UniProt: A0A2K1KJ16

Database: UniProt
Entry: A0A2K1KJ16_PHYPA

LinkDB:  A0A2K1KJ16_PHYPA 
Original site:  A0A2K1KJ16_PHYPA

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Ontology (3)   
   GO (3)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (6)   
   InterPro (4)   
   Pfam (1)   
   PROSITE (1)   
Literature (2)   
   PubMed (2)   
All databases (13)   

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ID   A0A2K1KJ16_PHYPA        Unreviewed;       639 AA.
AC   A0A2K1KJ16;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361166};
DE            EC=3.2.1.4 {ECO:0000256|RuleBase:RU361166};
GN   ORFNames=PHYPA_007449 {ECO:0000313|EMBL:PNR53774.1};
OS   Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC   Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae; Physcomitrium.
OX   NCBI_TaxID=3218 {ECO:0000313|EMBL:PNR53774.1};
RN   [1] {ECO:0000313|EMBL:PNR53774.1, ECO:0000313|Proteomes:UP000006727}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Gransden 2004 {ECO:0000313|EnsemblPlants:Pp3c5_9540V3.1,
RC   ECO:0000313|Proteomes:UP000006727};
RX   PubMed=18079367; DOI=10.1126/science.1150646;
RA   Rensing S.A., Lang D., Zimmer A.D., Terry A., Salamov A., Shapiro H.,
RA   Nishiyama T., Perroud P.-F., Lindquist E.A., Kamisugi Y., Tanahashi T.,
RA   Sakakibara K., Fujita T., Oishi K., Shin-I T., Kuroki Y., Toyoda A.,
RA   Suzuki Y., Hashimoto S.-I., Yamaguchi K., Sugano S., Kohara Y.,
RA   Fujiyama A., Anterola A., Aoki S., Ashton N., Barbazuk W.B., Barker E.,
RA   Bennetzen J.L., Blankenship R., Cho S.H., Dutcher S.K., Estelle M.,
RA   Fawcett J.A., Gundlach H., Hanada K., Heyl A., Hicks K.A., Hughes J.,
RA   Lohr M., Mayer K., Melkozernov A., Murata T., Nelson D.R., Pils B.,
RA   Prigge M., Reiss B., Renner T., Rombauts S., Rushton P.J., Sanderfoot A.,
RA   Schween G., Shiu S.-H., Stueber K., Theodoulou F.L., Tu H., Van de Peer Y.,
RA   Verrier P.J., Waters E., Wood A., Yang L., Cove D., Cuming A.C., Hasebe M.,
RA   Lucas S., Mishler B.D., Reski R., Grigoriev I.V., Quatrano R.S.,
RA   Boore J.L.;
RT   "The Physcomitrella genome reveals evolutionary insights into the conquest
RT   of land by plants.";
RL   Science 319:64-69(2008).
RN   [2] {ECO:0000313|EMBL:PNR53774.1, ECO:0000313|Proteomes:UP000006727}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Gransden 2004 {ECO:0000313|EnsemblPlants:Pp3c5_9540V3.1,
RC   ECO:0000313|Proteomes:UP000006727};
RX   PubMed=29237241; DOI=10.1111/tpj.13801;
RA   Lang D., Ullrich K.K., Murat F., Fuchs J., Jenkins J., Haas F.B.,
RA   Piednoel M., Gundlach H., Van Bel M., Meyberg R., Vives C., Morata J.,
RA   Symeonidi A., Hiss M., Muchero W., Kamisugi Y., Saleh O., Blanc G.,
RA   Decker E.L., van Gessel N., Grimwood J., Hayes R.D., Graham S.W.,
RA   Gunter L.E., McDaniel S.F., Hoernstein S.N.W., Larsson A., Li F.W.,
RA   Perroud P.F., Phillips J., Ranjan P., Rokshar D.S., Rothfels C.J.,
RA   Schneider L., Shu S., Stevenson D.W., Thummler F., Tillich M.,
RA   Villarreal Aguilar J.C., Widiez T., Wong G.K., Wymore A., Zhang Y.,
RA   Zimmer A.D., Quatrano R.S., Mayer K.F.X., Goodstein D., Casacuberta J.M.,
RA   Vandepoele K., Reski R., Cuming A.C., Tuskan G.A., Maumus F., Salse J.,
RA   Schmutz J., Rensing S.A.;
RT   "The Physcomitrella patens chromosome-scale assembly reveals moss genome
RT   structure and evolution.";
RL   Plant J. 93:515-533(2018).
RN   [3] {ECO:0000313|EnsemblPlants:Pp3c5_9540V3.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (DEC-2020) to UniProtKB.
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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 9 (cellulase E) family.
CC       {ECO:0000256|ARBA:ARBA00007072, ECO:0000256|PROSITE-ProRule:PRU10060,
CC       ECO:0000256|RuleBase:RU361166}.
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DR   EMBL; ABEU02000005; PNR53774.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2K1KJ16; -.
DR   STRING; 3218.A0A2K1KJ16; -.
DR   PaxDb; 3218-PP1S64_152V6-1; -.
DR   EnsemblPlants; Pp3c5_9540V3.1; Pp3c5_9540V3.1; Pp3c5_9540.
DR   EnsemblPlants; Pp3c5_9540V3.2; Pp3c5_9540V3.2; Pp3c5_9540.
DR   EnsemblPlants; Pp3c5_9540V3.3; Pp3c5_9540V3.3; Pp3c5_9540.
DR   EnsemblPlants; Pp3c5_9540V3.4; Pp3c5_9540V3.4; Pp3c5_9540.
DR   Gramene; Pp3c5_9540V3.1; Pp3c5_9540V3.1; Pp3c5_9540.
DR   Gramene; Pp3c5_9540V3.2; Pp3c5_9540V3.2; Pp3c5_9540.
DR   Gramene; Pp3c5_9540V3.3; Pp3c5_9540V3.3; Pp3c5_9540.
DR   Gramene; Pp3c5_9540V3.4; Pp3c5_9540V3.4; Pp3c5_9540.
DR   InParanoid; A0A2K1KJ16; -.
DR   OMA; MQNDHYC; -.
DR   OrthoDB; 1347382at2759; -.
DR   Proteomes; UP000006727; Chromosome 5.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; IPR001701; Glyco_hydro_9.
DR   InterPro; IPR033126; Glyco_hydro_9_Asp/Glu_AS.
DR   PANTHER; PTHR22298; ENDO-1,4-BETA-GLUCANASE; 1.
DR   PANTHER; PTHR22298:SF36; ENDOGLUCANASE 25; 1.
DR   Pfam; PF00759; Glyco_hydro_9; 1.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR   PROSITE; PS00698; GH9_3; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW   ECO:0000256|PROSITE-ProRule:PRU10060};
KW   Cellulose degradation {ECO:0000256|ARBA:ARBA00023001,
KW   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}; Membrane {ECO:0000256|SAM:Phobius};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW   ECO:0000256|PROSITE-ProRule:PRU10060};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006727};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        94..113
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          126..600
FT                   /note="Glycoside hydrolase family 9"
FT                   /evidence="ECO:0000259|Pfam:PF00759"
FT   ACT_SITE        578
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
FT   ACT_SITE        587
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
SQ   SEQUENCE   639 AA;  71649 MW;  EA97B44F0C4753F5 CRC64;
     MFNQQYRRPG SMEMSRKYWG SSLGTSTDFD YDEPSVQSLC DLERTRSLEG AVPRPMLDET
     QQSWLLEPKV EKKEPTVDLG CVSVTRRFFR WMNCIFWGIV VIIALALIIW KFGPKHGHSP
     PKPDNYTIAL SKALSFFDIQ KSGALPVNDR QRRFKWRRSS ALLDGQAAQP GSPAVKLAGG
     FYDGGNTIKF GFPGAYAMTM LSWSVIEYKA KFEASGEFDH ARELIKWGTD YILKTFNNTE
     VDKIICQVGI GGGPRPNDLY CWERPEDLDF FKDTRRSAIS VNSGSDLAAE MAAALSAASI
     VFRDDPKYSQ GLVNAAKALY AFAKLKPGSF VQNLPGPERA IYNATSFNDE LIWGSTWLYF
     ATGNTTYLGD ATIRSIENSN RKRGYTFGVF DWDNKLVGAQ LLLTRLRILQ GPGYPYEQTL
     KQYNNETNLV MCAYLPQFRT WNRTKGGMIL FNPNATQHLP TAVNAAFLAT LYADYLKAAD
     VPVLECGPNW YSPEVLRNFS RSQVDYALGK NPLKTSYVVG YSEKYPLQPR HRAASIPDDG
     KSYSCEQGWQ WRDRNFPNPH VLQGALVGGP DILDRFTDLR KNYIQNEPTI ANNAGLVGAL
     VALSTMPTGT QEHIDPHSIF SAIPVYVPSP PPPVVPWEP
//

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