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Database: UniProt
Entry: A0A2U1QMJ4_ARTAN
LinkDB: A0A2U1QMJ4_ARTAN
Original site: A0A2U1QMJ4_ARTAN 
ID   A0A2U1QMJ4_ARTAN        Unreviewed;       626 AA.
AC   A0A2U1QMJ4;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   22-FEB-2023, entry version 15.
DE   RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361166};
DE            EC=3.2.1.4 {ECO:0000256|RuleBase:RU361166};
GN   ORFNames=CTI12_AA010610 {ECO:0000313|EMBL:PWA99230.1};
OS   Artemisia annua (Sweet wormwood).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Asterales; Asteraceae; Asteroideae; Anthemideae;
OC   Artemisiinae; Artemisia.
OX   NCBI_TaxID=35608 {ECO:0000313|EMBL:PWA99230.1, ECO:0000313|Proteomes:UP000245207};
RN   [1] {ECO:0000313|EMBL:PWA99230.1, ECO:0000313|Proteomes:UP000245207}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Huhao1 {ECO:0000313|Proteomes:UP000245207};
RC   TISSUE=Leaf {ECO:0000313|EMBL:PWA99230.1};
RX   PubMed=29703587; DOI=10.1016/j.molp.2018.03.015;
RA   Shen Q., Zhang L., Liao Z., Wang S., Yan T., Shi P., Liu M., Fu X., Pan Q.,
RA   Wang Y., Lv Z., Lu X., Zhang F., Jiang W., Ma Y., Chen M., Hao X., Li L.,
RA   Tang Y., Lv G., Zhou Y., Sun X., Brodelius P.E., Rose J.K.C., Tang K.;
RT   "The genome of Artemisia annua provides insight into the evolution of
RT   Asteraceae family and artemisinin biosynthesis.";
RL   Mol. Plant 11:776-788(2018).
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}.
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:PWA99230.1}.
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DR   EMBL; PKPP01000029; PWA99230.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2U1QMJ4; -.
DR   Proteomes; UP000245207; Unassembled WGS sequence.
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; IPR033126; Glyco_hydro_9_Asp/Glu_AS.
DR   InterPro; IPR018221; Glyco_hydro_9_His_AS.
DR   PANTHER; PTHR22298; ENDO-1,4-BETA-GLUCANASE; 1.
DR   PANTHER; PTHR22298:SF141; ENDOGLUCANASE; 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.
DR   PROSITE; PS00698; GH9_3; 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:UP000245207};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|RuleBase:RU361166}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|RuleBase:RU361166"
FT   CHAIN           27..626
FT                   /note="Endoglucanase"
FT                   /evidence="ECO:0000256|RuleBase:RU361166"
FT                   /id="PRO_5015374114"
FT   DOMAIN          533..614
FT                   /note="Carbohydrate binding"
FT                   /evidence="ECO:0000259|SMART:SM01063"
FT   ACT_SITE        416
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10059"
FT   ACT_SITE        468
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
FT   ACT_SITE        477
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
SQ   SEQUENCE   626 AA;  69069 MW;  5F628DBC36A9B9FA CRC64;
     MEVFMRLYAM ATCLFLLIGI VPLALAGAHN YGQALTKSIL FFEAQRSGYL PGNQRVKWRG
     HSGLMDGKAN GVDLVGGYYD AGDNVKFGLP MAFTVTMMSW SIIEYGKQLA QSGELGHAMD
     AVKWGTDYLI KAHPQPHVLY GEVGDGNTDH YCWQRPEDMT TSRKAYRIDQ NNPGSDLAGE
     TAAAMAAASI VFRRYNPAYS RLLLTHATQL FDFADKYRGK YDSSITVAQK YYRSVSGYAD
     ELLWGAAWMY KATNNKFYLD YLGRNGDALG GTGWSMTEFG WDVKYAGVQT LVAKFLMSGK
     GRRHGAVFGK YQQKAESFMC SCLGKNTRNA QKTPAGLIYR QRWNNLQFVT SASFLLTVYA
     DYLTSARRNL RCSSGTVTPP QLLAFAKSQV DYILGDNPRA TSYMVGYGNN YPRQVHHRAS
     SIVSIKVNPS FVSCRGGYAT WFSRKASDPN LLTGAIVGGP DAYDNFADQR NNYQQTEPAT
     YNNAPLLGVL ARLNAGHAGY NQLLQVEVPL RETDAVQPEQ TPEAKVTPSA GLIAIEQKTT
     SSWTANGKTH YRYSVTLTNK SNKTIKNVNI SVTKLYGPLW GLTKTSSGSY GFPTWVNSLA
     AGKSIEFVYI HTNSPAEVSV SSYTLA
//
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