(data stored in SCRATCH zone)

SWISSPROT: D5EA33_METMS

ID   D5EA33_METMS            Unreviewed;       330 AA.
AC   D5EA33;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   11-DEC-2019, entry version 64.
DE   RecName: Full=tRNA N6-adenosine threonylcarbamoyltransferase {ECO:0000256|HAMAP-Rule:MF_01446};
DE            EC=2.3.1.234 {ECO:0000256|HAMAP-Rule:MF_01446};
DE   AltName: Full=N6-L-threonylcarbamoyladenine synthase {ECO:0000256|HAMAP-Rule:MF_01446};
DE            Short=t(6)A synthase {ECO:0000256|HAMAP-Rule:MF_01446};
DE   AltName: Full=t(6)A37 threonylcarbamoyladenosine biosynthesis protein Kae1 {ECO:0000256|HAMAP-Rule:MF_01446};
DE   AltName: Full=tRNA threonylcarbamoyladenosine biosynthesis protein Kae1 {ECO:0000256|HAMAP-Rule:MF_01446};
GN   Name=kae1 {ECO:0000256|HAMAP-Rule:MF_01446};
GN   OrderedLocusNames=Mmah_0507 {ECO:0000313|EMBL:ADE36034.1};
OS   Methanohalophilus mahii (strain ATCC 35705 / DSM 5219 / SLP).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanohalophilus.
OX   NCBI_TaxID=547558 {ECO:0000313|EMBL:ADE36034.1, ECO:0000313|Proteomes:UP000001059};
RN   [1] {ECO:0000313|EMBL:ADE36034.1, ECO:0000313|Proteomes:UP000001059}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35705 / DSM 5219 / SLP
RC   {ECO:0000313|Proteomes:UP000001059};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Lykidis A., Saunders E., Brettin T., Detter J.C., Han C., Land M.,
RA   Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D.,
RA   Spring S., Schneider S., Schroeder M., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Methanohalophilus mahii DSM 5219.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Required for the formation of a threonylcarbamoyl group on
CC       adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning
CC       with adenine. Is a component of the KEOPS complex that is probably
CC       involved in the transfer of the threonylcarbamoyl moiety of
CC       threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. Kae1 likely
CC       plays a direct catalytic role in this reaction, but requires other
CC       protein(s) of the complex to fulfill this activity. {ECO:0000256|HAMAP-
CC       Rule:MF_01446}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosine(37) in tRNA + L-threonylcarbamoyladenylate = AMP +
CC         H(+) + N(6)-L-threonylcarbamoyladenosine(37) in tRNA;
CC         Xref=Rhea:RHEA:37059, Rhea:RHEA-COMP:10162, Rhea:RHEA-COMP:10163,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:73682, ChEBI:CHEBI:74411,
CC         ChEBI:CHEBI:74418, ChEBI:CHEBI:456215; EC=2.3.1.234;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01446,
CC         ECO:0000256|SAAS:SAAS01118488};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01446};
CC       Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01446};
CC   -!- SUBUNIT: Monomer. Component of the KEOPS complex that consists of Kae1,
CC       Bud32, Cgi121 and Pcc1; the whole complex dimerizes.
CC       {ECO:0000256|HAMAP-Rule:MF_01446}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01446,
CC       ECO:0000256|SAAS:SAAS00346542}.
CC   -!- SIMILARITY: Belongs to the KAE1 / TsaD family. {ECO:0000256|HAMAP-
CC       Rule:MF_01446}.
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DR   EMBL; CP001994; ADE36034.1; -; Genomic_DNA.
DR   RefSeq; WP_013036977.1; NC_014002.1.
DR   EnsemblBacteria; ADE36034; ADE36034; Mmah_0507.
DR   GeneID; 8982648; -.
DR   KEGG; mmh:Mmah_0507; -.
DR   eggNOG; arCOG01183; Archaea.
DR   eggNOG; COG0533; LUCA.
DR   HOGENOM; HOG000109569; -.
DR   KO; K01409; -.
DR   OMA; HLEGHIY; -.
DR   OrthoDB; 34679at2157; -.
DR   BioCyc; MMAH547558:G1GHT-509-MONOMER; -.
DR   Proteomes; UP000001059; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000408; C:EKC/KEOPS complex; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0061711; F:N(6)-L-threonylcarbamoyladenine synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01446; Kae1; 1.
DR   InterPro; IPR000905; Gcp-like_dom.
DR   InterPro; IPR034680; Kae1/OSGEP.
DR   InterPro; IPR017861; KAE1/TsaD.
DR   InterPro; IPR022449; Kae1_arc.
DR   PANTHER; PTHR11735; PTHR11735; 1.
DR   PANTHER; PTHR11735:SF14; PTHR11735:SF14; 1.
DR   Pfam; PF00814; Peptidase_M22; 1.
DR   PRINTS; PR00789; OSIALOPTASE.
DR   TIGRFAMs; TIGR03722; arch_KAE1; 1.
DR   TIGRFAMs; TIGR00329; gcp_kae1; 1.
PE   3: Inferred from homology;
DR   PRODOM; D5EA33.
DR   SWISS-2DPAGE; D5EA33.
KW   Acyltransferase {ECO:0000256|HAMAP-Rule:MF_01446,
KW   ECO:0000256|SAAS:SAAS00195274};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01446, ECO:0000256|SAAS:SAAS00195276};
KW   Hydrolase {ECO:0000313|EMBL:ADE36034.1};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_01446, ECO:0000256|SAAS:SAAS00195263};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01446,
KW   ECO:0000256|SAAS:SAAS00195272}; Protease {ECO:0000313|EMBL:ADE36034.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001059};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01446,
KW   ECO:0000256|SAAS:SAAS00195271};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_01446,
KW   ECO:0000256|SAAS:SAAS00195265}.
FT   DOMAIN          24..295
FT                   /note="Peptidase_M22"
FT                   /evidence="ECO:0000259|Pfam:PF00814"
FT   REGION          132..136
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01446"
FT   METAL           111
FT                   /note="Iron"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01446"
FT   METAL           115
FT                   /note="Iron"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01446"
FT   METAL           132
FT                   /note="Iron"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01446"
FT   METAL           288
FT                   /note="Iron"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01446"
FT   BINDING         164
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01446"
FT   BINDING         177
FT                   /note="Substrate; via amide nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01446"
FT   BINDING         181
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01446"
FT   BINDING         260
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01446"
SQ   SEQUENCE   330 AA;  35860 MW;  F359A02984E3E8AC CRC64;
     MTLVLGIEGT AWNLSAAVVN EDEVVCEVTH TYKPTTGGIH PREAAQHHAQ FASWVISNLF
     GELAEKNINP KDIDAISFSQ GPGLGACLRT VATAARALSL SLEIPLVGVN HCVAHVEIGR
     WKTPAKDPVV LYASGANTQV LAYRRGKYRV FGETLDIGVG NALDKFARSA GLSHPGGPQI
     EMYAKDSVNY VNLPYVVKGM DFSFSGLSTA ATDALQKHTL EDVCYSLQEN AFAMLVEVTE
     RALAHTGKNE VLLGGGVGAN MRLREMLDIM CDDRGASFYV PEKRFMGDNG AMIAWLGLLM
     YKAGDTIRVD DSHVNPNYRP DMVDVTWLKE
//

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