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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)DescriptionActionsGraphical viewLength
Binding sitei212ATPPROSITE-ProRule annotation1
Binding sitei256ATPPROSITE-ProRule annotation1
Active sitei298PROSITE-ProRule annotation1
Binding sitei575ATPPROSITE-ProRule annotation1
Binding sitei619ATPPROSITE-ProRule annotation1
Active sitei661PROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi149 – 153ATPPROSITE-ProRule annotation5
Nucleotide bindingi307 – 311ATPPROSITE-ProRule annotation5
Nucleotide bindingi335 – 340ATPPROSITE-ProRule annotation6
Nucleotide bindingi512 – 516ATPPROSITE-ProRule annotation5
Nucleotide bindingi670 – 674ATPPROSITE-ProRule annotation5
Nucleotide bindingi699 – 704ATPPROSITE-ProRule annotation6

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
Proteomesi
  • UP000008854 Componenti: Chromosome 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002120091 – 746Taurocyamine kinaseAdd BLAST746

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

1746
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi36 – 44Combined sources9
Helixi52 – 56Combined sources5
Helixi59 – 65Combined sources7
Helixi76 – 85Combined sources10
Helixi99 – 102Combined sources4
Helixi104 – 114Combined sources11
Helixi118 – 120Combined sources3
Helixi132 – 134Combined sources3
Helixi140 – 142Combined sources3
Beta strandi147 – 156Combined sources10
Turni164 – 166Combined sources3
Helixi169 – 184Combined sources16
Helixi188 – 190Combined sources3
Beta strandi192 – 197Combined sources6
Helixi202 – 210Combined sources9
Helixi220 – 224Combined sources5
Turni225 – 234Combined sources10
Beta strandi236 – 240Combined sources5
Beta strandi245 – 264Combined sources20
Helixi266 – 281Combined sources16
Turni290 – 292Combined sources3
Helixi299 – 301Combined sources3
Beta strandi307 – 313Combined sources7
Helixi315 – 318Combined sources4
Helixi323 – 329Combined sources7
Beta strandi332 – 336Combined sources5
Beta strandi348 – 354Combined sources7
Beta strandi357 – 359Combined sources3
Helixi361 – 385Combined sources25
Turni386 – 388Combined sources3
Helixi399 – 406Combined sources8
Turni411 – 413Combined sources3
Helixi415 – 418Combined sources4
Helixi422 – 428Combined sources7
Helixi439 – 448Combined sources10
Helixi462 – 465Combined sources4
Helixi467 – 478Combined sources12
Beta strandi506 – 519Combined sources14
Turni527 – 529Combined sources3
Helixi532 – 547Combined sources16
Helixi551 – 553Combined sources3
Beta strandi555 – 562Combined sources8
Helixi565 – 573Combined sources9
Helixi583 – 588Combined sources6
Turni589 – 597Combined sources9
Beta strandi599 – 603Combined sources5
Beta strandi606 – 628Combined sources23
Helixi629 – 644Combined sources16
Turni653 – 655Combined sources3
Helixi662 – 664Combined sources3
Beta strandi669 – 676Combined sources8
Helixi680 – 682Combined sources3
Turni684 – 687Combined sources4
Helixi688 – 693Combined sources6
Beta strandi696 – 699Combined sources4
Helixi709 – 711Combined sources3
Beta strandi712 – 717Combined sources6
Beta strandi721 – 723Combined sources3
Helixi725 – 745Combined sources21

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4WO8X-ray2.20A31-746[»]
4WODX-ray1.90A31-746[»]
4WOEX-ray2.30A/B31-746[»]
SMRiP16641.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati31 – 393ApproximateAdd BLAST363
Domaini35 – 116Phosphagen kinase N-terminal 1PROSITE-ProRule annotationAdd BLAST82
Domaini146 – 382Phosphagen kinase C-terminal 1PROSITE-ProRule annotationAdd BLAST237
Repeati394 – 705ApproximateAdd BLAST312
Domaini398 – 479Phosphagen kinase N-terminal 2PROSITE-ProRule annotationAdd BLAST82
Domaini509 – 746Phosphagen kinase C-terminal 2PROSITE-ProRule annotationAdd BLAST238

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

eggNOGiKOG0042. Eukaryota.
KOG3581. Eukaryota.
COG0578. LUCA.
COG3869. LUCA.
HOGENOMiHOG000006584.
InParanoidiP16641.
OrthoDBiEOG091G0HZ0.

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti45N → S in ABU49846 (PubMed:18083248).Curated1
Sequence conflicti200 – 211MSEED…KLVND → CQRGQNQTSKRH in AAA29927 (PubMed:2324092).CuratedAdd BLAST12
Sequence conflicti244N → K in AAA29927 (PubMed:2324092).Curated1
Sequence conflicti264G → R in AAA29927 (PubMed:2324092).Curated1
Sequence conflicti282K → R in ABU49846 (PubMed:18083248).Curated1
Sequence conflicti523D → G in AAA29927 (PubMed:2324092).Curated1
Sequence conflicti523D → G no nucleotide entry (PubMed:18765922).Curated1
Sequence conflicti523D → G in ABU49845 (PubMed:22253936).Curated1
Sequence conflicti632V → A no nucleotide entry (PubMed:18765922).Curated1
Sequence conflicti681 – 746SSQPK…IEKGL → VLNRKSWMKFVRSDMPSKLE VLLW in AAA29927 (PubMed:2324092).CuratedAdd BLAST66

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.

Genome annotation databases

GeneDBiSmp_194770.1:pep.

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4WO8X-ray2.20A31-746[»]
4WODX-ray1.90A31-746[»]
4WOEX-ray2.30A/B31-746[»]
SMRiP16641.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi6183.Smp_194770__mRNA.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneDBiSmp_194770.1:pep.

Phylogenomic databases

eggNOGiKOG0042. Eukaryota.
KOG3581. Eukaryota.
COG0578. LUCA.
COG3869. LUCA.
HOGENOMiHOG000006584.
InParanoidiP16641.
OrthoDBiEOG091G0HZ0.

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. 2 hits.
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...

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: November 2, 2016
This is version 82 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

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 one 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.