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 24-JAN-2024, entry version 112. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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.P16641; -. DR EnsemblMetazoa; Smp_194770.1; Smp_194770.1; Smp_194770. DR GeneID; 8351992; -. DR KEGG; smm:Smp_194770; -. DR CTD; 8351992; -. DR eggNOG; KOG3581; Eukaryota. DR HOGENOM; CLU_019868_2_0_1; -. DR InParanoid; P16641; -. DR OrthoDB; 35839at2759; -. 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 CDD; cd07932; arginine_kinase_like; 2. DR Gene3D; 1.10.135.10; ATP:guanido phosphotransferase, N-terminal domain; 2. DR Gene3D; 3.30.590.10; Glutamine synthetase/guanido kinase, catalytic domain; 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:SF38; ARGININE KINASE; 1. DR PANTHER; PTHR11547; ARGININE OR CREATINE KINASE; 1. DR Pfam; PF00217; ATP-gua_Ptrans; 2. DR Pfam; PF02807; ATP-gua_PtransN; 2. DR SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 2. DR SUPFAM; SSF48034; Guanido kinase N-terminal domain; 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 //