ID A0A1J1IDP2_9DIPT Unreviewed; 1357 AA.
AC A0A1J1IDP2;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00012663};
DE EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663};
GN ORFNames=CLUMA_CG011758 {ECO:0000313|EMBL:CRK98399.1};
OS Clunio marinus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Chironomoidea; Chironomidae;
OC Clunio.
OX NCBI_TaxID=568069 {ECO:0000313|EMBL:CRK98399.1, ECO:0000313|Proteomes:UP000183832};
RN [1] {ECO:0000313|EMBL:CRK98399.1, ECO:0000313|Proteomes:UP000183832}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Syromyatnikov M.Y., Popov V.N.;
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine
CC residues in N-acetyl-beta-D-hexosaminides.; EC=3.2.1.52;
CC Evidence={ECO:0000256|ARBA:ARBA00001231};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 20 family.
CC {ECO:0000256|ARBA:ARBA00006285}.
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DR EMBL; CVRI01000047; CRK98399.1; -; Genomic_DNA.
DR STRING; 568069.A0A1J1IDP2; -.
DR OrthoDB; 178991at2759; -.
DR Proteomes; UP000183832; Unassembled WGS sequence.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004563; F:beta-N-acetylhexosaminidase activity; IEA:UniProtKB-EC.
DR GO; GO:0102148; F:N-acetyl-beta-D-galactosaminidase activity; IEA:UniProtKB-EC.
DR GO; GO:0052742; F:phosphatidylinositol kinase activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0046488; P:phosphatidylinositol metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006367; P:transcription initiation at RNA polymerase II promoter; IEA:InterPro.
DR CDD; cd06562; GH20_HexA_HexB-like; 1.
DR CDD; cd17305; PIPKc_PIP5KII; 1.
DR CDD; cd07977; TFIIE_beta_winged_helix; 1.
DR Gene3D; 3.30.810.10; 2-Layer Sandwich; 1.
DR Gene3D; 3.30.379.10; Chitobiase/beta-hexosaminidase domain 2-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 3.30.800.10; Phosphatidylinositol Phosphate Kinase II Beta; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 2.
DR InterPro; IPR025705; Beta_hexosaminidase_sua/sub.
DR InterPro; IPR015883; Glyco_hydro_20_cat.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR029018; Hex-like_dom2.
DR InterPro; IPR029019; HEX_eukaryotic_N.
DR InterPro; IPR027483; PInositol-4-P-4/5-kinase_C_sf.
DR InterPro; IPR002498; PInositol-4-P-4/5-kinase_core.
DR InterPro; IPR027484; PInositol-4-P-5-kinase_N.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR003166; TFIIE_bsu_DNA-bd.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR22600; BETA-HEXOSAMINIDASE; 1.
DR PANTHER; PTHR22600:SF48; BETA-N-ACETYLHEXOSAMINIDASE; 1.
DR Pfam; PF00728; Glyco_hydro_20; 1.
DR Pfam; PF14845; Glycohydro_20b2; 1.
DR Pfam; PF01504; PIP5K; 1.
DR Pfam; PF02186; TFIIE_beta; 1.
DR PRINTS; PR00738; GLHYDRLASE20.
DR SMART; SM00330; PIPKc; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF55545; beta-N-acetylhexosaminidase-like domain; 1.
DR SUPFAM; SSF56104; SAICAR synthase-like; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS51455; PIPK; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
DR PROSITE; PS51351; TFIIE_BETA_C; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00781};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Kinase {ECO:0000256|PROSITE-ProRule:PRU00781};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00781};
KW Reference proteome {ECO:0000313|Proteomes:UP000183832};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transferase {ECO:0000256|PROSITE-ProRule:PRU00781};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 747..771
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 41..413
FT /note="PIPK"
FT /evidence="ECO:0000259|PROSITE:PS51455"
FT DOMAIN 494..594
FT /note="TFIIE beta"
FT /evidence="ECO:0000259|PROSITE:PS51351"
FT DOMAIN 1220..1254
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT REGION 462..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..478
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1130
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR625705-1"
SQ SEQUENCE 1357 AA; 156201 MW; 63235B560C920C44 CRC64;
MLPLKIGIGN IWLINMATSA ARILKKKHYR VKHQKVKLFR ANDPMLSVFM WGINHSINEL
SHCLIPTLLL PDHFRANSKI KVDNHLFNKE NMPSHFKFKE YCPIVFKNLR ERFGIDDSDF
RDSLTRSEPI QMDSSGKSGA KFYRSFDNIY VIKSLTSEEV ERMHSFLKHY HPYVVEKHGS
TLLPNFLGMY RLTVDGVQYY FTIMRNVFSS HLKIHQKFDL KGSTVDRSCN ENELNKSLPT
FKDNDFTRQG IKISIGPAAK EKLHETLASD VEFLTKLHLM DYSLLIGIHD IQAEDAATEL
SDAHHDTDDS ECERVILAFL ISMRWENTPP DSPRQIEVHT INPDSDVYAI PSKEENKFIY
FIAIIDPLTN YGFKKQAAKA AKTVKYGSNV DGISTCDPEQ YGKRFLEFIL DRVIDSVPIV
NKIFLWDLKL NKVIMDAELL RQRELFKKRA LATPTVEKKL RAESSSSSAT SSKKPLAPWE
SKTPTPKEPM SYKTMTGSSQ KRFAILTKIV NYMKERHLNG EEHSLSIEEI LDETNQLDIG
GSTKTVIYDV LSIMKFCEFF LLIFQWLLTE ALPNNPKLDH LEGRFQFKPM YKIKDGKSLL
RLLKQHDLKG IGGVLLDDIQ ESLPHCEKVL KHRAPEIVFI TRPIDKKKIL FYNDKSANFS
VDEEFQKLWR SSTVNAIDDA KIEEYLEKQG IRSMQDHGIR KPMIPKRKKL ANKKRQFKRP
RDNEHLADIL ETYEVGIEMK AEKYATIVSF LAIFIIVIGL TALVVGFAIF VKPKKFYQTD
RLVVSKQAWG YKCEHNLCKK VELTEANIKT AVSLSVCRIY CNEDIGTVWP KPTGEVVISN
NVVKINPEEI VFKTNNFKKE PAYWAMAEER FMGMQQKKTP KNYDPKTGGK ALIVDVAVET
DDMIFNLDTK ESYKLEISEN PSEGVHAIIT APNFYGARNA LETLSQLIVY DNIRNEMLIV
GELKINDEPK FKYRGVLLDT SRNYFSVDAI KRTIEGMAMV KLNTFHWHIT DSHSFPFVVK
SQPELSRLGA YSPEKVYTSS DIEDIVRFAK ARGVRVLPEF DAPAHVGEGW QKKDLTTCFN
SQPWKDFCVE PPCGQLDPSK DEVYNVLEDI YREMVESFAY PDLFHMGGDE VSVSCWNSSE
SLQKWMLEKG WGLTESDFMQ LWGHFQDNAL ARLDKVNFQQ VPIILWTSRL TEEPFLTKYL
DKSRYIIQIW TKGDDPKVTT LLENGYKMIV SNYDALYLDC GFEAWVTEGN NWCSPYIGWQ
KIYDNRMETV GGPYVNQIYG AEAALWSEQA DEHSLDSRLW PRLSALAERL WSNPMGSWRT
AESRMLVNRY RLANIGGIGA EVLQPQWCLQ NEGECPI
//
