ID   C0MH70_STRS7            Unreviewed;       906 AA.
AC   C0MH70;
DT   05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   05-MAY-2009, sequence version 1.
DT   04-NOV-2026, entry version 88.
DE   SubName: Full=Glycosyl hydrolases family protein {ECO:0000313|EMBL:CAW98365.1};
GN   OrderedLocusNames=SZO_04460 {ECO:0000313|EMBL:CAW98365.1};
OS   Streptococcus equi subsp. zooepidemicus (strain H70).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=553483 {ECO:0000313|EMBL:CAW98365.1, ECO:0000313|Proteomes:UP000001368};
RN   [1] {ECO:0000313|EMBL:CAW98365.1, ECO:0000313|Proteomes:UP000001368}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H70 {ECO:0000313|EMBL:CAW98365.1,
RC   ECO:0000313|Proteomes:UP000001368};
RX   PubMed=19325880; DOI=10.1371/journal.ppat.1000346;
RA   Holden M.T.G., Heather Z., Paillot R., Steward K.F., Webb K., Ainslie F.,
RA   Jourdan T., Bason N.C., Holroyd N.E., Mungall K., Quail M.A., Sanders M.,
RA   Simmonds M., Willey D., Brooks K., Aanensen D.M., Spratt B.G., Jolley K.A.,
RA   Maiden M.C.J., Kehoe M., Chanter N., Bentley S.D., Robinson C.,
RA   Maskell D.J., Parkhill J., Waller A.S.;
RT   "Genomic evidence for the evolution of Streptococcus equi: host
RT   restriction, increased virulence, and genetic exchange with human
RT   pathogens.";
RL   PLoS Pathog. 5:E1000346-E1000346(2009).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family.
CC       {ECO:0000256|ARBA:ARBA00009792}.
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DR   EMBL; FM204884; CAW98365.1; -; Genomic_DNA.
DR   AlphaFoldDB; C0MH70; -.
DR   KEGG; seq:SZO_04460; -.
DR   eggNOG; COG0383; Bacteria.
DR   HOGENOM; CLU_003442_2_1_9; -.
DR   OMA; AAKIFWD; -.
DR   Proteomes; UP000001368; Chromosome.
DR   GO; GO:0004559; F:alpha-mannosidase activity; IEA:InterPro.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0006013; P:mannose metabolic process; IEA:InterPro.
DR   GO; GO:0009313; P:oligosaccharide catabolic process; IEA:TreeGrafter.
DR   CDD; cd10814; GH38N_AMII_SpGH38_like; 1.
DR   Gene3D; 2.60.40.2210; -; 1.
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   Gene3D; 2.70.98.30; Golgi alpha-mannosidase II, domain 4; 1.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR041509; GH38_beta-1.
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:SF2; MANNOSYLGLYCERATE HYDROLASE; 1.
DR   Pfam; PF09261; Alpha-mann_mid; 1.
DR   Pfam; PF17677; Glyco_hydro38C2; 1.
DR   Pfam; PF18438; Glyco_hydro_38; 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:ARBA00022801, ECO:0000313|EMBL:CAW98365.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001368}.
FT   DOMAIN          297..370
FT                   /note="Glycoside hydrolase family 38 central"
FT                   /evidence="ECO:0000259|SMART:SM00872"
SQ   SEQUENCE   906 AA;  102916 MW;  FCB802017AA5BFBE CRC64;
     MTPKKVHIIS HSHWDREWYM AYEQHHMRLI QLIDDLLDLF KTDPDFHSFH LDGQTIILDD
     YLQVKPEREA DIRQAIQAGK LRIGPFYILQ DAFLTSSESN VRNMLIGKED CEQWGASVPL
     GYFPDTFGNM GQTPQLMRKA GLNAAAFGRG IRPTGFNNQV DTSEKYSSQF SEMIWQGPDD
     SRILGLLFAN WYSNGNEIPT EEKKARQFWD QKLADAERFA STRHLLMMNG VDHQPVQLDV
     TKAIALANKL YPDYDFVHSC FEDYLADLSQ ELPEELSIVS GEMTSQETDG WYTLANTASA
     RIYLKQANTK VSRQLENITE PLATMAYEVT GTYPHDQLRY AWKTLMQNHP HDSICGCSVD
     SVHQEMMPRF DKAYEVGTYL AERSANQIAE AIDTSMFPED SCPFVLFNTC GHEKKTVSDL
     TLTWKVFPFG QRLPKAAYQE AKEYLETRQP QFQVIDAAGR VIEEAEILGT DIAFDYALPE
     RTFREAYFAI KVRLRLPLTL SAMSWQCLAL QATDQPNQAP NEALLHQDGS CLENDFLKVI
     IAANGLLTIE DKLNGNRFDS CLQYEDCGDI GNEYIFRQPD HDIPYLAHQG SCKLRVLTNT
     AHLAEIELTQ TFDIPLTADD CLQAEMEAVI DIQERQAKRS QEKAPFTVTT VIRMEKDSPR
     LQFQTSFNNQ MTNHRLRVLF PTHLKTDHHF ADSIFETVKR PNHTNAQFWK NPSNPQHQEA
     FVSLFDGKTG VTIGNYGLNE YEILPNTNTI AITLLRSVGE LGDWGYFPTP DAQCLGQQTV
     SFSFESINAT TRFASYWRAQ EAQVPVTMVQ TKRHSGQLPA QYAYIKGATD HVALTAFKRR
     LSDNALITRS YNVSNDEACA LTLAIPDHTA RVTSLLEEDQ HEPLPAELGK GDILTLAWKK
     SESAHL
//