ID S5SQA9_9PROT Unreviewed; 465 AA.
AC S5SQA9;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B {ECO:0000313|EMBL:AGS33274.1};
DE EC=6.3.5.6 {ECO:0000313|EMBL:AGS33274.1};
GN Name=gatB {ECO:0000313|EMBL:AGS33274.1};
GN ORFNames=NASALF_145 {ECO:0000313|EMBL:AGS33274.1};
OS Candidatus Nasuia deltocephalinicola str. NAS-ALF.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nasuia.
OX NCBI_TaxID=1343077 {ECO:0000313|EMBL:AGS33274.1, ECO:0000313|Proteomes:UP000015382};
RN [1] {ECO:0000313|EMBL:AGS33274.1, ECO:0000313|Proteomes:UP000015382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NAS-ALF {ECO:0000313|Proteomes:UP000015382};
RX PubMed=23918810; DOI=10.1093/gbe/evt118;
RA Bennett G.M., Moran N.A.;
RT "Small, smaller, smallest: the origins and evolution of ancient dual
RT symbioses in a Phloem-feeding insect.";
RL Genome Biol. Evol. 5:1675-1688(2013).
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DR EMBL; CP006059; AGS33274.1; -; Genomic_DNA.
DR AlphaFoldDB; S5SQA9; -.
DR KEGG; ndl:NASALF_145; -.
DR PATRIC; fig|1343077.3.peg.156; -.
DR HOGENOM; CLU_587532_0_0_4; -.
DR OrthoDB; 9804078at2; -.
DR Proteomes; UP000015382; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0050566; F:asparaginyl-tRNA synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
DR InterPro; IPR017959; Asn/Gln-tRNA_amidoTrfase_suB/E.
DR InterPro; IPR006075; Asn/Gln-tRNA_Trfase_suB/E_cat.
DR InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR PANTHER; PTHR11659; GLUTAMYL-TRNA GLN AMIDOTRANSFERASE SUBUNIT B MITOCHONDRIAL AND PROKARYOTIC PET112-RELATED; 1.
DR PANTHER; PTHR11659:SF0; GLUTAMYL-TRNA(GLN) AMIDOTRANSFERASE SUBUNIT B, MITOCHONDRIAL; 1.
DR Pfam; PF02934; GatB_N; 1.
DR SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:AGS33274.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000015382};
KW Transferase {ECO:0000313|EMBL:AGS33274.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 62..80
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 101..119
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 167..185
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 315..333
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 354..370
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 382..401
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 416..433
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 9..284
FT /note="Aspartyl/Glutamyl-tRNA(Gln) amidotransferase subunit
FT B/E catalytic"
FT /evidence="ECO:0000259|Pfam:PF02934"
SQ SEQUENCE 465 AA; 57915 MW; AE4E78EDA34F0AB9 CRC64;
MILRVIFLFG LECHYSIKFF RKIFNFLKIY KHKNFINNTI SYTDMGLAGI LPNFNLYFFK
KIVIFGFFLK SYLFYFSYFI RKSYFYPDIP KNYQISNLKS IFNFGLIIIY NNFILNSYYK
FIKINKIHIE EDAAKTFYNL KNNFLIIDFN RSNSFLLEIV SYYNLNSFYE ILLFLKNLNY
FLFFLKKKII KNFFRFDFNI SIKYLFYNYT IFKIEIKNIN SFFILKNIIN FEIKRQIYSL
IFIKFYKNET RFYNLIKKFT YFVRNKENFF NYRYFNEIDK NYLYLSLNFK KNFKLKILLF
FYIKIYYFYN FELILKYNFI LIEIILFIFK FKSSKVIFLF KNKIINYFIF KKKYNLTSIF
SLIILLKCYL NKILNLFNFK KILFFIFFKI LKNNLFIYNI IIKNNIFLIK NNIKKFLNYI
ILIYIKFIHI FIFNKKIFNF FMGIIIRLNI NFKKFFNSLN TKIII
//
