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Database: UniProt
Entry: A0A0V1MB72_9BILA
LinkDB: A0A0V1MB72_9BILA
Original site: A0A0V1MB72_9BILA 
ID   A0A0V1MB72_9BILA        Unreviewed;       426 AA.
AC   A0A0V1MB72;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   22-FEB-2023, entry version 18.
DE   RecName: Full=Adenylate kinase isoenzyme 6 homolog {ECO:0000256|HAMAP-Rule:MF_03173};
DE            Short=AK6 {ECO:0000256|HAMAP-Rule:MF_03173};
DE            EC=2.7.4.3 {ECO:0000256|HAMAP-Rule:MF_03173};
DE   AltName: Full=Dual activity adenylate kinase/ATPase {ECO:0000256|HAMAP-Rule:MF_03173};
DE            Short=AK/ATPase {ECO:0000256|HAMAP-Rule:MF_03173};
GN   Name=E02H1.6 {ECO:0000313|EMBL:KRZ68938.1};
GN   ORFNames=T10_6468 {ECO:0000313|EMBL:KRZ68938.1};
OS   Trichinella papuae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=268474 {ECO:0000313|EMBL:KRZ68938.1, ECO:0000313|Proteomes:UP000054843};
RN   [1] {ECO:0000313|EMBL:KRZ68938.1, ECO:0000313|Proteomes:UP000054843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS1980 {ECO:0000313|EMBL:KRZ68938.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Broad-specificity nucleoside monophosphate (NMP) kinase that
CC       catalyzes the reversible transfer of the terminal phosphate group
CC       between nucleoside triphosphates and monophosphates. May have a role in
CC       nuclear energy homeostasis. Has also ATPase activity.
CC       {ECO:0000256|HAMAP-Rule:MF_03173}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=AMP + ATP = 2 ADP; Xref=Rhea:RHEA:12973, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.4.3;
CC         Evidence={ECO:0000256|ARBA:ARBA00000582, ECO:0000256|HAMAP-
CC         Rule:MF_03173};
CC   -!- SUBUNIT: Monomer and homodimer. {ECO:0000256|HAMAP-Rule:MF_03173}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|HAMAP-Rule:MF_03173}.
CC   -!- SIMILARITY: Belongs to the adenylate kinase family. AK6 subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_03173}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_03173}.
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:KRZ68938.1}.
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DR   EMBL; JYDO01000150; KRZ68938.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V1MB72; -.
DR   STRING; 268474.A0A0V1MB72; -.
DR   Proteomes; UP000054843; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004017; F:adenylate kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   HAMAP; MF_00039; Adenylate_kinase_AK6; 1.
DR   InterPro; IPR020618; Adenyl_kinase_AK6.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR019265; RTRAF.
DR   PANTHER; PTHR15924; CLE; 1.
DR   PANTHER; PTHR15924:SF9; RNA TRANSCRIPTION, TRANSLATION AND TRANSPORT FACTOR PROTEIN; 1.
DR   Pfam; PF13238; AAA_18; 1.
DR   Pfam; PF10036; RLL; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_03173};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_03173, ECO:0000313|EMBL:KRZ68938.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03173};
KW   Nucleus {ECO:0000256|HAMAP-Rule:MF_03173};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054843};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_03173}.
FT   REGION          283..306
FT                   /note="NMPbind"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03173"
FT   REGION          358..368
FT                   /note="LID"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03173"
FT   BINDING         329
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03173"
FT   BINDING         355
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03173"
FT   BINDING         359
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03173"
SQ   SEQUENCE   426 AA;  48522 MW;  06612733A2FCDC2B CRC64;
     MLKKRLESLN YRGAHSLILE DDCQFRSLIR WLECEKIQYY GKGHCRQLSD INSPAWNKAF
     QQYLDNLHCT NSERSTRYGV VEWLLGFAVH VAYQNQISEA EPAAKRYADG ESRCINTEVD
     KMKHFQYDEP KFEDFVQTTA NLLGVTSHPD VVTTLKAINS AVHDKYSISP NEKRLEGHSP
     EVIGLSDFES ALEIKDKSLV EVAAVFRMLY VKKLRLLQSQ INELITVVQE MTANPKTDQR
     LGKVADFMLE RKLPNVMVVG TPATGKTTII SKVAELCDMA LMQLSEIAIK HGFTLDYDST
     YSCDVLDESR LLEHIKPQVL RGGNVIEYHG CDMFTSGTID AVVILHTDTE LLYDRLLARQ
     YSEHKIRSNM ECEIFRAIDD EVDQGFDDRT VVLHLLNNYP EDIDRNVGKI VSLIEDLKAR
     FAATSS
//
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