(data stored in SCRATCH zone)

SWISSPROT: D1CDK5_THET1

ID   D1CDK5_THET1            Unreviewed;       879 AA.
AC   D1CDK5;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   08-MAY-2019, entry version 72.
DE   RecName: Full=Alanine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00036};
DE            EC=6.1.1.7 {ECO:0000256|HAMAP-Rule:MF_00036};
DE   AltName: Full=Alanyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00036};
DE            Short=AlaRS {ECO:0000256|HAMAP-Rule:MF_00036};
GN   Name=alaS {ECO:0000256|HAMAP-Rule:MF_00036};
GN   OrderedLocusNames=Tter_0089 {ECO:0000313|EMBL:ACZ41011.1};
OS   Thermobaculum terrenum (strain ATCC BAA-798 / YNP1).
OC   Bacteria; Thermobaculum.
OX   NCBI_TaxID=525904 {ECO:0000313|EMBL:ACZ41011.1, ECO:0000313|Proteomes:UP000000323};
RN   [1] {ECO:0000313|EMBL:ACZ41011.1, ECO:0000313|Proteomes:UP000000323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323};
RX   PubMed=21304745;
RA   Kiss H., Cleland D., Lapidus A., Lucas S., Del Rio T.G., Nolan M.,
RA   Tice H., Han C., Goodwin L., Pitluck S., Liolios K., Ivanova N.,
RA   Mavromatis K., Ovchinnikova G., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Lu M., Brettin T.,
RA   Detter J.C., Goker M., Tindall B.J., Beck B., McDermott T.R.,
RA   Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Cheng J.F.;
RT   "Complete genome sequence of 'Thermobaculum terrenum' type strain
RT   (YNP1).";
RL   Stand. Genomic Sci. 3:153-162(2010).
RN   [2] {ECO:0000313|Proteomes:UP000000323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323};
RX   DOI=10.4056/sigs.1153107;
RA   Kiss H., Cleland D., Lapidus A., Lucas S., Glavina Del Rio T.,
RA   Nolan M., Tice H., Han C., Goodwin L., Pitluck S., Liolios K.,
RA   Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y., Jeffries C., Lu M.,
RA   Brettin T., Detter J., Goker M., Tindall B., Beck B., McDermott T.,
RA   Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P.,
RA   Kyrpides N., Klenk H., Cheng J.;
RT   "Complete genome sequence of Thermobaculum terrenum type strain
RT   (YNP1T).";
RL   Stand. Genomic Sci. 3:153-162(2010).
CC   -!- FUNCTION: Catalyzes the attachment of alanine to tRNA(Ala) in a
CC       two-step reaction: alanine is first activated by ATP to form Ala-
CC       AMP and then transferred to the acceptor end of tRNA(Ala). Also
CC       edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its
CC       editing domain. {ECO:0000256|HAMAP-Rule:MF_00036,
CC       ECO:0000256|SAAS:SAAS00015829}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-
CC         alanyl-tRNA(Ala); Xref=Rhea:RHEA:12540, Rhea:RHEA-COMP:9657,
CC         Rhea:RHEA-COMP:9923, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:57972, ChEBI:CHEBI:78442, ChEBI:CHEBI:78497,
CC         ChEBI:CHEBI:456215; EC=6.1.1.7; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00036, ECO:0000256|SAAS:SAAS01125460};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00036};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00036};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00036,
CC       ECO:0000256|SAAS:SAAS00832879}.
CC   -!- DOMAIN: Consists of three domains; the N-terminal catalytic
CC       domain, the editing domain and the C-terminal C-Ala domain. The
CC       editing domain removes incorrectly charged amino acids, while the
CC       C-Ala domain, along with tRNA(Ala), serves as a bridge to
CC       cooperatively bring together the editing and aminoacylation
CC       centers thus stimulating deacylation of misacylated tRNAs.
CC       {ECO:0000256|HAMAP-Rule:MF_00036}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family. {ECO:0000256|HAMAP-Rule:MF_00036,
CC       ECO:0000256|SAAS:SAAS00575517}.
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; CP001825; ACZ41011.1; -; Genomic_DNA.
DR   RefSeq; WP_012874046.1; NC_013525.1.
DR   STRING; 525904.Tter_0089; -.
DR   EnsemblBacteria; ACZ41011; ACZ41011; Tter_0089.
DR   KEGG; ttr:Tter_0089; -.
DR   eggNOG; ENOG4105CIM; Bacteria.
DR   eggNOG; COG0013; LUCA.
DR   HOGENOM; HOG000156965; -.
DR   KO; K01872; -.
DR   OMA; YHHTMFE; -.
DR   OrthoDB; 91428at2; -.
DR   BioCyc; TTER525904:G1GGS-89-MONOMER; -.
DR   Proteomes; UP000000323; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004813; F:alanine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006419; P:alanyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00036_B; Ala_tRNA_synth_B; 1.
DR   InterPro; IPR002318; Ala-tRNA-lgiase_IIc.
DR   InterPro; IPR018162; Ala-tRNA-ligase_IIc_anticod-bd.
DR   InterPro; IPR018165; Ala-tRNA-synth_IIc_core.
DR   InterPro; IPR018164; Ala-tRNA-synth_IIc_N.
DR   InterPro; IPR023033; Ala_tRNA_ligase_euk/bac.
DR   InterPro; IPR003156; DHHA1_dom.
DR   InterPro; IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   InterPro; IPR012947; tRNA_SAD.
DR   Pfam; PF02272; DHHA1; 1.
DR   Pfam; PF01411; tRNA-synt_2c; 1.
DR   Pfam; PF07973; tRNA_SAD; 1.
DR   PRINTS; PR00980; TRNASYNTHALA.
DR   SMART; SM00863; tRNA_SAD; 1.
DR   SUPFAM; SSF101353; SSF101353; 1.
DR   SUPFAM; SSF50447; SSF50447; 1.
DR   SUPFAM; SSF55186; SSF55186; 1.
DR   TIGRFAMs; TIGR00344; alaS; 1.
DR   PROSITE; PS50860; AA_TRNA_LIGASE_II_ALA; 1.
PE   3: Inferred from homology;
DR   PRODOM; D1CDK5.
DR   SWISS-2DPAGE; D1CDK5.
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00036,
KW   ECO:0000256|SAAS:SAAS00249969, ECO:0000313|EMBL:ACZ41011.1};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00036,
KW   ECO:0000256|SAAS:SAAS00250154}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000323};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00036,
KW   ECO:0000256|SAAS:SAAS00299154};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00036,
KW   ECO:0000256|SAAS:SAAS00249928, ECO:0000313|EMBL:ACZ41011.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00036,
KW   ECO:0000256|SAAS:SAAS00423853};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00036,
KW   ECO:0000256|SAAS:SAAS00250206};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00036,
KW   ECO:0000256|SAAS:SAAS00250204};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000323};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_00036,
KW   ECO:0000256|SAAS:SAAS00250135};
KW   tRNA-binding {ECO:0000256|HAMAP-Rule:MF_00036,
KW   ECO:0000256|SAAS:SAAS00250194};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00036, ECO:0000256|SAAS:SAAS00423813}.
FT   DOMAIN        1    709       AA_TRNA_LIGASE_II_ALA.
FT                                {ECO:0000259|PROSITE:PS50860}.
FT   COILED      725    759       {ECO:0000256|SAM:Coils}.
FT   METAL       564    564       Zinc. {ECO:0000256|HAMAP-Rule:MF_00036}.
FT   METAL       568    568       Zinc. {ECO:0000256|HAMAP-Rule:MF_00036}.
FT   METAL       666    666       Zinc. {ECO:0000256|HAMAP-Rule:MF_00036}.
FT   METAL       670    670       Zinc. {ECO:0000256|HAMAP-Rule:MF_00036}.
SQ   SEQUENCE   879 AA;  98020 MW;  985CE9CC73EB571D CRC64;
     MKSSEIRSKF LEFFEARGHT VVPSSSLVPA KDPTLLFTNS GMVQFKDVFL GRESRSYTRA
     TTAQKCMRAG GKHNDLENVG PSARHLTFFE MLGNFSFGDY FKREAIGYAW EFVTQVLGLE
     PSRLWATVHY TDDEAASLWQ EVAGLPESRI IRMGDEDNFW QMADVGPCGP NSEIFYDRGP
     EKGCGDPNCT PAHDCGRFWE FWNLVFMQYY QDESGNRTPL PKKNIDTGLG LERTSAIMQG
     VDSIFETDLF VPIMDEVQRI AGHSDEDRRR EIVAYRVIAD HSRSLAFLIA DGVTPGNEGR
     SYVLRRIIRR AIRFGRRIGI EGHFLSDTAR VVVDIMGHHY TELEDQWSFI DKVTRAEEEH
     FSRTLARGVA QLDDLIDKLS ASGQKEIPGE DAFRLYDTYG FPLDLTLELA RDRGFSVDTE
     GFKRAMERQR AQSRAASTFT AKMPAAYAAL SGEPTQFTGY TTLEDTGRVM AIIREGELVD
     KVEHGQEAEI LLDRTPFYAE AGGQVGDTGV ITGPEGDFHV LDTQRPVNGY ILHRGRVLHG
     SISVGQNVDL VVDARRRQDI MRNHTATHIL HKTLRDVLGP HARQAGSLVA PDRLRFDFTH
     PSQLSDEEFF EIERIINDVS QDDRKVYAQE KPYTEAIASG AMALFGEKYG DIVRVVSIED
     YGSELCGGTH VHHTGEIGPI YITSEGSIAS GVRRVEAVTG RGAIKYARER MELLERLGAK
     LKVPTSEIER QVALLQERLR EQERQIEQLR RQLAAGEIDQ MLRNVRQVDG TKLLVAQTSL
     DSREAMSDLA DRLRDRLRSG VVVVGSVLQG KPSIVAVVTP DLVQKGVHAG KLVKEISALV
     GGGGGGRPDR AEAGGRFPEK LEEALGSVDE VLARQLEGK
//

If you have problems or comments...

PBIL Back to PBIL home page