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Database: UniProt
Entry: S3CH21_GLAL2
LinkDB: S3CH21_GLAL2
Original site: S3CH21_GLAL2 
ID   S3CH21_GLAL2            Unreviewed;       740 AA.
AC   S3CH21;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   SubName: Full=p-loop containing nucleoside triphosphate hydrolase {ECO:0000313|EMBL:EPE25170.1};
GN   ORFNames=GLAREA_11751 {ECO:0000313|EMBL:EPE25170.1};
OS   Glarea lozoyensis (strain ATCC 20868 / MF5171).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Helotiaceae; Glarea.
OX   NCBI_TaxID=1116229 {ECO:0000313|EMBL:EPE25170.1, ECO:0000313|Proteomes:UP000016922};
RN   [1] {ECO:0000313|EMBL:EPE25170.1, ECO:0000313|Proteomes:UP000016922}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 20868 / MF5171 {ECO:0000313|Proteomes:UP000016922};
RX   PubMed=23688303; DOI=10.1186/1471-2164-14-339;
RA   Chen L., Yue Q., Zhang X., Xiang M., Wang C., Li S., Che Y.,
RA   Ortiz-Lopez F.J., Bills G.F., Liu X., An Z.;
RT   "Genomics-driven discovery of the pneumocandin biosynthetic gene cluster in
RT   the fungus Glarea lozoyensis.";
RL   BMC Genomics 14:339-339(2013).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide
CC         (1->4)-beta-linkages in chitin and chitodextrins.; EC=3.2.1.14;
CC         Evidence={ECO:0000256|ARBA:ARBA00000822};
CC   -!- SIMILARITY: Belongs to the AAA ATPase family. BCS1 subfamily.
CC       {ECO:0000256|ARBA:ARBA00007448}.
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DR   EMBL; KE145372; EPE25170.1; -; Genomic_DNA.
DR   RefSeq; XP_008088085.1; XM_008089894.1.
DR   AlphaFoldDB; S3CH21; -.
DR   STRING; 1116229.S3CH21; -.
DR   GeneID; 19470792; -.
DR   KEGG; glz:GLAREA_11751; -.
DR   eggNOG; KOG0743; Eukaryota.
DR   HOGENOM; CLU_375074_0_0_1; -.
DR   OrthoDB; 1537817at2759; -.
DR   Proteomes; UP000016922; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0004568; F:chitinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006032; P:chitin catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR003960; ATPase_AAA_CS.
DR   InterPro; IPR001223; Glyco_hydro18_cat.
DR   InterPro; IPR001579; Glyco_hydro_18_chit_AS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR23070; BCS1 AAA-TYPE ATPASE; 1.
DR   PANTHER; PTHR23070:SF11; MITOCHONDRIAL CHAPERONE BCS1; 1.
DR   Pfam; PF00004; AAA; 2.
DR   Pfam; PF00704; Glyco_hydro_18; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00674; AAA; 1.
DR   PROSITE; PS01095; GH18_1; 1.
DR   PROSITE; PS51910; GH18_2; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Chitin degradation {ECO:0000256|ARBA:ARBA00023024};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000489};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000489};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016922}.
FT   DOMAIN          439..740
FT                   /note="GH18"
FT                   /evidence="ECO:0000259|PROSITE:PS51910"
FT   REGION          217..252
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          412..436
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        220..234
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        235..250
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   740 AA;  83038 MW;  68DBB606586EED19 CRC64;
     MEETTEQKAT PQAVVPTYIL DAFIPGYSAL HNVILHVLGT DINYLVSSAA ILWLFSKVLY
     SPWETLMDLV EEYFMSSLTI EENNRDLCKI QLAYFAKREA ELRIRSINAA LNHDPEERTD
     EEMVSEMGWL NFAFSDANTP MRYSARGIPY RRGYLLYGPP GTGKSSLAYA VAGLFGLEIL
     FLSLMDKNLD EEKLSDLFAA LPEKCLVLLE DIDSAGLNRD MDESEDEDSE SEDEDDSKSA
     KKKASKENKN TSKNKGISLS GLLNTIDGVA SNEGRVLFMT TNCPEKLDSA FIRPGRIDLQ
     VEFTNATQFH AKEIFERMYA RQPIRTNASV STPEAIIDEK ETTSEDRIYG EEIKAMALEF
     ADHIPDGLLS PAEIQGFLLN RRKEPKKALE EVTTWVKGLL ESKKKGKKVV GAHSQAWHSA
     AKHPKAGTTH DHTHASDPSR LVMYVQTFKT PNKEPLSLLP LIEKHTKVTH IILASLHLHD
     VPGEIRLNDD RLESPVWDDL WHETWLLRQN GVKVMALLGG AAGGTYKRLN GTDAQFYAYY
     NPLLALIRKY HFDGLDLDVE ENVDISTPIR LMTALRRDMG PDFIITMSPL ASALTDELGQ
     NLSGFSYFEL EKFATMPGSD EKLVSWYNGL FYGPFARGPP VFDACVEAGW DPSRIVMIVL
     DCADDGQPNG FVHIEDLQET IKNLRALYPG FGGMGGWEYH DAGMSDWDVY QPWLWVKRVG
     DALFDPLQQA LGKGVADELR
//
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