ID G7MVI7_MACMU Unreviewed; 1106 AA.
AC G7MVI7;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Alpha-mannosidase {ECO:0000256|RuleBase:RU361199};
DE EC=3.2.1.- {ECO:0000256|RuleBase:RU361199};
GN ORFNames=EGK_16741 {ECO:0000313|EMBL:EHH26697.1};
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544 {ECO:0000313|EMBL:EHH26697.1};
RN [1] {ECO:0000313|EMBL:EHH26697.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CR-5 {ECO:0000313|EMBL:EHH26697.1};
RX PubMed=22002653; DOI=10.1038/nbt.1992;
RA Yan G., Zhang G., Fang X., Zhang Y., Li C., Ling F., Cooper D.N., Li Q.,
RA Li Y., van Gool A.J., Du H., Chen J., Chen R., Zhang P., Huang Z.,
RA Thompson J.R., Meng Y., Bai Y., Wang J., Zhuo M., Wang T., Huang Y.,
RA Wei L., Li J., Wang Z., Hu H., Yang P., Le L., Stenson P.D., Li B., Liu X.,
RA Ball E.V., An N., Huang Q., Zhang Y., Fan W., Zhang X., Li Y., Wang W.,
RA Katze M.G., Su B., Nielsen R., Yang H., Wang J., Wang X., Wang J.;
RT "Genome sequencing and comparison of two nonhuman primate animal models,
RT the cynomolgus and Chinese rhesus macaques.";
RL Nat. Biotechnol. 29:1019-1023(2011).
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}.
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DR EMBL; CM001258; EHH26697.1; -; Genomic_DNA.
DR Proteomes; UP000013456; Chromosome 6.
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 InterPro; IPR048534; Man2a1-like_dom.
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; 2.
DR Pfam; PF01074; Glyco_hydro_38N; 1.
DR Pfam; PF21260; Laman-like_dom; 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 Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
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}; 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 502..588
FT /note="Glycoside hydrolase family 38 central"
FT /evidence="ECO:0000259|SMART:SM00872"
SQ SEQUENCE 1106 AA; 127058 MW; 3987EA1646E2DFA8 CRC64;
MKLSRQFTVF GSAIFCVVIF SLYLMLDRGH LDYPRNPRRE GSFPQGQLSM LQEKIDHLER
LLAENNEIIS NIRDSVINLS ESVEDGPKSS QSNFSQGAGS RLLPSQLSLS VDTADCLFAS
QSGSHNSDVQ MLDVYSLISF DNPDGGVWKQ GFDITYESNE WDTEPLQVFV VPHSHNDPGW
LKTFNDYFRD KTQYIFNNMV LKLKEDSRRK FIWSEISYLS KWWDIIDIQK KDAVKSLIEN
GQLEIVTGGW VMPDEATAHY FALIDQLIEG HQWLENNIGV KPRSGWAIDP FGHSPTMAYL
LNRAELSHML IQRVHYAVKK HFAQHKTLEF FWRQNWDLGS VTDILCHMMP FYSYDIPHTC
GPDPKICCQF DFKRLPGGRF GCPWGVPPET IHPGNVQSRA QMLLDQYRKK SKLFRTKVLL
APLGDDFRYC EYTEWDLQFK NYQQLFDYMN SQSKFKVKIQ FGTLSDFFDA LDKADETQRD
KGQSMFPVLS GDFFTYADRD DHYWSGYFTS RPFYKRMDRI MESHLRAAEI LYYFALRQAH
KYKINKFLSS SLYTALTEAR RNLGLFQHHD AITGTAKDWV VVDYGTRLFH SLMVLEKIIG
TSAFFLILKD KLTYDSYSSD TFLEMDLKQK SQDSLPQKNI IRLSAEPRYL VVYNPLEQDR
ISVVSVYVSS PTVQVFSASG KPVEVQVSAV WDTANTISET AYEISFRAHI PPLGLKVYKI
LESASSNSHL ADYVLYNNKV EDRGIFTIKN MINTEEGITL ENSFVLLRFD QTGLMKQMMT
KEDGKHHEVS VQFSWYGTTI KRDKSGAYLF LPDGNAKPYV YTTPPFVRVT HGRIYSEVTC
FFDHVTHRVR LYHIQXXXXX YQIQPRMTLS KLPLQANVYP MTTMAYIQDA KHRLTLLSAQ
SLGVSSLNSG QIEVIMDRRL MQDDNRGLEQ GVQDNKITAN LFRILLEKRS AVNTEEEKNS
VSYPSLLSHI TSSFMNHPVF PMTNKFSSPN LDLQGEFSPL QSSLPCDIHL VNLRTIQSKV
GSGHSNEAAL ILHRKGFDCR FSSKGTGLFC STTQGKMLVQ KLFNKFIVES LTLSSLSLMH
SPPGTQNISE INLSPMEIST YRIRLR
//
