ID A0A137PDT7_CONC2 Unreviewed; 1097 AA.
AC A0A137PDT7;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=alpha-mannosidase {ECO:0000256|ARBA:ARBA00012752};
DE EC=3.2.1.24 {ECO:0000256|ARBA:ARBA00012752};
GN ORFNames=CONCODRAFT_15711 {ECO:0000313|EMBL:KXN73101.1};
OS Conidiobolus coronatus (strain ATCC 28846 / CBS 209.66 / NRRL 28638)
OS (Delacroixia coronata).
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota;
OC Entomophthoromycotina; Entomophthoromycetes; Entomophthorales;
OC Ancylistaceae; Conidiobolus.
OX NCBI_TaxID=796925 {ECO:0000313|EMBL:KXN73101.1, ECO:0000313|Proteomes:UP000070444};
RN [1] {ECO:0000313|EMBL:KXN73101.1, ECO:0000313|Proteomes:UP000070444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 28638 {ECO:0000313|EMBL:KXN73101.1,
RC ECO:0000313|Proteomes:UP000070444};
RX PubMed=25977457; DOI=10.1093/gbe/evv090;
RA Chang Y., Wang S., Sekimoto S., Aerts A.L., Choi C., Clum A., LaButti K.M.,
RA Lindquist E.A., Yee Ngan C., Ohm R.A., Salamov A.A., Grigoriev I.V.,
RA Spatafora J.W., Berbee M.L.;
RT "Phylogenomic Analyses Indicate that Early Fungi Evolved Digesting Cell
RT Walls of Algal Ancestors of Land Plants.";
RL Genome Biol. Evol. 7:1590-1601(2015).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family.
CC {ECO:0000256|ARBA:ARBA00009792}.
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DR EMBL; KQ964441; KXN73101.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A137PDT7; -.
DR STRING; 796925.A0A137PDT7; -.
DR EnsemblFungi; KXN73101; KXN73101; CONCODRAFT_15711.
DR OMA; DVFGFSW; -.
DR OrthoDB; 2786490at2759; -.
DR Proteomes; UP000070444; 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; 2.60.40.2220; -; 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:0000313|EMBL:KXN73101.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000070444}.
FT DOMAIN 515..595
FT /note="Glycoside hydrolase family 38 central"
FT /evidence="ECO:0000259|SMART:SM00872"
SQ SEQUENCE 1097 AA; 127441 MW; AF4D4230AE7D3D09 CRC64;
MVMQKHYDIT RQRIDRFLPG GYWGDQNLSH QYYTHRALNS PWVILEKYSV PDLKRIPFHE
AVKGRFLSSH RNVSIGPTWS THWFKVYIRI PSDWDGLFVG INWVFHGESL VYTREGEPIY
SMSADGGRDL FHLTDSCTPN QTFFFYIECA CNQLNGINGI EPPNPNNYYE IQQADLLVID
RNVYKLHHNF EILRQLSNDI PRDSNRADKA MFAANKIMNV WDKFNYNTIF ECIKISEDFL
KLKNGQGQME LTCIGNCHID TAWLWPYAET RRKVCRSWVA QLAHMDTYPD YHFTASQAQQ
FEWLLDNYPS TFDKMRQRVK DGRFHPVGGT WVEMDTNVPS GESLCKQFLY GQRFFNRHLK
FKSEVFWLPD TFGYAAQLPQ IVRKCGMKYF FTQKLSWNNI NQFPHTTFHW EALDGSKILS
HMAPSNTYVA QVHVLDLRRS VEGHKDRPYS NQALLLFGFG DGGGGPSPDM LERYDRLKDI
DGLPKLKMTG PDEFYRSLDK DSDKLVTWKG ELYFELHRGT YTNHGDVKRG NRLSEVLLHN
LEVASSYAYY AMNNSYRVPQ TELNRMWKMT LCNQFHDVLP GTCIELAYQE VFEYYNEIDQ
LGNRLLDDAL RNIFYSNTKI NPETETLTDL GVLNTLSWTR NEIIKVPLNK FKRGQDLNFD
QISHDGKVGY KAAVDLKPFT PTVLKLTDHP QLDEKMSEKK ASYGGESVSV SIDSTTNIFF
LENSFIKAKF SDRGQLISLY DKRVNRELIP EGAVAHQLQL FEDIPLNWDA WDVEVYHLEK
FKNFTDATVN ILEMGPVVAS LEIRYNLTLG SSAVIVVSLS SLSPRLDFHA KVDWRENRRF
LKVEFTFDIR NDHAHYETQW GNIKRPNHYN TSWDMAKFEV CGHRFCDLSE YGYGVAIVND
LKYGYACLDN KIRLSLLRSS KGPDGNSDMK VHEFQYGIYP HPNRFLASDA MQIAHEFSTP
SVYLPISHQP NFNRSPLFQL RGDSNVFLET VKRSEDLDEN LIVRLYEAYG GHARVRLMSP
LPVSSIKEVN ILEEDITTEE MGATYSDDDL EWEAQGFVQL EFKPFEIKTL RLSMRLNKLK
NPTLTEKLTS CFENICL
//
