ID A0A1Q8CV89_9PSEU Unreviewed; 1389 AA.
AC A0A1Q8CV89;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Alpha-mannosidase {ECO:0000313|EMBL:OLF18246.1};
GN ORFNames=BU204_06685 {ECO:0000313|EMBL:OLF18246.1};
OS Actinophytocola xanthii.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae.
OX NCBI_TaxID=1912961 {ECO:0000313|EMBL:OLF18246.1, ECO:0000313|Proteomes:UP000185596};
RN [1] {ECO:0000313|EMBL:OLF18246.1, ECO:0000313|Proteomes:UP000185596}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=11-183 {ECO:0000313|EMBL:OLF18246.1,
RC ECO:0000313|Proteomes:UP000185596};
RA Wang W., Yuan L.;
RT "The draft genome sequence of Actinophytocola sp. 11-183.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family.
CC {ECO:0000256|ARBA:ARBA00009792}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OLF18246.1}.
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DR EMBL; MSIE01000008; OLF18246.1; -; Genomic_DNA.
DR STRING; 1912961.BU204_06685; -.
DR OrthoDB; 1049785at2; -.
DR Proteomes; UP000185596; Unassembled WGS sequence.
DR GO; GO:0004559; F:alpha-mannosidase activity; IEA:InterPro.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006013; P:mannose metabolic process; IEA:InterPro.
DR CDD; cd10786; GH38N_AMII_like; 1.
DR Gene3D; 3.20.110.10; Glycoside hydrolase 38, N terminal domain; 1.
DR Gene3D; 1.20.1270.50; Glycoside hydrolase family 38, central domain; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR018905; A-galactase_NEW3.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR011682; Glyco_hydro_38_C.
DR InterPro; IPR015341; Glyco_hydro_38_cen.
DR InterPro; IPR037094; Glyco_hydro_38_cen_sf.
DR InterPro; IPR000602; Glyco_hydro_38_N.
DR InterPro; IPR027291; Glyco_hydro_38_N_sf.
DR InterPro; IPR028995; Glyco_hydro_57/38_cen_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR46017; ALPHA-MANNOSIDASE 2C1; 1.
DR PANTHER; PTHR46017:SF1; ALPHA-MANNOSIDASE 2C1; 1.
DR Pfam; PF09261; Alpha-mann_mid; 1.
DR Pfam; PF07748; Glyco_hydro_38C; 1.
DR Pfam; PF01074; Glyco_hydro_38N; 1.
DR Pfam; PF10633; NPCBM_assoc; 1.
DR SMART; SM00872; Alpha-mann_mid; 1.
DR SUPFAM; SSF88688; Families 57/38 glycoside transferase middle domain; 1.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 2.
DR SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000185596}.
FT DOMAIN 413..484
FT /note="Glycoside hydrolase family 38 central"
FT /evidence="ECO:0000259|SMART:SM00872"
SQ SEQUENCE 1389 AA; 146824 MW; 4C4A9FDD07012BCA CRC64;
MGAVVVDVTE LFVGSVGAPL QVVRVGFAGA GAARVHVEGE GVSTPAPVEV DVAGEVVVEV
GVDTGGAAVG RELAARAVVV SGTDRVEEEF TLRVAETGWT MHMVSHFHYD PVWWNTQAAY
TVAWDTLDFP GSQRGARQLA GFDLVRAHLD LALAEPEYRF VLAEVDYLKP YWDTFPGDRE
VLRRLIHEGR IEVLGGTYNE PNTNLTDPET TVRNLVHGMG FQRDVLGAAP ATAWQLDVFG
HDPAFPGLAA DAGLTSSSWA RGPFHQWGPM EVTEAGRGDP RRMQFTSEFE WISPSGRGLL
TSYMADHYGS GWAMDSAVRL EDACAAAYST FLQLKQVAST REVLLPVGGD YTPPNKWVTQ
VHRRFAERYV WPRFVCSLPR DFFAAVRTGL AERGEQASPQ TRDMNPIYTG KDVSYIDTKQ
AQRAAETAVL EAEAYAVFAR LLGGSPYPDA ALAKAWVQLA YGAHHDGITG SESDQVYLDL
LTSWRDAHDL AVDVRERALT VLSGLVTPAG GDGVPVVVWN SLNHSRTDVV TVLLEPAVSG
VEVMDAAGVM LPALIEHGGR SVTFLASDVP ALGWRAYRLR AGGEELGGWV PVEGLTADSD
RFRVTVDPER GGGVSSLLDN GHELVEQGRV GNELAVYEEY PQHPRFSEGP WHLLPRGPVT
TSAASSADVR VERCPIGERI TVRGNVGPVR FTQTITLWRG VGRVDCLTRV DEFTGADQLL
RVRWPCPVPG ALPVSEVGNA VVGRGFGLID VDSAVHPWTL DNPAHTWFGL SSAAALRLGD
GALRPIGVAE IIVPATADAA PLARPLAVAL ARCGVTATVS TAAGARYGDL GVDSNLPDVR
IALGGPEANG FTAELLSRCG LDDAGGTYWV APEKPLTEVW RPSADLRDCR ALGVLVVSGK
DGAELEVAVR SLVDDLADNV IEVGAGDPAQ PSYVERTVAL VNRGLPGFAV DSGGTLHASL
LRSCTGWPSG VWIDPPRRTV PDGSGFQLQH WTHEFEYALA AGSGDWRAAG IAATSAEFSR
PLHAVAGQAG SALPCAGSLL RVEPADRVRV AAVKAAGNPL VRGSAAVADP LAEVAVRLVA
HTGEPVLARI DSDVVTFADA AVANLLEERR EPLSSLEVEV GGCDAVTVLA RATPPVAAVT
GPAIGTEAEP VQPLFAKYWL HNRGPAPLGG LPLAVHLHPA AVDGPEATLE LTVASDSTDV
DLPGVVRFAL PRGWRADPDE VPFGLPPGGH LATTVTVTAP PGTRAGRYPV RAAVSPAGDE
LPASWRQVVE DVALVNVGAP TGEELLRLLG GPEPVRVRAG ETARLAVRVA STAGAAIALE
AALVSPWGTW DLAGPRLVGA EVPAEGEVEV GFDIAPAVGR PAGRWWALVR VAGAGKLLYS
PAVPLEVLG
//