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Protein

Taurocyamine kinase

Gene

Smp_194770

Organism
Schistosoma mansoni (Blood fluke)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

This family of enzymes reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate).1 Publication

Catalytic activityi

ATP + taurocyamine = ADP + N-phosphotaurocyamine.1 Publication

Cofactori

Mg2+1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei212 – 2121ATPPROSITE-ProRule annotation
Binding sitei256 – 2561ATPPROSITE-ProRule annotation
Active sitei298 – 2981PROSITE-ProRule annotation
Binding sitei575 – 5751ATPPROSITE-ProRule annotation
Binding sitei619 – 6191ATPPROSITE-ProRule annotation
Active sitei661 – 6611PROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi149 – 1535ATPPROSITE-ProRule annotation
Nucleotide bindingi307 – 3115ATPPROSITE-ProRule annotation
Nucleotide bindingi335 – 3406ATPPROSITE-ProRule annotation
Nucleotide bindingi512 – 5165ATPPROSITE-ProRule annotation
Nucleotide bindingi670 – 6745ATPPROSITE-ProRule annotation
Nucleotide bindingi699 – 7046ATPPROSITE-ProRule annotation

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Oxidoreductase, Transferase

Keywords - Ligandi

ATP-binding, Flavoprotein, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.3.4. 5608.

Names & Taxonomyi

Protein namesi
Recommended name:
Taurocyamine kinase (EC:2.7.3.4)
Alternative name(s):
ATP:guanidino kinase Smc74
ATP:guanidino phosphotransferase
Short name:
SmGK
Gene namesi
ORF Names:Smp_194770
OrganismiSchistosoma mansoni (Blood fluke)
Taxonomic identifieri6183 [NCBI]
Taxonomic lineageiEukaryotaMetazoaPlatyhelminthesTrematodaDigeneaStrigeididaSchistosomatoideaSchistosomatidaeSchistosoma
ProteomesiUP000008854 Componenti: Chromosome 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 746746Taurocyamine kinasePRO_0000212009Add
BLAST

Expressioni

Developmental stagei

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.1 Publication

Interactioni

Protein-protein interaction databases

STRINGi6183.Smp_194770__mRNA.

Structurei

Secondary structure

1
746
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi36 – 449Combined sources
Helixi52 – 565Combined sources
Helixi59 – 657Combined sources
Helixi76 – 8510Combined sources
Helixi99 – 1024Combined sources
Helixi104 – 11411Combined sources
Helixi118 – 1203Combined sources
Helixi132 – 1343Combined sources
Helixi140 – 1423Combined sources
Beta strandi147 – 15610Combined sources
Turni164 – 1663Combined sources
Helixi169 – 18416Combined sources
Helixi188 – 1903Combined sources
Beta strandi192 – 1976Combined sources
Helixi202 – 2109Combined sources
Helixi220 – 2245Combined sources
Turni225 – 23410Combined sources
Beta strandi236 – 2405Combined sources
Beta strandi245 – 26420Combined sources
Helixi266 – 28116Combined sources
Turni290 – 2923Combined sources
Helixi299 – 3013Combined sources
Beta strandi307 – 3137Combined sources
Helixi315 – 3184Combined sources
Helixi323 – 3297Combined sources
Beta strandi332 – 3365Combined sources
Beta strandi348 – 3547Combined sources
Beta strandi357 – 3593Combined sources
Helixi361 – 38525Combined sources
Turni386 – 3883Combined sources
Helixi399 – 4068Combined sources
Turni411 – 4133Combined sources
Helixi415 – 4184Combined sources
Helixi422 – 4287Combined sources
Helixi439 – 44810Combined sources
Helixi462 – 4654Combined sources
Helixi467 – 47812Combined sources
Beta strandi506 – 51914Combined sources
Turni527 – 5293Combined sources
Helixi532 – 54716Combined sources
Helixi551 – 5533Combined sources
Beta strandi555 – 5628Combined sources
Helixi565 – 5739Combined sources
Helixi583 – 5886Combined sources
Turni589 – 5979Combined sources
Beta strandi599 – 6035Combined sources
Beta strandi606 – 62823Combined sources
Helixi629 – 64416Combined sources
Turni653 – 6553Combined sources
Helixi662 – 6643Combined sources
Beta strandi669 – 6768Combined sources
Helixi680 – 6823Combined sources
Turni684 – 6874Combined sources
Helixi688 – 6936Combined sources
Beta strandi696 – 6994Combined sources
Helixi709 – 7113Combined sources
Beta strandi712 – 7176Combined sources
Beta strandi721 – 7233Combined sources
Helixi725 – 74521Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4WO8X-ray2.20A31-746[»]
4WODX-ray1.90A31-746[»]
4WOEX-ray2.30A/B31-746[»]
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati31 – 393363ApproximateAdd
BLAST
Domaini35 – 11682Phosphagen kinase N-terminal 1PROSITE-ProRule annotationAdd
BLAST
Domaini146 – 382237Phosphagen kinase C-terminal 1PROSITE-ProRule annotationAdd
BLAST
Repeati394 – 705312ApproximateAdd
BLAST
Domaini398 – 47982Phosphagen kinase N-terminal 2PROSITE-ProRule annotationAdd
BLAST
Domaini509 – 746238Phosphagen kinase C-terminal 2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the ATP:guanido phosphotransferase family.PROSITE-ProRule annotation
Contains 2 phosphagen kinase C-terminal domains.PROSITE-ProRule annotation
Contains 2 phosphagen kinase N-terminal domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

HOGENOMiHOG000006584.
InParanoidiP16641.

Family and domain databases

Gene3Di1.10.135.10. 2 hits.
3.30.590.10. 2 hits.
InterProiIPR000749. ATP-guanido_PTrfase.
IPR022415. ATP-guanido_PTrfase_AS.
IPR022414. ATP-guanido_PTrfase_cat.
IPR022413. ATP-guanido_PTrfase_N.
IPR014746. Gln_synth/guanido_kin_cat_dom.
[Graphical view]
PANTHERiPTHR11547. PTHR11547. 1 hit.
PfamiPF00217. ATP-gua_Ptrans. 2 hits.
PF02807. ATP-gua_PtransN. 2 hits.
[Graphical view]
SUPFAMiSSF48034. SSF48034. 2 hits.
PROSITEiPS00112. PHOSPHAGEN_KINASE. 2 hits.
PS51510. PHOSPHAGEN_KINASE_C. 2 hits.
PS51509. PHOSPHAGEN_KINASE_N. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P16641-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTCTSAFIKV VRFIQVVIDT REIRSLCTIR MQVESLQNLQ AKIRNDERNH
60 70 80 90 100
SLTKKYLTDD IVKKYQATKT SLGGTLAQCV NTNAYNPGAL LPRSCDLNAY
110 120 130 140 150
ETFRDFFDAV IADYHKVPDG KIQHPKSNFG DLKSLSFTDL NTYGNLVVST
160 170 180 190 200
RVRLGRTVEG FGFGPTLTKE TRIELENKIS TALHNLSGEY EGTYYPLTGM
210 220 230 240 250
SEEDRIKLVN DHFLFRNDDN VLRDAGGYID WPTGRGIFIN KQKNFLVWIN
260 270 280 290 300
EEDHIRVISM QKGGDLIAVY KRLADAIQEL SKSLKFAFND RLGFITFCPS
310 320 330 340 350
NLGTTLRASV HAKIPMLASL PNFKEICEKH GIQPRGTHGE HTESVGGIYD
360 370 380 390 400
LSNKRRLGLT ELDAVTEMHS GVRALLELEV MLQEYNKGAP EGVMPVEPLT
410 420 430 440 450
YLAKLLEGAS IEKCYTRKYL TPEIIKKYDG KRTTHGATLA HMIRNGAYNN
460 470 480 490 500
RSICPRTGEA ECYSTFIDYL DPLICDYHGV KDSAFKHPAP TFGDLSKLPF
510 520 530 540 550
GDLDPTGKFI VSTRVRVGRS VEDFLFPTIM SKTDRIKLEQ VISGALKGLT
560 570 580 590 600
GEHAGTYYPL TDMKEEDRKQ LVEDHFLFKN DDPVLRDAGG YRDWPVGRGI
610 620 630 640 650
FHNNSKTFLV WVCEEDHMRI ISMQQGGNLA AVYKRLIEGI NAIGKSMKFA
660 670 680 690 700
HSDKYGYITC CPSNLGTSMR ASVLLKIPKL SSQPKKLDEI CAKYMLQARG
710 720 730 740
LYGEHTESPD GTYDISNKRR LGLTELQAAH EMAEGVAKMI EIEKGL
Length:746
Mass (Da):83,891
Last modified:June 13, 2012 - v3
Checksum:i03B55FFD75E979B1
GO

Sequence cautioni

The sequence AAA29927.1 differs from that shown. Reason: Frameshift at positions 416, 434 and 644. Curated
The sequence CCD76533.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti45 – 451N → S in ABU49846 (PubMed:18083248).Curated
Sequence conflicti200 – 21112MSEED…KLVND → CQRGQNQTSKRH in AAA29927 (PubMed:2324092).CuratedAdd
BLAST
Sequence conflicti244 – 2441N → K in AAA29927 (PubMed:2324092).Curated
Sequence conflicti264 – 2641G → R in AAA29927 (PubMed:2324092).Curated
Sequence conflicti282 – 2821K → R in ABU49846 (PubMed:18083248).Curated
Sequence conflicti523 – 5231D → G in AAA29927 (PubMed:2324092).Curated
Sequence conflicti523 – 5231D → G no nucleotide entry (PubMed:18765922).Curated
Sequence conflicti523 – 5231D → G in ABU49845 (PubMed:22253936).Curated
Sequence conflicti632 – 6321V → A no nucleotide entry (PubMed:18765922).Curated
Sequence conflicti681 – 74666SSQPK…IEKGL → VLNRKSWMKFVRSDMPSKLE VLLW in AAA29927 (PubMed:2324092).CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA35743.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA35743.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4WO8X-ray2.20A31-746[»]
4WODX-ray1.90A31-746[»]
4WOEX-ray2.30A/B31-746[»]
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi6183.Smp_194770__mRNA.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOGENOMiHOG000006584.
InParanoidiP16641.

Enzyme and pathway databases

BRENDAi2.7.3.4. 5608.

Family and domain databases

Gene3Di1.10.135.10. 2 hits.
3.30.590.10. 2 hits.
InterProiIPR000749. ATP-guanido_PTrfase.
IPR022415. ATP-guanido_PTrfase_AS.
IPR022414. ATP-guanido_PTrfase_cat.
IPR022413. ATP-guanido_PTrfase_N.
IPR014746. Gln_synth/guanido_kin_cat_dom.
[Graphical view]
PANTHERiPTHR11547. PTHR11547. 1 hit.
PfamiPF00217. ATP-gua_Ptrans. 2 hits.
PF02807. ATP-gua_PtransN. 2 hits.
[Graphical view]
SUPFAMiSSF48034. SSF48034. 2 hits.
PROSITEiPS00112. PHOSPHAGEN_KINASE. 2 hits.
PS51510. PHOSPHAGEN_KINASE_C. 2 hits.
PS51509. PHOSPHAGEN_KINASE_N. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.

Entry informationi

Entry nameiKTRC_SCHMA
AccessioniPrimary (citable) accession number: P16641
Secondary accession number(s): A7UAX4
, A7UAX5, C4QUJ5, G4VAV2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: June 13, 2012
Last modified: July 22, 2015
This is version 78 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.