ID F8P9H8_SERL9 Unreviewed; 1149 AA.
AC F8P9H8;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=alpha-mannosidase {ECO:0000256|ARBA:ARBA00012752};
DE EC=3.2.1.24 {ECO:0000256|ARBA:ARBA00012752};
GN ORFNames=SERLADRAFT_442443 {ECO:0000313|EMBL:EGO20307.1};
OS Serpula lacrymans var. lacrymans (strain S7.9) (Dry rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Coniophorineae; Serpulaceae; Serpula.
OX NCBI_TaxID=578457;
RN [1] {ECO:0000313|EMBL:EGO20307.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=S7.9 {ECO:0000313|EMBL:EGO20307.1};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Eastwood D.C., Floudas D., Binder M., Majcherczyk A., Schneider P.,
RA Aerts A., Asiegbu F.O., Baker S.E., Barry K., Bendiksby M., Blumentritt M.,
RA Coutinho P.M., Cullen D., Cullen D., Gathman A., Goodell B., Henrissat B.,
RA Ihrmark K., Kauserud H., Kohler A., LaButti K., Lapidus A., Lavin J.L.,
RA Lee Y.-H., Lindquist E., Lilly W., Lucas S., Morin E., Murat C.,
RA Oguiza J.A., Park J., Pisabarro A.G., Riley R., Rosling A., Salamov A.,
RA Schmidt O., Schmutz J., Skrede I., Stenlid J., Wiebenga A., Xie X.,
RA Kues U., Hibbett D.S., Hoffmeister D., Hogberg N., Martin F.,
RA Grigoriev I.V., Watkinson S.C.;
RT "Evolution of plant cell wall degrading machinery underlies the functional
RT diversity of forest fungi.";
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family.
CC {ECO:0000256|ARBA:ARBA00009792}.
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DR EMBL; GL945441; EGO20307.1; -; Genomic_DNA.
DR RefSeq; XP_007323052.1; XM_007322990.1.
DR AlphaFoldDB; F8P9H8; -.
DR GeneID; 18815728; -.
DR KEGG; sla:SERLADRAFT_442443; -.
DR HOGENOM; CLU_003442_0_1_1; -.
DR OrthoDB; 2786490at2759; -.
DR Proteomes; UP000008064; 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 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:0000313|EMBL:EGO20307.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 553..635
FT /note="Glycoside hydrolase family 38 central"
FT /evidence="ECO:0000259|SMART:SM00872"
SQ SEQUENCE 1149 AA; 128463 MW; C15CA730E458FAFB CRC64;
MSGSEYPQLN FGTGAKWIKN LTRDRLNNFS GGHFSDVNLS SVLFTHRLDA PEYVKLQVWS
APGLTKPFFE EATKQKFKPA KKGDSFGPSL SVNIPADWQQ YERVQFEFDP GCEAMIYSTE
GVPLQGITGG YGGDRRVEYI IPLDARQQGH HEFIIESSCN GMFGVPWNGD TIAPPDMNRY
FQLASADLVV PNQEAWRLLW DFTTLREIID TLPGNSPLQN KALVTANEIM NIFRRGNSTD
IANARKLAEN VFGEGWEAKG AEIYAEGPER AQIVSISYCH IDTAWLWPYS VTQQKTARSW
STQIDLMERY PEHRFACSQA QQFKWLEQQY PPLFERVREK VKSGQFHLIG GAWVENDGNM
PSGEALVRQF LYGQKYFESR FGKRCETAWL PDSFGLTAAY PQLIRDAGMK YFFTQKLSWN
NIANLGAELR NVFPHSTFNW VGIDGSQVLC HMTPVDTYTA QASVGDVNKG VTNHKNLESN
DTALLVFGNG DGGGGALPKM LENLRRIRAA TNGHRDLPSV NMGHSVEEFF ENIDKDSQQG
KRLPNWRGEL YLEFHRGTYT SHGSIKKGNR KSEILLRDLE RVATFATLFK AKDSTYVYPK
KTIDDSWEKV LLNQFHDVLP GSAIGMVYDD AEKLYGEVRK ACDSALEEAF QALFAKSIPV
LGDRSIKALS QPSDLIAINT TSFSRRDVVK IPLQGSGSAL KSLKSKIVQV STDGAFGYAL
MNCSEGDNVA TATGLFADSL PVSGGLVVFT NGSDHFVLRN ASVQLTISDG RITSLVDVKL
GRELIPKGST GGLVIFEDRP NYWDAWDVEI HHLETPNLLK FSKVEVVAEG PLRAAVKTQV
KYGQSTIDVT ISLDAITASH HEHSRSFFTF DAVVDWHERH EFLKFELPLN INSADATYET
QFGHLQRPTH KNTTLDAAKF EVCGHKYADL SEYGYGVAFL SESKYGFACH GNVLRISLLR
GATAPDAEQD QGKHEFSWAV MPHKGHFLES DVPMAAFLFN SPLHVRLVPS VQQADKVSVV
KQPFHLDGGS NIFLETIKRG EDDFAPNGSN TTIILRLYEA FGGHGQVKLK IASHVPILKA
YVTNLLEDDK AELRLFETAD RDRPRQLKLD FRGFEVKTVK LVLGSNRIAE ATKSRSSQRD
SWVTVDDDL
//
