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O15991

- KLOM_EISFO

UniProt

O15991 - KLOM_EISFO

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Protein

Lombricine kinase

Gene
N/A
Organism
Eisenia foetida (Common brandling worm) (Common dung-worm)
Status
Reviewed - Annotation score: 2 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

ATP + lombricine = ADP + N-phospholombricine.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei179 – 1791ATP By similarity
Binding sitei224 – 2241ATP By similarity
Binding sitei280 – 2801ATP By similarity
Binding sitei323 – 3231ATP By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi116 – 1205ATP By similarity
Nucleotide bindingi308 – 3136ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. lombricine kinase activity Source: UniProtKB-EC
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-18469.

Names & Taxonomyi

Protein namesi
Recommended name:
Lombricine kinase (EC:2.7.3.5)
Short name:
LK
OrganismiEisenia foetida (Common brandling worm) (Common dung-worm)
Taxonomic identifieri6396 [NCBI]
Taxonomic lineageiEukaryotaMetazoaLophotrochozoaAnnelidaClitellataOligochaetaHaplotaxidaLumbricinaLumbricidaeLumbricinaeEisenia

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 371371Lombricine kinasePRO_0000211985Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.

Structurei

3D structure databases

ProteinModelPortaliO15991.
SMRiO15991. Positions 2-368.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 8686Phosphagen kinase N-terminalAdd
BLAST
Domaini113 – 355243Phosphagen kinase C-terminalAdd
BLAST

Sequence similaritiesi

Family and domain databases

Gene3Di1.10.135.10. 1 hit.
3.30.590.10. 1 hit.
InterProiIPR022415. ATP-guanido_PTrfase_AS.
IPR022414. ATP-guanido_PTrfase_cat.
IPR022413. ATP-guanido_PTrfase_N.
IPR014746. Gln_synth/guanido_kin_cat_dom.
[Graphical view]
PfamiPF00217. ATP-gua_Ptrans. 1 hit.
PF02807. ATP-gua_PtransN. 1 hit.
[Graphical view]
SUPFAMiSSF48034. SSF48034. 1 hit.
PROSITEiPS00112. PHOSPHAGEN_KINASE. 1 hit.
PS51510. PHOSPHAGEN_KINASE_C. 1 hit.
PS51509. PHOSPHAGEN_KINASE_N. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O15991-1 [UniParc]FASTAAdd to Basket

« Hide

MPKFTARQNF PDYKSNGHKC MVGRHLTEDM YERLYELRTP NGVSIDKCIQ    50
PSVDNTGRII GLVAGDPESY EVFKELFDAV INEKHGGFGP TDKHPPPDLN 100
ANALVGGQFD PKYVKSARIR TGRSVKGFCL PPSISRAERR EVERIIVDAL 150
AGLEGDLAGV YYPLKKMTPE QEKQLIADHF LFQKPTGHLM VNSGAVRDWP 200
DARGIWHNKD KTFLIWINEE DQVRIIAMQH GGDVKAVFER FSRGLTQIEG 250
LMKKHGHEFA WSERLGYICT CPSNLGTGLR ASVHLQLHKL SKHPKFEEII 300
LAFHLQKRGT GGEHTEAVDD VYDISNRARL KKSEREFVQL LIDGVGKLIE 350
YEKLLEAGKS IDDVLPASLK G 371
Length:371
Mass (Da):41,781
Last modified:January 1, 1998 - v1
Checksum:i8F8409D72F92ACB9
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB008013 mRNA. Translation: BAA22872.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB008013 mRNA. Translation: BAA22872.1 .

3D structure databases

ProteinModelPortali O15991.
SMRi O15991. Positions 2-368.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

BioCyci MetaCyc:MONOMER-18469.

Family and domain databases

Gene3Di 1.10.135.10. 1 hit.
3.30.590.10. 1 hit.
InterProi IPR022415. ATP-guanido_PTrfase_AS.
IPR022414. ATP-guanido_PTrfase_cat.
IPR022413. ATP-guanido_PTrfase_N.
IPR014746. Gln_synth/guanido_kin_cat_dom.
[Graphical view ]
Pfami PF00217. ATP-gua_Ptrans. 1 hit.
PF02807. ATP-gua_PtransN. 1 hit.
[Graphical view ]
SUPFAMi SSF48034. SSF48034. 1 hit.
PROSITEi PS00112. PHOSPHAGEN_KINASE. 1 hit.
PS51510. PHOSPHAGEN_KINASE_C. 1 hit.
PS51509. PHOSPHAGEN_KINASE_N. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Evolution of phosphagen kinase. VI. Isolation, characterization and cDNA-derived amino acid sequence of lombricine kinase from the earthworm Eisenia foetida, and identification of a possible candidate for the guanidine substrate recognition site."
    Suzuki T., Kawasaki Y., Furukohri T., Ellington W.R.
    Biochim. Biophys. Acta 1343:152-159(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.

Entry informationi

Entry nameiKLOM_EISFO
AccessioniPrimary (citable) accession number: O15991
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 1, 1998
Last modified: July 9, 2014
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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