ID D8SD28_SELML Unreviewed; 1061 AA.
AC D8SD28;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Alpha-mannosidase {ECO:0000256|RuleBase:RU361199};
DE EC=3.2.1.- {ECO:0000256|RuleBase:RU361199};
GN ORFNames=SELMODRAFT_154366 {ECO:0000313|EMBL:EFJ17959.1};
OS Selaginella moellendorffii (Spikemoss).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Lycopodiopsida; Selaginellales; Selaginellaceae; Selaginella.
OX NCBI_TaxID=88036 {ECO:0000313|Proteomes:UP000001514};
RN [1] {ECO:0000313|EMBL:EFJ17959.1, ECO:0000313|Proteomes:UP000001514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551031; DOI=10.1126/science.1203810;
RA Banks J.A., Nishiyama T., Hasebe M., Bowman J.L., Gribskov M.,
RA dePamphilis C., Albert V.A., Aono N., Aoyama T., Ambrose B.A., Ashton N.W.,
RA Axtell M.J., Barker E., Barker M.S., Bennetzen J.L., Bonawitz N.D.,
RA Chapple C., Cheng C., Correa L.G., Dacre M., DeBarry J., Dreyer I.,
RA Elias M., Engstrom E.M., Estelle M., Feng L., Finet C., Floyd S.K.,
RA Frommer W.B., Fujita T., Gramzow L., Gutensohn M., Harholt J., Hattori M.,
RA Heyl A., Hirai T., Hiwatashi Y., Ishikawa M., Iwata M., Karol K.G.,
RA Koehler B., Kolukisaoglu U., Kubo M., Kurata T., Lalonde S., Li K., Li Y.,
RA Litt A., Lyons E., Manning G., Maruyama T., Michael T.P., Mikami K.,
RA Miyazaki S., Morinaga S., Murata T., Mueller-Roeber B., Nelson D.R.,
RA Obara M., Oguri Y., Olmstead R.G., Onodera N., Petersen B.L., Pils B.,
RA Prigge M., Rensing S.A., Riano-Pachon D.M., Roberts A.W., Sato Y.,
RA Scheller H.V., Schulz B., Schulz C., Shakirov E.V., Shibagaki N.,
RA Shinohara N., Shippen D.E., Soerensen I., Sotooka R., Sugimoto N.,
RA Sugita M., Sumikawa N., Tanurdzic M., Theissen G., Ulvskov P., Wakazuki S.,
RA Weng J.K., Willats W.W., Wipf D., Wolf P.G., Yang L., Zimmer A.D., Zhu Q.,
RA Mitros T., Hellsten U., Loque D., Otillar R., Salamov A., Schmutz J.,
RA Shapiro H., Lindquist E., Lucas S., Rokhsar D., Grigoriev I.V.;
RT "The Selaginella genome identifies genetic changes associated with the
RT evolution of vascular plants.";
RL Science 332:960-963(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; GL377612; EFJ17959.1; -; Genomic_DNA.
DR RefSeq; XP_002981258.1; XM_002981212.1.
DR AlphaFoldDB; D8SD28; -.
DR STRING; 88036.D8SD28; -.
DR EnsemblPlants; EFJ17959; EFJ17959; SELMODRAFT_154366.
DR GeneID; 9658305; -.
DR Gramene; EFJ17959; EFJ17959; SELMODRAFT_154366.
DR KEGG; smo:SELMODRAFT_154366; -.
DR eggNOG; KOG1958; Eukaryota.
DR HOGENOM; CLU_004690_1_0_1; -.
DR InParanoid; D8SD28; -.
DR OMA; WRQNWDM; -.
DR OrthoDB; 5474711at2759; -.
DR Proteomes; UP000001514; Unassembled WGS sequence.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0004559; F:alpha-mannosidase activity; IBA:GO_Central.
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 GO; GO:0006491; P:N-glycan processing; IBA:GO_Central.
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 Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU361199};
KW Reference proteome {ECO:0000313|Proteomes:UP000001514};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361199}.
FT DOMAIN 385..470
FT /note="Glycoside hydrolase family 38 central"
FT /evidence="ECO:0000259|SMART:SM00872"
SQ SEQUENCE 1061 AA; 119183 MW; 5E273981FD2292C5 CRC64;
MDISTKELYD AIAFENKDGG AWTQGWAVKY RGDEWNREKL KVFVVPHSHN DPGWLRTVEE
YYQERTKHIL STVVGALRKD PRRKFIWEEM SYLHRWWQDA SDSEKQDFIR LVKSGQLEVV
GGGWVMNDEA NSHHFAIIEQ ITAGNLWLRD TIGVTPRNAW AIDPFGHSAT MAYLLRRMGF
ANMLIQRTHY EVKKELAQRQ SLEFMWRQGW DSANSTAIFC HMMPFYSYDI PHTCGPEPAV
CCQFDYWRLV RVGQAQRCPW GYNPEEINEG NVRERAMLLL DQYRKKSTLY RSNTLLVPLG
DDFRYVTPQE AELQFTNYQV IFDYISAHPE LKASVQFGTL EDYFSTLRDE VARSTKSSSR
ANEDEVPGFP SLSGDFFTYA DRMHDYWSGY YVSRPFYKAV DRVLEHTLRA ANILYVFTHA
KCRPKDTSSF PASYSNAIVS ASQNLALFQH HDGVTGTARD HVVEDYGTRM HTSLVELQAF
MAASVEALLL QQQCKSENFR QWYEPEESRS KFNMLAVKKS VRLASGQARR VVFFNPLEEA
VEHVVMVVVD DPAVCVFGPS WASVDSQISP EWDETGSNLS TGRHRLHWTA LVPALGLATF
FVSSAEGVAD GSSCKRAVPA RIRVFNSDDK FSCPNGYSCS LETVETLEIT NGFQTLGFDS
TTGMLRSIQI SKAASPSTLV AVEEDVAYYS SAGSGAYLFL PDGEAKSLVQ AGGLVLVTEG
RAMQEVHVVL KTSIGGGELS RSARLYHSGA TGRKSVQALS VEINYHVALL DHRFNNKEII
ARFKTGIDSG RVFHSDLNGF QTIRRETYDK IPLQGNYYPM PSLAFVQDSR GKRFSVHSRQ
ALGVASLQTG WLEVMLDRRL TQDDGRGLGQ GVMDNRPLNI VFQLLLEENV TSSASFHQKL
SVPSLLSHRV GAQLNYPMHA FLGKIVESSV VIQETSMDTQ WSSLASAFPC DLHLVGIKAL
RPSQLEDVEY GLLLQRRGWD ESYCRKGGTD SCSTLATSAK VDLHSTFSNL VVSKVTPSSL
NFLHDHAETL PGRKGAGASA AGIGIVEMSP MEIQAYKLMV E
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