ID A0A3B3S2T0_9TELE Unreviewed; 589 AA.
AC A0A3B3S2T0;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Immune-associated nucleotide-binding protein 3-like {ECO:0000313|Ensembl:ENSPKIP00000024440.1};
OS Paramormyrops kingsleyae.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000024440.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000024440.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC GTPase superfamily. AIG1/Toc34/Toc159-like paraseptin GTPase family.
CC IAN subfamily. {ECO:0000256|ARBA:ARBA00008535}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A3B3S2T0; -.
DR STRING; 1676925.ENSPKIP00000024440; -.
DR Ensembl; ENSPKIT00000005147.1; ENSPKIP00000024440.1; ENSPKIG00000007702.1.
DR GeneTree; ENSGT01100000263538; -.
DR OrthoDB; 4263631at2759; -.
DR Proteomes; UP000261540; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR CDD; cd01852; AIG1; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR006703; G_AIG1.
DR InterPro; IPR045058; GIMA/IAN/Toc.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR10903:SF180; GTPASE IMAP FAMILY MEMBER 5; 1.
DR PANTHER; PTHR10903; GTPASE, IMAP FAMILY MEMBER-RELATED; 1.
DR Pfam; PF04548; AIG1; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51720; G_AIG1; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 349..368
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 374..393
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 400..420
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 440..462
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 49..263
FT /note="AIG1-type G"
FT /evidence="ECO:0000259|PROSITE:PS51720"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 569..589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 259..286
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 14..46
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..589
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 589 AA; 61723 MW; D91A1285CD5A5CE9 CRC64;
MDMQALLSGE GDTLEVMCDR DGERRKEREP SQEDNKTGTD TEDNDEPIMT ELRLVLIGKT
GSGKSSSGNT ILGQKHFLSK LSASSVTQTC EQGILEYGGE EKERGGGRQR RKRVVVVDMP
GFGDTRFDAE HIRTEIAKCV AQMAPGPHAF LVVIQLGRYT EDEARAVKEV EQIFGEQAVL
NHSVIVFTRG DDLEEMDIEE YLRDTAPEDL KSLLERCGSR YHVLNNRKPE DREQVWGLLE
KVKRMVEVNG GGCYTDNVFQ EAEAVIREEQ ERLMNEREAA KAMEGLFMDG AKRRKYDLKA
VTPDSGEERQ EQWKRRKGAK SQMVSLDSAV WGFRKEAIHS AKVLDKIKIL VAAAATGVVV
GAVCGAAVPL AVAAGAALVG QAVGMGGAIG TVVAATSGTA VMTVGSAMGV VLGGSVGALV
GADAETPLDA SVEALRQVGV MGATAVGVAA GVGVVLGAGA ALGACGTAVS STAPVAAEGV
CAVGVANSTV AQAVGSVEMT GPLMVAEGAQ AVGVVGPMGA DMAAAGGRVA TGFDRIISAA
TEIGKVATGI AVAGGLVVKV VKEKVRQRAG PSESSTVEKM SWEFSWNKK
//