ID A0A0D2QW38_GOSRA Unreviewed; 1167 AA.
AC A0A0D2QW38;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Alpha-mannosidase {ECO:0000256|RuleBase:RU361199};
DE EC=3.2.1.- {ECO:0000256|RuleBase:RU361199};
GN ORFNames=B456_001G258600 {ECO:0000313|EMBL:KJB11430.1};
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:KJB11430.1, ECO:0000313|Proteomes:UP000032304};
RN [1] {ECO:0000313|EMBL:KJB11430.1, 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; CM001740; KJB11430.1; -; Genomic_DNA.
DR RefSeq; XP_012443723.1; XM_012588269.1.
DR AlphaFoldDB; A0A0D2QW38; -.
DR STRING; 29730.A0A0D2QW38; -.
DR EnsemblPlants; KJB11430; KJB11430; B456_001G258600.
DR GeneID; 105768375; -.
DR Gramene; KJB11430; KJB11430; B456_001G258600.
DR KEGG; gra:105768375; -.
DR eggNOG; KOG1958; Eukaryota.
DR OrthoDB; 5474711at2759; -.
DR Proteomes; UP000032304; Chromosome 1.
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; cd10809; GH38N_AMII_GMII_SfManIII_like; 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: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 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:UP000032304};
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 46..76
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 499..584
FT /note="Glycoside hydrolase family 38 central"
FT /evidence="ECO:0000259|SMART:SM00872"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1167 AA; 133878 MW; D903855256BEDD4F CRC64;
MSLSSYLGSN TRRGGGWAQS LLPSSSPTVK STLKVHPTRK SRKRTVLINF LLTNFFTIAL
SLSFIFFILT LFFFGIPKPI SSHLQPPSST RRLTTRKPVT RKQPWLNPNQ TGAAVDITTK
DLYDKIEFLD KPGGAWTQGW KVSYKGDEWD SEKLKIFVVP HSHNDPGWKF TVEEYYQRQS
RLILDTVVHT LSKDRRRKFI WEEMSYLERW WRDASEDKRE TFTNLVKNGQ LEIVGGGWVM
NDEANSHYFA IIEQITEGNM WLNDTIGFVP KNSWAIDPFG YSPTMAYLFR RMGFENMLIQ
RTHYELKKEL AWNKNLEYVW RQSWDANETT DIFVHMMPFY SYDIPHTCGP EPAICCQFDF
ARSHGFSYEL CPWGQYPVET NPENVQERAL KLLDQYRKKS TLYRTNTLLV PLGDDFRYVT
AEEAEAQFRN YQMIFDYINS TPSLNAEAKF GTLDDYFQTL REEADRINYS VPREIGSGQI
SGFPSLSGDF FTYADRQKDY WSGYYVSRPF FKAVDRVLEQ TLRASEMLMA FLLGHCQRPQ
CEKLPMRYAY KLTAARRNLA LFQHHDGVTG TAKDHVVLDY GTRMHTSLQD LQIFMSKAIE
VLLGIRQEKY DQTPALFDPE QVRSKYDALP MHRAISARKG TVQSVVLFNP LEQTREEVVM
VVVSRPDVSV LDSNWTCVQS QVSPELQHDE SKIFTGRHRI HWKASIPAMG LQTYYIANGF
AGCEKAKPAK LKFSSKLSSG PCLAPYACSK VEGDTVEIVN RHQVLTFDVK HGLLQKVIHK
NGLQNVVVEE IALYSSSGGA YLFLPDGDAQ PIIKSGGNLV ISEGPLMQEV YSYPKTSWEK
TPVSHSTRIY NGGNTVQDFL IEKEYHVELL GKDFNDRELI VRYKTDTNNK RIFYSDLNGF
QMSRRETYDK IPLQGNYYPM PSLAFMQGSN GQRFSVHSRQ ALGAASLKEG WLEIMLDRRL
VRDDGRGLGQ GVMDNHVMNV VFHILMESNI SSTSDPVSNP LPLSPSLLSH RVNAQLNYPL
HAFIAKKPQE ISAPTHSRSF SPLAAPLPCD LHIVSFKVPR PSKYSQQQQQ LVDPRLVLML
HRRNWDSSYC KKARSQCTAV ADESVNLFNM FKDLTVLNAR ATSLNLLHDD TEMLGYTEQF
GDVARDGRVI IPPMEIQAYK FELRPRQ
//
