ID   G8NVN1_GRAMM            Unreviewed;      1106 AA.
AC   G8NVN1;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   SubName: Full=Glycosyl hydrolase 38 domain protein {ECO:0000313|EMBL:AEU37703.1};
GN   OrderedLocusNames=AciX8_3405 {ECO:0000313|EMBL:AEU37703.1};
OS   Granulicella mallensis (strain ATCC BAA-1857 / DSM 23137 / MP5ACTX8).
OC   Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC   Granulicella.
OX   NCBI_TaxID=682795 {ECO:0000313|EMBL:AEU37703.1, ECO:0000313|Proteomes:UP000007113};
RN   [1] {ECO:0000313|EMBL:AEU37703.1, ECO:0000313|Proteomes:UP000007113}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1857 / DSM 23137 / MP5ACTX8
RC   {ECO:0000313|Proteomes:UP000007113};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Lu M., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Mikhailova N., Pagani I., Rawat S., Mannisto M.,
RA   Haggblom M., Woyke T.;
RT   "Complete sequence of Granulicella mallensis MP5ACTX8.";
RL   Submitted (NOV-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; CP003130; AEU37703.1; -; Genomic_DNA.
DR   AlphaFoldDB; G8NVN1; -.
DR   STRING; 682795.AciX8_3405; -.
DR   KEGG; gma:AciX8_3405; -.
DR   eggNOG; COG0383; Bacteria.
DR   HOGENOM; CLU_003442_1_2_0; -.
DR   OrthoDB; 9772207at2; -.
DR   Proteomes; UP000007113; Chromosome.
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; cd10789; GH38N_AMII_ER_cytosolic; 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   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:AEU37703.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007113};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..1106
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003512978"
FT   DOMAIN          550..627
FT                   /note="Glycoside hydrolase family 38 central"
FT                   /evidence="ECO:0000259|SMART:SM00872"
SQ   SEQUENCE   1106 AA;  122931 MW;  11B79602088D7ED1 CRC64;
     MRLCVFPLAV LLSAALLPAQ SFTPVRELKN LSPGAVAKLH TLETLDALPA ADWHFHAGDL
     PHGESPALDD SSWPLVHGHS KAPKDAVWYR REIEIPKTLN GYDITGARVW FQFQADANGP
     MPQIIYFNGK RVALGDDLEP IVLFEPAKPG DKILVAVKLL HTVDDKTFRG VTLRIEPSSS
     GQRPDPDDIR VQCIAAANLL PQLKTPRPDL LPKVEAAVEA IDMKALAAAD QTAFDASLRK
     AQGILSELHP MLSEAKVDLA GNAHIDAAWL WPRSETVDAV KRTFSTALQL MNEYPDYTYS
     QSAAQYTEWM AEKYPDINAQ IKQRVKEGRW EIVGGMWIEP DLNMPDGESL VRQLLVGQRY
     FQEQYGVTAR IGWNPDSFGY NWQLPQIYKR SGLDYFVTQK MHWNDTNQLP FRIFWWESPD
     GSKVLTYFPT DYVHDNVNPT RISADFAESA QRNPGTSEML DLYGIGDHGG GPTRAMLEQA
     DHWIEKGKTD AVPAMHYSTA QKYFDDVEHN LNPDSPTWNY DSLAKGYTAP PASAAGAVGL
     PTWKDELYLE FHRGVFTTQA QHKANMRNSE VATLDAEKLA SFAWLDGKTY PAAELTEDWK
     KITFNQFHDL AAGSGIGIIY KDAQRDYTEV FHSDREISDA AINTLSATVD THVSTGVPVM
     VFNAMAWPRS ETVNLNVQLP EDAKSVRLLD AHGQPVPSQV VSQDAATHQF TLIARVKDVP
     SLGYTVLHAE AVTGNAKASA ENDLRLDEKS DAITLSNAHL KLVLDRKTGC ITSLVSLPAN
     TEFLAPKACG NELQTFKDTP KQYDAWNVDP GTFDHYTPIS SVDAVTVLTH GSLRDTIRVT
     RTWQKSHFTQ DISLDAGADQ VEVANDIDWQ EQHVLLKAAF PLAASSAKAT YEIPYGSIER
     PTTRSNSWEK ARFEVPAMRW ADLGDAHQGL SLINDSKYGY DAVDNMLRLT LLRSATWPDP
     DADRGRQRFT YAIYPHAGDW KQALTVHRGF ELNDPLKAQQ VFSHTGTLPT EHSWGTVENA
     NVTLTAVKKA EDSNALVFRM YEWAGKASEV KLHVPRGAQY AVESNLMEKV EGSHLALTGD
     VVTVPIKPYE ILTVQVFYSG SNVATK
//