KTRC_SCHMA
ID KTRC_SCHMA Reviewed; 746 AA.
AC P16641; A7UAX4; A7UAX5; C4QUJ5; G4VAV2;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 3.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Taurocyamine kinase;
DE EC=2.7.3.4;
DE AltName: Full=ATP:guanidino kinase Smc74;
DE AltName: Full=ATP:guanidino phosphotransferase;
DE Short=SmGK;
GN ORFNames=Smp_194770;
OS Schistosoma mansoni (Blood fluke).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=6183;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC STRAIN=Puerto Rican;
RX PubMed=2324092; DOI=10.1016/s0021-9258(19)39187-2;
RA Stein L.D., Harn D.A., David J.R.;
RT "A cloned ATP:guanidino kinase in the trematode Schistosoma mansoni has a
RT novel duplicated structure.";
RL J. Biol. Chem. 265:6582-6588(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS),
RP FUNCTION, CATALYTIC ACTIVITY, AND COFACTOR.
RX PubMed=18765922; DOI=10.1107/s1744309108025979;
RA Awama A.M., Paracuellos P., Laurent S., Dissous C., Marcillat O., Gouet P.;
RT "Crystallization and X-ray analysis of the Schistosoma mansoni guanidino
RT kinase.";
RL Acta Crystallogr. F 64:854-857(2008).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Puerto Rican;
RX PubMed=19606141; DOI=10.1038/nature08160;
RA Berriman M., Haas B.J., LoVerde P.T., Wilson R.A., Dillon G.P.,
RA Cerqueira G.C., Mashiyama S.T., Al-Lazikani B., Andrade L.F., Ashton P.D.,
RA Aslett M.A., Bartholomeu D.C., Blandin G., Caffrey C.R., Coghlan A.,
RA Coulson R., Day T.A., Delcher A., DeMarco R., Djikeng A., Eyre T.,
RA Gamble J.A., Ghedin E., Gu Y., Hertz-Fowler C., Hirai H., Hirai Y.,
RA Houston R., Ivens A., Johnston D.A., Lacerda D., Macedo C.D., McVeigh P.,
RA Ning Z., Oliveira G., Overington J.P., Parkhill J., Pertea M., Pierce R.J.,
RA Protasio A.V., Quail M.A., Rajandream M.A., Rogers J., Sajid M.,
RA Salzberg S.L., Stanke M., Tivey A.R., White O., Williams D.L., Wortman J.,
RA Wu W., Zamanian M., Zerlotini A., Fraser-Liggett C.M., Barrell B.G.,
RA El-Sayed N.M.;
RT "The genome of the blood fluke Schistosoma mansoni.";
RL Nature 460:352-358(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Puerto Rican;
RX PubMed=22253936; DOI=10.1371/journal.pntd.0001455;
RA Protasio A.V., Tsai I.J., Babbage A., Nichol S., Hunt M., Aslett M.A.,
RA De Silva N., Velarde G.S., Anderson T.J., Clark R.C., Davidson C.,
RA Dillon G.P., Holroyd N.E., LoVerde P.T., Lloyd C., McQuillan J.,
RA Oliveira G., Otto T.D., Parker-Manuel S.J., Quail M.A., Wilson R.A.,
RA Zerlotini A., Dunne D.W., Berriman M.;
RT "A systematically improved high quality genome and transcriptome of the
RT human blood fluke Schistosoma mansoni.";
RL PLoS Negl. Trop. Dis. 6:E1455-E1455(2012).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-683.
RC STRAIN=C, and IC;
RX PubMed=18083248; DOI=10.1016/j.molbiopara.2007.11.003;
RA Roger E., Mitta G., Mone Y., Bouchut A., Rognon A., Grunau C., Boissier J.,
RA Theron A., Gourbal B.E.;
RT "Molecular determinants of compatibility polymorphism in the Biomphalaria
RT glabrata/Schistosoma mansoni model: New candidates identified by a global
RT comparative proteomics approach.";
RL Mol. Biochem. Parasitol. 157:205-216(2008).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-52 AND 362-415.
RX PubMed=7739678; DOI=10.1016/0166-6851(94)90177-5;
RA Shoemaker C.B.;
RT "The Schistosoma mansoni phosphagen kinase gene contains two closely
RT apposed transcription initiation sites and arose from a fused gene
RT duplication.";
RL Mol. Biochem. Parasitol. 68:319-322(1994).
CC -!- FUNCTION: This family of enzymes reversibly catalyzes the transfer of
CC phosphate between ATP and various phosphogens (e.g. creatine
CC phosphate). {ECO:0000269|PubMed:18765922}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + taurocyamine = ADP + H(+) + N-phosphotaurocyamine;
CC Xref=Rhea:RHEA:22516, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57838, ChEBI:CHEBI:58064, ChEBI:CHEBI:456216; EC=2.7.3.4;
CC Evidence={ECO:0000269|PubMed:18765922};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:18765922};
CC -!- DEVELOPMENTAL STAGE: Expressed at low levels in 37-day sporocysts,
CC increases 25-fold in the infective cercarial and early schistosomular
CC stages. Levels decrease dramatically in adults, adult males have
CC approximately twice the expression level as in adult females.
CC {ECO:0000269|PubMed:2324092}.
CC -!- SIMILARITY: Belongs to the ATP:guanido phosphotransferase family.
CC {ECO:0000255|PROSITE-ProRule:PRU00842, ECO:0000255|PROSITE-
CC ProRule:PRU00843}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA29927.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CCD76533.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; J05410; AAA29927.1; ALT_FRAME; mRNA.
DR EMBL; HE601624; CCD76533.1; ALT_SEQ; Genomic_DNA.
DR EMBL; EU042595; ABU49845.1; -; mRNA.
DR EMBL; EU042596; ABU49846.1; -; mRNA.
DR EMBL; L31768; AAA29912.1; -; Genomic_DNA.
DR EMBL; L31769; AAA29913.1; -; Genomic_DNA.
DR PIR; A35743; A35743.
DR RefSeq; XP_018649405.1; XM_018795055.1.
DR PDB; 4WO8; X-ray; 2.20 A; A=31-746.
DR PDB; 4WOD; X-ray; 1.90 A; A=31-746.
DR PDB; 4WOE; X-ray; 2.30 A; A/B=31-746.
DR PDBsum; 4WO8; -.
DR PDBsum; 4WOD; -.
DR PDBsum; 4WOE; -.
DR AlphaFoldDB; P16641; -.
DR SMR; P16641; -.
DR STRING; 6183.Smp_194770.1; -.
DR EnsemblMetazoa; Smp_194770.1; Smp_194770.1; Smp_194770.
DR GeneID; 8351992; -.
DR KEGG; smm:Smp_194770; -.
DR WBParaSite; Smp_194770.1; Smp_194770.1; Smp_194770.
DR CTD; 8351992; -.
DR eggNOG; KOG3581; Eukaryota.
DR HOGENOM; CLU_019868_2_0_1; -.
DR InParanoid; P16641; -.
DR OrthoDB; 825025at2759; -.
DR BRENDA; 2.7.3.4; 5608.
DR Proteomes; UP000008854; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004111; F:creatine kinase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0050324; F:taurocyamine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0046314; P:phosphocreatine biosynthetic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.135.10; -; 2.
DR InterPro; IPR000749; ATP-guanido_PTrfase.
DR InterPro; IPR022415; ATP-guanido_PTrfase_AS.
DR InterPro; IPR022414; ATP-guanido_PTrfase_cat.
DR InterPro; IPR022413; ATP-guanido_PTrfase_N.
DR InterPro; IPR036802; ATP-guanido_PTrfase_N_sf.
DR InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR PANTHER; PTHR11547; PTHR11547; 2.
DR Pfam; PF00217; ATP-gua_Ptrans; 2.
DR Pfam; PF02807; ATP-gua_PtransN; 2.
DR SUPFAM; SSF48034; SSF48034; 2.
DR SUPFAM; SSF55931; SSF55931; 2.
DR PROSITE; PS00112; PHOSPHAGEN_KINASE; 2.
DR PROSITE; PS51510; PHOSPHAGEN_KINASE_C; 2.
DR PROSITE; PS51509; PHOSPHAGEN_KINASE_N; 2.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Flavoprotein; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Oxidoreductase; Reference proteome; Repeat;
KW Transferase.
FT CHAIN 1..746
FT /note="Taurocyamine kinase"
FT /id="PRO_0000212009"
FT REPEAT 31..393
FT /note="Approximate"
FT DOMAIN 35..116
FT /note="Phosphagen kinase N-terminal 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00842"
FT DOMAIN 146..382
FT /note="Phosphagen kinase C-terminal 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT REPEAT 394..705
FT /note="Approximate"
FT DOMAIN 398..479
FT /note="Phosphagen kinase N-terminal 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00842"
FT DOMAIN 509..746
FT /note="Phosphagen kinase C-terminal 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT ACT_SITE 298
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10029"
FT ACT_SITE 661
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10029"
FT BINDING 149..153
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 212
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 256
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 307..311
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 335..340
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 512..516
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 575
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 619
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 670..674
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 699..704
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT CONFLICT 45
FT /note="N -> S (in Ref. 5; ABU49846)"
FT /evidence="ECO:0000305"
FT CONFLICT 200..211
FT /note="MSEEDRIKLVND -> CQRGQNQTSKRH (in Ref. 1; AAA29927)"
FT /evidence="ECO:0000305"
FT CONFLICT 244
FT /note="N -> K (in Ref. 1; AAA29927)"
FT /evidence="ECO:0000305"
FT CONFLICT 264
FT /note="G -> R (in Ref. 1; AAA29927)"
FT /evidence="ECO:0000305"
FT CONFLICT 282
FT /note="K -> R (in Ref. 5; ABU49846)"
FT /evidence="ECO:0000305"
FT CONFLICT 523
FT /note="D -> G (in Ref. 1; AAA29927, 2; no nucleotide entry
FT and 4; ABU49845)"
FT /evidence="ECO:0000305"
FT CONFLICT 632
FT /note="V -> A (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 681..746
FT /note="SSQPKKLDEICAKYMLQARGLYGEHTESPDGTYDISNKRRLGLTELQAAHEM
FT AEGVAKMIEIEKGL -> VLNRKSWMKFVRSDMPSKLEVLLW (in Ref. 1;
FT AAA29927)"
FT /evidence="ECO:0000305"
FT HELIX 36..44
FT /evidence="ECO:0007829|PDB:4WOD"
FT HELIX 52..56
FT /evidence="ECO:0007829|PDB:4WOD"
FT HELIX 59..65
FT /evidence="ECO:0007829|PDB:4WOD"
FT HELIX 76..85
FT /evidence="ECO:0007829|PDB:4WOD"
FT HELIX 99..102
FT /evidence="ECO:0007829|PDB:4WOD"
FT HELIX 104..114
FT /evidence="ECO:0007829|PDB:4WOD"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:4WOE"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:4WOD"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:4WOD"
FT STRAND 147..156
FT /evidence="ECO:0007829|PDB:4WOD"
FT TURN 164..166
FT /evidence="ECO:0007829|PDB:4WOD"
FT HELIX 169..184
FT /evidence="ECO:0007829|PDB:4WOD"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:4WOD"
FT STRAND 192..197
FT /evidence="ECO:0007829|PDB:4WOD"
FT HELIX 202..210
FT /evidence="ECO:0007829|PDB:4WOD"
FT HELIX 220..224
FT /evidence="ECO:0007829|PDB:4WOD"
FT TURN 225..234
FT /evidence="ECO:0007829|PDB:4WOD"
FT STRAND 236..240
FT /evidence="ECO:0007829|PDB:4WOD"
FT STRAND 245..264
FT /evidence="ECO:0007829|PDB:4WOD"
FT HELIX 266..281
FT /evidence="ECO:0007829|PDB:4WOD"
FT TURN 290..292
FT /evidence="ECO:0007829|PDB:4WOD"
FT HELIX 299..301
FT /evidence="ECO:0007829|PDB:4WOD"
FT STRAND 307..313
FT /evidence="ECO:0007829|PDB:4WOD"
FT HELIX 315..318
FT /evidence="ECO:0007829|PDB:4WOD"
FT HELIX 323..329
FT /evidence="ECO:0007829|PDB:4WOD"
FT STRAND 332..336
FT /evidence="ECO:0007829|PDB:4WOD"
FT STRAND 348..354
FT /evidence="ECO:0007829|PDB:4WOD"
FT STRAND 357..359
FT /evidence="ECO:0007829|PDB:4WOD"
FT HELIX 361..385
FT /evidence="ECO:0007829|PDB:4WOD"
FT TURN 386..388
FT /evidence="ECO:0007829|PDB:4WOD"
FT HELIX 399..406
FT /evidence="ECO:0007829|PDB:4WOD"
FT TURN 411..413
FT /evidence="ECO:0007829|PDB:4WOD"
FT HELIX 415..418
FT /evidence="ECO:0007829|PDB:4WOD"
FT HELIX 422..428
FT /evidence="ECO:0007829|PDB:4WOD"
FT HELIX 439..448
FT /evidence="ECO:0007829|PDB:4WOD"
FT HELIX 462..465
FT /evidence="ECO:0007829|PDB:4WOD"
FT HELIX 467..478
FT /evidence="ECO:0007829|PDB:4WOD"
FT STRAND 506..519
FT /evidence="ECO:0007829|PDB:4WOD"
FT TURN 527..529
FT /evidence="ECO:0007829|PDB:4WOD"
FT HELIX 532..547
FT /evidence="ECO:0007829|PDB:4WOD"
FT HELIX 551..553
FT /evidence="ECO:0007829|PDB:4WOD"
FT STRAND 555..562
FT /evidence="ECO:0007829|PDB:4WOD"
FT HELIX 565..573
FT /evidence="ECO:0007829|PDB:4WOD"
FT HELIX 583..588
FT /evidence="ECO:0007829|PDB:4WOD"
FT TURN 589..597
FT /evidence="ECO:0007829|PDB:4WOD"
FT STRAND 599..603
FT /evidence="ECO:0007829|PDB:4WOD"
FT STRAND 606..628
FT /evidence="ECO:0007829|PDB:4WOD"
FT HELIX 629..644
FT /evidence="ECO:0007829|PDB:4WOD"
FT TURN 653..655
FT /evidence="ECO:0007829|PDB:4WOD"
FT HELIX 662..664
FT /evidence="ECO:0007829|PDB:4WOD"
FT STRAND 669..676
FT /evidence="ECO:0007829|PDB:4WOD"
FT HELIX 680..682
FT /evidence="ECO:0007829|PDB:4WOD"
FT TURN 684..687
FT /evidence="ECO:0007829|PDB:4WOD"
FT HELIX 688..693
FT /evidence="ECO:0007829|PDB:4WOD"
FT STRAND 696..699
FT /evidence="ECO:0007829|PDB:4WOD"
FT HELIX 709..711
FT /evidence="ECO:0007829|PDB:4WOE"
FT STRAND 712..717
FT /evidence="ECO:0007829|PDB:4WOD"
FT STRAND 721..723
FT /evidence="ECO:0007829|PDB:4WOD"
FT HELIX 725..745
FT /evidence="ECO:0007829|PDB:4WOD"
SQ SEQUENCE 746 AA; 83891 MW; 03B55FFD75E979B1 CRC64;
MTCTSAFIKV VRFIQVVIDT REIRSLCTIR MQVESLQNLQ AKIRNDERNH SLTKKYLTDD
IVKKYQATKT SLGGTLAQCV NTNAYNPGAL LPRSCDLNAY ETFRDFFDAV IADYHKVPDG
KIQHPKSNFG DLKSLSFTDL NTYGNLVVST RVRLGRTVEG FGFGPTLTKE TRIELENKIS
TALHNLSGEY EGTYYPLTGM SEEDRIKLVN DHFLFRNDDN VLRDAGGYID WPTGRGIFIN
KQKNFLVWIN EEDHIRVISM QKGGDLIAVY KRLADAIQEL SKSLKFAFND RLGFITFCPS
NLGTTLRASV HAKIPMLASL PNFKEICEKH GIQPRGTHGE HTESVGGIYD LSNKRRLGLT
ELDAVTEMHS GVRALLELEV MLQEYNKGAP EGVMPVEPLT YLAKLLEGAS IEKCYTRKYL
TPEIIKKYDG KRTTHGATLA HMIRNGAYNN RSICPRTGEA ECYSTFIDYL DPLICDYHGV
KDSAFKHPAP TFGDLSKLPF GDLDPTGKFI VSTRVRVGRS VEDFLFPTIM SKTDRIKLEQ
VISGALKGLT GEHAGTYYPL TDMKEEDRKQ LVEDHFLFKN DDPVLRDAGG YRDWPVGRGI
FHNNSKTFLV WVCEEDHMRI ISMQQGGNLA AVYKRLIEGI NAIGKSMKFA HSDKYGYITC
CPSNLGTSMR ASVLLKIPKL SSQPKKLDEI CAKYMLQARG LYGEHTESPD GTYDISNKRR
LGLTELQAAH EMAEGVAKMI EIEKGL
