ID A0A016UIR9_9BILA Unreviewed; 304 AA.
AC A0A016UIR9;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Gtr1/RagA G protein region {ECO:0008006|Google:ProtNLM};
GN Name=Acey_s0039.g128 {ECO:0000313|EMBL:EYC14742.1};
GN Synonyms=Acey-ragc-1 {ECO:0000313|EMBL:EYC14742.1};
GN ORFNames=Y032_0039g128 {ECO:0000313|EMBL:EYC14742.1};
OS Ancylostoma ceylanicum.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=53326 {ECO:0000313|EMBL:EYC14742.1, ECO:0000313|Proteomes:UP000024635};
RN [1] {ECO:0000313|Proteomes:UP000024635}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX PubMed=25730766; DOI=10.1038/ng.3237;
RA Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA Aroian R.V.;
RT "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT ceylanicum identify infection-specific gene families.";
RL Nat. Genet. 47:416-422(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC Evidence={ECO:0000256|ARBA:ARBA00001702};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000256|ARBA:ARBA00001702};
CC -!- SIMILARITY: Belongs to the GTR/RAG GTP-binding protein family.
CC {ECO:0000256|ARBA:ARBA00007756, ECO:0000256|RuleBase:RU367014}.
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:EYC14742.1}.
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DR EMBL; JARK01001375; EYC14742.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A016UIR9; -.
DR Proteomes; UP000024635; Unassembled WGS sequence.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR CDD; cd11385; RagC_like; 1.
DR Gene3D; 3.30.450.190; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR006762; Gtr1_RagA.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR039400; RagC/D.
DR PANTHER; PTHR11259:SF2; GH16429P; 1.
DR PANTHER; PTHR11259; RAS-RELATED GTP BINDING RAG/GTR YEAST; 1.
DR Pfam; PF04670; Gtr1_RagA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|RuleBase:RU367014};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU367014};
KW Reference proteome {ECO:0000313|Proteomes:UP000024635}.
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 304 AA; 34170 MW; 29FB06638104A7B3 CRC64;
MSTFYEEDDG DATDYSYGLD DNSDGEARPT VVLMGQKRSG KTSIRKVVFQ KMSPNETLFV
ESTARVTKDV IASSFINFET LEFPGQMDPF DSSLDPVATF KRCGALLFIV DAQDEYVDSL
KKMSENFTHA FRINPNIKFE VFIHKADGLT EESRVDAQYD IYHRVKCELA EQGLEDFNVT
FHLTSIYDHS IFEAFSKVVQ NLVKRLPTLE RLLDIFNQGS NVEKSFLFDV ASKIYIATDT
TPVEMAAYEL CCDMIDVTID ISGIYGLPTT LYNPRKPISC HAESSTLSMS LGDTDPNVLF
MGGL
//
