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Database: UniProt/SWISS-PROT
Entry: KTRC_SCHMA
LinkDB: KTRC_SCHMA
Original site: 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   28-FEB-2018, entry version 91.
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; Platyhelminthes; Trematoda; Digenea; Strigeidida;
OC   Schistosomatoidea; Schistosomatidae; Schistosoma.
OX   NCBI_TaxID=6183;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC   STRAIN=Puerto Rican;
RX   PubMed=2324092;
RA   Stein L.D., Harn D.A., David J.R.;
RT   "A cloned ATP:guanidino kinase in the trematode Schistosoma mansoni
RT   has a 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.,
RA   Gouet P.;
RT   "Crystallization and X-ray analysis of the Schistosoma mansoni
RT   guanidino 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.,
RA   Ashton P.D., Aslett M.A., Bartholomeu D.C., Blandin G., Caffrey C.R.,
RA   Coghlan A., Coulson R., Day T.A., Delcher A., DeMarco R., Djikeng A.,
RA   Eyre T., Gamble J.A., Ghedin E., Gu Y., Hertz-Fowler C., Hirai H.,
RA   Hirai Y., Houston R., Ivens A., Johnston D.A., Lacerda D.,
RA   Macedo C.D., McVeigh P., Ning Z., Oliveira G., Overington J.P.,
RA   Parkhill J., Pertea M., Pierce R.J., Protasio A.V., Quail M.A.,
RA   Rajandream M.A., Rogers J., Sajid M., Salzberg S.L., Stanke M.,
RA   Tivey A.R., White O., Williams D.L., Wortman J., Wu W., Zamanian M.,
RA   Zerlotini A., Fraser-Liggett C.M., Barrell B.G., 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
RT   the 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.,
RA   Boissier J., Theron A., Gourbal B.E.;
RT   "Molecular determinants of compatibility polymorphism in the
RT   Biomphalaria glabrata/Schistosoma mansoni model: New candidates
RT   identified by a global 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
CC       of phosphate between ATP and various phosphogens (e.g. creatine
CC       phosphate). {ECO:0000269|PubMed:18765922}.
CC   -!- CATALYTIC ACTIVITY: ATP + taurocyamine = ADP + N-
CC       phosphotaurocyamine. {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
CC       schistosomular stages. Levels decrease dramatically in adults,
CC       adult males have approximately twice the expression level as in
CC       adult females. {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; Positions=416, 434, 644; Evidence={ECO:0000305};
CC       Sequence=CCD76533.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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   SMR; P16641; -.
DR   STRING; 6183.Smp_194770__mRNA; -.
DR   GeneDB; Smp_194770.1:pep; -.
DR   GeneID; 8351992; -.
DR   KEGG; smm:Smp_194770; -.
DR   CTD; 8351992; -.
DR   eggNOG; KOG0042; Eukaryota.
DR   eggNOG; KOG3581; Eukaryota.
DR   eggNOG; COG0578; LUCA.
DR   eggNOG; COG3869; LUCA.
DR   HOGENOM; HOG000006584; -.
DR   InParanoid; P16641; -.
DR   KO; K00933; -.
DR   OrthoDB; EOG091G0HZ0; -.
DR   BRENDA; 2.7.3.4; 5608.
DR   Proteomes; UP000008854; Chromosome 1.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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   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; Complete proteome; Flavoprotein; Kinase;
KW   Magnesium; Metal-binding; Nucleotide-binding; Oxidoreductase;
KW   Reference proteome; Repeat; Transferase.
FT   CHAIN         1    746       Taurocyamine kinase.
FT                                /FTId=PRO_0000212009.
FT   REPEAT       31    393       Approximate.
FT   DOMAIN       35    116       Phosphagen kinase N-terminal 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00842}.
FT   DOMAIN      146    382       Phosphagen kinase C-terminal 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00843}.
FT   REPEAT      394    705       Approximate.
FT   DOMAIN      398    479       Phosphagen kinase N-terminal 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00842}.
FT   DOMAIN      509    746       Phosphagen kinase C-terminal 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00843}.
FT   NP_BIND     149    153       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00843}.
FT   NP_BIND     307    311       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00843}.
FT   NP_BIND     335    340       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00843}.
FT   NP_BIND     512    516       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00843}.
FT   NP_BIND     670    674       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00843}.
FT   NP_BIND     699    704       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00843}.
FT   ACT_SITE    298    298       {ECO:0000255|PROSITE-ProRule:PRU10029}.
FT   ACT_SITE    661    661       {ECO:0000255|PROSITE-ProRule:PRU10029}.
FT   BINDING     212    212       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00843}.
FT   BINDING     256    256       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00843}.
FT   BINDING     575    575       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00843}.
FT   BINDING     619    619       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00843}.
FT   CONFLICT     45     45       N -> S (in Ref. 5; ABU49846).
FT                                {ECO:0000305}.
FT   CONFLICT    200    211       MSEEDRIKLVND -> CQRGQNQTSKRH (in Ref. 1;
FT                                AAA29927). {ECO:0000305}.
FT   CONFLICT    244    244       N -> K (in Ref. 1; AAA29927).
FT                                {ECO:0000305}.
FT   CONFLICT    264    264       G -> R (in Ref. 1; AAA29927).
FT                                {ECO:0000305}.
FT   CONFLICT    282    282       K -> R (in Ref. 5; ABU49846).
FT                                {ECO:0000305}.
FT   CONFLICT    523    523       D -> G (in Ref. 1; AAA29927, 2; no
FT                                nucleotide entry and 4; ABU49845).
FT                                {ECO:0000305}.
FT   CONFLICT    632    632       V -> A (in Ref. 2; no nucleotide entry).
FT                                {ECO:0000305}.
FT   CONFLICT    681    746       SSQPKKLDEICAKYMLQARGLYGEHTESPDGTYDISNKRRL
FT                                GLTELQAAHEMAEGVAKMIEIEKGL -> VLNRKSWMKFVR
FT                                SDMPSKLEVLLW (in Ref. 1; AAA29927).
FT                                {ECO:0000305}.
FT   HELIX        36     44       {ECO:0000244|PDB:4WOD}.
FT   HELIX        52     56       {ECO:0000244|PDB:4WOD}.
FT   HELIX        59     65       {ECO:0000244|PDB:4WOD}.
FT   HELIX        76     85       {ECO:0000244|PDB:4WOD}.
FT   HELIX        99    102       {ECO:0000244|PDB:4WOD}.
FT   HELIX       104    114       {ECO:0000244|PDB:4WOD}.
FT   HELIX       118    120       {ECO:0000244|PDB:4WOE}.
FT   HELIX       132    134       {ECO:0000244|PDB:4WOD}.
FT   HELIX       140    142       {ECO:0000244|PDB:4WOD}.
FT   STRAND      147    156       {ECO:0000244|PDB:4WOD}.
FT   TURN        164    166       {ECO:0000244|PDB:4WOD}.
FT   HELIX       169    184       {ECO:0000244|PDB:4WOD}.
FT   HELIX       188    190       {ECO:0000244|PDB:4WOD}.
FT   STRAND      192    197       {ECO:0000244|PDB:4WOD}.
FT   HELIX       202    210       {ECO:0000244|PDB:4WOD}.
FT   HELIX       220    224       {ECO:0000244|PDB:4WOD}.
FT   TURN        225    234       {ECO:0000244|PDB:4WOD}.
FT   STRAND      236    240       {ECO:0000244|PDB:4WOD}.
FT   STRAND      245    264       {ECO:0000244|PDB:4WOD}.
FT   HELIX       266    281       {ECO:0000244|PDB:4WOD}.
FT   TURN        290    292       {ECO:0000244|PDB:4WOD}.
FT   HELIX       299    301       {ECO:0000244|PDB:4WOD}.
FT   STRAND      307    313       {ECO:0000244|PDB:4WOD}.
FT   HELIX       315    318       {ECO:0000244|PDB:4WOD}.
FT   HELIX       323    329       {ECO:0000244|PDB:4WOD}.
FT   STRAND      332    336       {ECO:0000244|PDB:4WOD}.
FT   STRAND      348    354       {ECO:0000244|PDB:4WOD}.
FT   STRAND      357    359       {ECO:0000244|PDB:4WOD}.
FT   HELIX       361    385       {ECO:0000244|PDB:4WOD}.
FT   TURN        386    388       {ECO:0000244|PDB:4WOD}.
FT   HELIX       399    406       {ECO:0000244|PDB:4WOD}.
FT   TURN        411    413       {ECO:0000244|PDB:4WOD}.
FT   HELIX       415    418       {ECO:0000244|PDB:4WOD}.
FT   HELIX       422    428       {ECO:0000244|PDB:4WOD}.
FT   HELIX       439    448       {ECO:0000244|PDB:4WOD}.
FT   HELIX       462    465       {ECO:0000244|PDB:4WOD}.
FT   HELIX       467    478       {ECO:0000244|PDB:4WOD}.
FT   STRAND      506    519       {ECO:0000244|PDB:4WOD}.
FT   TURN        527    529       {ECO:0000244|PDB:4WOD}.
FT   HELIX       532    547       {ECO:0000244|PDB:4WOD}.
FT   HELIX       551    553       {ECO:0000244|PDB:4WOD}.
FT   STRAND      555    562       {ECO:0000244|PDB:4WOD}.
FT   HELIX       565    573       {ECO:0000244|PDB:4WOD}.
FT   HELIX       583    588       {ECO:0000244|PDB:4WOD}.
FT   TURN        589    597       {ECO:0000244|PDB:4WOD}.
FT   STRAND      599    603       {ECO:0000244|PDB:4WOD}.
FT   STRAND      606    628       {ECO:0000244|PDB:4WOD}.
FT   HELIX       629    644       {ECO:0000244|PDB:4WOD}.
FT   TURN        653    655       {ECO:0000244|PDB:4WOD}.
FT   HELIX       662    664       {ECO:0000244|PDB:4WOD}.
FT   STRAND      669    676       {ECO:0000244|PDB:4WOD}.
FT   HELIX       680    682       {ECO:0000244|PDB:4WOD}.
FT   TURN        684    687       {ECO:0000244|PDB:4WOD}.
FT   HELIX       688    693       {ECO:0000244|PDB:4WOD}.
FT   STRAND      696    699       {ECO:0000244|PDB:4WOD}.
FT   HELIX       709    711       {ECO:0000244|PDB:4WOE}.
FT   STRAND      712    717       {ECO:0000244|PDB:4WOD}.
FT   STRAND      721    723       {ECO:0000244|PDB:4WOD}.
FT   HELIX       725    745       {ECO:0000244|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
//
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