ID A0A0D2U0E2_CAPO3 Unreviewed; 1117 AA.
AC A0A0D2U0E2;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=alpha-mannosidase {ECO:0000256|ARBA:ARBA00012752};
DE EC=3.2.1.24 {ECO:0000256|ARBA:ARBA00012752};
GN ORFNames=CAOG_000287 {ECO:0000313|EMBL:KJE88681.1};
OS Capsaspora owczarzaki (strain ATCC 30864).
OC Eukaryota; Filasterea; Capsaspora.
OX NCBI_TaxID=595528 {ECO:0000313|EMBL:KJE88681.1, ECO:0000313|Proteomes:UP000008743};
RN [1] {ECO:0000313|Proteomes:UP000008743}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 30864 {ECO:0000313|Proteomes:UP000008743};
RA Russ C., Cuomo C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA Lang F.B.F., Roger A.J., Ruiz-Trillo I., Young S.K., Zeng Q., Gargeya S.,
RA Alvarado L., Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Capsaspora owczarzaki ATCC 30864.";
RL Submitted (FEB-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; KE346360; KJE88681.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D2U0E2; -.
DR STRING; 595528.A0A0D2U0E2; -.
DR EnsemblProtists; KJE88681; KJE88681; CAOG_000287.
DR eggNOG; KOG4342; Eukaryota.
DR InParanoid; A0A0D2U0E2; -.
DR PhylomeDB; A0A0D2U0E2; -.
DR Proteomes; UP000008743; 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; cd10813; GH38N_AMII_Man2C1; 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:0000256|ARBA:ARBA00023295};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000008743}.
FT DOMAIN 601..681
FT /note="Glycoside hydrolase family 38 central"
FT /evidence="ECO:0000259|SMART:SM00872"
SQ SEQUENCE 1117 AA; 125011 MW; 3E0E6914BCA1F7A3 CRC64;
MDGDAKVRFF KLVTMLTKPP VAYETGRGAR QLHKVFVRVC TMEVCHGWYP GSRRCLNRND
QALDTTARQP PPPQKHTNVT IERVEKLLSG IYFTDANLGH PHLVYGGDLP CATRQPFAHL
LHRPATGTSR PTFAQVLSDG DGGFTRVERT KSFGPSWTTH WFAFDLVIPP AWAGREVHFR
WNSNSEALIY DEHGEPRQGL TGGDGCDVRS EYIVTRSARE GGETRRIYVE MAANGMFGVG
DNGLINPPNE NRFFDISLCE LAVFDRELWL LIQDVRTLYD LSKTFADNSP RKLQAALSAN
KIANLIDPRD RSTYPAARTV AAAFFSQRNG DSQHSISAIG HCHIDTAWLW PYDETIRKCA
RSFATVDRYM DDYPELKFAC SQAQQLDWIR LYYPGLFSRL RERVKQGRFI PVGGAWQDGN
IPSGEAMARQ FLYGQTFFQR EFGITCKEFW LPDTFGYSAQ LPQLMRQAGI SRFVTQKLSW
NLINKFPHNT FHWEGIDGSR VLTHFPPADT YNSQVLPDEV MKSITNFKDH GRSRESMMLF
GHGDGGGGPQ MVMLERMRRM QDCDGVPKIN VRSPDEFFTR VEAEMAQEDQ LLTWVGELYL
ELHRGTYTSQ ANNKKGNRKG ELLLRNVEML VSIVQALNLP GPAEAKSELD RLWKLLLLNQ
FHDVLPGSSI AMVYRDSDRH YADITASGNS LLQTALSTLS SSSKTSNESL VVMNTLSWER
TSVVQTADGG FGNDLRLVTV PAIGTSLVPS ESIQDISAPV VAQKTDSNTW ILENNVLRAE
FNAQGALISL IQSETGREAI ARGGDGGNRF VLFDDIPLFW DAWDMQEYHL EKSHLVHSDA
GVVVRPTVSP LVGELEFTIP ISARSTIRQT VRLTHGQRFV EFATQVDWHE ARKCLKVEFP
MNVRTSLATY DIQFGFVQRP THTNTSWDMA KFEVCGHRYG DLSEHGFGIA LLNDCKYGYS
ARGNVMRLSL LRAPKAPDAE CDMGLHTFTY AIMPHQGSFQ EGGVVRAAAE LNSPLLVVPG
HAQSRSFFSL LPASTSVVIE AIKPAESAPK KLVLRLFESY GGQARVTLAS TLPIASVQLS
NIIEVDSGSP LDWNQATGVT LTFHAFEVKT LLVTLQE
//