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Database: UniProt
Entry: A0A087H1Q3_ARAAL
LinkDB: A0A087H1Q3_ARAAL
Original site: A0A087H1Q3_ARAAL 
ID   A0A087H1Q3_ARAAL        Unreviewed;       629 AA.
AC   A0A087H1Q3;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361166};
DE            EC=3.2.1.4 {ECO:0000256|RuleBase:RU361166};
GN   OrderedLocusNames=AALP_Aa4g071900 {ECO:0000313|EMBL:KFK36055.1};
OS   Arabis alpina (Alpine rock-cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Arabideae; Arabis.
OX   NCBI_TaxID=50452 {ECO:0000313|EMBL:KFK36055.1, ECO:0000313|Proteomes:UP000029120};
RN   [1] {ECO:0000313|Proteomes:UP000029120}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Pajares {ECO:0000313|Proteomes:UP000029120};
RX   PubMed=27246759; DOI=10.1038/nplants.2014.23;
RA   Willing E.M., Rawat V., Mandakova T., Maumus F., James G.V.,
RA   Nordstroem K.J., Becker C., Warthmann N., Chica C., Szarzynska B.,
RA   Zytnicki M., Albani M.C., Kiefer C., Bergonzi S., Castaings L.,
RA   Mateos J.L., Berns M.C., Bujdoso N., Piofczyk T., de Lorenzo L.,
RA   Barrero-Sicilia C., Mateos I., Piednoel M., Hagmann J., Chen-Min-Tao R.,
RA   Iglesias-Fernandez R., Schuster S.C., Alonso-Blanco C., Roudier F.,
RA   Carbonero P., Paz-Ares J., Davis S.J., Pecinka A., Quesneville H.,
RA   Colot V., Lysak M.A., Weigel D., Coupland G., Schneeberger K.;
RT   "Genome expansion of Arabis alpina linked with retrotransposition and
RT   reduced symmetric DNA methylation.";
RL   Nat. Plants 1:14023-14023(2015).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-glucosidic linkages in
CC         cellulose, lichenin and cereal beta-D-glucans.; EC=3.2.1.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00000966,
CC         ECO:0000256|RuleBase:RU361166};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 9 (cellulase E) family.
CC       {ECO:0000256|ARBA:ARBA00007072, ECO:0000256|PROSITE-ProRule:PRU10059,
CC       ECO:0000256|RuleBase:RU361166}.
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DR   EMBL; CM002872; KFK36055.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A087H1Q3; -.
DR   EnsemblPlants; KFK36055; KFK36055; AALP_AA4G071900.
DR   Gramene; KFK36055; KFK36055; AALP_AA4G071900.
DR   eggNOG; ENOG502QRF6; Eukaryota.
DR   OMA; GFDKYYN; -.
DR   OrthoDB; 1347382at2759; -.
DR   Proteomes; UP000029120; Chromosome 4.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.50.10.10; -; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR019028; CBM_49.
DR   InterPro; IPR001701; Glyco_hydro_9.
DR   InterPro; IPR018221; Glyco_hydro_9_His_AS.
DR   PANTHER; PTHR22298; ENDO-1,4-BETA-GLUCANASE; 1.
DR   PANTHER; PTHR22298:SF41; ENDOGLUCANASE 5; 1.
DR   Pfam; PF09478; CBM49; 1.
DR   Pfam; PF00759; Glyco_hydro_9; 1.
DR   SMART; SM01063; CBM49; 1.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR   PROSITE; PS00592; GH9_2; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW   ECO:0000256|PROSITE-ProRule:PRU10059};
KW   Cellulose degradation {ECO:0000256|ARBA:ARBA00023001,
KW   ECO:0000256|RuleBase:RU361166};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PROSITE-
KW   ProRule:PRU10059};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU10059};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW   ECO:0000256|PROSITE-ProRule:PRU10059};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029120};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|RuleBase:RU361166}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|RuleBase:RU361166"
FT   CHAIN           25..629
FT                   /note="Endoglucanase"
FT                   /evidence="ECO:0000256|RuleBase:RU361166"
FT                   /id="PRO_5005106548"
FT   DOMAIN          537..617
FT                   /note="Carbohydrate binding"
FT                   /evidence="ECO:0000259|SMART:SM01063"
FT   ACT_SITE        416
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10059"
SQ   SEQUENCE   629 AA;  69528 MW;  BED20935E87A0CC2 CRC64;
     MGKFGGSLFR VSLLLTVILG AATAAAEYYN YANALDKTFL FFEAQRSGKL PAAQRVKWRS
     HSGLKDGLAQ GVSLEGGYYD AGDHVKFGLP MAFAVTMLSW AAVDNRKELS SSNQMQQTLW
     SIRWGTDYFI KAHPQPNVLW GQVGDGESDH YCWERAEDMT TSRTAYKLDQ YHPGSDLAGE
     TAAALAAASL AFKPFNSSYS SLLLTHAKEL FSFADKYRGL YTDSIPNAKP FYMSSGYSDE
     LLWAAAWLHR ATGDQYYLKY VVDNAGYMGG TGWGMKEFSW DNKYAGVQIL LSKVLLEGKG
     GAYTSTLKQY QMKGDYFACA CLKKNGGYNI QTTPGGLMYV REWNNLQYAS AAAFLLAVYS
     DYLSAANAKL NCPDGSVQPQ ALLDFATSQA DYILGKNRQG MSYLVGYGPK YPIRVHHRGA
     SIASIFTQRS SVNCVQGFDS WYKRSQADPN VIYGALVGGP DQNDYYSDER SNYEQSEPTL
     SGTAPLVGLF AKLSGKSGSY GGGGSYKPYQ QTKPPASSSY YKATQSTYTP KQSEAAIEFL
     HSITTNWMAG NKRYYRHKVI IKNNSQKPIS DLKLKIEDLS GPIWGLDTTG QKNTYQLPQW
     QKVLKAGQAY DFVYVQGGPQ AKVTVLSYH
//
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