ID A0A061FYP2_THECC Unreviewed; 988 AA.
AC A0A061FYP2;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Alpha-mannosidase {ECO:0000256|RuleBase:RU361199};
DE EC=3.2.1.- {ECO:0000256|RuleBase:RU361199};
GN ORFNames=TCM_014749 {ECO:0000313|EMBL:EOY22635.1};
OS Theobroma cacao (Cacao) (Cocoa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Byttnerioideae; Theobroma.
OX NCBI_TaxID=3641 {ECO:0000313|EMBL:EOY22635.1, ECO:0000313|Proteomes:UP000026915};
RN [1] {ECO:0000313|EMBL:EOY22635.1, ECO:0000313|Proteomes:UP000026915}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Matina 1-6 {ECO:0000313|Proteomes:UP000026915};
RX PubMed=23731509; DOI=10.1186/gb-2013-14-6-r53;
RA Motamayor J.C., Mockaitis K., Schmutz J., Haiminen N., Iii D.L.,
RA Cornejo O., Findley S.D., Zheng P., Utro F., Royaert S., Saski C.,
RA Jenkins J., Podicheti R., Zhao M., Scheffler B.E., Stack J.C., Feltus F.A.,
RA Mustiga G.M., Amores F., Phillips W., Marelli J.P., May G.D., Shapiro H.,
RA Ma J., Bustamante C.D., Schnell R.J., Main D., Gilbert D., Parida L.,
RA Kuhn D.N.;
RT "The genome sequence of the most widely cultivated cacao type and its use
RT to identify candidate genes regulating pod color.";
RL Genome Biol. 14:R53.1-R53.24(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}.
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DR EMBL; CM001881; EOY22635.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A061FYP2; -.
DR EnsemblPlants; EOY22635; EOY22635; TCM_014749.
DR Gramene; EOY22635; EOY22635; TCM_014749.
DR Proteomes; UP000026915; Chromosome 3.
DR GO; GO:0004559; F:alpha-mannosidase activity; IEA:UniProtKB-EC.
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; cd10810; GH38N_AMII_LAM_like; 1.
DR Gene3D; 2.60.40.1360; -; 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; 2.
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:SF3; LYSOSOMAL ALPHA-MANNOSIDASE; 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, ECO:0000313|EMBL:EOY22635.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU361199};
KW Reference proteome {ECO:0000313|Proteomes:UP000026915};
KW Signal {ECO:0000256|RuleBase:RU361199};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361199}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|RuleBase:RU361199"
FT CHAIN 22..988
FT /note="Alpha-mannosidase"
FT /evidence="ECO:0000256|RuleBase:RU361199"
FT /id="PRO_5017854567"
FT DOMAIN 354..428
FT /note="Glycoside hydrolase family 38 central"
FT /evidence="ECO:0000259|SMART:SM00872"
SQ SEQUENCE 988 AA; 111474 MW; 27408AC3AC04AAEA CRC64;
MAIGAWILIA LMCVFWCEVE SKYMVYNTTS KIAPGKLNVH LVAHTHDDVG WLKTVDQYYV
GSNNSIQGAC VQNVLDSIVP ALLADKNRKF IYVEQAFFQR WWRDQSEAVQ ETVKQLINSG
QLELINGGMC MHDEAATHYI DMIDQTTLGH RFIKSEFNVT PRIGWQIDPF GHSAVQAYLL
SAEVGFDSLF FARIDYQDRA KRKDEKSLEV VWRGSKSLGS SSQIFAGVFP ENYDPPSNFN
YEVNDDSPIV QDNMELFDYN VPERVNEFVA AALSQANITR TNHVMWTMGT DFKYQYAHTW
FRQMDKFIHY VNQDGRVNAL YSTPSIYTDA KYATNKAWPL KTDDYFPYAD RINAYWTGYF
TSRPALKGYV RTMSSYYLAA RQLEFFKGRS KVGPNTDSLA DALAIAQHHD AVSGTSKQHV
ADDYAKRLSI GYEETAKVVE SSLASMTRSS SKADSGSPVT EFHQCLLLNI SYCPPSEVDL
SNGKNLVVVV YNPLGWKRED VIRIPVIDEN VIVKDSGGKE IESQLLPLQN ASLAIRNYYS
VAYLGKFPSA TPKYWLAFSA SAPPIGFNTY FISRGKRPVI ATASKSHVVY SSEEKRSDVI
EVGPGDVKLV YSKNQGKLIR YINSRTMVKE SVRQSYSFYS GDDGSVDEQA SGAYIFRPNH
TYHTRSDGQA SFTVLRGPLL DEVHQRINSW IYQITRVYKG KEYAEFEFTV GPIPIDDGIG
KEVVTQISTH MKTNKTFYTD SSGRDFIERI DLGLYIKDDS KELSVLVDRS VGGASIKDGQ
LELMLHRRLL HDDNRGVAEA LNETVCVQNK CSGLTIVGKY YLRIDPLGEA AKWRRSFGQE
IYSPFLLAFT EQDGDEWANS RILSFSGMDP SYVLPDNVAM ITLQELDDGK VLLRLAHLYE
IGEDKDLSVM ASVQVKKVFA HKKINEVTEM SLSANQGRAE MEKKRLVWKV EGSSGESPKV
VRGGPVDPSI LVVELAPMEI RTFVIEFH
//