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Database: UniProt
Entry: A0A372RKE1_9GLOM
LinkDB: A0A372RKE1_9GLOM
Original site: A0A372RKE1_9GLOM 
ID   A0A372RKE1_9GLOM        Unreviewed;       520 AA.
AC   A0A372RKE1;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Adenylate kinase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=C1646_664641 {ECO:0000313|EMBL:RGB39379.1};
OS   Rhizophagus sp. MUCL 43196.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC   Glomeromycetes; Glomerales; Glomeraceae; Rhizophagus.
OX   NCBI_TaxID=1803374 {ECO:0000313|EMBL:RGB39379.1, ECO:0000313|Proteomes:UP000263633};
RN   [1] {ECO:0000313|EMBL:RGB39379.1, ECO:0000313|Proteomes:UP000263633}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MUCL 43196 {ECO:0000313|EMBL:RGB39379.1,
RC   ECO:0000313|Proteomes:UP000263633};
RA   Morin E., San Clemente H., Chen E.C.H., De La Providencia I., Hainaut M.,
RA   Kuo A., Kohler A., Murat C., Tang N., Roy S., Loubradou J., Henrissat B.,
RA   Grigoriev I.V., Corradi N., Roux C., Martin F.M.;
RT   "Comparative genomics reveals the genomic features of Rhizophagus
RT   irregularis, R. cerebriforme, R. diaphanum and Gigaspora rosea, and their
RT   symbiotic lifestyle signature.";
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the adenylate kinase family.
CC       {ECO:0000256|ARBA:ARBA00007220, ECO:0000256|RuleBase:RU003330}.
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:RGB39379.1}.
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DR   EMBL; QKKE01000077; RGB39379.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A372RKE1; -.
DR   STRING; 1803374.A0A372RKE1; -.
DR   InParanoid; A0A372RKE1; -.
DR   Proteomes; UP000263633; 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; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR000850; Adenylat/UMP-CMP_kin.
DR   InterPro; IPR033690; Adenylat_kinase_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR23359:SF260; ADENYLATE KINASE; 1.
DR   PANTHER; PTHR23359; NUCLEOTIDE KINASE; 1.
DR   Pfam; PF00406; ADK; 1.
DR   PRINTS; PR00094; ADENYLTKNASE.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00113; ADENYLATE_KINASE; 1.
PE   3: Inferred from homology;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU003330};
KW   Reference proteome {ECO:0000313|Proteomes:UP000263633};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003330}.
SQ   SEQUENCE   520 AA;  60374 MW;  B5CBFA9BB906F2F3 CRC64;
     MATFLSPTIT IRISHVSRHF ISIREAIFLT KNHNLGSMLP LYSPNPKSYL HTLSSKRANL
     NFINENSYIS IENFRRISTS SLRAFPPNAE VPKFQPNNGT VRYLPPPSDS LGGSQISPET
     EETEVQRVND RINEIKNAKL IFNQSWKNIE DEYGRDKLWL PREIIWLMGA PASGKGTHTK
     SLLKARGIDN PAISMSKLLT SPECQELINK GQMISDGKVL ESLFRALLNC DPTIGCLVDG
     FPRTEIQVEC LKLLYDKMHE LRREFWDTPQ RDKFPRPTFR ICVLYVDEEV SVERQLMRGK
     QIREHNARVR QTGQDELIEE RVTDYDEMLI RARYRIFKEH FGALMKLAKI FPFHLINAVG
     TIEEVMFLIL KEFEYQSSLE LDHDTYDAIA HIPLATKISI HARQDLISRL EHYQDTEPEL
     FLKAIQFVNS QVIPMVQRHA ISGHALVRTA SQELGNQHLV DMIMDVLSER GYHVMFDVRV
     QEIPARINPE TWEIILEKRH DYMFSLRFPK HIIQPLEQKF
//
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