UniProt: A0A0V8T9P9

Database: UniProt
Entry: A0A0V8T9P9_9CELL

LinkDB:  A0A0V8T9P9_9CELL 
Original site:  A0A0V8T9P9_9CELL

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Ontology (2)   
   GO (2)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (12)   
   InterPro (8)   
   Pfam (2)   
   PROSITE (2)   
All databases (17)   

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ID   A0A0V8T9P9_9CELL        Unreviewed;       629 AA.
AC   A0A0V8T9P9;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361166};
DE            EC=3.2.1.4 {ECO:0000256|RuleBase:RU361166};
DE   Flags: Fragment;
GN   ORFNames=ATM99_08250 {ECO:0000313|EMBL:KSW29417.1};
OS   Cellulomonas sp. B6.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC   Cellulomonas.
OX   NCBI_TaxID=1295626 {ECO:0000313|EMBL:KSW29417.1, ECO:0000313|Proteomes:UP000054319};
RN   [1] {ECO:0000313|EMBL:KSW29417.1, ECO:0000313|Proteomes:UP000054319}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B6 {ECO:0000313|EMBL:KSW29417.1,
RC   ECO:0000313|Proteomes:UP000054319};
RA   Piccinni F.E., Campos E.;
RT   "Draft Genome Sequence of Cellulolytic and Xylanolytic Cellulomonas strain
RT   Isolated from Decaying Forest Soil.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU361166};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 9 (cellulase E) family.
CC       {ECO:0000256|PROSITE-ProRule:PRU10060, 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:KSW29417.1}.
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DR   EMBL; LNTD01000062; KSW29417.1; -; Genomic_DNA.
DR   RefSeq; WP_062101819.1; NZ_LNTD01000062.1.
DR   AlphaFoldDB; A0A0V8T9P9; -.
DR   STRING; 1295626.ATM99_08250; -.
DR   OrthoDB; 9758662at2; -.
DR   Proteomes; UP000054319; Unassembled WGS sequence.
DR   GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd02850; E_set_Cellulase_N; 1.
DR   Gene3D; 1.50.10.10; -; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR004197; Cellulase_Ig-like.
DR   InterPro; IPR001701; Glyco_hydro_9.
DR   InterPro; IPR033126; Glyco_hydro_9_Asp/Glu_AS.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR006311; TAT_signal.
DR   PANTHER; PTHR22298; ENDO-1,4-BETA-GLUCANASE; 1.
DR   PANTHER; PTHR22298:SF29; ENDOGLUCANASE; 1.
DR   Pfam; PF02927; CelD_N; 1.
DR   Pfam; PF00759; Glyco_hydro_9; 1.
DR   SUPFAM; SSF81296; E set domains; 1.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR   PROSITE; PS00698; GH9_3; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW   ECO:0000256|PROSITE-ProRule:PRU10060};
KW   Cellulose degradation {ECO:0000256|RuleBase:RU361166};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PROSITE-
KW   ProRule:PRU10060};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU10060};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW   ECO:0000256|PROSITE-ProRule:PRU10060};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054319};
KW   Signal {ECO:0000256|RuleBase:RU361166}.
FT   SIGNAL          1..36
FT                   /evidence="ECO:0000256|RuleBase:RU361166"
FT   CHAIN           37..629
FT                   /note="Endoglucanase"
FT                   /evidence="ECO:0000256|RuleBase:RU361166"
FT                   /id="PRO_5039754754"
FT   DOMAIN          41..122
FT                   /note="Cellulase Ig-like"
FT                   /evidence="ECO:0000259|Pfam:PF02927"
FT   DOMAIN          135..598
FT                   /note="Glycoside hydrolase family 9"
FT                   /evidence="ECO:0000259|Pfam:PF00759"
FT   REGION          606..629
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        612..629
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        577
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
FT   ACT_SITE        586
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
FT   NON_TER         629
FT                   /evidence="ECO:0000313|EMBL:KSW29417.1"
SQ   SEQUENCE   629 AA;  65831 MW;  858BA08B56DD9646 CRC64;
     MSPITRRRAR RRAWAAGLAV ATALTVAGVT APAAVAAPDP GTPVKVNQVA YVPGVAKVAT
     LVSTSTTPVA WTLKDASGRT VAQGTSTVKG ADALSGDRTH LIDFSSYDTA GTGYVLSAGG
     ASSHPFDISA DPVRKLRSDS LAFFYHQRSG IAIEAQYVGS TYARAAGHLG VAPNQGDTSV
     PCRQSCGYSL DVRGGWYDAG DHGKYVVNGG IATWQLQNTY ERTLHVAGAD RAALGDGKAA
     IPERTNGVPD VLDEARWEVE FLLRMQVPAG RTDAGMVHHK MHDENWTGIP TIPAQDAQRR
     ILAPVSTAAT LNMAAVAAQA SRLWAPYDAA FSARALSAAR TAYAAAKANP NRIASDADGT
     GGGAYGDPSV TDEFYWAAAE LFATTGEAAY RADVTGSPFY RGTSFAERGY DWGWTGGLGD
     TTLALVPTDL PAADVAATRA AIVSFADATL GRLANQAYPA PNNAGTVYYW GSNGQVVNNA
     NALALAYDFT GQTKYRTAAY GALDYLQGRN PLNQSYIAGY GENPVRNVHH RFWAHQADAS
     LPTAPPGSLA GGPNSELQDP LAAAQLAGCA PQKCYVDHIE AYSVNEVAIN WNSALVWLSA
     WAAEQAGGTT PEPTPTPTPT PTVSPTPTP
//

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