(data stored in ACNUC7421 zone)

HOGENOM: ACAM1_1_PE1658

ID   ACAM1_1_PE1658                       STANDARD;      PRT;   455 AA.
AC   ACAM1_1_PE1658; B0CBB0;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=tRNA modification GTPase MnmE; EC=3.6.- -;
DE   (ACAM1_1.PE1658).
GN   Name=mnmE; Synonyms=trmE; OrderedLocusNames=AM1_1728;
OS   ACARYOCHLORIS MARINA MBIC11017.
OC   Bacteria; Cyanobacteria; Acaryochloris.
OX   NCBI_TaxID=329726;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ACAM1_1.PE1658.
CC       Acaryochloris marina MBIC11017, complete genome.
CC   -!- ANNOTATIONS ORIGIN:MNME_ACAM1
CC   -!- FUNCTION: Exhibits a very high intrinsic GTPase hydrolysis rate.
CC       Involved in the addition of a carboxymethylaminomethyl (cmnm)
CC       group at the wobble position (U34) of certain tRNAs, forming tRNA-
CC       cmnm(5)s(2)U34 (By similarity).
CC   -!- COFACTOR: Binds 1 potassium ion per subunit (By similarity).
CC   -!- SUBUNIT: Homodimer (By similarity). Heterotetramer of two MnmE and
CC       two MnmG subunits (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the Era/MnmE GTP-binding protein family.
CC       MnmE subfamily.
CC   -!- SIMILARITY: Contains 1 G (guanine nucleotide-binding) domain.
CC   -!- GENE_FAMILY: HOG000200713 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; B0CBB0; -.
DR   EMBL; CP000828; ABW26749.1; -; Genomic_DNA.
DR   RefSeq; YP_001516063.1; NC_009925.1.
DR   ProteinModelPortal; B0CBB0; -.
DR   STRING; B0CBB0; -.
DR   GeneID; 5680544; -.
DR   GenomeReviews; CP000828_GR; AM1_1728.
DR   KEGG; amr:AM1_1728; -.
DR   OMA; PGEFSEQ; -.
DR   ProtClustDB; PRK05291; -.
DR   BioCyc; AMAR329726:AM1_1728-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   GO; GO:0006400; P:tRNA modification; IEA:InterPro.
DR   HAMAP; MF_00379; GTPase_MnmE; 1; -.
DR   InterPro; IPR018948; GTP-bd_TrmE_N.
DR   InterPro; IPR004520; GTPase_TrmE.
DR   InterPro; IPR002917; MMR_HSR1_GTP-bd.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR001806; Small_GTPase.
DR   Gene3D; G3DSA:3.30.1360.120; GTP_bd_TrmE_N; 1.
DR   Pfam; PF01926; MMR_HSR1; 1.
DR   Pfam; PF10396; TrmE_N; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   TIGRFAMs; TIGR00450; MnmE_trmE_thdF; 1.
DR   TIGRFAMs; TIGR00231; Small_GTP; 1.
DR   HOGENOMDNA; ACAM1_1.PE1658; -.
KW   tRNA modification GTPase TrmE;
KW   Complete proteome; Cytoplasm; GTP-binding; Hydrolase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Potassium; tRNA processing.
SQ   SEQUENCE   455 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MKQTTIAAIA TAIVPQQGSI GIVRLSGVEA VSIAKQLFQT PGKQQWESHR VLYGYIQQPL
     TQQIIDEGLL LLMLAPRSYT REDVVEFHCH GGMIAVQQVL EACLQAGAEL AQPGEFTLRA
     FLNGRLDLTQ AEGVADLVGA RSPQAAQAAL AGVQGKLASP IRELRQRCLD TLAEVEARVD
     FEDDLPPLDE AGVQAELQDI HATLQAILAT ADQGELLRNG LTVAIIGRPN VGKSSLLNAW
     CRCDRAIVTD LPGTTRDVVE SQLVVGGIPI QVLDTAGIRE TEDQVEQIGV TRSHQAAQSA
     DLVLLTIDAS VGWTSDDQQL YQAFQDLPLI LIVNKVDLVP QEQVVYPEAI AQVVSTIAAQ
     NQGISELETA ILETVQTQSL KAANLDWAIN QRQAAALQKA QAALEHVQGA IADQLPLDFW
     TIDLRGAIQA LGEITGEDIT ESVLDRIFSR FCIGK
//

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