ID Q7PIQ5_ANOGA Unreviewed; 397 AA. AC Q7PIQ5; DT 15-DEC-2003, integrated into UniProtKB/TrEMBL. DT 09-JAN-2007, sequence version 3. DT 24-JAN-2024, entry version 141. DE RecName: Full=arginine kinase {ECO:0000256|ARBA:ARBA00012230}; DE EC=2.7.3.3 {ECO:0000256|ARBA:ARBA00012230}; GN Name=1276313 {ECO:0000313|EnsemblMetazoa:AGAP029820-PA}; GN ORFNames=AgaP_AGAP005627 {ECO:0000313|EMBL:EAA44056.3}; OS Anopheles gambiae (African malaria mosquito). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae; OC Anophelinae; Anopheles. OX NCBI_TaxID=7165 {ECO:0000313|EMBL:EAA44056.3}; RN [1] {ECO:0000313|EMBL:EAA44056.3, ECO:0000313|Proteomes:UP000007062} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PEST {ECO:0000313|EMBL:EAA44056.3, RC ECO:0000313|Proteomes:UP000007062}; RX PubMed=12364791; DOI=10.1126/science.1076181; RA Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R., RA Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R., RA Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z., RA Kraft C.L., Abril J.F., Anthouard V., Arensburger P., Atkinson P.W., RA Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C., RA Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K., RA Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V., RA Dana A., Delcher A., Dew I., Evans C.A., Flanigan M., RA Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R., RA Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J., RA Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I., RA Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A., RA McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D., RA O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H., RA Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J., RA Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B., RA Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M., RA Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I., RA Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J., RA Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M., RA Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C., RA Collins F.H., Hoffman S.L.; RT "The genome sequence of the malaria mosquito Anopheles gambiae."; RL Science 298:129-149(2002). RN [2] {ECO:0000313|EMBL:EAA44056.3} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PEST {ECO:0000313|EMBL:EAA44056.3}; RG The Anopheles Genome Sequencing Consortium; RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:EAA44056.3} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PEST {ECO:0000313|EMBL:EAA44056.3}; RX PubMed=14747013; DOI=10.1016/j.pt.2003.11.003; RA Mongin E., Louis C., Holt R.A., Birney E., Collins F.H.; RT "The Anopheles gambiae genome: an update."; RL Trends Parasitol. 20:49-52(2004). RN [4] {ECO:0000313|EMBL:EAA44056.3} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PEST {ECO:0000313|EMBL:EAA44056.3}; RX PubMed=17210077; DOI=10.1186/gb-2007-8-1-r5; RA Sharakhova M.V., Hammond M.P., Lobo N.F., Krzywinski J., Unger M.F., RA Hillenmeyer M.E., Bruggner R.V., Birney E., Collins F.H.; RT "Update of the Anopheles gambiae PEST genome assembly."; RL Genome Biol. 8:R5.1-R5.13(2007). RN [5] {ECO:0000313|EMBL:EAA44056.3} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PEST {ECO:0000313|EMBL:EAA44056.3}; RG VectorBase; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. RN [6] {ECO:0000313|EnsemblMetazoa:AGAP029820-PA} RP IDENTIFICATION. RC STRAIN=PEST {ECO:0000313|EnsemblMetazoa:AGAP029820-PA}; RG EnsemblMetazoa; RL Submitted (MAY-2020) to UniProtKB. CC -!- SIMILARITY: Belongs to the ATP:guanido phosphotransferase family. CC {ECO:0000256|ARBA:ARBA00006798, ECO:0000256|PROSITE-ProRule:PRU00842, CC ECO:0000256|RuleBase:RU000505}. 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; AAAB01008960; EAA44056.3; -; Genomic_DNA. DR EMBL; AAAB01008960; EDO63704.1; -; Genomic_DNA. DR RefSeq; XP_001688698.1; XM_001688646.1. DR RefSeq; XP_315641.3; XM_315641.4. DR AlphaFoldDB; Q7PIQ5; -. DR STRING; 7165.Q7PIQ5; -. DR PaxDb; 7165-AGAP005627-PF; -. DR EnsemblMetazoa; AGAP029820-RA; AGAP029820-PA; AGAP029820. DR GeneID; 1276313; -. DR VEuPathDB; VectorBase:AGAP029820; -. DR eggNOG; KOG3581; Eukaryota. DR InParanoid; Q7PIQ5; -. DR Proteomes; UP000007062; Chromosome 2L. DR GO; GO:0004054; F:arginine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004111; F:creatine kinase activity; IEA:InterPro. DR GO; GO:0016301; F:kinase activity; IBA:GO_Central. 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; 1. DR Gene3D; 1.10.135.10; ATP:guanido phosphotransferase, N-terminal domain; 1. DR Gene3D; 3.30.590.10; Glutamine synthetase/guanido kinase, catalytic domain; 1. 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; 1. DR Pfam; PF02807; ATP-gua_PtransN; 1. DR SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 1. DR SUPFAM; SSF48034; Guanido kinase N-terminal domain; 1. DR PROSITE; PS00112; PHOSPHAGEN_KINASE; 1. DR PROSITE; PS51510; PHOSPHAGEN_KINASE_C; 1. DR PROSITE; PS51509; PHOSPHAGEN_KINASE_N; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE- KW ProRule:PRU00843}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PROSITE- KW ProRule:PRU00843}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU00843}; Reference proteome {ECO:0000313|Proteomes:UP000007062}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE- KW ProRule:PRU00843}. FT DOMAIN 48..132 FT /note="Phosphagen kinase N-terminal" FT /evidence="ECO:0000259|PROSITE:PS51509" FT DOMAIN 160..397 FT /note="Phosphagen kinase C-terminal" FT /evidence="ECO:0000259|PROSITE:PS51510" FT REGION 1..40 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..16 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 163..167 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00843" FT BINDING 226 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00843" FT BINDING 270 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00843" FT BINDING 321..325 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00843" FT BINDING 350..355 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00843" SQ SEQUENCE 397 AA; 43773 MW; 3C880D14D37E722D CRC64; MGGCASKDKK DSKVVENETA AGTGGGTDAE AANGGEGNKS DTMVDAAVME KMEAGFAKLA ASDSKSLLKK YLTKEVFDAL KNKKTSFGST LLDCVQSGFE NPDSGVGIYA PDAEAYSLFA DLFDPIIEDY HKGFKKTDKH PASDFGDVNA FGNVDPTGEF VVSTRVRCGR SMEGYPFNPC LTEAQYKEME GKVSTTLSGL EGELKGKFYP LTGMDKAVQQ QLIDDHFLFK EGDRFLQAAN ACRYWPSGRG IYHNDNKTFL VWCNEEDHLR IISMQMGGDL GQVYRRLVTA VNDIEKRIPF SHHDRLGFLT FCPTNLGTTI RASVHIKVPK LAKDYAKLEA TADKYNLQVR GTRGEHSEAE GGIYDISNKR RMGLTEFQAV KEMYDGISEI IKIEKSL //