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Database: UniProt
Entry: A0A1L9VT19_ASPGL
LinkDB: A0A1L9VT19_ASPGL
Original site: A0A1L9VT19_ASPGL 
ID   A0A1L9VT19_ASPGL        Unreviewed;       281 AA.
AC   A0A1L9VT19;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Cytidyltransferase-like domain-containing protein {ECO:0000259|Pfam:PF01467};
GN   ORFNames=ASPGLDRAFT_120537 {ECO:0000313|EMBL:OJJ87036.1};
OS   Aspergillus glaucus CBS 516.65.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Aspergillus.
OX   NCBI_TaxID=1160497 {ECO:0000313|EMBL:OJJ87036.1, ECO:0000313|Proteomes:UP000184300};
RN   [1] {ECO:0000313|Proteomes:UP000184300}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 516.65 {ECO:0000313|Proteomes:UP000184300};
RX   PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA   de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA   Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA   Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA   Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA   Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA   Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA   Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA   Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA   Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA   Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA   Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA   Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA   Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA   Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA   Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA   Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA   van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA   Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA   Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA   Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA   Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT   "Comparative genomics reveals high biological diversity and specific
RT   adaptations in the industrially and medically important fungal genus
RT   Aspergillus.";
RL   Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(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}.
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DR   EMBL; KV878891; OJJ87036.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1L9VT19; -.
DR   STRING; 1160497.A0A1L9VT19; -.
DR   VEuPathDB; FungiDB:ASPGLDRAFT_120537; -.
DR   OrthoDB; 1331302at2759; -.
DR   UniPathway; UPA00253; UER00600.
DR   Proteomes; UP000184300; 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:UP000184300}.
FT   DOMAIN          48..119
FT                   /note="Cytidyltransferase-like"
FT                   /evidence="ECO:0000259|Pfam:PF01467"
FT   REGION          234..255
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        234..252
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   281 AA;  31435 MW;  09F1BE380445E24F CRC64;
     MATPSIQAMR SHYTTSWKNF LASSKNLEIL SSVPADCPQS PSVLYVLDSS FNPPTLAHLQ
     IAASALREKP DSPARLLLLL ATQNADKPAK PASFEDRLLM MELFAHDLLS HLQSSQQQQQ
     QLPQIDIGVT RKPYFVDKAA EIENADIYPA SLEQVHLTGY DTLIRIFNPK YYPPEHTLQP
     LAPFLSQHRL RVTMRPNDEW GSQEEQQNFL VNLAQGGRAS EGGKPEWAQR IQLVQGSRSE
     DPPVSSTKAR EAIQQDPELL GTLVPPRVRD FLSRETPYAG S
//
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