ID B4Q8W4_DROSI Unreviewed; 417 AA.
AC B4Q8W4;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 24-JAN-2024, entry version 75.
DE RecName: Full=Hydroxylysine kinase {ECO:0000256|ARBA:ARBA00040505};
DE EC=2.7.1.81 {ECO:0000256|ARBA:ARBA00038873};
GN Name=Dsim\GD24148 {ECO:0000313|EMBL:EDX05396.1};
GN ORFNames=Dsim_GD24148 {ECO:0000313|EMBL:EDX05396.1}, Dsimw501_GD24148
GN {ECO:0000313|EMBL:KMY90853.1};
OS Drosophila simulans (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7240 {ECO:0000313|EMBL:EDX05396.1, ECO:0000313|Proteomes:UP000000304};
RN [1] {ECO:0000313|EMBL:EDX05396.1, ECO:0000313|Proteomes:UP000000304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mixed {ECO:0000313|EMBL:EDX05396.1}, and mosaic
RC {ECO:0000313|Proteomes:UP000000304};
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RA Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B., Markow T.A.,
RA Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., Pollard D.A., Sackton T.B.,
RA Larracuente A.M., Singh N.D., Abad J.P., Abt D.N., Adryan B., Aguade M.,
RA Akashi H., Anderson W.W., Aquadro C.F., Ardell D.H., Arguello R.,
RA Artieri C.G., Barbash D.A., Barker D., Barsanti P., Batterham P.,
RA Batzoglou S., Begun D., Bhutkar A., Blanco E., Bosak S.A., Bradley R.K.,
RA Brand A.D., Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C.,
RA Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S.,
RA Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A.,
RA Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A., Daub J.,
RA David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., Edwards K.,
RA Eickbush T., Evans J.D., Filipski A., Findeiss S., Freyhult E., Fulton L.,
RA Fulton R., Garcia A.C., Gardiner A., Garfield D.A., Garvin B.E., Gibson G.,
RA Gilbert D., Gnerre S., Godfrey J., Good R., Gotea V., Gravely B.,
RA Greenberg A.J., Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A.,
RA Haerty W., Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V.,
RA Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A., Hubisz M.J.,
RA Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., Jeck W.R.,
RA Johnson J., Jones C.D., Jordan W.C., Karpen G.H., Kataoka E.,
RA Keightley P.D., Kheradpour P., Kirkness E.F., Koerich L.B., Kristiansen K.,
RA Kudrna D., Kulathinal R.J., Kumar S., Kwok R., Lander E., Langley C.H.,
RA Lapoint R., Lazzaro B.P., Lee S.J., Levesque L., Li R., Lin C.F., Lin M.F.,
RA Lindblad-Toh K., Llopart A., Long M., Low L., Lozovsky E., Lu J., Luo M.,
RA Machado C.A., Makalowski W., Marzo M., Matsuda M., Matzkin L.,
RA McAllister B., McBride C.S., McKernan B., McKernan K., Mendez-Lago M.,
RA Minx P., Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E.,
RA Negre B., Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L.,
RA Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S., Pesole G.,
RA Phillippy A.M., Ponting C.P., Pop M., Porcelli D., Powell J.R.,
RA Prohaska S., Pruitt K., Puig M., Quesneville H., Ram K.R., Rand D.,
RA Rasmussen M.D., Reed L.K., Reenan R., Reily A., Remington K.A.,
RA Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., Rohde C., Rozas J.,
RA Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., Sanchez-Gracia A.,
RA Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., Schlenke T.,
RA Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., Sisneros N.B.,
RA Smith C.D., Smith T.F., Spieth J., Stage D.E., Stark A., Stephan W.,
RA Strausberg R.L., Strempel S., Sturgill D., Sutton G., Sutton G.G., Tao W.,
RA Teichmann S., Tobari Y.N., Tomimura Y., Tsolas J.M., Valente V.L.,
RA Venter E., Venter J.C., Vicario S., Vieira F.G., Vilella A.J.,
RA Villasante A., Walenz B., Wang J., Wasserman M., Watts T., Wilson D.,
RA Wilson R.K., Wing R.A., Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G.,
RA Yamamoto D., Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E.,
RA Zhang P., Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA Bayul T., Berlin A., Bessette D., Bloom T., Blye J., Boguslavskiy L.,
RA Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA Chin C., Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
RN [2] {ECO:0000313|EMBL:EDX05396.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Mixed {ECO:0000313|EMBL:EDX05396.1}, and W501
RC {ECO:0000313|EMBL:KMY90853.1};
RG FlyBase;
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KMY90853.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W501 {ECO:0000313|EMBL:KMY90853.1};
RX PubMed=22936249; DOI=10.1101/gr.141689.112;
RA Hu T.T., Eisen M.B., Thornton K.R., Andolfatto P.;
RT "A second-generation assembly of the Drosophila simulans genome provides
RT new insights into patterns of lineage-specific divergence.";
RL Genome Res. 23:89-98(2013).
RN [4] {ECO:0000313|EMBL:KMY90853.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=W501 {ECO:0000313|EMBL:KMY90853.1};
RA Hu T., Eisen M.B., Thornton K.R., Andolfatto P.;
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the GTP-dependent phosphorylation of 5-hydroxy-L-
CC lysine. {ECO:0000256|ARBA:ARBA00037368}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5R)-5-hydroxy-L-lysine + GTP = (5R)-5-phosphooxy-L-lysine +
CC GDP + H(+); Xref=Rhea:RHEA:19049, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:37565, ChEBI:CHEBI:57882, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:58357; EC=2.7.1.81;
CC Evidence={ECO:0000256|ARBA:ARBA00036820};
CC -!- SIMILARITY: Belongs to the aminoglycoside phosphotransferase family.
CC {ECO:0000256|ARBA:ARBA00006219}.
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DR EMBL; CM000361; EDX05396.1; -; Genomic_DNA.
DR EMBL; CM002910; KMY90853.1; -; Genomic_DNA.
DR EMBL; CM002910; KMY90854.1; -; Genomic_DNA.
DR EMBL; CM002910; KMY90855.1; -; Genomic_DNA.
DR RefSeq; XP_016025433.1; XM_016180344.1.
DR RefSeq; XP_016025434.1; XM_016180345.1.
DR RefSeq; XP_016025435.1; XM_016180346.1.
DR AlphaFoldDB; B4Q8W4; -.
DR SMR; B4Q8W4; -.
DR STRING; 7240.B4Q8W4; -.
DR EnsemblMetazoa; FBtr0224058; FBpp0222550; FBgn0195503.
DR EnsemblMetazoa; FBtr0348627; FBpp0313545; FBgn0195503.
DR EnsemblMetazoa; FBtr0348630; FBpp0313548; FBgn0195503.
DR GeneID; 6732697; -.
DR KEGG; dsi:Dsimw501_GD24148; -.
DR HOGENOM; CLU_042971_1_0_1; -.
DR OMA; AAHSCQL; -.
DR OrthoDB; 5398335at2759; -.
DR Proteomes; UP000000304; Chromosome 2l.
DR Proteomes; UP000035880; Chromosome 2L.
DR Bgee; FBgn0195503; Expressed in adult organism and 3 other cell types or tissues.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.90.1200.10; -; 1.
DR InterPro; IPR002575; Aminoglycoside_PTrfase.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR PANTHER; PTHR21064:SF1; HYDROXYLYSINE KINASE; 1.
DR PANTHER; PTHR21064; UNCHARACTERIZED; 1.
DR Pfam; PF01636; APH; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000000304};
KW Transferase {ECO:0000313|EMBL:KMY90853.1}.
FT DOMAIN 92..324
FT /note="Aminoglycoside phosphotransferase"
FT /evidence="ECO:0000259|Pfam:PF01636"
FT REGION 28..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 417 AA; 47298 MW; 290151FADB883083 CRC64;
MEQWNNVELT NMSKKSYTLN HAYDAAEKLN KENTAKSSNG NGTSADESAA ADGDLLKPGS
DVRPKVEPED VESLLRRLYG ITISEVKEIV AYDDRNFFVK EDSNVKNPLI VTHCPHGYVL
KILNSLDSKK EDFVDAQNQM LLYLGKHSVK CPRPVANATG KYYSVERLNG NSNVVRLLEF
IPGEIFHQVP VTKHLLYRSG EYLARLDRAL KNFTHQAYET HKTLWMLQSV PELRQFLYVV
KDQELRLICD EVIDAFEAKV LSQLPSMEHQ IIHGDFNEQN IVVEQVPNQT EYTIKGVIDF
GDTSKSPLIF EIGIALTYMI LQANDLANGG IFLSGYTSLN PIENSELALL KYCVAARLVQ
SLVMGLYTHT LHPTNEYLLV TQEKGWKLLQ KLWRESLGDI DELWASTGHQ YLTQSNK
//
