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Database: UniProt
Entry: A0A2H0ZX45_CANAR
LinkDB: A0A2H0ZX45_CANAR
Original site: A0A2H0ZX45_CANAR 
ID   A0A2H0ZX45_CANAR        Unreviewed;       273 AA.
AC   A0A2H0ZX45;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=Cytidyltransferase-like domain-containing protein {ECO:0000259|Pfam:PF01467};
GN   ORFNames=B9J08_002039 {ECO:0000313|EMBL:PIS54892.1};
OS   Candida auris (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Metschnikowiaceae; Metschnikowiaceae incertae sedis;
OC   Candida/Metschnikowiaceae.
OX   NCBI_TaxID=498019 {ECO:0000313|EMBL:PIS54892.1, ECO:0000313|Proteomes:UP000230249};
RN   [1] {ECO:0000313|EMBL:PIS54892.1, ECO:0000313|Proteomes:UP000230249}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B8441 {ECO:0000313|EMBL:PIS54892.1,
RC   ECO:0000313|Proteomes:UP000230249};
RX   PubMed=27988485; DOI=.1093/cid/ciw691;
RA   Lockhart S.R., Etienne K.A., Vallabhaneni S., Farooqi J., Chowdhary A.,
RA   Govender N.P., Colombo A.L., Calvo B., Cuomo C.A., Desjardins C.A.,
RA   Berkow E.L., Castanheira M., Magobo R.E., Jabeen K., Asghar R.J.,
RA   Meis J.F., Jackson B., Chiller T., Litvintseva A.P.;
RT   "Simultaneous emergence of multidrug-resistant Candida auris on 3
RT   continents confirmed by whole-genome sequencing and epidemiological
RT   analyses.";
RL   Clin. Infect. Dis. 64:134-140(2017).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + beta-nicotinamide D-ribonucleotide + H(+) = diphosphate
CC         + NAD(+); Xref=Rhea:RHEA:21360, ChEBI:CHEBI:14649, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57540; EC=2.7.7.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001084};
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004790}.
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:PIS54892.1}.
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DR   EMBL; PEKT02000005; PIS54892.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2H0ZX45; -.
DR   STRING; 498019.A0A2H0ZX45; -.
DR   EnsemblFungi; B9J08_002039-t37_1; B9J08_002039-t37_1-p1; B9J08_002039.
DR   VEuPathDB; FungiDB:B9J08_002039; -.
DR   VEuPathDB; FungiDB:CJI96_0002713; -.
DR   VEuPathDB; FungiDB:CJI97_002230; -.
DR   VEuPathDB; FungiDB:CJJ07_002150; -.
DR   VEuPathDB; FungiDB:CJJ09_003126; -.
DR   VEuPathDB; FungiDB:QG37_00261; -.
DR   OMA; RLVMMEL; -.
DR   UniPathway; UPA00253; UER00600.
DR   Proteomes; UP000230249; Unassembled WGS sequence.
DR   GO; GO:0000309; F:nicotinamide-nucleotide adenylyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd02165; NMNAT; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   InterPro; IPR004821; Cyt_trans-like.
DR   InterPro; IPR005248; NadD/NMNAT.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   PANTHER; PTHR31285; NICOTINAMIDE MONONUCLEOTIDE ADENYLYLTRANSFERASE; 1.
DR   PANTHER; PTHR31285:SF0; NICOTINAMIDE MONONUCLEOTIDE ADENYLYLTRANSFERASE; 1.
DR   Pfam; PF01467; CTP_transf_like; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE   4: Predicted;
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642};
KW   Reference proteome {ECO:0000313|Proteomes:UP000230249}.
FT   DOMAIN          42..222
FT                   /note="Cytidyltransferase-like"
FT                   /evidence="ECO:0000259|Pfam:PF01467"
SQ   SEQUENCE   273 AA;  31370 MW;  E2BE50EC524E2713 CRC64;
     MMSRFKKPLE DFLASAKDFA VIYSTSSAPL VSRNTRRICI LDSSFNPPHL AHYAMAREAL
     QYQFESKMLQ RDQLSFVLLL SVKNADKLVP QPASFEHRLA MMQLMADYLH ENLDVDVSIG
     LTSHAKFVDK SVSLLNYIRD LSIEQVKLTF LVGFDTLVRI FEPKYYLPDK LSDSLNEFMK
     TTDLFCLTRP DNVNSYQNQV DYVRHIRHGK IAHIPQAWSD SVHLFSFDNS EDIDKLGSVS
     SSAIREALCQ NPDQPVPVIP QIRNYITENK LYQ
//
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