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UniProtKB/Swiss-Prot entry Q2GG34


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name COAE_EHRCR
Primary accession number Q2GG34
Secondary accession numbers None
Integrated into Swiss-Prot on June 27, 2006
Sequence was last modified on March 21, 2006 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 21)
Name and origin of the protein
Protein name Dephospho-CoA kinase
Synonyms EC 2.7.1.24
Dephosphocoenzyme A kinase
Gene name
Name: coaE
OrderedLocusNames: ECH_0801
From
Ehrlichia chaffeensis (strain Arkansas) [TaxID: 205920] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales; Anaplasmataceae; Ehrlichia.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1371/journal.pgen.0020021; PubMed=16482227 [NCBI, ExPASy, EBI, Israel, Japan]
Dunning Hotopp J.C., Lin M., Madupu R., Crabtree J., Angiuoli S.V., Eisen J.A., Seshadri R., Ren Q., Wu M., Utterback T.R., Smith S., Lewis M., Khouri H., Zhang C., Niu H., Lin Q., Ohashi N., Zhi N., Nelson W.C., Brinkac L.M., Dodson R.J., Rosovitz M.J., Sundaram J.P., Daugherty S.C., Davidsen T., Durkin A.S., Gwinn M.L., Haft D.H., Selengut J.D., Sullivan S.A., Zafar N., Zhou L., Benahmed F., Forberger H., Halpin R., Mulligan S., Robinson J., White O., Rikihisa Y., Tettelin H.;
"Comparative genomics of emerging human ehrlichiosis agents.";
PLoS Genet. 2:208-222(2006).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
CP000236; ABD44854.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_507599.1; -.
3D structure databases
ModBase Q2GG34.
Enzyme and pathway databases
BioCyc ECHA205920:ECH_0801-MON; -.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from HAMAP).
GO:0004140; Molecular function: dephospho-CoA kinase activity (inferred from electronic annotation from HAMAP).
GO:0015937; Biological process: coenzyme A biosynthetic process (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_00376; -; 1.
PBIL [Tree]
InterPro IPR001977; Depp_CoAkinase.
Graphical view of domain structure.
Pfam PF01121; CoaE; 1.
Pfam graphical view of domain structure.
ProDom PD003329; Depp_CoAkinase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR00152; Depp_CoAkinase; 1.
PROSITE PS51219; DPCK; 1.
PROSITE graphical view of domain structure (profiles).
ProtoNet Q2GG34.
Genome annotation databases
GeneID 3927164; -.
GenomeReviews CP000236_GR; ECH_0801.
KEGG ech:ECH_0801; -.
TIGR ECH_0801; -.
Phylogenomic databases
HOGENOM Q2GG34; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
ATP-binding; Coenzyme A biosynthesis; Complete proteome; Cytoplasm; Kinase; Nucleotide-binding; Transferase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom To Length Description FTId
CHAIN   1   202  202     Dephospho-CoA kinase. PRO_0000243284
DOMAIN   3   202  200     DPCK. 
NP_BIND   8    15  8     ATP (Potential). 
Sequence information
Length: 202 AA [This is the length of the unprocessed precursor] Molecular weight: 23334 Da [This is the MW of the unprocessed precursor] CRC64: 60C10D1AF84CD639 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MVIFGLTGGI GSGKSLVASY FKTLFKAVVF DADQVVCQLY NCDNSVIKLV KTYFPDSVDH 

        70         80         90        100        110        120 
GVVNKNSLRQ HFFAYSNLWV EFQSTLHSII LEKQKNFIMF HNRQSTKYVV LDVPLLIESN 

       130        140        150        160        170        180 
FYSCCNFIIH VTTNRLLQMQ RVLYRGLSIR EFESIIAIQL SENDRKKFAN FTIRTGLSKG 

       190        200 
DVLFQIQKIM FDISHRSKYL SC 

Q2GG34 in FASTA format

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BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

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