ID A0A1C4ZU48_MICEC Unreviewed; 660 AA.
AC A0A1C4ZU48;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Glucosylceramidase {ECO:0000313|EMBL:SCF36396.1};
GN ORFNames=GA0070618_5772 {ECO:0000313|EMBL:SCF36396.1};
OS Micromonospora echinospora (Micromonospora purpurea).
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=1877 {ECO:0000313|EMBL:SCF36396.1, ECO:0000313|Proteomes:UP000198253};
RN [1] {ECO:0000313|EMBL:SCF36396.1, ECO:0000313|Proteomes:UP000198253}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43816 {ECO:0000313|EMBL:SCF36396.1,
RC ECO:0000313|Proteomes:UP000198253};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 30 family.
CC {ECO:0000256|ARBA:ARBA00005382, ECO:0000256|RuleBase:RU361188}.
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DR EMBL; LT607413; SCF36396.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C4ZU48; -.
DR InParanoid; A0A1C4ZU48; -.
DR OrthoDB; 9806701at2; -.
DR Proteomes; UP000198253; Chromosome i.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004348; F:glucosylceramidase activity; IEA:InterPro.
DR GO; GO:0006665; P:sphingolipid metabolic process; IEA:InterPro.
DR CDD; cd00161; RICIN; 1.
DR Gene3D; 2.80.10.50; -; 2.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR InterPro; IPR033452; GH30_C.
DR InterPro; IPR001139; Glyco_hydro_30.
DR InterPro; IPR033453; Glyco_hydro_30_TIM-barrel.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR11069; GLUCOSYLCERAMIDASE; 1.
DR PANTHER; PTHR11069:SF23; LYSOSOMAL ACID GLUCOSYLCERAMIDASE; 1.
DR Pfam; PF02055; Glyco_hydro_30; 1.
DR Pfam; PF17189; Glyco_hydro_30C; 1.
DR Pfam; PF00652; Ricin_B_lectin; 1.
DR SMART; SM00458; RICIN; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|RuleBase:RU361188};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361188};
KW Membrane {ECO:0000256|SAM:Phobius}; Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 533..659
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|SMART:SM00458"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 517..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 660 AA; 70359 MW; 28C2B621DFFF3D21 CRC64;
MPRAASPPPA RSGPDPAGRP VGLPGRRRSH VRRTALTAGG LTVAVVAALV GITAAPSALA
AGESVTVHLT TTSDSGGRTV TRGLQQQPSV NFAANSAPAT HTISVDENIR HQQFVGAGAS
ITDTTAYLFR GGPISAATRD AVMRKLFHPV DGIGLSFVRN PIGASDLSRP GHVSLDDTCC
DLNDFGANGY DTNVRLLTQQ AKQLNPQLRV KGVPWSAPGW MKDNGRMDQM GWLKWEYYPL
YAQYLVRYVQ SYQAAGVPVD YLSVQNEPNC CQAANPPAMN YPGMSWNPSG LVEFTKNHLY
PAFRAAGITT KVMHFDWNYG DYGSFGSQIV ADTALRNDPL SAGIAWHDYF GSPSVGTQVR
QQYPSMTQFN TEHSGGTWVT NQHNEDMGDI IEHARNWSSA EVKWSLALNQ NMGPHNGGCG
TCTGLVTVQE GGSRAGQVDY TIEYYTMGHL TKFVKPGAHR IDSTDNGTVQ NVAYVNPDGS
KALIAHNGGT GSQSIRVLWG GQSFTYTLPA RTSATFTWSG DQSGGPTTPP PSGGTGPITG
LAGKCVDVAG AGTANGTAVQ LYACNGTAAQ RWTRATDGTL RALGKCLDVA GPSTADGAQT
HLWDCHGGAS QRWTYTANRE LVNAYANKCL DVTDRNSADG TRLQIWTCQG DTNQKWTVPA
//
