQPT AGYLPHHATL ASNGMLYITY SDTPGPYDGG KGDVWKYNTA
     TQAWTNISPI PSSSADDYFG YGGLAVDAQN PNTLLVTSLN SWWPDALIYR STDGGATWSG
     IWEWANYPER TFRYTQDIST SPWLDFGGNA TAPEVAPKLG WMIGDIEIDP FNSDRMLYGT
     GATIYGTDNL TAWDTGGKVA LDVRAHGLEE TAVLELVSPP EGVHLVSALG DIAGFYHTDL
     TKAPPWSASL KFGSSTSIDF AGTRPNVMAR TGYVGEGSTV KRVACSWDGG QNWSHASSEP
     TGSVGGGKIA MASDASMIVW SGTTAPVSYS MGCGNSWSAS AGIPAGAVVI ADRVKSTTFY
     GIANGTLYRS TDAARNFTAV ATGLPTKSAK IEAVLGIEGD LWLAGGQDGL FHSTDGGTTF
     SKIAGVQVAN VVGFGKAAPS QSYQAIYITG AIDGVEGFFR SDDGGTTWVR INDDQHQYGS
     TNETITGDPR IYGRVYIGTN GRGIIYGDIA GSTPTNTPAP ATATATRIPT ATSTSVPPTA
     TSVPPTATST RVPTATPLTS TAIPYTPTPT STRVPTATPI TPTSLPYTPT STPAPGGCRI
     NYVVNQWNTA FTGGVTITNL GAPISGGWTL TWNFANGQTV TSSWNTVLTQ TGSAVTAKHS
     ADWNANIPTN GTQSFGFIAS HNGTNAVPTN FVLNGVACSV AP
//