MNME_NOSS1
ID MNME_NOSS1 Reviewed; 459 AA.
AC Q8YN91;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=tRNA modification GTPase MnmE {ECO:0000255|HAMAP-Rule:MF_00379};
DE EC=3.6.-.- {ECO:0000255|HAMAP-Rule:MF_00379};
GN Name=mnmE {ECO:0000255|HAMAP-Rule:MF_00379};
GN Synonyms=trmE {ECO:0000255|HAMAP-Rule:MF_00379}; OrderedLocusNames=all4677;
OS Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=103690;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT "Complete genomic sequence of the filamentous nitrogen-fixing
RT cyanobacterium Anabaena sp. strain PCC 7120.";
RL DNA Res. 8:205-213(2001).
CC -!- FUNCTION: Exhibits a very high intrinsic GTPase hydrolysis rate.
CC Involved in the addition of a carboxymethylaminomethyl (cmnm) group at
CC the wobble position (U34) of certain tRNAs, forming tRNA-
CC cmnm(5)s(2)U34. {ECO:0000255|HAMAP-Rule:MF_00379}.
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00379};
CC Note=Binds 1 potassium ion per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_00379};
CC -!- SUBUNIT: Homodimer. Heterotetramer of two MnmE and two MnmG subunits.
CC {ECO:0000255|HAMAP-Rule:MF_00379}.
CC -!- INTERACTION:
CC Q8YN91; Q8YN91: mnmE; NbExp=2; IntAct=EBI-15808035, EBI-15808035;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00379}.
CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC GTPase superfamily. TrmE GTPase family. {ECO:0000255|HAMAP-
CC Rule:MF_00379}.
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 EMBL; BA000019; BAB76376.1; -; Genomic_DNA.
DR PIR; AE2390; AE2390.
DR PDB; 3GEH; X-ray; 3.20 A; A=1-459.
DR PDBsum; 3GEH; -.
DR AlphaFoldDB; Q8YN91; -.
DR SMR; Q8YN91; -.
DR DIP; DIP-48421N; -.
DR STRING; 103690.17133814; -.
DR EnsemblBacteria; BAB76376; BAB76376; BAB76376.
DR KEGG; ana:all4677; -.
DR eggNOG; COG0486; Bacteria.
DR OMA; CEIQCHG; -.
DR EvolutionaryTrace; Q8YN91; -.
DR Proteomes; UP000002483; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006400; P:tRNA modification; IEA:UniProtKB-UniRule.
DR CDD; cd04164; trmE; 1.
DR Gene3D; 1.20.120.430; -; 1.
DR Gene3D; 3.30.1360.120; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00379; GTPase_MnmE; 1.
DR InterPro; IPR031168; G_TrmE.
DR InterPro; IPR006073; GTP-bd.
DR InterPro; IPR018948; GTP-bd_TrmE_N.
DR InterPro; IPR004520; GTPase_MnmE.
DR InterPro; IPR027368; MnmE_dom2.
DR InterPro; IPR025867; MnmE_helical.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR027266; TrmE/GcvT_dom1.
DR Pfam; PF01926; MMR_HSR1; 1.
DR Pfam; PF12631; MnmE_helical; 1.
DR Pfam; PF10396; TrmE_N; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00450; mnmE_trmE_thdF; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51709; G_TRME; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; GTP-binding; Hydrolase; Magnesium; Metal-binding;
KW Nucleotide-binding; Potassium; Reference proteome; tRNA processing.
FT CHAIN 1..459
FT /note="tRNA modification GTPase MnmE"
FT /id="PRO_0000188845"
FT DOMAIN 221..380
FT /note="TrmE-type G"
FT BINDING 25
FT /ligand="(6S)-5-formyl-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57457"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00379"
FT BINDING 87
FT /ligand="(6S)-5-formyl-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57457"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00379"
FT BINDING 126
FT /ligand="(6S)-5-formyl-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57457"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00379"
FT BINDING 231..236
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00379"
FT BINDING 231
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00379"
FT BINDING 235
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00379"
FT BINDING 250..256
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00379"
FT BINDING 250
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00379"
FT BINDING 252
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00379"
FT BINDING 255
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00379"
FT BINDING 256
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00379"
FT BINDING 275..278
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00379"
FT BINDING 459
FT /ligand="(6S)-5-formyl-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57457"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00379"
FT STRAND 7..10
FT /evidence="ECO:0007829|PDB:3GEH"
FT STRAND 22..28
FT /evidence="ECO:0007829|PDB:3GEH"
FT HELIX 31..38
FT /evidence="ECO:0007829|PDB:3GEH"
FT STRAND 51..57
FT /evidence="ECO:0007829|PDB:3GEH"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:3GEH"
FT STRAND 67..74
FT /evidence="ECO:0007829|PDB:3GEH"
FT STRAND 79..83
FT /evidence="ECO:0007829|PDB:3GEH"
FT STRAND 85..90
FT /evidence="ECO:0007829|PDB:3GEH"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:3GEH"
FT HELIX 96..106
FT /evidence="ECO:0007829|PDB:3GEH"
FT HELIX 116..123
FT /evidence="ECO:0007829|PDB:3GEH"
FT HELIX 129..140
FT /evidence="ECO:0007829|PDB:3GEH"
FT HELIX 144..155
FT /evidence="ECO:0007829|PDB:3GEH"
FT TURN 156..158
FT /evidence="ECO:0007829|PDB:3GEH"
FT HELIX 159..179
FT /evidence="ECO:0007829|PDB:3GEH"
FT STRAND 182..186
FT /evidence="ECO:0007829|PDB:3GEH"
FT TURN 191..193
FT /evidence="ECO:0007829|PDB:3GEH"
FT HELIX 194..220
FT /evidence="ECO:0007829|PDB:3GEH"
FT STRAND 222..228
FT /evidence="ECO:0007829|PDB:3GEH"
FT HELIX 234..245
FT /evidence="ECO:0007829|PDB:3GEH"
FT HELIX 257..262
FT /evidence="ECO:0007829|PDB:3GEH"
FT STRAND 263..266
FT /evidence="ECO:0007829|PDB:3GEH"
FT STRAND 269..273
FT /evidence="ECO:0007829|PDB:3GEH"
FT STRAND 302..309
FT /evidence="ECO:0007829|PDB:3GEH"
FT TURN 310..312
FT /evidence="ECO:0007829|PDB:3GEH"
FT HELIX 316..325
FT /evidence="ECO:0007829|PDB:3GEH"
FT STRAND 330..335
FT /evidence="ECO:0007829|PDB:3GEH"
FT HELIX 342..344
FT /evidence="ECO:0007829|PDB:3GEH"
FT STRAND 357..361
FT /evidence="ECO:0007829|PDB:3GEH"
FT TURN 362..365
FT /evidence="ECO:0007829|PDB:3GEH"
FT HELIX 368..379
FT /evidence="ECO:0007829|PDB:3GEH"
FT STRAND 382..386
FT /evidence="ECO:0007829|PDB:3GEH"
FT HELIX 395..414
FT /evidence="ECO:0007829|PDB:3GEH"
FT TURN 415..418
FT /evidence="ECO:0007829|PDB:3GEH"
FT HELIX 421..423
FT /evidence="ECO:0007829|PDB:3GEH"
FT HELIX 425..439
FT /evidence="ECO:0007829|PDB:3GEH"
FT STRAND 440..442
FT /evidence="ECO:0007829|PDB:3GEH"
FT HELIX 445..453
FT /evidence="ECO:0007829|PDB:3GEH"
SQ SEQUENCE 459 AA; 49783 MW; 655CB9FADC159F66 CRC64;
MAITGTIAAI ATAIVPQQGS VGIVRVSGSQ AIAIAQTLFD APGKQVWESH RILYGYIRHP
QTRQIVDEAL LLLMKAPRSY TREDVVEFHC HGGIIAVQQV LQLCLESGAR LAQPGEFTLR
AFLNGRLDLT QAESIADLVG ARSPQAAQTA LAGLQGKLAH PIRQLRANCL DILAEIEARI
DFEEDLPPLD DEAIISDIEN IAAEISQLLA TKDKGELLRT GLKVAIVGRP NVGKSSLLNA
WSQSDRAIVT DLPGTTRDVV ESQLVVGGIP VQVLDTAGIR ETSDQVEKIG VERSRQAANT
ADLVLLTIDA ATGWTTGDQE IYEQVKHRPL ILVMNKIDLV EKQLITSLEY PENITQIVHT
AAAQKQGIDS LETAILEIVQ TGKVQAADMD LAINQRQAAA LTQAKMSLEQ VQATITQQLP
LDFWTIDLRG AIQALGEITG EEVTESVLDR IFSRFCIGK
