ID A0A0P7Z5S7_SCLFO Unreviewed; 455 AA.
AC A0A0P7Z5S7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Lengsin {ECO:0000256|ARBA:ARBA00039404};
DE AltName: Full=Glutamate-ammonia ligase domain-containing protein 1 {ECO:0000256|ARBA:ARBA00042675};
GN ORFNames=Z043_104708 {ECO:0000313|EMBL:KPP75989.1};
OS Scleropages formosus (Asian bonytongue) (Osteoglossum formosum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Osteoglossidae; Scleropages.
OX NCBI_TaxID=113540 {ECO:0000313|EMBL:KPP75989.1, ECO:0000313|Proteomes:UP000034805};
RN [1] {ECO:0000313|EMBL:KPP75989.1, ECO:0000313|Proteomes:UP000034805}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Aro1 {ECO:0000313|EMBL:KPP75989.1};
RA Tan M.H., Gan H.M., Croft L.J., Austin C.M.;
RT "The genome of the Asian arowana (Scleropages formosus).";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May act as a component of the cytoskeleton or as a chaperone
CC for the reorganization of intermediate filament proteins during
CC terminal differentiation in the lens. Does not seem to have enzymatic
CC activity. {ECO:0000256|ARBA:ARBA00037583}.
CC -!- SUBUNIT: Dodecamer. Interacts with BFSP2 and VIM.
CC {ECO:0000256|ARBA:ARBA00038790}.
CC -!- SIMILARITY: Belongs to the glutamine synthetase family.
CC {ECO:0000256|ARBA:ARBA00009897, ECO:0000256|PROSITE-ProRule:PRU01330,
CC ECO:0000256|RuleBase:RU000384}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPP75989.1}.
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DR EMBL; JARO02001267; KPP75989.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P7Z5S7; -.
DR STRING; 113540.ENSSFOP00015039224; -.
DR Proteomes; UP000034805; Unassembled WGS sequence.
DR GO; GO:0004356; F:glutamine synthetase activity; IEA:InterPro.
DR GO; GO:0006542; P:glutamine biosynthetic process; IEA:InterPro.
DR Gene3D; 3.10.20.70; Glutamine synthetase, N-terminal domain; 1.
DR Gene3D; 3.30.590.10; Glutamine synthetase/guanido kinase, catalytic domain; 1.
DR InterPro; IPR008147; Gln_synt_N.
DR InterPro; IPR036651; Gln_synt_N_sf.
DR InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR InterPro; IPR008146; Gln_synth_cat_dom.
DR PANTHER; PTHR43407; GLUTAMINE SYNTHETASE; 1.
DR PANTHER; PTHR43407:SF1; LENGSIN; 1.
DR Pfam; PF00120; Gln-synt_C; 1.
DR SMART; SM01230; Gln-synt_C; 1.
DR SUPFAM; SSF54368; Glutamine synthetase, N-terminal domain; 1.
DR SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 1.
DR PROSITE; PS51986; GS_BETA_GRASP; 1.
DR PROSITE; PS51987; GS_CATALYTIC; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000034805}.
FT DOMAIN 34..128
FT /note="GS beta-grasp"
FT /evidence="ECO:0000259|PROSITE:PS51986"
FT DOMAIN 135..455
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
SQ SEQUENCE 455 AA; 50463 MW; 469FEC29E6F83A5D CRC64;
MDSGNIPNAD THGPYSFSNY TSAIEHIKQK ITREEIGFVR FEATDLHGVS RSKMVPARYF
QEKAMHGIAI PRNYLELTLS PKDNEVDHIN AANFNSDVLL MPDLSTFRAL PWASQTARVI
CDSCSVTGNP LRTSPRLVAK QLLRSLHNLG FSLQSSFTYE CCVFGAPEKI NPKMFFFPGA
TLMSNDLSFF QQLINSMYFM GTDVESFASA NGPGQMEISF QPEFGICAAD SAFTFRTGIK
ELARKQGYIA SFFTDDGFYN SGIFSHSVWD ASGRRNLFFS AGGELSEIGK KWLAGLVHHS
AALSCFMAPG VSCRRRLAKA AKEPKHTIYA TWGCNDNSCN FNIKSHGSRG MHIENRLGSA
MANPYLVLAV TLAAGIDGIK QNLSVDADHT GNLIQQKKVV IPVKLEDALT ALDEDDIIKG
ALGDTFVQYF IAMKKYEIET EELDTERNKC LEYFI
//
