ID A0A1C3YKR7_GIBZE Unreviewed; 1136 AA.
AC A0A1C3YKR7;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=alpha-mannosidase {ECO:0000256|ARBA:ARBA00012752};
DE EC=3.2.1.24 {ECO:0000256|ARBA:ARBA00012752};
GN ORFNames=FGRAMPH1_01T23287 {ECO:0000313|EMBL:SCB65125.1};
OS Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084
OS / PH-1) (Wheat head blight fungus) (Fusarium graminearum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=229533 {ECO:0000313|EMBL:SCB65125.1, ECO:0000313|Proteomes:UP000070720};
RN [1] {ECO:0000313|Proteomes:UP000070720}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1
RC {ECO:0000313|Proteomes:UP000070720};
RX PubMed=17823352; DOI=10.1126/science.1143708;
RA Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A.,
RA Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T.,
RA Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S.,
RA Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S.,
RA Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R.,
RA Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T.,
RA Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT "The Fusarium graminearum genome reveals a link between localized
RT polymorphism and pathogen specialization.";
RL Science 317:1400-1402(2007).
RN [2] {ECO:0000313|Proteomes:UP000070720}
RP GENOME REANNOTATION.
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1
RC {ECO:0000313|Proteomes:UP000070720};
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.B., Woloshuk C., Xie X., Xu J.R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.H., Li L., Manners J.M., Miranda-Saavedra D., Mukherjee M.,
RA Park G., Park J., Park S.Y., Proctor R.H., Regev A., Ruiz-Roldan M.C.,
RA Sain D., Sakthikumar S., Sykes S., Schwartz D.C., Turgeon B.G.,
RA Wapinski I., Yoder O., Young S., Zeng Q., Zhou S., Galagan J., Cuomo C.A.,
RA Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
RN [3] {ECO:0000313|EMBL:SCB65125.1, ECO:0000313|Proteomes:UP000070720}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1
RC {ECO:0000313|Proteomes:UP000070720};
RX PubMed=26198851; DOI=10.1186/s12864-015-1756-1;
RA King R., Urban M., Hammond-Kosack M.C., Hassani-Pak K.,
RA Hammond-Kosack K.E.;
RT "The completed genome sequence of the pathogenic ascomycete fungus Fusarium
RT graminearum.";
RL BMC Genomics 16:544-544(2015).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family.
CC {ECO:0000256|ARBA:ARBA00009792}.
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DR EMBL; HG970335; SCB65125.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C3YKR7; -.
DR STRING; 229533.A0A1C3YKR7; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G23287; -.
DR eggNOG; KOG4342; Eukaryota.
DR InParanoid; A0A1C3YKR7; -.
DR Proteomes; UP000070720; Chromosome 4.
DR GO; GO:0004559; F:alpha-mannosidase activity; IEA:UniProtKB-EC.
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; cd10812; GH38N_AMII_ScAms1_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 InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR041147; GH38_C.
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 PANTHER; PTHR46017; ALPHA-MANNOSIDASE 2C1; 1.
DR PANTHER; PTHR46017:SF1; ALPHA-MANNOSIDASE 2C1; 1.
DR Pfam; PF09261; Alpha-mann_mid; 1.
DR Pfam; PF17677; Glyco_hydro38C2; 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};
KW Hydrolase {ECO:0000256|ARBA:ARBA00023295};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000070720}.
FT DOMAIN 609..688
FT /note="Glycoside hydrolase family 38 central"
FT /evidence="ECO:0000259|SMART:SM00872"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1136 AA; 128751 MW; DAEC1C727D513E5D CRC64;
MSSINNTFDR VSSTSAVCPR HSPSPEDQLR PPVSGKQRRI SNRSAPPAPG HPDIFTMGGG
TEPKGNDSSY PLFAERPVGV PKTSILKGRI EPFYKSGQYY KVNLQANMDN ARYSGKPHVQ
LSVWDAPDLS RPTFEDAVSH EFRETHTGTS FGPSWSTHWF KVILRIPEDI KDEELIELHW
DASNEGTIWT EDGVPIQGLT GSGERIEWII PDSFRDGEEH TIYIEMACNG MFGNAPNGTT
TIAPPDPNRR FNLSKADIVA VNVPARKLHI DIWEIGDAAR ELPENSAEQN HALAVAMKII
NTFEVNNQDS ILKCREIARE ILGPDVDSHK VYEVGKDPVV FGIGHCHIDS CWLWPWAETK
RKVVRSWMNQ CDLMERYPEA NFACSQAQQY KWLKTYYPAA YKRVKQKVKE GQFHPIGGSW
VEHDTNLPSG ESLVRQFFYG QRFFEAEFGS RCRTFWLPDT FGYSSQLPQL CRLADMDRFL
TQKLSWNNIN NFPHTTFMWV SPDGSQVICH MPPSETYTAN ADFGDLKRSI EKHKTMRVDS
SSLLVFGKGD GGGGPTWQHF EKLRRCAGIS NTIGGIPKIK MGLTVDDYFD RLNQKATEFP
TWYGELYFEL HRGTYTTQAN NKYYNRKAEV MLRDIEQLAT FASIKNKKYK YPTKDLDDMW
ESVLLCQFHD CLPGSSIEMC YDDSDKVYAE VFETGKRLLN DLYDALHVTS QFSSSLDESV
AINTLPWHRK ELVELSDSEV GVACGDGQLL ALRSFKVQEE KPAVTVMEQS TDVYVLQNDQ
LRVVVDNGVI TSIYDIENDR EVVEKGGEAN KFVIFDDIPL YWQAWDVEVY HLDARRNVEY
GKTKIFEQKP HRVTLVTEIK VSENSSIKSY TTLSAALKGQ PPQIDVKANV NWHEDSKFLK
VEFPVNVVNN EASYETAFSI TKRPTHYNTS WDMAKFEVCC HKFADLSENN YGVSILNDCK
YGFATAGKMM RLSLLRSPKA PDANADMGRH TIRWAILPHK GGLSSTTVKA AYAFNNPLKP
VTASKVVLES LSSAPIKLVN TDESDSLVLD TIKRGQDDED VTRKEGLRVN KGQSIIIRVY
ESLGGRSRGT IKTSFDVKRV TKTNILEDDL EEIEYEDGKI PITLRPFEVA TFKLQL
//
