ID S7PIW1_MYOBR Unreviewed; 1144 AA.
AC S7PIW1;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Alpha-mannosidase {ECO:0000256|RuleBase:RU361199};
DE EC=3.2.1.- {ECO:0000256|RuleBase:RU361199};
GN ORFNames=D623_10033135 {ECO:0000313|EMBL:EPQ07912.1};
OS Myotis brandtii (Brandt's bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=109478 {ECO:0000313|EMBL:EPQ07912.1, ECO:0000313|Proteomes:UP000052978};
RN [1] {ECO:0000313|Proteomes:UP000052978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23962925; DOI=10.1038/ncomms3212;
RA Seim I., Fang X., Xiong Z., Lobanov A.V., Huang Z., Ma S., Feng Y.,
RA Turanov A.A., Zhu Y., Lenz T.L., Gerashchenko M.V., Fan D., Hee Yim S.,
RA Yao X., Jordan D., Xiong Y., Ma Y., Lyapunov A.N., Chen G., Kulakova O.I.,
RA Sun Y., Lee S.G., Bronson R.T., Moskalev A.A., Sunyaev S.R., Zhang G.,
RA Krogh A., Wang J., Gladyshev V.N.;
RT "Genome analysis reveals insights into physiology and longevity of the
RT Brandt's bat Myotis brandtii.";
RL Nat. Commun. 4:2212-2212(2013).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU361199};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|RuleBase:RU361199};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family.
CC {ECO:0000256|ARBA:ARBA00009792, ECO:0000256|RuleBase:RU361199}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KE162363; EPQ07912.1; -; Genomic_DNA.
DR RefSeq; XP_005866509.1; XM_005866447.2.
DR AlphaFoldDB; S7PIW1; -.
DR GeneID; 102241544; -.
DR KEGG; myb:102241544; -.
DR CTD; 4124; -.
DR eggNOG; KOG1958; Eukaryota.
DR OrthoDB; 5474711at2759; -.
DR Proteomes; UP000052978; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; cd11666; GH38N_Man2A1; 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; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
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; IPR013780; Glyco_hydro_b.
DR PANTHER; PTHR11607; ALPHA-MANNOSIDASE; 1.
DR PANTHER; PTHR11607:SF70; ALPHA-MANNOSIDASE 2; 1.
DR Pfam; PF09261; Alpha-mann_mid; 1.
DR Pfam; PF07748; Glyco_hydro_38C; 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 Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361199};
KW Hydrolase {ECO:0000256|RuleBase:RU361199};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU361199};
KW Reference proteome {ECO:0000313|Proteomes:UP000052978};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361199}.
FT TRANSMEM 7..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 503..589
FT /note="Glycoside hydrolase family 38 central"
FT /evidence="ECO:0000259|SMART:SM00872"
SQ SEQUENCE 1144 AA; 131264 MW; 21671D2396084573 CRC64;
MKLSRQFTVF GSAIFCVVIF SLYLMLDRGH LDYPKGQRRE GSFPQGQLSM LQEKIDHLEH
LLAENNEIIS NIRDSVINLS ESVEDGPKSS QGNFSQRAGS PFLPSKKLSL TVDPEDCLFA
SQSGSQNADV QMLDVYSLIP FDNPDGGVWK QGFDITYKLN DWDTKPLQVF VVPHSHNDPG
WLKTFDDYFR EKTQYIFNNM VIKLKEDSRR KFIWSEISYL SKWWDTIDIQ KKDAVKSLLE
NGQFEIVTGG WVMPDEAAAH YFAIIDQLIE GHQWLEKNLG VKPRSGWAID PFGHSPTMAY
LLKRAGFSHM LIQRVHYAVK KHFALHKTLE FFWRQNWDLG SVTDIFCHMM PFYSYDIPHT
CGPDPKICCQ FDFKRLPGGR FGCPWGVPPE TINLGNVQNR AEMLLDQYRK KSKLFRTTVL
LAPLGDDFRY VERTEWDHQF KNYQMLFDYM NSQPRYNVKI QFGTLSDYFD ALDKEDATSR
MNSQSLFPVL SGDFFTYADR DDHYWSGYFT SRPFYKRMDR ILESHLRAAE ILYYFALKQA
QKFKISAFLS SSSYTALTEA RRNVGLFQHH DAITGTAKDW VVVDYGTRLF HSLMNLKKII
GSSTLLLLLK DKHSYESYSF DTLLDMDLKQ KSQGSLPQKN IIKLSAEPRY LVVYNPSEQE
RTSLVSVCVS SPTVKVSSAS GKPVKIQMSA VWNTATTISQ TAYEISFLAQ MPPLGLQVYT
LLESSSSYPH VAEYVLYNGN IENKGIFNVK NMKNAEEITL ENSFIKLQFG QSGLMEEMIN
KEDGEPHKVK VQFSWYGTTS KKDKSGAYLF LPDGEAKPYV YTTQPLVRVQ RGRFYSDVTC
FFEHVTHSVR LYNIQGIEGQ SVEVSNIVDI RKEYNREIAM RISSNINSQN RFYTDLNGYQ
IQPRMTMNKL PLQANVYPMT TMAYIQDAQH RLTLLSAQSL GVSSLESGQI EVIMDRRLMQ
DDNRGLEQGV HDNKITANLF RILLEKRTVV NMEEEKKAVS YPSLLSHITS SFLNHPVFTM
TEKSPVPTLQ LLGEFSPLLS SLPCDIHLLN LRTIQSKVDG KQSDEAALIL HRKGFDCRFS
SRDTGLLCST TQGKILIQKL FNKFTVANLV PSSLSLMHSP PDIRNISEIN LRPMEISTFR
IQLR
//
