ID   W6Z1G4_COCMI            Unreviewed;      1120 AA.
AC   W6Z1G4;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=alpha-mannosidase {ECO:0000256|ARBA:ARBA00012752};
DE            EC=3.2.1.24 {ECO:0000256|ARBA:ARBA00012752};
GN   ORFNames=COCMIDRAFT_100539 {ECO:0000313|EMBL:EUC43548.1};
OS   Bipolaris oryzae ATCC 44560.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX   NCBI_TaxID=930090 {ECO:0000313|EMBL:EUC43548.1};
RN   [1] {ECO:0000313|EMBL:EUC43548.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 44560 {ECO:0000313|EMBL:EUC43548.1};
RX   PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA   Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA   Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA   Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA   LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA   Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT   "Comparative genome structure, secondary metabolite, and effector coding
RT   capacity across Cochliobolus pathogens.";
RL   PLoS Genet. 9:E1003233-E1003233(2013).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family.
CC       {ECO:0000256|ARBA:ARBA00009792}.
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DR   EMBL; KI964026; EUC43548.1; -; Genomic_DNA.
DR   RefSeq; XP_007689958.1; XM_007691768.1.
DR   AlphaFoldDB; W6Z1G4; -.
DR   STRING; 930090.W6Z1G4; -.
DR   GeneID; 19117695; -.
DR   KEGG; bor:COCMIDRAFT_100539; -.
DR   eggNOG; KOG4342; Eukaryota.
DR   HOGENOM; CLU_003442_0_1_1; -.
DR   OrthoDB; 2786490at2759; -.
DR   Proteomes; UP000054032; Unassembled WGS sequence.
DR   GO; GO:0004559; F:alpha-mannosidase activity; IEA:InterPro.
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:EUC43548.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          560..644
FT                   /note="Glycoside hydrolase family 38 central"
FT                   /evidence="ECO:0000259|SMART:SM00872"
SQ   SEQUENCE   1120 AA;  127108 MW;  067403A939555B29 CRC64;
     MGGESHRIIP VTVSNDYPKL SDGPVGKQIH SIYESRLRQF FDGGQYREQS LIGKLTEAVA
     SGPEWIKLSV YSPPDLSRPL FDEATSHAFH PTKVGESFGP SWSTHWFKVQ LTLPDYFLDK
     EHLEFVWDAN NEGLIWTEDG RTVHGLTGGG ERTQWILPKA FRDGKEHTFY IEMACNGMFG
     NAPGGDSIQP PKPDRYYTLH TAEVQAVNLD ARGLYFDFWE ISDAAREFPS DSTQIHDAQQ
     VCNRIMDTFI AGNGSRESIK AARKIAAEYV GKNVDSHKVY QGDQEAIVHG IGYCHIDTCW
     LWPFDETKRK VNRSWSNQCD LIDRYPELRF CCSQAQQYKW LEQYYPSTFD RVKKKVKEGS
     FQPIGGSWVE HDTNLPGGES LIRQFLYGQR YFESKFGQRC RTFWLPDTFG YSSQLPQICR
     ISGMTRFLTQ KLSWNNINNF PHTTFNWVSL DNSQVICHMP PCETYTCEAN FGDVKRSVTQ
     HKSLDQDKTS LLVFGKGDGG GGPTWQHLEK LRRCRGISDT TGLLPRIKLG DSADDFFDRL
     EKKVANGDEL VTWYGELYFE LHRGTYTTQA NNKRNNRKSE IMLRDIEYLA TLATIKNGFG
     KKSSYKYPKK EIDDMWENVL LCQFHDCLPG SSIEMCYDDS DRIYASVFAT GEKLLSDALA
     ELGFGDQTTW NENTKLMAIN TLPWNRCEVI KLPAEARQSV YGREETRYGL AYSKGSDKGF
     GALEIAPMAS RIPPSKAFIE EIRPNVYQMR NSQFEVEVTD GAITSLFDIQ AKRELIPKGA
     KAGQLVIFDD KPLYWQAWDV EVYHLKSRQE LKPSKVTITE NSMHRVSLEV ETKISEKSWI
     KTTLSLPAAG AAPSAIEFDA EIEWHETMKF LKVEFPVDIV NTEASYETQF GIVRRPTHYN
     TSWDMAKFEV CCHKWADLSE ATYGVSILND NKYGFATAGN VMRLSLLRAA KAPDAHADMG
     NHKTRYAIFP HEGPLDHRTI RKAFEFNNPL KIVGTTYDKH DSSLLNPFHI YNAPNLVLDT
     IKRGEDDEDV SRGELPVKKG HGVILRIYDA LGGKSKGVLT WGNLNVTKVV KVNALEDEEE
     NEGALRICSL KTGGPDEAME TGVEIEVRAF EVASYKLVLG
//