(data stored in ACNUC16935 zone)

SWISSPROT: C8VLL3_EMENI

ID   C8VLL3_EMENI            Unreviewed;       619 AA.
AC   C8VLL3;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   05-JUL-2017, entry version 44.
DE   RecName: Full=Glucoamylase {ECO:0000256|PIRNR:PIRNR001031};
DE            EC=3.2.1.3 {ECO:0000256|PIRNR:PIRNR001031};
DE   AltName: Full=1,4-alpha-D-glucan glucohydrolase {ECO:0000256|PIRNR:PIRNR001031};
DE   AltName: Full=Glucan 1,4-alpha-glucosidase {ECO:0000256|PIRNR:PIRNR001031};
GN   ORFNames=ANIA_11143 {ECO:0000313|EMBL:CBF84695.1};
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL
OS   194 / M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=227321 {ECO:0000313|EMBL:CBF84695.1, ECO:0000313|Proteomes:UP000000560};
RN   [1] {ECO:0000313|Proteomes:UP000000560}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139
RC   {ECO:0000313|Proteomes:UP000000560};
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.J., Wortman J.R.,
RA   Batzoglou S., Lee S.I., Basturkmen M., Spevak C.C., Clutterbuck J.,
RA   Kapitonov V., Jurka J., Scazzocchio C., Farman M., Butler J.,
RA   Purcell S., Harris S., Braus G.H., Draht O., Busch S., D'Enfert C.,
RA   Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S.,
RA   Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U.,
RA   Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T.,
RA   Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W.,
RA   Caddick M., Hynes M., Paoletti M., Fischer R., Miller B., Dyer P.,
RA   Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [2] {ECO:0000313|Proteomes:UP000000560}
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139
RC   {ECO:0000313|Proteomes:UP000000560};
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P.,
RA   von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E.,
RA   Fekete E., Flipphi M., Estrada C.G., Geysens S., Goldman G.,
RA   de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K.,
RA   Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S.,
RA   Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E.,
RA   Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A.,
RA   Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P.,
RA   Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R.,
RA   Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I.,
RA   Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B.,
RA   van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N.,
RA   Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J.,
RA   de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W.,
RA   Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a
RT   community effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of terminal (1->4)-linked alpha-D-
CC       glucose residues successively from non-reducing ends of the chains
CC       with release of beta-D-glucose. {ECO:0000256|PIRNR:PIRNR001031}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 15 family.
CC       {ECO:0000256|PIRNR:PIRNR001031}.
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DR   EMBL; BN001307; CBF84695.1; -; Genomic_DNA.
DR   STRING; 162425.CADANIAP00007964; -.
DR   EnsemblFungi; CADANIAT00007964; CADANIAP00007964; CADANIAG00007964.
DR   InParanoid; C8VLL3; -.
DR   OMA; EGNPWFI; -.
DR   OrthoDB; EOG092C1YYH; -.
DR   Proteomes; UP000000560; Chromosome VII.
DR   GO; GO:0000324; C:fungal-type vacuole; IBA:GO_Central.
DR   GO; GO:0004339; F:glucan 1,4-alpha-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IBA:GO_Central.
DR   GO; GO:2001070; F:starch binding; IEA:InterPro.
DR   GO; GO:0016052; P:carbohydrate catabolic process; IBA:GO_Central.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd05811; CBM20_glucoamylase; 1.
DR   Gene3D; 2.60.40.10; -; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase-like.
DR   InterPro; IPR013784; Carb-bd-like_fold.
DR   InterPro; IPR034836; CBM20_glucoamylase.
DR   InterPro; IPR002044; CBM_fam20.
DR   InterPro; IPR000165; Glucoamylase.
DR   InterPro; IPR008291; Glucoamylase_SBD.
DR   InterPro; IPR011613; Glyco_hydro_15/PHK.
DR   InterPro; IPR013783; Ig-like_fold.
DR   Pfam; PF00686; CBM_20; 1.
DR   Pfam; PF00723; Glyco_hydro_15; 1.
DR   PIRSF; PIRSF001031; Glu-a-glcsd_SBD; 1.
DR   PRINTS; PR00736; GLHYDRLASE15.
DR   SMART; SM01065; CBM_2; 1.
DR   SUPFAM; SSF48208; SSF48208; 1.
DR   SUPFAM; SSF49452; SSF49452; 1.
DR   PROSITE; PS51166; CBM20; 1.
PE   3: Inferred from homology;
DR   PRODOM; C8VLL3.
DR   SWISS-2DPAGE; C8VLL3.
KW   Carbohydrate metabolism {ECO:0000256|PIRNR:PIRNR001031};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000560};
KW   Glycosidase {ECO:0000256|PIRNR:PIRNR001031};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR001031};
KW   Polysaccharide degradation {ECO:0000256|PIRNR:PIRNR001031};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000560};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     17       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        18    619       Glucoamylase. {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5002993627.
FT   DOMAIN      513    619       CBM20 (carbohydrate binding type-20).
FT                                {ECO:0000259|PROSITE:PS51166}.
FT   ACT_SITE    209    209       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR001031-1}.
FT   ACT_SITE    212    212       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR001031-1}.
FT   BINDING     153    153       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001031-2}.
SQ   SEQUENCE   619 AA;  68712 MW;  62E4C0A8B0BA9A01 CRC64;
     MAFLSLYTQF FILGVVTLWV THGPRPLQQT LAAGDLDIWL PSEANIARTA LLDLIGDKGR
     WAEGAAAGVL VASPSRSDPD YFYTWTRDSS LVFKTLVEMF RAGDSDLLPI IQDWISSQAR
     IQGVENPSGG LADGRGLGEA KFTAEETAFA GSWGRPQRDG PALRATTMIE FGWWLLSQGY
     HQLAANTVWP VVHNDISYLT EYWNQSGFDL WEDLYGRSFF TLAVTYRALT EASLFARSIG
     SSCAECESQA PQVLCLLQSF WTGRFIRSNL DTGRTGKDAS TLLGVIHTFS PRSECDDVTF
     QPCSARALAN HYRVVDAFRD LYDINADRSQ DQAIAIGRYP EDQYFGGNPW FLCTIAAAEQ
     LYSAIYQWTH LGSITITAVS LPFFQTLHPT AVPGTYSSST EIYHQLIDAV RTYADGFMRI
     VQTYASHNGS LAEQFSRYDG SHLSANDLAW SYASLLTAHR RRNAIAPSPW GNPGQPSIPS
     YCEPTSASGT YSLATITTWP PMNGLPTTTS APCQVPSLVS VTFELTASTV WGEEIRLVGS
     SGELGYWVSE RGITFSTDRY SSSQPIWWAT VWLPAGQTVE YKYIRVREGY VVWEGDSNRL
     LTIPAVCGVK SIYRRESWR
//

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