ID   J4G5E8_9APHY            Unreviewed;      1180 AA.
AC   J4G5E8;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=GS catalytic domain-containing protein {ECO:0000259|PROSITE:PS51987};
GN   ORFNames=FIBRA_03423 {ECO:0000313|EMBL:CCM01373.1};
OS   Fibroporia radiculosa.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Fibroporiaceae; Fibroporia.
OX   NCBI_TaxID=599839 {ECO:0000313|EMBL:CCM01373.1, ECO:0000313|Proteomes:UP000006352};
RN   [1] {ECO:0000313|EMBL:CCM01373.1, ECO:0000313|Proteomes:UP000006352}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TFFH 294 {ECO:0000313|EMBL:CCM01373.1,
RC   ECO:0000313|Proteomes:UP000006352};
RX   PubMed=22247176; DOI=10.1128/AEM.06745-11;
RA   Tang J.D., Perkins A.D., Sonstegard T.S., Schroeder S.G., Burgess S.C.,
RA   Diehl S.V.;
RT   "Short-read sequencing for genomic analysis of the brown rot fungus
RT   Fibroporia radiculosa.";
RL   Appl. Environ. Microbiol. 78:2272-2281(2012).
CC   -!- SIMILARITY: Belongs to the glutamine synthetase family.
CC       {ECO:0000256|PROSITE-ProRule:PRU01331, ECO:0000256|RuleBase:RU000384}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC       {ECO:0000256|ARBA:ARBA00005641}.
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DR   EMBL; HE797030; CCM01373.1; -; Genomic_DNA.
DR   RefSeq; XP_012180656.1; XM_012325266.1.
DR   AlphaFoldDB; J4G5E8; -.
DR   STRING; 599839.J4G5E8; -.
DR   GeneID; 24096284; -.
DR   HOGENOM; CLU_273107_0_0_1; -.
DR   InParanoid; J4G5E8; -.
DR   OrthoDB; 69117at2759; -.
DR   Proteomes; UP000006352; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004356; F:glutamine synthetase activity; IEA:InterPro.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:1901136; P:carbohydrate derivative catabolic process; IEA:UniProt.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProt.
DR   GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR   Gene3D; 3.30.590.10; Glutamine synthetase/guanido kinase, catalytic domain; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 2.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR041036; GH5_C.
DR   InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR   InterPro; IPR008146; Gln_synth_cat_dom.
DR   InterPro; IPR001547; Glyco_hydro_5.
DR   InterPro; IPR018087; Glyco_hydro_5_CS.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR31308; -; 1.
DR   PANTHER; PTHR31308:SF1; PROTEIN, PUTATIVE-RELATED; 1.
DR   Pfam; PF00150; Cellulase; 1.
DR   Pfam; PF00120; Gln-synt_C; 1.
DR   Pfam; PF18564; Glyco_hydro_5_C; 1.
DR   SMART; SM01230; Gln-synt_C; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 1.
DR   PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
DR   PROSITE; PS51987; GS_CATALYTIC; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006352};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        1155..1175
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          143..497
FT                   /note="GS catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51987"
SQ   SEQUENCE   1180 AA;  130602 MW;  CBB044926437E364 CRC64;
     MSTKSTLAYG VRYTPDSPAN PVDALISSAA RVLFQTIHSY SCRYVRVQWV DLINTARFRV
     LPLQHFQKLF TAERAGVCLT HATLGLVGPG ITPGFSGTGE YLLVIDPASV RPCVFAPEHA
     VVMGWIQEKV PSPSTGIVCD LCPRTMLNRI VADAQQRAGL KFLAGFESEF ILLSETSPRP
     VFVNHADWST SAKLLAGRKE TVVLEEIVDA LMGAGIEVQM YHAEAAPGQY EIVTGPLPPL
     ESADAIVHTR ETIRNVASKH GLHATFAPRL HSDNCGSGAH MHLSMHSAMP KALRASDASR
     GPTLTPTERS FLQTLLAHLP SLCALMLPTA ASYARVEDGI WSGGTYSCWG TDNKEAPVRL
     CGPGGEHHLE LKCVDGTANP YLVLAGVLAA GMRGVAEGAL LTVGDCEVPV ALMNDEERKA
     VGLQNPGRLP RTIKDARELL RKDDHLRGVL GENFVAKFTA VNEVLEAHLQ AESAEATVAR
     LVGPTNHNHD TFPANHAAVT FVGRPFPLEE APEHFSRLRR WGLTFIRFLL TWEAVEHAGP
     GIYDMEYLDY VRELLSVLPQ YGITAFVVMH QDVWSRYSGG SGSPAWTLET VGFDLHGLEE
     PGAAWLKGVK GGGHVEEERG LWPCGYQKLA AATMATCFWA GDTFAPKLKV KDANGKEISI
     QAFLQNAFLN MWEVVAKTLG DLEGVLGFEM MNEPHRGYVE LQSMHAFDYN TDLHLGHVPT
     AFQSFTLGAG HPTEIGFWTR SFPMPTRLTS KGVLNTARQR AWRDNGPTQG KCLWEMHGVW
     GWDKIKDEGV VLRESYFTKD PVSGRKVDWY TDFYFPFVKT WTDRVRSASS PNMIVFIEPI
     PNEFCPTSWT PERRPTDMAF APHWYDLNAL FAKAFGDFTV NVQGLSRGMF PLKAFYWGHQ
     GARDNFSLQI RNLVEAGYRS LGETPVIIGE CGIPMDMNKG ESFQTDRWTW QTRMMDAMVT
     ALEQSLVGFT LWNYNPDNDD TRGDDWNGEN FSWYSRRRGL PASWLDFKQT SATLDNGARI
     LRATVRPYPA KTAGIPLKFD YEMNTGRFTF EWVVPSDLSK KGSGASASVQ QPPVAGHPAL
     TSKDTEIFMP SMLARERQIV IEGLGQDDRY RYDEQRQTLT VTTGALTPGQ VHRIVVSLKP
     PLKASFEVNS FWDDFGGHIL GAAVVISSLL IYILLSNISV
//