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Database: UniProt
Entry: W2XZB7_PHYPR
LinkDB: W2XZB7_PHYPR
Original site: W2XZB7_PHYPR 
ID   W2XZB7_PHYPR            Unreviewed;       925 AA.
AC   W2XZB7;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=adenylate kinase {ECO:0000256|ARBA:ARBA00012955};
DE            EC=2.7.4.3 {ECO:0000256|ARBA:ARBA00012955};
GN   ORFNames=F441_00212 {ECO:0000313|EMBL:ETP27274.1};
OS   Phytophthora parasitica CJ01A1.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=1317063 {ECO:0000313|EMBL:ETP27274.1, ECO:0000313|Proteomes:UP000018958};
RN   [1] {ECO:0000313|EMBL:ETP27274.1, ECO:0000313|Proteomes:UP000018958}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CJ01A1 {ECO:0000313|EMBL:ETP27274.1,
RC   ECO:0000313|Proteomes:UP000018958};
RG   The Broad Institute Genomics Platform;
RA   Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA   Machado M., Johnson C.S., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Phytophthora parasitica CJ01A1.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000256|ARBA:ARBA00004514}.
CC   -!- SIMILARITY: Belongs to the adenylate kinase family.
CC       {ECO:0000256|ARBA:ARBA00007220}.
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:ETP27274.1}.
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DR   EMBL; ANIX01000040; ETP27274.1; -; Genomic_DNA.
DR   AlphaFoldDB; W2XZB7; -.
DR   EnsemblProtists; ETP27274; ETP27274; F441_00212.
DR   Proteomes; UP000018958; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt.
DR   GO; GO:0004017; F:adenylate kinase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; 2.
DR   HAMAP; MF_00235; Adenylate_kinase_Adk; 2.
DR   InterPro; IPR006259; Adenyl_kin_sub.
DR   InterPro; IPR000850; Adenylat/UMP-CMP_kin.
DR   InterPro; IPR033690; Adenylat_kinase_CS.
DR   InterPro; IPR036193; ADK_active_lid_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR01351; adk; 1.
DR   PANTHER; PTHR23359:SF81; ADENYLATE KINASE 8; 1.
DR   PANTHER; PTHR23359; NUCLEOTIDE KINASE; 1.
DR   Pfam; PF00406; ADK; 2.
DR   PRINTS; PR00094; ADENYLTKNASE.
DR   SUPFAM; SSF57774; Microbial and mitochondrial ADK, insert 'zinc finger' domain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS00113; ADENYLATE_KINASE; 1.
PE   3: Inferred from homology;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   REGION          284..347
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          887..925
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        887..902
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   925 AA;  101236 MW;  9DBDE058A2401174 CRC64;
     MDLAVRACVE ADEAAVELLP APESSTRRKL FGLTHAGALI ETSQVTLCAE VKDAATSSEG
     NAATSHATLA GFASFDDQIP AALARWPEVR DYLKKRLLFG KPQGCLLLVA FRYDPAVASE
     RKVLPALLHQ LFTIRPELGG VVLAAHIGVD LEELGVLSQI FSCYEAVGLS TGGLLMFYRA
     VRTDYTPSVF VRQALSTDAE IDRLQAMVKT NEEAKRHAVH TWFDVATDPT RVLSNQDEHR
     ACFVAQCVDT QQPCGLLACT DSIDTDQVDN YARLFSDMYR KANLIHDDPQ PSSPEPSNPA
     TSAPPGARIS IAPAPSPAPT RNLARSSGGP PNIIVLGPTG AGKSTQSTRL AREFGVVYVC
     TGDLLREAAN DPTNQHADLS RFISAGDLVP DDVVKDIVLN RLTQPDCKTR GWLLEGYPRT
     DTQARVLLSQ GAKPDLVAIL ELSDDDASQR DGVGAREAPV GRRLAVYREH REAVQQNFVK
     ISTIIHVDAA KSRDATTKKL VHEIHRARGS RGPLRVRNPP RLIITGAPAS GKGTQCELLV
     RALHVVHLST GDMLRQAIRD CTSLGNQAQS YMDNGQLVPD ELIVNVVLER LAQPDCKTQG
     WLLDGFPRTE AQAQALLAAR IIPDCVLALD VPDDEVVKRI AGRRLDPQTG KTYHMEFNPP
     PSDVAERVIQ RTDDTEETVR TRLEQFHAHS KAVVTTLGGV CELIQADGTR SVDQVAEQLL
     GGAERCLLRN NAAIISLFSM NAMYQTRAPL FLANVFEHFK DKDCVLLCLP ESCRRPAITS
     GFRSVRGDPS VSTIARLKQQ DEDKAASNHK AKHVKHDKHK LSVLYAFHRD ELPFLANFTL
     DLISNDEIQH AEPVVVKGKG VKGFGLTVKS WTHKCFELLR FGGRKEKKVK PQQAEKRLRA
     ASLETGKTGS AEPSDGHADD RNTIY
//
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