RABL_MIMIV
ID RABL_MIMIV Reviewed; 215 AA.
AC Q5UQ27;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Probable Rab-related GTPase;
DE Flags: Precursor;
GN OrderedLocusNames=MIMI_R214;
OS Acanthamoeba polyphaga mimivirus (APMV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC Imitervirales; Mimiviridae; Mimivirus.
OX NCBI_TaxID=212035;
OH NCBI_TaxID=5757; Acanthamoeba polyphaga (Amoeba).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rowbotham-Bradford;
RX PubMed=15486256; DOI=10.1126/science.1101485;
RA Raoult D., Audic S., Robert C., Abergel C., Renesto P., Ogata H.,
RA La Scola B., Susan M., Claverie J.-M.;
RT "The 1.2-megabase genome sequence of Mimivirus.";
RL Science 306:1344-1350(2004).
CC -!- FUNCTION: May be involved in protein transport.
CC -!- SUBCELLULAR LOCATION: Host cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; AY653733; AAV50487.1; -; Genomic_DNA.
DR PDB; 5XC3; X-ray; 1.50 A; A=9-184.
DR PDB; 5XC5; X-ray; 1.40 A; A=9-184.
DR PDBsum; 5XC3; -.
DR PDBsum; 5XC5; -.
DR SMR; Q5UQ27; -.
DR Proteomes; UP000001134; Genome.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR Pfam; PF00071; Ras; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51419; RAB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; GTP-binding; Host cell membrane; Host membrane; Lipoprotein;
KW Membrane; Methylation; Nucleotide-binding; Prenylation; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..212
FT /note="Probable Rab-related GTPase"
FT /id="PRO_0000121331"
FT PROPEP 213..215
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000370840"
FT MOTIF 42..50
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 20..27
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 69..73
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 127..130
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 212
FT /note="Cysteine methyl ester; by host"
FT /evidence="ECO:0000255"
FT LIPID 211
FT /note="S-geranylgeranyl cysteine; by host"
FT /evidence="ECO:0000250"
FT LIPID 212
FT /note="S-geranylgeranyl cysteine; by host"
FT /evidence="ECO:0000250"
FT STRAND 14..21
FT /evidence="ECO:0007829|PDB:5XC5"
FT HELIX 26..34
FT /evidence="ECO:0007829|PDB:5XC5"
FT STRAND 49..56
FT /evidence="ECO:0007829|PDB:5XC5"
FT STRAND 62..69
FT /evidence="ECO:0007829|PDB:5XC5"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:5XC5"
FT HELIX 77..80
FT /evidence="ECO:0007829|PDB:5XC5"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:5XC5"
FT STRAND 88..95
FT /evidence="ECO:0007829|PDB:5XC5"
FT HELIX 99..115
FT /evidence="ECO:0007829|PDB:5XC5"
FT STRAND 121..127
FT /evidence="ECO:0007829|PDB:5XC5"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:5XC5"
FT HELIX 140..149
FT /evidence="ECO:0007829|PDB:5XC5"
FT STRAND 153..156
FT /evidence="ECO:0007829|PDB:5XC5"
FT HELIX 162..177
FT /evidence="ECO:0007829|PDB:5XC5"
SQ SEQUENCE 215 AA; 24732 MW; B5325702EDC2E6F2 CRC64;
MNSYIKEKME NNGYKIILIG SSGVGKSSIV HQFLFNRKIS NVSPTIGAAF ASKQVIAKNG
KTLKLNIWDT AGQERFRSIT KMYYTNSLGC LVVFDVTDRE SFDDVYYWIN DLRINCHTTY
YILVVANKID IDKNNWRVSE NEIKKFCRDN DCDYVFASSF ESDTVNNLFG KMIDKMSEIK
INPDSRRNDI IYLSDKSSGI DDFIDKISQN CCYIS