ID W5MQ21_LEPOC Unreviewed; 710 AA.
AC W5MQ21;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Adenylate kinase 7 {ECO:0000313|Ensembl:ENSLOCP00000010480.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000010480.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000010480.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR EMBL; AHAT01003930; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5MQ21; -.
DR STRING; 7918.ENSLOCP00000010480; -.
DR Ensembl; ENSLOCT00000010495.1; ENSLOCP00000010480.1; ENSLOCG00000008611.1.
DR eggNOG; KOG3078; Eukaryota.
DR GeneTree; ENSGT00390000015102; -.
DR HOGENOM; CLU_015567_1_0_1; -.
DR InParanoid; W5MQ21; -.
DR OMA; LCRSRMM; -.
DR Proteomes; UP000018468; Linkage group LG7.
DR Bgee; ENSLOCG00000008611; Expressed in embryo and 8 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004017; F:adenylate kinase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004127; F:cytidylate kinase activity; IBA:GO_Central.
DR GO; GO:0004550; F:nucleoside diphosphate kinase activity; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd01428; ADK; 1.
DR CDD; cd22967; DD_AK7; 1.
DR Gene3D; 1.20.890.10; cAMP-dependent protein kinase regulatory subunit, dimerization-anchoring domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR000850; Adenylat/UMP-CMP_kin.
DR InterPro; IPR047499; DD_AK7.
DR InterPro; IPR007858; Dpy-30_motif.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR23359:SF105; ADENYLATE KINASE 7; 1.
DR PANTHER; PTHR23359; NUCLEOTIDE KINASE; 1.
DR Pfam; PF00406; ADK; 1.
DR Pfam; PF05186; Dpy-30; 1.
DR PRINTS; PR00094; ADENYLTKNASE.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT REGION 45..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 606..660
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 45..59
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 710 AA; 81271 MW; 0EA8FBBAD5DD3750 CRC64;
QSSMANEEKE NIVRSKRVFI NQIDTYTSKH IGKYLSNCAV GASLEEIEGE EEEEEEEKAA
QDELPKPKEG TFQIVGTVSK PEEKKIGFAQ EEYSISTREE LLDRLMECDV VIYNISENAD
QVDEASWAIS ALHSELDNFS SPKMFILIST VMTWALSKPV DPDDPEIPFT EDDYRRRRPH
PNFKDHISTE KLVIKLGKTK KSRLSTYVVA SGLRYGMGEQ IFHFFFKASW LGELPSIPVF
GQGTNIIPTI HINDLAGVIQ NVIDHKPKTH YLLAVDDSKN SLEDIVKTVS SVLGPGKTQR
VPKEDAFLNR ELMQADIDSL AVSLRMETVF LKENFNIRWV TETGLIENIE HIVKEYKQTR
GLLPIKICIL GPPAVGKSTV AEKICECYKL HHVKIKGVIT EAIAKLEVQS RMEEGENEGE
ESGGGAQELL EALKENMEQN SGRLDDQYVI RLMKDKLKSK PCQNQGFVLD GFPKTYEQAK
ELFYGDEDEP EDAKSKIPPF DKKIIPEYVF SLDATDEFLK NRVLNLPESV VAGTHYTQDQ
FLRRLAAFRE ANVEDETVLN YFDELEIHPE HIHISSRDDA EYTAVIEQIE KVVGKPRNYG
PTVEELEELE RRNADERLRR EAAEQAERER REAGEAADRM ARWEEWNRRL EEVKQQEQEQ
LEAQAVPLRN YLMRNVMPTL TQGLLQCCRV KPDDPVDFLA EYLFKNNPQI
//