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UMP-CMP kinase (EC 2.7.4.14) (Deoxycytidylate kinase) (CK) (dCMP kinase) (Uridine monophosphate/cytidine monophosphate kinase) (UMP/CMP kinase) (UMP/CMPK)

 A0A1S2YLI4_CICAR        Unreviewed;       241 AA.
A0A1S2YLI4;
12-APR-2017, integrated into UniProtKB/TrEMBL.
12-APR-2017, sequence version 1.
28-MAR-2018, entry version 7.
RecName: Full=UMP-CMP kinase {ECO:0000256|HAMAP-Rule:MF_03172};
EC=2.7.4.14 {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/cytidine monophosphate kinase {ECO:0000256|HAMAP-Rule:MF_03172};
Short=UMP/CMP kinase {ECO:0000256|HAMAP-Rule:MF_03172};
Short=UMP/CMPK {ECO:0000256|HAMAP-Rule:MF_03172};
Name=LOC101502164 {ECO:0000313|RefSeq:XP_004506608.1};
Cicer arietinum (Chickpea) (Garbanzo).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae;
Cicereae; Cicer.
NCBI_TaxID=3827 {ECO:0000313|Proteomes:UP000087171, ECO:0000313|RefSeq:XP_004506608.1};
[1] {ECO:0000313|Proteomes:UP000087171}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. CDC Frontier {ECO:0000313|Proteomes:UP000087171};
PubMed=26259924; DOI=10.1038/srep12806;
Parween S., Nawaz K., Roy R., Pole A.K., Venkata Suresh B., Misra G.,
Jain M., Yadav G., Parida S.K., Tyagi A.K., Bhatia S.,
Chattopadhyay D.;
"An advanced draft genome assembly of a desi type chickpea (Cicer
arietinum L.).";
Sci. Rep. 5:12806-12806(2015).
[2] {ECO:0000313|RefSeq:XP_004506608.1}
IDENTIFICATION.
TISSUE=Etiolated seedlings {ECO:0000313|RefSeq:XP_004506608.1};
RefSeq;
Submitted (JUN-2017) to UniProtKB.
-!- 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 CMP as phosphate acceptors. {ECO:0000256|HAMAP-Rule:MF_03172}.
-!- CATALYTIC ACTIVITY: ATP + (d)CMP = ADP + (d)CDP.
{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}.
-!- 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: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_03172}.
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RefSeq; XP_004506608.1; XM_004506551.1.
GeneID; 101502164; -.
Proteomes; UP000087171; Genome assembly.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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-UniRule.
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:UP000087171};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03172};
Kinase {ECO:0000256|HAMAP-Rule:MF_03172,
ECO:0000256|RuleBase:RU003330, ECO:0000313|RefSeq:XP_004506608.1};
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:UP000087171};
Transferase {ECO:0000256|HAMAP-Rule:MF_03172,
ECO:0000256|RuleBase:RU003330, ECO:0000313|RefSeq:XP_004506608.1}.
NP_BIND 63 68 ATP. {ECO:0000256|HAMAP-Rule:MF_03172}.
NP_BIND 110 112 NMP. {ECO:0000256|HAMAP-Rule:MF_03172}.
NP_BIND 137 140 NMP. {ECO:0000256|HAMAP-Rule:MF_03172}.
BINDING 89 89 NMP. {ECO:0000256|HAMAP-Rule:MF_03172}.
BINDING 144 144 CMP. {ECO:0000256|HAMAP-Rule:MF_03172}.
BINDING 176 176 ATP. {ECO:0000256|HAMAP-Rule:MF_03172}.
BINDING 180 180 NMP. {ECO:0000256|HAMAP-Rule:MF_03172}.
BINDING 191 191 NMP. {ECO:0000256|HAMAP-Rule:MF_03172}.
BINDING 219 219 ATP; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_03172}.
SEQUENCE 241 AA; 27244 MW; CD95065F18B1A3D0 CRC64;
MLRRTIASLK SSISLHITEE ASIHNAYHCR TFTTQSPLHL REKDRICPKH IDSVITFVLG
GPGSGKGTQC AKIVETFGFK HLSAGDLLRK EIVSDSEYGS MILDTIREGK IVPSEVTVKL
ILRELESGDN HKFLIDGFPR SEENRIAFEH ITGSEPNFVL FFDCPEEEMV KRVLSRNQGR
IDDNIDTIKK RLKVFESLNL PVIDYYAKKG KLHRINAVGT EDEIFEQVRP VFAACEKATI
T


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