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Uridylate kinase (UK) (EC 2.7.4.14) (ATP:UMP phosphotransferase) (Deoxycytidylate kinase) (CK) (dCMP kinase) (Uridine monophosphate kinase) (UMP kinase) (UMPK)

 A0A084GAL7_9PEZI        Unreviewed;       332 AA.
A0A084GAL7;
29-OCT-2014, integrated into UniProtKB/TrEMBL.
29-OCT-2014, sequence version 1.
27-SEP-2017, entry version 24.
RecName: Full=Uridylate kinase {ECO:0000256|HAMAP-Rule:MF_03172};
Short=UK {ECO:0000256|HAMAP-Rule:MF_03172};
EC=2.7.4.14 {ECO:0000256|HAMAP-Rule:MF_03172};
AltName: Full=ATP:UMP phosphotransferase {ECO:0000256|HAMAP-Rule:MF_03172};
AltName: Full=Deoxycytidylate kinase {ECO:0000256|HAMAP-Rule:MF_03172};
Short=CK {ECO:0000256|HAMAP-Rule:MF_03172};
Short=dCMP kinase {ECO:0000256|HAMAP-Rule:MF_03172};
AltName: Full=Uridine monophosphate kinase {ECO:0000256|HAMAP-Rule:MF_03172};
Short=UMP kinase {ECO:0000256|HAMAP-Rule:MF_03172};
Short=UMPK {ECO:0000256|HAMAP-Rule:MF_03172};
ORFNames=SAPIO_CDS3362 {ECO:0000313|EMBL:KEZ44379.1};
Scedosporium apiospermum.
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
Sordariomycetes; Hypocreomycetidae; Microascales; Microascaceae;
Scedosporium.
NCBI_TaxID=563466 {ECO:0000313|EMBL:KEZ44379.1, ECO:0000313|Proteomes:UP000028545};
[1] {ECO:0000313|EMBL:KEZ44379.1, ECO:0000313|Proteomes:UP000028545}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=IHEM 14462 {ECO:0000313|EMBL:KEZ44379.1,
ECO:0000313|Proteomes:UP000028545};
Vandeputte P., Rechenmann M., Bouchara J.-P.;
Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Catalyzes the phosphorylation of pyrimidine nucleoside
monophosphates at the expense of ATP. Plays an important role in
de novo pyrimidine nucleotide biosynthesis. Has preference for UMP
and dUMP as phosphate acceptors, but can also use CMP, dCMP and
AMP. {ECO:0000256|HAMAP-Rule:MF_03172}.
-!- CATALYTIC ACTIVITY: ATP + UMP = ADP + UDP. {ECO:0000256|HAMAP-
Rule:MF_03172}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000256|HAMAP-Rule:MF_03172};
Note=Binds 1 Mg(2+) ion per monomer. {ECO:0000256|HAMAP-
Rule:MF_03172};
-!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_03172}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03172}.
Nucleus {ECO:0000256|HAMAP-Rule:MF_03172}. Note=Predominantly
cytoplasmic. {ECO:0000256|HAMAP-Rule:MF_03172}.
-!- DOMAIN: Consists of three domains, a large central CORE domain and
two small peripheral domains, NMPbind and LID, which undergo
movements during catalysis. The LID domain closes over the site of
phosphoryl transfer upon ATP binding. Assembling and dissambling
the active center during each catalytic cycle provides an
effective means to prevent ATP hydrolysis. {ECO:0000256|HAMAP-
Rule:MF_03172}.
-!- SIMILARITY: Belongs to the adenylate kinase family. UMP-CMP kinase
subfamily. {ECO:0000256|HAMAP-Rule:MF_03172}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:KEZ44379.1}.
-----------------------------------------------------------------------
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EMBL; JOWA01000088; KEZ44379.1; -; Genomic_DNA.
RefSeq; XP_016644178.1; XM_016786172.1.
EnsemblFungi; KEZ44379; KEZ44379; SAPIO_CDS3362.
GeneID; 27722434; -.
Proteomes; UP000028545; Unassembled WGS sequence.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004127; F:cytidylate kinase activity; IEA:UniProtKB-EC.
GO; GO:0009041; F:uridylate kinase activity; IEA:UniProtKB-UniRule.
GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:UniProtKB-UniRule.
CDD; cd01428; ADK; 1.
HAMAP; MF_00235; Adenylate_kinase_Adk; 1.
HAMAP; MF_03172; Adenylate_kinase_UMP_CMP_kin; 1.
InterPro; IPR000850; Adenylat/UMP-CMP_kin.
InterPro; IPR033690; Adenylat_kinase_CS.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR006266; UMP_CMP_kinase.
PANTHER; PTHR23359; PTHR23359; 1.
PRINTS; PR00094; ADENYLTKNASE.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR01359; UMP_CMP_kin_fam; 1.
PROSITE; PS00113; ADENYLATE_KINASE; 1.
3: Inferred from homology;
ATP-binding {ECO:0000256|HAMAP-Rule:MF_03172};
Complete proteome {ECO:0000313|Proteomes:UP000028545};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03172};
Kinase {ECO:0000256|HAMAP-Rule:MF_03172,
ECO:0000256|RuleBase:RU003330, ECO:0000313|EMBL:KEZ44379.1};
Membrane {ECO:0000256|SAM:Phobius};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03172};
Nucleus {ECO:0000256|HAMAP-Rule:MF_03172};
Pyrimidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_03172};
Reference proteome {ECO:0000313|Proteomes:UP000028545};
Transferase {ECO:0000256|HAMAP-Rule:MF_03172,
ECO:0000256|RuleBase:RU003330, ECO:0000313|EMBL:KEZ44379.1};
Transmembrane {ECO:0000256|SAM:Phobius};
Transmembrane helix {ECO:0000256|SAM:Phobius}.
TRANSMEM 83 104 Helical. {ECO:0000256|SAM:Phobius}.
NP_BIND 142 147 ATP. {ECO:0000256|HAMAP-Rule:MF_03172}.
NP_BIND 190 192 NMP. {ECO:0000256|HAMAP-Rule:MF_03172}.
NP_BIND 223 226 NMP. {ECO:0000256|HAMAP-Rule:MF_03172}.
REGION 162 192 NMPbind. {ECO:0000256|HAMAP-
Rule:MF_03172}.
REGION 260 270 LID. {ECO:0000256|HAMAP-Rule:MF_03172}.
BINDING 168 168 NMP. {ECO:0000256|HAMAP-Rule:MF_03172}.
BINDING 230 230 NMP. {ECO:0000256|HAMAP-Rule:MF_03172}.
BINDING 261 261 ATP. {ECO:0000256|HAMAP-Rule:MF_03172}.
BINDING 267 267 NMP. {ECO:0000256|HAMAP-Rule:MF_03172}.
BINDING 278 278 NMP. {ECO:0000256|HAMAP-Rule:MF_03172}.
BINDING 306 306 ATP; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_03172}.
SEQUENCE 332 AA; 36540 MW; 441D382B2203CDC4 CRC64;
MAVPLQRLAA RQAYSPSTRV LFRSAAAPRR NPGLGHRFVP RQTSCVSCLQ RSSFSFPSAS
RQYSSQSSSN PTPPRPKKDP YRVAFWPFAI LIGIATGAWV LLVNNRKDMN AQLKSASKGA
DDETPRFNDS DVTVIFVLGG PGAGKGTQCA RLVEKYGFIH LSAGDLLRAE QSRPGSEFGA
LIDDCIKNGA IVPMEVTVKL LENAMEDAMR RDNTTTGRFL IDGFPRKMDQ AHKFEDTVCR
ARAVLFYDCP EDVMQTRLLE RGKTSGRADD NAESIKKRFK TFVETSMPVV DLFEEQGRVI
KIDSSPAPDV VFKNTSEKLA ATLGKDVIPT SA


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