ID A0A091N1S0_9PASS Unreviewed; 374 AA.
AC A0A091N1S0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Glutathione S-transferase LANCL1 {ECO:0000256|ARBA:ARBA00039457};
DE EC=2.5.1.18 {ECO:0000256|ARBA:ARBA00012452};
DE AltName: Full=LanC-like protein 1 {ECO:0000256|ARBA:ARBA00043169};
DE Flags: Fragment;
GN ORFNames=N310_13957 {ECO:0000313|EMBL:KFP82892.1};
OS Acanthisitta chloris (rifleman).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Acanthisittidae;
OC Acanthisitta.
OX NCBI_TaxID=57068 {ECO:0000313|EMBL:KFP82892.1, ECO:0000313|Proteomes:UP000053537};
RN [1] {ECO:0000313|EMBL:KFP82892.1, ECO:0000313|Proteomes:UP000053537}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N310 {ECO:0000313|EMBL:KFP82892.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-chloro-2,4-dinitrobenzene + glutathione = 2,4-dinitrophenyl-
CC S-glutathione + chloride + H(+); Xref=Rhea:RHEA:51220,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17996, ChEBI:CHEBI:34718,
CC ChEBI:CHEBI:57925, ChEBI:CHEBI:133977; EC=2.5.1.18;
CC Evidence={ECO:0000256|ARBA:ARBA00035808};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glutathione + RX = a halide anion + an S-substituted
CC glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:90779; EC=2.5.1.18;
CC Evidence={ECO:0000256|ARBA:ARBA00000710};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004202};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004202}. Cytoplasm
CC {ECO:0000256|ARBA:ARBA00004496}. Membrane
CC {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004170}.
CC -!- SIMILARITY: Belongs to the LanC-like protein family.
CC {ECO:0000256|ARBA:ARBA00007179}.
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DR EMBL; KK840251; KFP82892.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091N1S0; -.
DR Proteomes; UP000053537; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0031179; P:peptide modification; IEA:InterPro.
DR CDD; cd04794; euk_LANCL; 1.
DR Gene3D; 1.50.10.10; -; 1.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR007822; LANC-like.
DR InterPro; IPR020464; LanC-like_prot_euk.
DR PANTHER; PTHR12736:SF5; GLUTATHIONE S-TRANSFERASE LANCL1; 1.
DR PANTHER; PTHR12736; LANC-LIKE PROTEIN; 1.
DR Pfam; PF05147; LANC_like; 1.
DR PRINTS; PR01951; LANCEUKARYTE.
DR PRINTS; PR01950; LANCSUPER.
DR SMART; SM01260; LANC_like; 1.
DR SUPFAM; SSF158745; LanC-like; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00022475};
KW Reference proteome {ECO:0000313|Proteomes:UP000053537};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP82892.1"
FT NON_TER 374
FT /evidence="ECO:0000313|EMBL:KFP82892.1"
SQ SEQUENCE 374 AA; 42187 MW; D852A706AB82885A CRC64;
QLSPEFTQRL NNTIRELLQQ VERGLKSADP HDCTVLYVPF AGIALLYLHL YDVFEDPAYL
QVAYEYVKKS LSCLTRRSIT FLCGDAGPLA VAAVVYHKLN NHKQAEDCIT RLLHLHKADP
RVPDELLYGR MGYVSALIFV NKHFGGEKIP QSHIQQVCEA VIASGESLAK KRNFTAKSPL
MYEWYQEYYV GAAHGLAGIY YYLMQPCLGV SQGKLHNTVK PSVDYVCQLK FPSGNYPPCI
GDTRDLLVHW CHGAPGVIYM LLQAYKVFGE QQYLSDALQC AEVIWQYGLL KKGYGLCHGT
AGNAYSFLAL YNLTQNMKYL YRACKFAEWC LSYGQHGCRT PDTPFSLFEG MAGTIYFLAD
LLVPTKAKFP AFEL
//
