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
//