ID A0A0D2NJH7_GOSRA Unreviewed; 1022 AA.
AC A0A0D2NJH7;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Alpha-mannosidase {ECO:0000256|RuleBase:RU361199};
DE EC=3.2.1.- {ECO:0000256|RuleBase:RU361199};
GN ORFNames=B456_006G000300 {ECO:0000313|EMBL:KJB33197.1};
OS Gossypium raimondii (New World cotton).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=29730 {ECO:0000313|EMBL:KJB33197.1, ECO:0000313|Proteomes:UP000032304};
RN [1] {ECO:0000313|EMBL:KJB33197.1, ECO:0000313|Proteomes:UP000032304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23257886; DOI=10.1038/nature11798;
RA Paterson A.H., Wendel J.F., Gundlach H., Guo H., Jenkins J., Jin D.,
RA Llewellyn D., Showmaker K.C., Shu S., Udall J., Yoo M.J., Byers R.,
RA Chen W., Doron-Faigenboim A., Duke M.V., Gong L., Grimwood J., Grover C.,
RA Grupp K., Hu G., Lee T.H., Li J., Lin L., Liu T., Marler B.S., Page J.T.,
RA Roberts A.W., Romanel E., Sanders W.S., Szadkowski E., Tan X., Tang H.,
RA Xu C., Wang J., Wang Z., Zhang D., Zhang L., Ashrafi H., Bedon F.,
RA Bowers J.E., Brubaker C.L., Chee P.W., Das S., Gingle A.R., Haigler C.H.,
RA Harker D., Hoffmann L.V., Hovav R., Jones D.C., Lemke C., Mansoor S.,
RA ur Rahman M., Rainville L.N., Rambani A., Reddy U.K., Rong J.K.,
RA Saranga Y., Scheffler B.E., Scheffler J.A., Stelly D.M., Triplett B.A.,
RA Van Deynze A., Vaslin M.F., Waghmare V.N., Walford S.A., Wright R.J.,
RA Zaki E.A., Zhang T., Dennis E.S., Mayer K.F., Peterson D.G., Rokhsar D.S.,
RA Wang X., Schmutz J.;
RT "Repeated polyploidization of Gossypium genomes and the evolution of
RT spinnable cotton fibres.";
RL Nature 492:423-427(2012).
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; CM001745; KJB33197.1; -; Genomic_DNA.
DR RefSeq; XP_012483332.1; XM_012627878.1.
DR AlphaFoldDB; A0A0D2NJH7; -.
DR STRING; 29730.A0A0D2NJH7; -.
DR EnsemblPlants; KJB33197; KJB33197; B456_006G000300.
DR GeneID; 105798011; -.
DR Gramene; KJB33197; KJB33197; B456_006G000300.
DR KEGG; gra:105798011; -.
DR eggNOG; KOG1959; Eukaryota.
DR OMA; LVEIEWQ; -.
DR OrthoDB; 5474711at2759; -.
DR Proteomes; UP000032304; Chromosome 6.
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:SF60; 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};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU361199};
KW Reference proteome {ECO:0000313|Proteomes:UP000032304};
KW Signal {ECO:0000256|RuleBase:RU361199};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361199}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|RuleBase:RU361199"
FT CHAIN 25..1022
FT /note="Alpha-mannosidase"
FT /evidence="ECO:0000256|RuleBase:RU361199"
FT /id="PRO_5017849569"
FT DOMAIN 360..434
FT /note="Glycoside hydrolase family 38 central"
FT /evidence="ECO:0000259|SMART:SM00872"
SQ SEQUENCE 1022 AA; 114826 MW; 56BA92035E285F5E CRC64;
MPMAMMPMAI ILLVAILLAG GVSSAESSYI EYNTTQRIVP GKINVHLVPH SHDDVGWLKT
VDQYYFGGNN SIRGACVQNV LDSVISALFD DKNRKFIYVE MAFFQRWWRQ QSNAKKIKVK
ELVNSGQLEF INGGMCMHDE ATPHYIDLID QTTLGHKYIK DEFNQIPRVG WQIDPFGHSA
VQAYLLGAEL GFDSLFFARI DYQDRAKRLK EKTLEVVWQG SKSLGSSSQI FTGIFPRHYD
PPDGFTFEIN DVSPPIQDDV LLFDYNVQER VNDFIAAALA QANVTRTNHI MWAMGTDFRY
QYANSWFRQM DKFIHYVNQD GRINALYSTP SIYTDAKYAE NVQWPLKTDD FFPYADKPNA
YWTGYFTSRP AFKGYVRVLS AYYLAARQLE FFKGRSASGP NTEALADALA IAQHHDAVSG
TERQHVAADY ALRLSIGYKE AEKVVASSLA FLADSRSSTE QKNSVTSFQQ CPLLNISFCP
PSEAALSSGK SLVIIIYNSL GWKREETIRI PVSSERVVVK DSEGREIESQ LIPLSNSTLR
IRSQYIKAYL GKKPREIAKY WVAFSVSVPP LGFSTYIVAT TKETEGRSPT ISTMNTYEAS
ENNTIEVGQG SLKLLYSADE GKLTRYVNTR NSVTAFAEQS YGYYSGNDGT DKDPQASGAY
VFRPNGTFSI KSENQTPLTV VRGPLLDEVH QQLNSWISQV TRVYKGKEHA EVEFSIGPIP
VNDGIGKEII TQITTTMRTN KTFYTDSNGR DFIKRIQDFR KDWDLQVNQP IAGNYYPVNL
GIYVQDDSTE LSVLVDRSVG ASSLADGQIE LMLHRRLIHD DIRGVGEVLN ETVCVSEGCD
GLTILGKFYL RIDHIGEGAK WRRTVGQEIY SPLLLAFSEQ DGNDWMSSHI PTFSGIDPSY
SLPDNIAIIT LQELENGKVL LRLAHLFETG EDKEYSVMAS VELKKLFPNK KIKKVTEMSL
SANQERGEME KRRLAWKVEG GGGESKVVRG GAVDPAKLLV ELAPMEIRTF LIDVDYIQMV
GG
//
