ID A0A2A2LNJ1_9BILA Unreviewed; 723 AA.
AC A0A2A2LNJ1;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Adenylate kinase isoenzyme 5 {ECO:0008006|Google:ProtNLM};
GN ORFNames=WR25_00286 {ECO:0000313|EMBL:PAV87557.1};
OS Diploscapter pachys.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Diploscapter.
OX NCBI_TaxID=2018661 {ECO:0000313|EMBL:PAV87557.1, ECO:0000313|Proteomes:UP000218231};
RN [1] {ECO:0000313|EMBL:PAV87557.1, ECO:0000313|Proteomes:UP000218231}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PF1309 {ECO:0000313|EMBL:PAV87557.1};
RA Fradin H., Zegar C., Gutwein M., Lucas J., Kovtun M., Corcoran D.,
RA Baugh L.R., Kiontke K., Gunsalus K., Fitch D.H., Piano F.;
RT "Genome architecture and evolution of a unichromosomal asexual nematode.";
RL Curr. Biol. 0:0-0(2017).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PAV87557.1}.
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DR EMBL; LIAE01006560; PAV87557.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A2LNJ1; -.
DR STRING; 2018661.A0A2A2LNJ1; -.
DR Proteomes; UP000218231; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0019205; F:nucleobase-containing compound kinase activity; IEA:InterPro.
DR GO; GO:0006139; P:nucleobase-containing compound metabolic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd01428; ADK; 2.
DR CDD; cd22978; DD_AK5; 1.
DR Gene3D; 1.20.890.10; cAMP-dependent protein kinase regulatory subunit, dimerization-anchoring domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR HAMAP; MF_00235; Adenylate_kinase_Adk; 1.
DR InterPro; IPR000850; Adenylat/UMP-CMP_kin.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR23359:SF111; ADENYLATE KINASE ISOENZYME 5-LIKE PROTEIN; 1.
DR PANTHER; PTHR23359; NUCLEOTIDE KINASE; 1.
DR Pfam; PF00406; ADK; 2.
DR PRINTS; PR00094; ADENYLTKNASE.
DR SUPFAM; SSF47391; Dimerization-anchoring domain of cAMP-dependent PK regulatory subunit; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
PE 3: Inferred from homology;
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Reference proteome {ECO:0000313|Proteomes:UP000218231};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT REGION 55..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 358..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..128
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..386
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..517
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 723 AA; 81227 MW; 20015A365E1B8AA0 CRC64;
MGAEARVYLQ EHSIPQLFEG LMTGLLYNRP EDPLRFLEDA IGHIRKHPNE TVAWDTFLNN
KEPHKGKQSK SKRKEPKEAV TSTKDKDKGE KSEKGEKKHS KSSKKSEEKH EKKQSVEVVE
KEGEEPQQQQ MVLHRTPSVI RAAEVAQIPN VPVILFMGEL IDSGGPGGGK TRHAAKVANA
LSSNGLVHIC MPDVIRSALS KYKDRYPEWK DANENYLRGE LIPNNLALSL LKAEMGRHPD
AAAFFLEGFP REARQVEDFE RQVKSVNMAM ILDYDERTLR DHMERRGLGM EIIDQKIKEF
KQKTLPSAKY FDDQKLLHLI PGEKDDQTIY ERMKGLVMRA IETGIPVLSN QSVDEADARL
QSAQSGTIRS PKTNGSPLTR PTQSQEEVIR NESRVEVGRE SVLPPINSTP PKSTSPEKEK
ELSRKSSKDS TALPPINNNN NSKPSSRPTS QAVTRNSEKR DSASSSQRSI PPSRNSTNPA
ADSKRIGSRQ ETIKTNGAST ANSEERRSST IQDAVPQSLP NNAPVVLIIG APGSQKQDIA
RRVAQKYDGF TMFSMGDLLR RKVSEMKEDE LWQRIGKKVD VGESVPLKIC RQVLYNEIHN
VGASSWGFVI EGFPRTQTQL NDMEHTLGRL DVAILIDCTE QFCMEVVRKR REAHRNARPD
DEPDVLAIRM DMFKQNTLPM LKYLDDKGKL RVVRGGTIDG DFDADTVFKD VSMAIDHTLF
IEG
//