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}.
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; 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
//