ID A0A183MGG0_9TREM Unreviewed; 507 AA.
AC A0A183MGG0;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Lengsin {ECO:0000256|ARBA:ARBA00039404};
DE AltName: Full=Glutamate-ammonia ligase domain-containing protein 1 {ECO:0000256|ARBA:ARBA00042675};
GN ORFNames=SMRZ_LOCUS15135 {ECO:0000313|EMBL:VDP17558.1};
OS Schistosoma margrebowiei.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=48269 {ECO:0000313|WBParaSite:SMRZ_0001513601-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:SMRZ_0001513601-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDP17558.1, ECO:0000313|Proteomes:UP000277204}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Zambia {ECO:0000313|EMBL:VDP17558.1,
RC ECO:0000313|Proteomes:UP000277204};
RG Pathogen Informatics;
RL Submitted (NOV-2018) 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:PRU01331,
CC ECO:0000256|RuleBase:RU000384}.
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DR EMBL; UZAI01016881; VDP17558.1; -; Genomic_DNA.
DR STRING; 48269.A0A183MGG0; -.
DR WBParaSite; SMRG1_8900.1; SMRG1_8900.1; SMRG1_8900.
DR WBParaSite; SMRZ_0001513601-mRNA-1; SMRZ_0001513601-mRNA-1; SMRZ_0001513601.
DR Proteomes; UP000050790; Unassembled WGS sequence.
DR Proteomes; UP000277204; Unassembled WGS sequence.
DR GO; GO:0004356; F:glutamine synthetase activity; IEA:InterPro.
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 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; SSF55931; Glutamine synthetase/guanido kinase; 1.
DR PROSITE; PS51987; GS_CATALYTIC; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000277204}.
FT DOMAIN 149..507
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
FT REGION 417..438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 507 AA; 57925 MW; 631A303EB6678649 CRC64;
MDSNSNNKDE TLKMDDVKER FIEEVEKFDY IRLSFPDLNG IHLSKLLSTR FARKIAKGES
EVYSGAITGG PRGEVFDVPE IIKRKHVNSK LKPDFPTLHP CYWISNGKAQ HSHNNNTDND
DNPRTRKYSI CAVLCDLAWP NNEPMKTHPR VAVKKLIDEL QTKYNLRLFS AFEPEFRAFQ
KGTFETTCLK PTKTGETNLR SFKLPVPYTK FGDIYRTSLL SVYEDFFIDI DHNMKLANID
IQDYSNEDGE GQLESPLVPS WGLSAADNYF ILKQAIKEIG EKHNMEISFM TKPLLNASSS
GCHYNHSLWY ADTGRNAFYD NADPDGLSVT ARHWIGGLIE HLPAMLAICS PTINCYRRLN
KFFAPGAVNW DFRDRFVAIR VKNFDEKNTY IENRIPSSAS CPYHVLAATL AAGMDGLDRQ
LEPPPPGQKP SESKNGNHVK LLPSSFQEAL QNLKEDEIFT KKLGKDFFEW YTLVKELGDL
GSLGHLDIKD NQEETLAFER YEYLKFT
//
