ID D8RWH1_SELML Unreviewed; 989 AA.
AC D8RWH1;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Alpha-mannosidase {ECO:0000256|RuleBase:RU361199};
DE EC=3.2.1.- {ECO:0000256|RuleBase:RU361199};
GN ORFNames=SELMODRAFT_103066 {ECO:0000313|EMBL:EFJ23549.1};
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:EFJ23549.1, 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; GL377592; EFJ23549.1; -; Genomic_DNA.
DR RefSeq; XP_002975348.1; XM_002975302.1.
DR AlphaFoldDB; D8RWH1; -.
DR STRING; 88036.D8RWH1; -.
DR EnsemblPlants; EFJ23549; EFJ23549; SELMODRAFT_103066.
DR Gramene; EFJ23549; EFJ23549; SELMODRAFT_103066.
DR KEGG; smo:SELMODRAFT_103066; -.
DR eggNOG; KOG1959; Eukaryota.
DR HOGENOM; CLU_004690_2_0_1; -.
DR InParanoid; D8RWH1; -.
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..22
FT /evidence="ECO:0000256|RuleBase:RU361199"
FT CHAIN 23..989
FT /note="Alpha-mannosidase"
FT /evidence="ECO:0000256|RuleBase:RU361199"
FT /id="PRO_5017853131"
FT DOMAIN 354..429
FT /note="Glycoside hydrolase family 38 central"
FT /evidence="ECO:0000259|SMART:SM00872"
SQ SEQUENCE 989 AA; 110036 MW; E7F5BC6C7C8E49F0 CRC64;
MAGGRSLLTI LVFLAIAELG ASKRYNTTAG IVAGKINVHL VPHTHDDVGW LKTVDQYYIG
SNNTIQEAGV QYILDSILMY LTSNPDRKFV YVEQAFFQRW WREQTEEVQS VVKELIHSGR
LELINGGWCM HDEAATHYID MIEQTTLGHK YIKEQFGVTP RIGWQIDPFG HSAVQAYLLG
AELGFDALFF ARIDYQDRRQ RYKDKSLEVI WQGSNTLGSD AQVFTSIFPV HYGPPDGHGL
AYEESDEIPV QDDPLLFDYN VNERVDAFVA AAQSQANITR TNHIMWTMGN DFKYALAGKW
FVQMDKFIHY VNLDGRVNAL YSTPSMYLDA KHAADETWPL KTDDFFPYAD DKKSFWTGYF
TSRAAFKGYV REISGFLQAR ALQLEFLAGR KKDVPNTDSL WDALSISQHH DGVSGTEKQH
VTNDYAKRLA IGAAESDLVV KSALKALTSS SEENFVKCPL LNVSFCPLTE HAKKNLVVTA
YNPLAWQRED YVRIPVNEEG LVVKDASGKA VPSQLVPVSD ATKRTRSYYV RANLGVAPGT
PPSYWLYFKA AVPPLGVSTY YVSIGSADTG KFLSKFENSN GSSSIEAGFD TKLTFSSKTG
YLTRISNGKS GAETPVQQSY YWYAGYAGSG QHSGAYIFLP DGQTATPVAS EVSLKIVRGP
LVEEVHQEVA PWIYQIFRLY KDVGHAEVEF VVGPIPVDDG IGKEVITRFT TGIPSEGVFY
SDSNGRDFIK RVRDFRSDWK LEVTQPVAGN YYPVNLGVYL TDKKTDFSIL VDRSVGAGSI
SDGQLEVMLH RRLLVDDGRG VGEALDEVVC LPQGNSSNCE GLTVQGISYI NVNPVAKAAR
WRRYEGQKKL FPLQLYFGTT DGENKINGFT SFASGYALPE NVGLITLQAL DNGDALLRLA
HLYEADEDED LSKTATVDLS KLFPGRKIKS ATELSLSANQ EKSNIKPLKW KIAKAGITRK
SPRGAALDAS KMEVELGCME IRTIQIHFE
//
