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
//