(data stored in ACNUC7421 zone)

SWISSPROT: C8W3V3_DESAS

ID   C8W3V3_DESAS            Unreviewed;       353 AA.
AC   C8W3V3;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   16-JAN-2019, entry version 68.
DE   RecName: Full=Protein-arginine kinase {ECO:0000256|HAMAP-Rule:MF_00602, ECO:0000256|SAAS:SAAS00894317};
DE            EC=2.7.14.1 {ECO:0000256|HAMAP-Rule:MF_00602, ECO:0000256|SAAS:SAAS00894303};
GN   Name=mcsB {ECO:0000256|HAMAP-Rule:MF_00602};
GN   OrderedLocusNames=Dtox_0254 {ECO:0000313|EMBL:ACV61207.1};
OS   Desulfotomaculum acetoxidans (strain ATCC 49208 / DSM 771 / VKM
OS   B-1644) (Desulfofarcimen acetoxidans).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Desulfofarcimen.
OX   NCBI_TaxID=485916 {ECO:0000313|EMBL:ACV61207.1, ECO:0000313|Proteomes:UP000002217};
RN   [1] {ECO:0000313|EMBL:ACV61207.1, ECO:0000313|Proteomes:UP000002217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49208 / DSM 771 / VKM B-1644
RC   {ECO:0000313|Proteomes:UP000002217};
RX   PubMed=21304664; DOI=10.4056/sigs.39508;
RA   Spring S., Lapidus A., Schroder M., Gleim D., Sims D., Meincke L.,
RA   Glavina Del Rio T., Tice H., Copeland A., Cheng J.F., Lucas S.,
RA   Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S., Ivanova N.,
RA   Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P., Saunders E.,
RA   Brettin T., Detter J.C., Goker M., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Han C.;
RT   "Complete genome sequence of Desulfotomaculum acetoxidans type strain
RT   (5575).";
RL   Stand. Genomic Sci. 1:242-253(2009).
CC   -!- FUNCTION: Catalyzes the specific phosphorylation of arginine
CC       residues in proteins. {ECO:0000256|HAMAP-Rule:MF_00602}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-arginyl-[protein] = ADP + H(+) + N(omega)-
CC         phospho-L-arginyl-[protein]; Xref=Rhea:RHEA:43384, Rhea:RHEA-
CC         COMP:10532, Rhea:RHEA-COMP:10533, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29965, ChEBI:CHEBI:30616, ChEBI:CHEBI:83226,
CC         ChEBI:CHEBI:456216; EC=2.7.14.1; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00602, ECO:0000256|SAAS:SAAS01117987};
CC   -!- SIMILARITY: Belongs to the ATP:guanido phosphotransferase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00602, ECO:0000256|PROSITE-
CC       ProRule:PRU00843, ECO:0000256|RuleBase:RU000505,
CC       ECO:0000256|SAAS:SAAS00894300}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00602}.
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DR   EMBL; CP001720; ACV61207.1; -; Genomic_DNA.
DR   RefSeq; WP_015755928.1; NC_013216.1.
DR   STRING; 485916.Dtox_0254; -.
DR   EnsemblBacteria; ACV61207; ACV61207; Dtox_0254.
DR   KEGG; dae:Dtox_0254; -.
DR   eggNOG; ENOG41066A3; Bacteria.
DR   eggNOG; COG3869; LUCA.
DR   HOGENOM; HOG000082112; -.
DR   KO; K19405; -.
DR   OMA; ACPTNVG; -.
DR   OrthoDB; 904915at2; -.
DR   BioCyc; DACE485916:G1GFV-264-MONOMER; -.
DR   Proteomes; UP000002217; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016775; F:phosphotransferase activity, nitrogenous group as acceptor; IEA:UniProtKB-UniRule.
DR   GO; GO:0004672; F:protein kinase activity; IEA:UniProtKB-UniRule.
DR   CDD; cd07930; bacterial_phosphagen_kinase; 1.
DR   HAMAP; MF_00602; Prot_Arg_kinase; 1.
DR   InterPro; IPR023660; Arg_Kinase.
DR   InterPro; IPR000749; ATP-guanido_PTrfase.
DR   InterPro; IPR022415; ATP-guanido_PTrfase_AS.
DR   InterPro; IPR022414; ATP-guanido_PTrfase_cat.
DR   InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR   PANTHER; PTHR11547; PTHR11547; 1.
DR   Pfam; PF00217; ATP-gua_Ptrans; 1.
DR   SUPFAM; SSF55931; SSF55931; 1.
DR   PROSITE; PS00112; PHOSPHAGEN_KINASE; 1.
DR   PROSITE; PS51510; PHOSPHAGEN_KINASE_C; 1.
PE   3: Inferred from homology;
DR   PRODOM; C8W3V3.
DR   SWISS-2DPAGE; C8W3V3.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00602, ECO:0000256|PROSITE-
KW   ProRule:PRU00843, ECO:0000256|SAAS:SAAS00894316};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002217};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00602, ECO:0000256|PROSITE-
KW   ProRule:PRU00843, ECO:0000256|RuleBase:RU000505,
KW   ECO:0000256|SAAS:SAAS00894304};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00602,
KW   ECO:0000256|PROSITE-ProRule:PRU00843, ECO:0000256|SAAS:SAAS00894308};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002217};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00602, ECO:0000256|PROSITE-
KW   ProRule:PRU00843, ECO:0000256|RuleBase:RU000505,
KW   ECO:0000256|SAAS:SAAS00894312}.
FT   DOMAIN       24    256       Phosphagen kinase C-terminal.
FT                                {ECO:0000259|PROSITE:PS51510}.
FT   NP_BIND      27     31       ATP. {ECO:0000256|HAMAP-Rule:MF_00602,
FT                                ECO:0000256|PROSITE-ProRule:PRU00843}.
FT   NP_BIND     178    182       ATP. {ECO:0000256|HAMAP-Rule:MF_00602,
FT                                ECO:0000256|PROSITE-ProRule:PRU00843}.
FT   NP_BIND     209    214       ATP. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00843}.
FT   BINDING      93     93       ATP. {ECO:0000256|HAMAP-Rule:MF_00602,
FT                                ECO:0000256|PROSITE-ProRule:PRU00843}.
FT   BINDING     127    127       ATP. {ECO:0000256|HAMAP-Rule:MF_00602,
FT                                ECO:0000256|PROSITE-ProRule:PRU00843}.
SQ   SEQUENCE   353 AA;  39501 MW;  9B5B7A36BE1118DD CRC64;
     MSLRDIINNT FSNWMDSTAP EADIVISSRI RIARNLKQWP FPHMLPVENA EQVIHAVKAA
     VSNENFINSF GSLELVWMSE LTPVERRILV EKHLISPDLL DNYNKKAVIL RSDEAVSIMI
     NEEDHLRLQC VLPGLQLKDA WSLMNKLDDG LEFTLDYSYS DRLGYLTACP TNVGTGLRAS
     VMIHLPGLVL ANQIGGVLSA IAKLGITVRG MYGEGTQALG NIFQISNQIT LGQAEEEIIN
     NIISITRQLL AQERAARQAL LKERNEFLAD RVCRSLGILK HARMINAEET MRMFSDVRLG
     VDLNIIEGID TGLLSELMVL SRPAYLIKKA GKEITTVDQD ILRAELIRER LNG
//

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