ID   L5M6L3_MYODS            Unreviewed;       714 AA.
AC   L5M6L3;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Family 31 glucosidase KIAA1161 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=MDA_GLEAN10021640 {ECO:0000313|EMBL:ELK34279.1};
OS   Myotis davidii (David's myotis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC   Myotis.
OX   NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK34279.1, ECO:0000313|Proteomes:UP000010556};
RN   [1] {ECO:0000313|Proteomes:UP000010556}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23258410; DOI=10.1126/science.1230835;
RA   Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA   Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA   Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA   Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA   Wang J.;
RT   "Comparative analysis of bat genomes provides insight into the evolution of
RT   flight and immunity.";
RL   Science 339:456-460(2013).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family.
CC       {ECO:0000256|ARBA:ARBA00007806, ECO:0000256|RuleBase:RU361185}.
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DR   EMBL; KB103229; ELK34279.1; -; Genomic_DNA.
DR   RefSeq; XP_006758628.1; XM_006758565.2.
DR   RefSeq; XP_006758629.1; XM_006758566.2.
DR   RefSeq; XP_015416047.1; XM_015560561.1.
DR   RefSeq; XP_015416048.1; XM_015560562.1.
DR   RefSeq; XP_015416049.1; XM_015560563.1.
DR   AlphaFoldDB; L5M6L3; -.
DR   GeneID; 102752741; -.
DR   KEGG; myd:102752741; -.
DR   CTD; 57462; -.
DR   eggNOG; KOG1065; Eukaryota.
DR   OrthoDB; 2725689at2759; -.
DR   Proteomes; UP000010556; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd06592; GH31_NET37; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR048395; Glyco_hydro_31_C.
DR   InterPro; IPR000322; Glyco_hydro_31_TIM.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR43053; GLYCOSIDASE FAMILY 31; 1.
DR   PANTHER; PTHR43053:SF7; MYOGENESIS-REGULATING GLYCOSIDASE; 1.
DR   Pfam; PF01055; Glyco_hydro_31_2nd; 2.
DR   Pfam; PF21365; Glyco_hydro_31_3rd; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|RuleBase:RU361185};
KW   Hydrolase {ECO:0000256|RuleBase:RU361185};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010556};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        56..77
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          323..469
FT                   /note="Glycoside hydrolase family 31 TIM barrel"
FT                   /evidence="ECO:0000259|Pfam:PF01055"
FT   DOMAIN          529..615
FT                   /note="Glycoside hydrolase family 31 TIM barrel"
FT                   /evidence="ECO:0000259|Pfam:PF01055"
FT   DOMAIN          630..711
FT                   /note="Glycosyl hydrolase family 31 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21365"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   714 AA;  81124 MW;  B927232DAE6B2CB8 CRC64;
     MPQNLEKSQA YPRRRPGRDT GLKSPEAASA TAMYTFLPDN VSSVKPKATS KEAKPLLGSV
     VLGLLLVLAA VVAWCFYSAS LRKAERLRAE QLDLNLGGFS IRNQKGEQVF RLAFRSGALD
     LDSCSRDGAL LGCSRRADGR PLHFFIQTVR PKDTVMCYRV RWEEEEPGLA VEHAMFLGDE
     AAHWYGGAEM RTQHWPIRLE GQQEPQPFVT SDVYSSDAAF GGILERYWLS SRAAAIKVND
     SVPFHLGWNG TERSLRLQAR YSHTPFKPPA GLPAALELSY RVCVGSDITS IHKYMVRRYF
     NKPSKVPAPE TFRDPIWSTW VLYGREVDQD KVQRFAQQIR QHRFNSSHLE IDDMYTPAYG
     DFDFDEVKFP NASDMFRRLR DAGFQVTLWV HPFVNYNSSS FGEGVERELF VREPSGRLPA
     LVRWWNGIGA VLDFTRPEAR DWFQGHLRRL RSHYEVASFK FDAGEVSYLP RDFSTYRPLP
     DPNIWSRRYT EMALPFFSLA EVRVGYQSQN ISCFFRLVDR DSVWGYDLGL RSLIPAVLTV
     SMLGYPFILP DMVGGNVVPE RTAGGGKVPD RELYVRWLEV AAFMPAMQFS VPPWQYDAEV
     VAIAHKFTAL RASLVAPLLL ELAGEVTDTG DPIVRPLWWI APGDETAHRI DSQFLIGDTL
     LVAPVLEPGK QERDVYLPAG KWRSYKGELF DKTPVLLTDY PVDLDEIAYF IWAS
//