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Database: UniProt
Entry: A0A0N1H4B0_9EURO
LinkDB: A0A0N1H4B0_9EURO
Original site: A0A0N1H4B0_9EURO 
ID   A0A0N1H4B0_9EURO        Unreviewed;       275 AA.
AC   A0A0N1H4B0;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   31-JUL-2019, entry version 16.
DE   RecName: Full=Nicotinamide-nucleotide adenylyltransferase {ECO:0000256|RuleBase:RU362021};
DE            EC=2.7.7.1 {ECO:0000256|RuleBase:RU362021};
GN   ORFNames=AB675_11289 {ECO:0000313|EMBL:KPI40135.1};
OS   Phialophora attae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC   Phialophora.
OX   NCBI_TaxID=1664694 {ECO:0000313|EMBL:KPI40135.1, ECO:0000313|Proteomes:UP000038010};
RN   [1] {ECO:0000313|EMBL:KPI40135.1, ECO:0000313|Proteomes:UP000038010}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 131958 {ECO:0000313|EMBL:KPI40135.1,
RC   ECO:0000313|Proteomes:UP000038010};
RA   Moreno L.F., Stielow B.J., de Hoog S., Vicente V.A., Weiss V.A.,
RA   de Vries M., Cruz L.M., Souza E.M.;
RT   "Draft genome of the ant-associated black yeast Phialophora attae CBS
RT   131958.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + beta-nicotinamide D-ribonucleotide + H(+) =
CC         diphosphate + NAD(+); Xref=Rhea:RHEA:21360, ChEBI:CHEBI:14649,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:57540; EC=2.7.7.1;
CC         Evidence={ECO:0000256|RuleBase:RU362021};
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from
CC       nicotinamide D-ribonucleotide: step 1/1.
CC       {ECO:0000256|RuleBase:RU362021}.
CC   -!- SIMILARITY: Belongs to the eukaryotic NMN adenylyltransferase
CC       family. {ECO:0000256|RuleBase:RU362021}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KPI40135.1}.
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DR   EMBL; LFJN01000013; KPI40135.1; -; Genomic_DNA.
DR   RefSeq; XP_018000098.1; XM_018140119.1.
DR   EnsemblFungi; KPI40135; KPI40135; AB675_11289.
DR   GeneID; 28731999; -.
DR   OrthoDB; 1308027at2759; -.
DR   UniPathway; UPA00253; UER00600.
DR   Proteomes; UP000038010; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000309; F:nicotinamide-nucleotide adenylyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.620; -; 1.
DR   InterPro; IPR004821; Cyt_trans-like.
DR   InterPro; IPR005248; NadD/NMNAT.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   Pfam; PF01467; CTP_transf_like; 1.
DR   TIGRFAMs; TIGR00482; TIGR00482; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU362021};
KW   Complete proteome {ECO:0000313|Proteomes:UP000038010};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   NAD {ECO:0000256|RuleBase:RU362021};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU362021};
KW   Nucleotidyltransferase {ECO:0000256|RuleBase:RU362021,
KW   ECO:0000313|EMBL:KPI40135.1};
KW   Pyridine nucleotide biosynthesis {ECO:0000256|RuleBase:RU362021};
KW   Reference proteome {ECO:0000313|Proteomes:UP000038010};
KW   Transferase {ECO:0000256|RuleBase:RU362021,
KW   ECO:0000313|EMBL:KPI40135.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     23     43       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       26    212       CTP_transf_like. {ECO:0000259|Pfam:
FT                                PF01467}.
FT   REGION      241    275       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
SQ   SEQUENCE   275 AA;  30457 MW;  BBF5E80929C4BA1E CRC64;
     MDAYNFPEAR LKKKLDDPSK TPLLLVACGS FSPITFLHLR MFVMAGDYVK HNTQFEVVGG
     YLSPVSDATG SKVWRQQSTV AMCQLAIDKA SHWLMVDTWE AEKKEYSPTA HVLDHFDNEI
     NQIRKGIDAG DGTRKQVRIA LLAGADLIQT MSTPGVWSEA DLDHILGRYG TFIIERSGTD
     IDEALASLQP YRENIHVIQQ LIQNDVSSTK IRLFLRRGMS VQYLIPAPVV EYIEQNHLFG
     EDGRTSSIPS APTSDGPLEE SKGKEKASSS AASTS
//
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