ID A0A2K1KE22_PHYPA Unreviewed; 1035 AA.
AC A0A2K1KE22;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Alpha-mannosidase {ECO:0000256|RuleBase:RU361199};
DE EC=3.2.1.- {ECO:0000256|RuleBase:RU361199};
GN ORFNames=PHYPA_008405 {ECO:0000313|EMBL:PNR52031.1};
OS Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae; Physcomitrium.
OX NCBI_TaxID=3218 {ECO:0000313|EMBL:PNR52031.1};
RN [1] {ECO:0000313|EMBL:PNR52031.1, ECO:0000313|Proteomes:UP000006727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004 {ECO:0000313|EnsemblPlants:Pp3c6_2440V3.1,
RC ECO:0000313|Proteomes:UP000006727};
RX PubMed=18079367; DOI=10.1126/science.1150646;
RA Rensing S.A., Lang D., Zimmer A.D., Terry A., Salamov A., Shapiro H.,
RA Nishiyama T., Perroud P.-F., Lindquist E.A., Kamisugi Y., Tanahashi T.,
RA Sakakibara K., Fujita T., Oishi K., Shin-I T., Kuroki Y., Toyoda A.,
RA Suzuki Y., Hashimoto S.-I., Yamaguchi K., Sugano S., Kohara Y.,
RA Fujiyama A., Anterola A., Aoki S., Ashton N., Barbazuk W.B., Barker E.,
RA Bennetzen J.L., Blankenship R., Cho S.H., Dutcher S.K., Estelle M.,
RA Fawcett J.A., Gundlach H., Hanada K., Heyl A., Hicks K.A., Hughes J.,
RA Lohr M., Mayer K., Melkozernov A., Murata T., Nelson D.R., Pils B.,
RA Prigge M., Reiss B., Renner T., Rombauts S., Rushton P.J., Sanderfoot A.,
RA Schween G., Shiu S.-H., Stueber K., Theodoulou F.L., Tu H., Van de Peer Y.,
RA Verrier P.J., Waters E., Wood A., Yang L., Cove D., Cuming A.C., Hasebe M.,
RA Lucas S., Mishler B.D., Reski R., Grigoriev I.V., Quatrano R.S.,
RA Boore J.L.;
RT "The Physcomitrella genome reveals evolutionary insights into the conquest
RT of land by plants.";
RL Science 319:64-69(2008).
RN [2] {ECO:0000313|EMBL:PNR52031.1, ECO:0000313|Proteomes:UP000006727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004 {ECO:0000313|EnsemblPlants:Pp3c6_2440V3.1,
RC ECO:0000313|Proteomes:UP000006727};
RX PubMed=29237241; DOI=10.1111/tpj.13801;
RA Lang D., Ullrich K.K., Murat F., Fuchs J., Jenkins J., Haas F.B.,
RA Piednoel M., Gundlach H., Van Bel M., Meyberg R., Vives C., Morata J.,
RA Symeonidi A., Hiss M., Muchero W., Kamisugi Y., Saleh O., Blanc G.,
RA Decker E.L., van Gessel N., Grimwood J., Hayes R.D., Graham S.W.,
RA Gunter L.E., McDaniel S.F., Hoernstein S.N.W., Larsson A., Li F.W.,
RA Perroud P.F., Phillips J., Ranjan P., Rokshar D.S., Rothfels C.J.,
RA Schneider L., Shu S., Stevenson D.W., Thummler F., Tillich M.,
RA Villarreal Aguilar J.C., Widiez T., Wong G.K., Wymore A., Zhang Y.,
RA Zimmer A.D., Quatrano R.S., Mayer K.F.X., Goodstein D., Casacuberta J.M.,
RA Vandepoele K., Reski R., Cuming A.C., Tuskan G.A., Maumus F., Salse J.,
RA Schmutz J., Rensing S.A.;
RT "The Physcomitrella patens chromosome-scale assembly reveals moss genome
RT structure and evolution.";
RL Plant J. 93:515-533(2018).
RN [3] {ECO:0000313|EnsemblPlants:Pp3c6_2440V3.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (DEC-2020) to UniProtKB.
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; ABEU02000006; PNR52031.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K1KE22; -.
DR STRING; 3218.A0A2K1KE22; -.
DR PaxDb; 3218-PP1S77_136V6-1; -.
DR EnsemblPlants; Pp3c6_2440V3.1; Pp3c6_2440V3.1; Pp3c6_2440.
DR EnsemblPlants; Pp3c6_2440V3.2; Pp3c6_2440V3.2; Pp3c6_2440.
DR Gramene; Pp3c6_2440V3.1; Pp3c6_2440V3.1; Pp3c6_2440.
DR Gramene; Pp3c6_2440V3.2; Pp3c6_2440V3.2; Pp3c6_2440.
DR InParanoid; A0A2K1KE22; -.
DR OrthoDB; 5474711at2759; -.
DR Proteomes; UP000006727; Chromosome 6.
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:UP000006727};
KW Signal {ECO:0000256|RuleBase:RU361199};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361199}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|RuleBase:RU361199"
FT CHAIN 22..1035
FT /note="Alpha-mannosidase"
FT /evidence="ECO:0000256|RuleBase:RU361199"
FT /id="PRO_5033844077"
FT DOMAIN 361..435
FT /note="Glycoside hydrolase family 38 central"
FT /evidence="ECO:0000259|SMART:SM00872"
SQ SEQUENCE 1035 AA; 116524 MW; 7D0F2577C05A209E CRC64;
MGSFETAILL LHCILACQTL ALEQPFRFAA KAYNTSGSTV EGKINVHLVS HTHDDVGWLK
TVDQYYVGSN NSIAVAAVQY VLDSVVTALQ QDPNRKFIYV EQAFFQRWWR QQSPTQQKIV
EALVDSGQLE FINGGFCMHD EATTHYVDMI DQTTLGHRFI KKQFGKIPRI AWQIDPFGHS
AVQAYLLGAE MGFDGLFFGR ADYQDKINRQ KERTMEVIWR GSKSLGESAQ IFTGLMTHHY
DPPHEFQFEI KSETSPIQDD PSLYGYNLPE KLDLFVEYVT NQSKEFRTHH IMWAMGEDFS
YGNANTWFKQ IDKLIHYANM DGRVNAFYST PSMYLDAVHA ANATWHLKTD DYFPYSDCPH
CFWTGYFTSR PALKGYVRKL SALLQAARQV EFLVGKVSSG PNTDSLEEAV AILQHHDGVS
GTERQHVADD YAARLSKGQS ESEDVFNKAL ASLISTKAAE SKLLIEKMSS TPGHRVLMNP
VNSPDLNLVQ CNLLNVSYCP PTEVELKSGR SFVVVAYNPL GWEREDFVRV PVSSSKIEVI
DAEENEIPSQ LIPITEADRT LRDKYVNLHA GVSAGTAPKY FLVFAAAVPP LGYNSFIVRP
SSASGSNIAK LSSYETRRAP LTVHLKSSQL HLTFSKDTGL LTHMSNKKTG VSIPVEQSYC
WYNGSSGVTE EDPHMASGAY LFRPNTSECF PLKNFQQIVT VFRGPLVEEV HQQFSPWASQ
VIRVYKNAEQ AEVQFTVGPI PIDDSNGKEI VTKFTTPLRT EKTFYTDSNG RDFLKRVRDF
RPDWNLEVKE PVAGNYYPLN LGIYMKDSET DVSVLVDRAL GAASTADGQL EIMLHRRLLY
DDHRGVGEAL NETVCGSNGR CEGLTVLGSL YININPSEEA SQWRRIKGQQ ILMPLQLAFS
VLEDGNKEVL HSPKFSAFKS GYELPQNVAL ITLQELDDRQ VLLRLANIFE VDESEQLSKM
ATVYLPDIFP NLKIKDVVEL SLSANQKKSH MKKLTWTVEG NEKVQKNILR GRPLGRDDTS
VEIAPMEIRT FLITL
//
