ID J4GTU9_9APHY Unreviewed; 606 AA.
AC J4GTU9;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=GS catalytic domain-containing protein {ECO:0000259|PROSITE:PS51987};
GN ORFNames=FIBRA_06908 {ECO:0000313|EMBL:CCM04720.1};
OS Fibroporia radiculosa.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Fibroporiaceae; Fibroporia.
OX NCBI_TaxID=599839 {ECO:0000313|EMBL:CCM04720.1, ECO:0000313|Proteomes:UP000006352};
RN [1] {ECO:0000313|EMBL:CCM04720.1, ECO:0000313|Proteomes:UP000006352}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TFFH 294 {ECO:0000313|EMBL:CCM04720.1,
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 SKP1 family.
CC {ECO:0000256|ARBA:ARBA00009993}.
CC -!- SIMILARITY: Belongs to the glutamine synthetase family.
CC {ECO:0000256|PROSITE-ProRule:PRU01331, ECO:0000256|RuleBase:RU000384}.
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DR EMBL; HE797165; CCM04720.1; -; Genomic_DNA.
DR RefSeq; XP_012184003.1; XM_012328613.1.
DR AlphaFoldDB; J4GTU9; -.
DR STRING; 599839.J4GTU9; -.
DR GeneID; 24099631; -.
DR HOGENOM; CLU_017290_0_1_1; -.
DR InParanoid; J4GTU9; -.
DR OrthoDB; 2783297at2759; -.
DR Proteomes; UP000006352; Unassembled WGS sequence.
DR GO; GO:0004356; F:glutamine synthetase activity; IEA:InterPro.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR Gene3D; 3.30.590.10; Glutamine synthetase/guanido kinase, catalytic domain; 1.
DR InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR InterPro; IPR008146; Gln_synth_cat_dom.
DR InterPro; IPR001232; SKP1-like.
DR InterPro; IPR036296; SKP1-like_dim_sf.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR016072; Skp1_comp_dimer.
DR PANTHER; PTHR43785; GAMMA-GLUTAMYLPUTRESCINE SYNTHETASE; 1.
DR PANTHER; PTHR43785:SF15; TYPE-1 GLUTAMINE SYNTHETASE 2; 1.
DR Pfam; PF00120; Gln-synt_C; 1.
DR Pfam; PF01466; Skp1; 1.
DR SMART; SM01230; Gln-synt_C; 1.
DR SMART; SM00512; Skp1; 1.
DR SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 1.
DR SUPFAM; SSF81382; Skp1 dimerisation domain-like; 1.
DR PROSITE; PS51987; GS_CATALYTIC; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000006352}.
FT DOMAIN 130..527
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
SQ SEQUENCE 606 AA; 67595 MW; 31C81D0A1342CC79 CRC64;
MVKTSDARAT ENAPNSIEQL NDLLKDDTKV KVAGIDVDGL LRGKFMSKEK FMSAASSDGF
GFCSVIFGWD MHDTVYSREL LISNRANGYR DILASIDLST YRRIPWENNV PFFLVSFLDP
ETKEPICADP RGVLKKVVES ADKQGWQCYA GCEYEVGTAI FRNVRRYVFL TSSVAIFQYF
QFKETPHTLA EKNFNSLQPL TSGMHGYSLL RTQLNNNYFH DIFDESLNFG VPLEGHHTET
GPGVYETALA YTMASRMADN AILFKYLVKS VGMKHGIVPS FMAKPWGNLP GCSGHIHVSL
RDRNGKSIFA VSDAELGIGR RNAAYPDTKF ISQEAEWFLA GVLEGLPDVM PLLVPTINGY
KRLVGGEAFW APNAVTYGYD SRAASVRILS PPSVPPYATR MEIRVPGADM NPYFAMSAIF
ALGMRGIAKE LQLSGPPVSQ LTLEDKKNGR VQMLPQSLES ATERMMRSDS IAREEAVFGQ
DFVDHFGGTR QHEVRLWNEA VTSWEGTASA EQELPLAAIH SSVFAKILEY CILYRGRPTD
EGAVRRDDEW DQSFITNLGS TDAFFDIIMA ANFLNFKPLL DLGCRRVAKM IQGKTPSEIR
ALMNIL
//
