Type-2 serine--tRNA ligase - Methanococcus maripaludis (strain S2 / LL)

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O30520 (SYS2_METMP) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 76. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Type-2 serine--tRNA ligase
EC=6.1.1.11

Alternative name(s):
Seryl-tRNA synthetase
Short name=SerRS
Seryl-tRNA(Ser/Sec) synthetase

Gene names

Name:	serS
Ordered Locus Names:	MMP0879

Organism

Methanococcus maripaludis (strain S2 / LL) [Complete proteome] [HAMAP]

Taxonomic identifier

267377 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanococci › Methanococcales › Methanococcaceae › Methanococcus

Protein attributes

Sequence length	514 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec). Ref.1 Ref.3
Catalytic activity	ATP + L-serine + tRNA(Ser) = AMP + diphosphate + L-seryl-tRNA(Ser). HAMAP MF_01278 ATP + L-serine + tRNA(Sec) = AMP + diphosphate + L-seryl-tRNA(Sec). HAMAP MF_01278
Cofactor	Binds 1 Zn²⁺ ion per subunit. This ion is coordinated with 2 cysteines, 1 glutamate and a water molecule that dissociates from the zinc ion to allow the coordination of the amino group of the serine substrate, which is essential for catalysis By similarity.
Pathway	Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1. HAMAP MF_01278
Subunit structure	Homodimer. Ref.3
Subcellular location	Cytoplasm By similarity HAMAP MF_01278.
Domain	Consists of two distinct domains, a catalytic core and a N-terminal extension that is presumably involved in tRNA binding By similarity. HAMAP MF_01278
Sequence similarities	Belongs to the class-II aminoacyl-tRNA synthetase family. Type-2 seryl-tRNA synthetase subfamily.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Aminoacyl-tRNA synthetase Ligase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	seryl-tRNA aminoacylation Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW serine-tRNA ligase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 514

514

Type-2 serine--tRNA ligase HAMAP MF_01278

PRO_0000122176

Regions

Nucleotide binding

344 – 346

ATP By similarity

Nucleotide binding

355 – 356

ATP By similarity

Region

361 – 363

Serine binding By similarity

Sites

Metal binding

315

Zinc; catalytic By similarity

Metal binding

363

Zinc; catalytic By similarity

Metal binding

470

Zinc; catalytic By similarity

Binding site

313

Serine; via carbonyl oxygen By similarity

Binding site

344

Serine By similarity

Binding site

477

ATP By similarity

Experimental info

Sequence conflict

S → E in AAD03476. Ref.1

Sequence conflict

E → Q in AAD03476. Ref.1

Sequence conflict

100

T → S in AAD03476. Ref.1

Sequence conflict

129

N → G in AAD03476. Ref.1

Sequence conflict

169

F → K in AAD03476. Ref.1

Sequence conflict

186

T → K in AAD03476. Ref.1

Sequence conflict

239

V → I in AAD03476. Ref.1

Sequence conflict

282

R → K in AAD03476. Ref.1

Sequence conflict

297

D → E in AAD03476. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

O30520 [UniParc].

Last modified April 13, 2004. Version 2.
Checksum: 75141EDFA3CFD878
Show »

FASTA

514

59,587

        10         20         30         40         50         60 
MRFELEGRII FSKDVSEETQ KDIIEVLENG DIFLKGVPEG KENEASKIEG YEFEGKDLKL 

        70         80         90        100        110        120 
NMTSGTYTRA HEGIVRLKKP IMEKVGRKHQ IGIRDVAIDT YVVTITATPS KVAELKGLKV 

       130        140        150        160        170        180 
PECEVELDNE KIKILFKNLG DGELKRNIID RAIKFVKTEL DKQEQDLTFE VCKIAPGTIV 

       190        200        210        220        230        240 
SDYKATREIT FDKDPTELAE PYGWVKRFPG RGQWFYTAPM AKLFRAFESL IVEECIEKVG 

       250        260        270        280        290        300 
FDECLFPKLI PLDVMYKMRY LEGLPEGMYY VCPPKREPEM FRDFVNEMMI KKEIPIDKLK 

       310        320        330        340        350        360 
TLLRDPGYVL APAQCEPFYT FFDHELVDVD SPSKFFDKSG WTYRWEGGGA KGLDRVNEFL 

       370        380        390        400        410        420 
RGECVWMGSP EFVEKVRDDT LKYAEKLAEK LDLEYWTEVG DDPFYLEGRK NEDRGIEFPD 

       430        440        450        460        470        480 
VPKYEMRLWL PHVKDERKGV AVTSANIHGT HFVEGFGIKD YKDRKVWTGC TGYGLSRWLI 

       490        500        510 
GFLAQYGYNY EDWPEIIQKK VGKLPEIPKL ITWP

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence divergence of seryl-tRNA synthetases in archaea." Kim H.-S., Vothknecht U.C., Hedderich R., Celic I., Soell D. J. Bacteriol. 180:6446-6449(1998) [PubMed: 9851985] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
[2]	"Complete genome sequence of the genetically tractable hydrogenotrophic methanogen Methanococcus maripaludis." Hendrickson E.L., Kaul R., Zhou Y., Bovee D., Chapman P., Chung J., Conway de Macario E., Dodsworth J.A., Gillett W., Graham D.E., Hackett M., Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J., Major T.A., Moore B.C. Leigh J.A. J. Bacteriol. 186:6956-6969(2004) [PubMed: 15466049] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: S2 / LL.
[3]	"The unusual methanogenic seryl-tRNA synthetase recognizes tRNASer species from all three kingdoms of life." Bilokapic S., Korencic D., Soell D., Weygand-Durasevic I. Eur. J. Biochem. 271:694-702(2004) [PubMed: 14764085] [Abstract] Cited for: FUNCTION, SUBUNIT.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF009822 Genomic DNA. Translation: AAD03476.1. BX950229 Genomic DNA. Translation: CAF30435.1.
RefSeq	NP_987999.1. NC_005791.1.
3D structure databases
ProteinModelPortal	O30520.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2762696.
GenomeReviews	Gene locus MMP0879 in contig BX950229_GR.
KEGG	mmp:MMP0879.
NMPDR	fig\|267377.1.peg.879.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG542255.
OMA	AQCEPFY.
ProtClustDB	PRK00960.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-14955. MMAR267377:MMP0879-MONOMER.
Family and domain databases
HAMAP	MF_01278. Ser_tRNA_synth_type2. [Tree]
InterPro	IPR002314. aa-tRNA-synt_IIb_cons-dom. IPR004503. Ser-tRNA-synth_IIa_arc. [Graphical view]
KO	K01875.
Pfam	PF00587. tRNA-synt_2b. 1 hit. [Graphical view]
TIGRFAMs	TIGR00415. SerS_MJ. 1 hit.
PROSITE	PS50862. AA_TRNA_LIGASE_II. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYS2_METMP

Accession

Primary (citable) accession number: O30520

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	April 13, 2004
Last modified:	January 25, 2012
This is version 76 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents