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Database: UniProt
Entry: A0A0J9XPV2_BRUMA
LinkDB: A0A0J9XPV2_BRUMA
Original site: A0A0J9XPV2_BRUMA 
ID   A0A0J9XPV2_BRUMA        Unreviewed;       670 AA.
AC   A0A0J9XPV2;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Bm4197, isoform b {ECO:0000313|EMBL:CDP92627.1};
DE   Flags: Fragment;
GN   ORFNames=Bm4197 {ECO:0000313|EMBL:CDP92627.1,
GN   ECO:0000313|WormBase:Bm4197b}, BM_Bm4197
GN   {ECO:0000313|EMBL:CDP92627.1};
OS   Brugia malayi (Filarial nematode worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia.
OX   NCBI_TaxID=6279 {ECO:0000313|EMBL:CDP92627.1};
RN   [1] {ECO:0000313|EMBL:CDP92627.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=FR3 {ECO:0000313|EMBL:CDP92627.1};
RX   PubMed=17885136; DOI=10.1126/science.1145406;
RA   Ghedin E., Wang S., Spiro D., Caler E., Zhao Q., Crabtree J., Allen J.E.,
RA   Delcher A.L., Guiliano D.B., Miranda-Saavedra D., Angiuoli S.V., Creasy T.,
RA   Amedeo P., Haas B., El-Sayed N.M., Wortman J.R., Feldblyum T., Tallon L.,
RA   Schatz M., Shumway M., Koo H., Salzberg S.L., Schobel S., Pertea M.,
RA   Pop M., White O., Barton G.J., Carlow C.K., Crawford M.J., Daub J.,
RA   Dimmic M.W., Estes C.F., Foster J.M., Ganatra M., Gregory W.F.,
RA   Johnson N.M., Jin J., Komuniecki R., Korf I., Kumar S., Laney S., Li B.W.,
RA   Li W., Lindblom T.H., Lustigman S., Ma D., Maina C.V., Martin D.M.,
RA   McCarter J.P., McReynolds L., Mitreva M., Nutman T.B., Parkinson J.,
RA   Peregrin-Alvarez J.M., Poole C., Ren Q., Saunders L., Sluder A.E.,
RA   Smith K., Stanke M., Unnasch T.R., Ware J., Wei A.D., Weil G.,
RA   Williams D.J., Zhang Y., Williams S.A., Fraser-Liggett C., Slatko B.,
RA   Blaxter M.L., Scott A.L.;
RT   "Draft genome of the filarial nematode parasite Brugia malayi.";
RL   Science 317:1756-1760(2007).
RN   [2] {ECO:0000313|EMBL:CDP92627.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=FR3 {ECO:0000313|EMBL:CDP92627.1};
RA   Gao Y.W., Fan S.T., Sun H.T., Wang Z., Gao X.L., Li Y.G., Wang T.C.,
RA   Zhang K., Xu W.W., Yu Z.J., Xia X.Z.;
RL   Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family.
CC       {ECO:0000256|ARBA:ARBA00009792}.
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DR   EMBL; LN856843; CDP92627.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0J9XPV2; -.
DR   WormBase; Bm4197b; BM48613; WBGene00224458; -.
DR   GO; GO:0004559; F:alpha-mannosidase activity; IEA:InterPro.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0006013; P:mannose metabolic process; IEA:InterPro.
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   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
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   PANTHER; PTHR11607; ALPHA-MANNOSIDASE; 1.
DR   PANTHER; PTHR11607:SF3; LYSOSOMAL ALPHA-MANNOSIDASE; 1.
DR   Pfam; PF09261; Alpha-mann_mid; 1.
DR   Pfam; PF01074; Glyco_hydro_38N; 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; 1.
DR   SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
PE   3: Inferred from homology;
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          157..230
FT                   /note="Glycoside hydrolase family 38 central"
FT                   /evidence="ECO:0000259|SMART:SM00872"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:CDP92627.1"
SQ   SEQUENCE   670 AA;  76611 MW;  2359D70E093531DD CRC64;
     QLHWAPLVNV LPNAYYTVTS ACGTDEMICC QFDVSKTSRS SCMERAKVDN VQKIALYGER
     MANQYRSLQT FYNSEAVLVA AGDDFLYSDS DDLKIVHRVY SALFKYINRN YDRFNMRVQF
     GTVADYFKSL KGNAKRRASI LSGDFFPYMD NAFSNAPFWT GFYNHRAYFK CFERIIQREL
     RLVDLLSVAI GIYLNSDVEI ARRNLALSIH HDAITGTSKR HVMDDYMLRL RSALHIILKE
     QERLLSISDE TFTTLFVNNS VKTKGMYLPR ITFSFADGIE SYKIQIVSQK TFSTMELVKI
     NVSSPFITVT HNDKLLTIQV VRILKQSDLF ELVYNDGSME TNFALYFNRI NDYGGAYTMV
     SAGLSLENIT DKNRLSPTII QGPIYSSITQ QLSSQLAYSI TIINSTDDNA RSIQIDLFTN
     VTLSPGYDRK MKLEANIYPM ITETVIEDDK LRCTVLGAQS TGVTAKMGLV TLMVDREMYN
     DDGKGLDYYE ASESHPSHLR YRIIFEPKTS EMKNFDDLKT IDKNELENKS SPMNTMYHSQ
     LVQQTLEELL YPAALFLSSS INSTDNNEMS SVLIDLPRLP DNIQLITIRY IARKTILLSM
     RQLPYDCSVE LYCKSDSNTD LTRQFFSSFN GSIYLSNLTG TKKGIQIMPE IIPSYLIQSF
     HIVTFLVVHR
//
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