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Database: UniProt
Entry: N1RHG5_FUSC4
LinkDB: N1RHG5_FUSC4
Original site: N1RHG5_FUSC4 
ID   N1RHG5_FUSC4            Unreviewed;      1107 AA.
AC   N1RHG5;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=alpha-mannosidase {ECO:0000256|ARBA:ARBA00012752};
DE            EC=3.2.1.24 {ECO:0000256|ARBA:ARBA00012752};
GN   ORFNames=FOC4_g10010309 {ECO:0000313|EMBL:EMT63837.1};
OS   Fusarium oxysporum f. sp. cubense (strain race 4) (Panama disease fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=2502994 {ECO:0000313|EMBL:EMT63837.1, ECO:0000313|Proteomes:UP000016929};
RN   [1] {ECO:0000313|Proteomes:UP000016929}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=race 4 {ECO:0000313|Proteomes:UP000016929};
RA   Fang X., Huang J.;
RT   "Genome sequencing and comparative transcriptomics of race 1 and race 4 of
RT   banana pathogen: Fusarium oxysporum f. sp. cubense.";
RL   Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000016929}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=race 4 {ECO:0000313|Proteomes:UP000016929};
RX   PubMed=24743270;
RA   Guo L., Han L., Yang L., Zeng H., Fan D., Zhu Y., Feng Y., Wang G.,
RA   Peng C., Jiang X., Zhou D., Ni P., Liang C., Liu L., Wang J., Mao C.,
RA   Fang X., Peng M., Huang J.;
RT   "Genome and Transcriptome Analysis of the Fungal Pathogen Fusarium
RT   oxysporum f. sp. cubense Causing Banana Vascular Wilt Disease.";
RL   PLoS ONE 9:E95543-E95543(2014).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family.
CC       {ECO:0000256|ARBA:ARBA00009792}.
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DR   EMBL; KB726992; EMT63837.1; -; Genomic_DNA.
DR   AlphaFoldDB; N1RHG5; -.
DR   STRING; 1229665.N1RHG5; -.
DR   HOGENOM; CLU_003442_0_1_1; -.
DR   Proteomes; UP000016929; Unassembled WGS sequence.
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   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:UP000016929}.
FT   DOMAIN          580..659
FT                   /note="Glycoside hydrolase family 38 central"
FT                   /evidence="ECO:0000259|SMART:SM00872"
FT   REGION          16..69
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1107 AA;  125571 MW;  2CA1E01EEBE49D97 CRC64;
     MSINNTFDRL LSASAACRRH SPSPEDQPLH SSSGKLRRLS NRSAPPAPGH PDIYTMGGGS
     ENKGDDSSYP LFAERPVGVP KTSILKGRIE PFYKSGQYYK VNLQANMYNG RYSGKPHVQL
     SVWDAPDLSR PTFEEATSHE FKETHTGTSF GPSWSTHWFK VVLRIPDETK DEELIELHWD
     ANNEGTIWTE DGVPIQGLTG SGERIEWIIP DSFRDGEEHT IYIEMACNGM FGNAPNGTTT
     IAPPDPNRRF NLSKADIVAI NVPARKLHLD MWEIGDAARE LPENSAEQNH ALSVAMKIIN
     TFEVNNQESI LKCREIAREI LGPDVDSHKV YEGGKEPVVF GIGHCHIDSC WLWPWAETKR
     KVVRSWMNQC DLMDRYPESN FACSQAQQYK WLKTYYPAAY KRVKQKVKEG QFHPIGGSWV
     EHDTNLPSGE SLVRQFFYGQ RFFEAEFGSR CRTFWLPDTF GYSSQLPQLC RLAGMDRFLT
     QKLSWNNINN FPHTTFMWRS IANHKTMRVD SSSLLVFGKG DGGGGPTWQH FEKLRRCAGI
     SNTIGGIPKI KMGLTVDGYF DRLNRKASEF PTWYGELYFE LHRGTYTTQA NNKYYNRKAE
     VMLRDIEQLA TFASIKNKSY KYPTKDLDDM WEAVLLCQFH DCLPGSSIEM CYDDSDKVYA
     EVFETGKRLL KDLYESLNVS SEFSTCLNES VAINTLPWHR KELVELSETE VGVACGDGQL
     LNLRTFKTQE EKPAVTVMEQ STDVYVLQNE QLRVVVESGV ITSLYDVVND REVIEKGGEA
     NKFVIFDDIP LYWQAWDVEV YHLDARRKVE YGKTKIFEQK PHRVTLVTDV KISENSYIKS
     YTTLSAALKG QPSRVDVRAD VNWHEDSKFL KVEFPVNVVN TEASYETAFS ITKRPTHYNT
     SWDMAKFEVC CHKFADLSEN NYGVSILNDS KYGFATAGKT MRLSLLRAPK APDANADMGR
     HSIRWAILPH KGSLSSTTVK AAYAFNNPLK PVTASKAVLE SVSGAPIKLV NIDESDSLVL
     DTIKRGQDDE DVSRDDGLRI NKGQSIILRV YESLGGRSRG VIETSFDVKR VTKTNILEDE
     LEEIQKEDGK IPITLRPFEV ATFKLEL
//
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