ID A0A2Y9QWL1_TRIMA Unreviewed; 1014 AA.
AC A0A2Y9QWL1;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Alpha-mannosidase {ECO:0000256|RuleBase:RU361199};
DE EC=3.2.1.- {ECO:0000256|RuleBase:RU361199};
GN Name=LOC101344297 {ECO:0000313|RefSeq:XP_023587755.1};
OS Trichechus manatus latirostris (Florida manatee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Sirenia; Trichechidae; Trichechus.
OX NCBI_TaxID=127582 {ECO:0000313|Proteomes:UP000248480, ECO:0000313|RefSeq:XP_023587755.1};
RN [1] {ECO:0000313|RefSeq:XP_023587755.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 RefSeq; XP_023587755.1; XM_023731987.1.
DR AlphaFoldDB; A0A2Y9QWL1; -.
DR Proteomes; UP000248480; Unplaced.
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 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; 1.
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 Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU361199};
KW Reference proteome {ECO:0000313|Proteomes:UP000248480};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361199}.
FT DOMAIN 372..458
FT /note="Glycoside hydrolase family 38 central"
FT /evidence="ECO:0000259|SMART:SM00872"
SQ SEQUENCE 1014 AA; 116862 MW; 9711089C78EF90A3 CRC64;
MLDVYSLIPF DNPDGGVWKQ GFDITYKSYE WDTEPLQVFV VPHSHNDPGW LKTFDDYFRD
KTQYIFNNMV VKLKEDSRRK FMWSEISYLS KWWDVIDTQK KDAVKSLLEN GQFEIVTGGW
VMPDEAGPHY FALIDQLIEG HQWLEKNLGV KPQSGWSIDP FGHSPTMAYL LKRAGFSHML
IQRVHYAVKK HFALHKTLEF FWRQNWDMGS VTDIFCHMMP FYSYDIPHTC GPDPKICCQF
DFKRLPGGRV GCPWGIPPET IYLGNVQNRA QMLLDQYRKK SKLFRTKVVL APLGDDFRYS
ERTEWDQQFK NYQLLFDYMN SQPQLNVKIQ FGTLSDYFDA LDKADKNSGK SSQSVFPVLS
GDFFTYADRD DHYWSGYFTS RPFYKRMDRV MESHLRTAEI LYYFALRKAQ KYKISKFLSS
SHYTALSEAR RNLGLFQHHD AITGTAKDWV VVDYGTRLFH SLMNLKKIIG DSALLLILKD
KHTYDSYSSN NFLEMDLEQK SQDSLPQKNI IRLSAEPRYL VIYNPSEQDQ NSVVSVYVSS
PTVQVSSATG IPVEIQVSAV WDTADAISQT AYEISFLAHI PPLGLKVYKI LESASSKSFL
ADYVLYNGKT EVKGIFNIKN IKSAEEGIML ENSFIKLRFG QYGLMQEMMN KEDGKHHVVK
LEFSWYGTSN KKDKSGAYLF LPDREARLYG YTTLPFVRVM RGRIYSEVTS FFDHITHRVR
LYNIQGVEGQ SVEISNIVDI RKEYNREIAM RISSDINSQN RFYTDLNGYQ IQPRVTMSKL
PLQANVYPMT TMAYIQDAEH RLTLLSAQSL GVSSLKSGQI EVIMDRRLMQ DDNRGLGQGV
HDNKITANLF RILLEKRSVT NLEEEKKSVS YPSLLSHITS SFLNHPVFPM IEKVSSPTPQ
LLGEFSPLMS SLPCDIHLVN LRTIQSKVGH GHSDEAAFIL HRKGFDCQFP SRDTGLLCST
TQGKILVQKL FNKFTVESLT PSSLSLMHSP PDARNISEIN LSPMEISTFR IRLR
//