ID D8SMM2_SELML Unreviewed; 1041 AA.
AC D8SMM2;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Alpha-mannosidase {ECO:0000256|RuleBase:RU361199};
DE EC=3.2.1.- {ECO:0000256|RuleBase:RU361199};
GN ORFNames=SELMODRAFT_120549 {ECO:0000313|EMBL:EFJ14298.1};
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:EFJ14298.1, 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GL377628; EFJ14298.1; -; Genomic_DNA.
DR RefSeq; XP_002984653.1; XM_002984607.1.
DR AlphaFoldDB; D8SMM2; -.
DR STRING; 88036.D8SMM2; -.
DR EnsemblPlants; EFJ14298; EFJ14298; SELMODRAFT_120549.
DR Gramene; EFJ14298; EFJ14298; SELMODRAFT_120549.
DR KEGG; smo:SELMODRAFT_120549; -.
DR eggNOG; KOG1959; Eukaryota.
DR HOGENOM; CLU_004690_2_0_1; -.
DR InParanoid; D8SMM2; -.
DR OMA; LEFIWRP; -.
DR Proteomes; UP000001514; Unassembled WGS sequence.
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 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};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU361199};
KW Reference proteome {ECO:0000313|Proteomes:UP000001514};
KW Signal {ECO:0000256|RuleBase:RU361199};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361199}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|RuleBase:RU361199"
FT CHAIN 28..1041
FT /note="Alpha-mannosidase"
FT /evidence="ECO:0000256|RuleBase:RU361199"
FT /id="PRO_5017850456"
FT DOMAIN 373..447
FT /note="Glycoside hydrolase family 38 central"
FT /evidence="ECO:0000259|SMART:SM00872"
SQ SEQUENCE 1041 AA; 117191 MW; 043E527BA0490469 CRC64;
MAIGARAARR CAAALLLLFV LTLLRDAARL DRFLGRSPPL LPLAPGIYNT SGGPLPHKIN
VHIVPHTHDD VGWLKTVDQY YVGSNNSIQI AAVQYIIDSV IQSLEDNPDR KFIYAFFQRW
WREQTPAKQK IVHRMVESGQ LEFVNGAWCM HDEAGASYID MIDQTTLGHR FIKSQFNKMP
RIGWQIDPFG HSAVQAYLLG AEVGFDGLFF ARADYQDIAK RRATRGMEFV WQGSRTLSSS
SQIFGGILAN HYSPPEGMNF DFKSNDPLIQ DNPLLYDYNL QERIDLFDTC IYFQSEQFRS
NHIMWTMGQD FNYEQANTWF KQLDKLVHYM NKDGRINVFY STPSIYVDSK NAANITWPLK
TEDFFPYANC SHCYWTGYFS SRLALKGYVR RLSAYLMAAR QLEFVVGRNF SADNTDSLED
ALAILQHHDA VTGTEQQHVA NDYAKRLATG ASKVLILLTS SKYLSVLPKG ISGRSALSFD
QCLLLNISYC PPSEAKLEDG TSLVVVLYNT LGWSRKEMVR IPVSSTRLQV RDSTGNAIPS
QLIPLDSVTR KLKEIYVKAY TGNSSSNDDV YTLVFKASVP PLGFNSYFIS ASNGTHGKLI
SFGWTTRCKS VYVGCASLSS FKNHESPREV SSSKTKLKFS SSGQLQQFTD RKSGIVSAVK
LSYCWYNSSD GVTEEARGQS SGAYVFRPNS SSCYPVDSKE MVSSYIKGSL VEEVHQTFSS
WVFQVLRLYK DAQYAEIEYT IGPVPVNSSD AGKEIVTRIS TDLESEKIFY TDSNGRDFLK
RVRDFRSDWE LNVTEPISGN YYPINLGIYL QQDNTEFSVL VDRAIGGSSL KDGDIELMVQ
RRLLHDDHRG VQEALNETIC IDSNECEGLT VRGKFLLGLH STQESARWRR NQGQRLYSPL
EMFFSKLSSS TGKIGNPTFS ATESGYELPQ NIAIITLQEL ENGDVLLRLA HLYEAGEDIE
LSTVVRVDLQ KIFGLRQVAS VVELNLSANQ ERASMKPLQW QLDPNVEDAA AVHVRGPLLK
PSDRHIDIAP MEIRTLLVTF G
//
