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P16641 (KTRC_SCHMA) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Taurocyamine kinase

EC=2.7.3.4
Alternative name(s):
ATP:guanidino kinase Smc74
ATP:guanidino phosphotransferase
Short name=SmGK
Gene names
ORF Names:Smp_194770
OrganismSchistosoma mansoni (Blood fluke) [Reference proteome]
Taxonomic identifier6183 [NCBI]
Taxonomic lineageEukaryotaMetazoaPlatyhelminthesTrematodaDigeneaStrigeididaSchistosomatoideaSchistosomatidaeSchistosoma

Protein attributes

Sequence length746 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This family of enzymes reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate). Ref.2

Catalytic activity

ATP + taurocyamine = ADP + N-phosphotaurocyamine. Ref.2

Cofactor

Magnesium. Ref.2

Developmental stage

Expressed at low levels in 37-day sporocysts, increases 25-fold in the infective cercarial and early schistosomular stages. Levels decrease dramatically in adults, adult males have approximately twice the expression level as in adult females. Ref.1

Sequence similarities

Belongs to the ATP:guanido phosphotransferase family.

Contains 2 phosphagen kinase C-terminal domains.

Contains 2 phosphagen kinase N-terminal domains.

Sequence caution

The sequence AAA29927.1 differs from that shown. Reason: Frameshift at positions 416, 434 and 644.

The sequence CCD76533.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 746746Taurocyamine kinase
PRO_0000212009

Regions

Repeat31 – 393363Approximate
Domain35 – 11682Phosphagen kinase N-terminal 1
Domain146 – 382237Phosphagen kinase C-terminal 1
Repeat394 – 705312Approximate
Domain398 – 47982Phosphagen kinase N-terminal 2
Domain509 – 746238Phosphagen kinase C-terminal 2
Nucleotide binding149 – 1535ATP By similarity
Nucleotide binding307 – 3115ATP By similarity
Nucleotide binding335 – 3406ATP By similarity
Nucleotide binding512 – 5165ATP By similarity
Nucleotide binding670 – 6745ATP By similarity
Nucleotide binding699 – 7046ATP By similarity

Sites

Active site2981 By similarity
Active site6611 By similarity
Binding site2121ATP By similarity
Binding site2561ATP By similarity
Binding site5751ATP By similarity
Binding site6191ATP By similarity

Experimental info

Sequence conflict451N → S in ABU49846. Ref.5
Sequence conflict200 – 21112MSEED…KLVND → CQRGQNQTSKRH in AAA29927. Ref.1
Sequence conflict2441N → K in AAA29927. Ref.1
Sequence conflict2641G → R in AAA29927. Ref.1
Sequence conflict2821K → R in ABU49846. Ref.5
Sequence conflict5231D → G in AAA29927. Ref.1
Sequence conflict5231D → G no nucleotide entry Ref.2
Sequence conflict5231D → G in ABU49845. Ref.4
Sequence conflict6321V → A no nucleotide entry Ref.2
Sequence conflict681 – 74666SSQPK…IEKGL → VLNRKSWMKFVRSDMPSKLE VLLW in AAA29927. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P16641 [UniParc].

Last modified June 13, 2012. Version 3.
Checksum: 03B55FFD75E979B1

FASTA74683,891
        10         20         30         40         50         60 
MTCTSAFIKV VRFIQVVIDT REIRSLCTIR MQVESLQNLQ AKIRNDERNH SLTKKYLTDD 

        70         80         90        100        110        120 
IVKKYQATKT SLGGTLAQCV NTNAYNPGAL LPRSCDLNAY ETFRDFFDAV IADYHKVPDG 

       130        140        150        160        170        180 
KIQHPKSNFG DLKSLSFTDL NTYGNLVVST RVRLGRTVEG FGFGPTLTKE TRIELENKIS 

       190        200        210        220        230        240 
TALHNLSGEY EGTYYPLTGM SEEDRIKLVN DHFLFRNDDN VLRDAGGYID WPTGRGIFIN 

       250        260        270        280        290        300 
KQKNFLVWIN EEDHIRVISM QKGGDLIAVY KRLADAIQEL SKSLKFAFND RLGFITFCPS 

       310        320        330        340        350        360 
NLGTTLRASV HAKIPMLASL PNFKEICEKH GIQPRGTHGE HTESVGGIYD LSNKRRLGLT 

       370        380        390        400        410        420 
ELDAVTEMHS GVRALLELEV MLQEYNKGAP EGVMPVEPLT YLAKLLEGAS IEKCYTRKYL 

       430        440        450        460        470        480 
TPEIIKKYDG KRTTHGATLA HMIRNGAYNN RSICPRTGEA ECYSTFIDYL DPLICDYHGV 

       490        500        510        520        530        540 
KDSAFKHPAP TFGDLSKLPF GDLDPTGKFI VSTRVRVGRS VEDFLFPTIM SKTDRIKLEQ 

       550        560        570        580        590        600 
VISGALKGLT GEHAGTYYPL TDMKEEDRKQ LVEDHFLFKN DDPVLRDAGG YRDWPVGRGI 

       610        620        630        640        650        660 
FHNNSKTFLV WVCEEDHMRI ISMQQGGNLA AVYKRLIEGI NAIGKSMKFA HSDKYGYITC 

       670        680        690        700        710        720 
CPSNLGTSMR ASVLLKIPKL SSQPKKLDEI CAKYMLQARG LYGEHTESPD GTYDISNKRR 

       730        740 
LGLTELQAAH EMAEGVAKMI EIEKGL 

« Hide

References

« Hide 'large scale' references
[1]"A cloned ATP:guanidino kinase in the trematode Schistosoma mansoni has a novel duplicated structure."
Stein L.D., Harn D.A., David J.R.
J. Biol. Chem. 265:6582-6588(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE.
Strain: Puerto Rican.
[2]"Crystallization and X-ray analysis of the Schistosoma mansoni guanidino kinase."
Awama A.M., Paracuellos P., Laurent S., Dissous C., Marcillat O., Gouet P.
Acta Crystallogr. F 64:854-857(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY, COFACTOR.
[3]"The genome of the blood fluke Schistosoma mansoni."
Berriman M., Haas B.J., LoVerde P.T., Wilson R.A., Dillon G.P., Cerqueira G.C., Mashiyama S.T., Al-Lazikani B., Andrade L.F., Ashton P.D., Aslett M.A., Bartholomeu D.C., Blandin G., Caffrey C.R., Coghlan A., Coulson R., Day T.A., Delcher A. expand/collapse author list , DeMarco R., Djikeng A., Eyre T., Gamble J.A., Ghedin E., Gu Y., Hertz-Fowler C., Hirai H., Hirai Y., Houston R., Ivens A., Johnston D.A., Lacerda D., Macedo C.D., McVeigh P., Ning Z., Oliveira G., Overington J.P., Parkhill J., Pertea M., Pierce R.J., Protasio A.V., Quail M.A., Rajandream M.A., Rogers J., Sajid M., Salzberg S.L., Stanke M., Tivey A.R., White O., Williams D.L., Wortman J., Wu W., Zamanian M., Zerlotini A., Fraser-Liggett C.M., Barrell B.G., El-Sayed N.M.
Nature 460:352-358(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Puerto Rican.
[4]"A systematically improved high quality genome and transcriptome of the human blood fluke Schistosoma mansoni."
Protasio A.V., Tsai I.J., Babbage A., Nichol S., Hunt M., Aslett M.A., De Silva N., Velarde G.S., Anderson T.J., Clark R.C., Davidson C., Dillon G.P., Holroyd N.E., LoVerde P.T., Lloyd C., McQuillan J., Oliveira G., Otto T.D. expand/collapse author list , Parker-Manuel S.J., Quail M.A., Wilson R.A., Zerlotini A., Dunne D.W., Berriman M.
PLoS Negl. Trop. Dis. 6:E1455-E1455(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Puerto Rican.
[5]"Molecular determinants of compatibility polymorphism in the Biomphalaria glabrata/Schistosoma mansoni model: New candidates identified by a global comparative proteomics approach."
Roger E., Mitta G., Mone Y., Bouchut A., Rognon A., Grunau C., Boissier J., Theron A., Gourbal B.E.
Mol. Biochem. Parasitol. 157:205-216(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-683.
Strain: C and IC.
[6]"The Schistosoma mansoni phosphagen kinase gene contains two closely apposed transcription initiation sites and arose from a fused gene duplication."
Shoemaker C.B.
Mol. Biochem. Parasitol. 68:319-322(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-52 AND 362-415.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J05410 mRNA. Translation: AAA29927.1. Frameshift.
HE601624 Genomic DNA. Translation: CCD76533.1. Sequence problems.
EU042595 mRNA. Translation: ABU49845.1.
EU042596 mRNA. Translation: ABU49846.1.
L31768 Genomic DNA. Translation: AAA29912.1.
L31769 Genomic DNA. Translation: AAA29913.1.
PIRA35743.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOGENOMHOG000006584.

Family and domain databases

Gene3D1.10.135.10. 2 hits.
3.30.590.10. 2 hits.
InterProIPR022415. ATP-guanido_PTrfase_AS.
IPR022414. ATP-guanido_PTrfase_cat.
IPR022413. ATP-guanido_PTrfase_N.
IPR014746. Gln_synth/guanido_kin_cat_dom.
[Graphical view]
PfamPF00217. ATP-gua_Ptrans. 2 hits.
PF02807. ATP-gua_PtransN. 2 hits.
[Graphical view]
SUPFAMSSF48034. SSF48034. 2 hits.
PROSITEPS00112. PHOSPHAGEN_KINASE. 2 hits.
PS51510. PHOSPHAGEN_KINASE_C. 2 hits.
PS51509. PHOSPHAGEN_KINASE_N. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameKTRC_SCHMA
AccessionPrimary (citable) accession number: P16641
Secondary accession number(s): A7UAX4 expand/collapse secondary AC list , A7UAX5, C4QUJ5, G4VAV2
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: June 13, 2012
Last modified: October 16, 2013
This is version 71 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families