UniProt: A0A061H4B2

Database: UniProt
Entry: A0A061H4B2_9BASI

LinkDB:  A0A061H4B2_9BASI 
Original site:  A0A061H4B2_9BASI

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Ontology (9)   
   GO (9)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (16)   
   InterPro (10)   
   Pfam (4)   
   PROSITE (1)   
   SMART (1)   
Literature (1)   
   PubMed (1)   
All databases (30)   

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ID   A0A061H4B2_9BASI        Unreviewed;       861 AA.
AC   A0A061H4B2;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   RecName: Full=N-acetyltransferase domain-containing protein {ECO:0000259|PROSITE:PS51731};
GN   ORFNames=PFL1_04956 {ECO:0000313|EMBL:EPQ27418.1};
OS   Pseudozyma flocculosa PF-1.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Pseudozyma.
OX   NCBI_TaxID=1277687 {ECO:0000313|EMBL:EPQ27418.1, ECO:0000313|Proteomes:UP000053664};
RN   [1] {ECO:0000313|EMBL:EPQ27418.1, ECO:0000313|Proteomes:UP000053664}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PF-1 {ECO:0000313|EMBL:EPQ27418.1,
RC   ECO:0000313|Proteomes:UP000053664};
RX   PubMed=23800965; DOI=10.1105/tpc.113.113969;
RA   Lefebvre F., Joly D.L., Labbe C., Teichmann B., Linning R., Belzile F.,
RA   Bakkeren G., Belanger R.R.;
RT   "The transition from a phytopathogenic smut ancestor to an anamorphic
RT   biocontrol agent deciphered by comparative whole-genome analysis.";
RL   Plant Cell 25:1946-1959(2013).
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC       L-ornithine from L-glutamate: step 2/4. {ECO:0000256|ARBA:ARBA00004828,
CC       ECO:0000256|PIRNR:PIRNR036440}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC       L-ornithine from L-glutamate: step 3/4. {ECO:0000256|ARBA:ARBA00004862,
CC       ECO:0000256|PIRNR:PIRNR036440}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173,
CC       ECO:0000256|PIRNR:PIRNR036440}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the NAGSA
CC       dehydrogenase family. {ECO:0000256|ARBA:ARBA00007239,
CC       ECO:0000256|PIRNR:PIRNR036440}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the acetylglutamate
CC       kinase family. {ECO:0000256|ARBA:ARBA00006830,
CC       ECO:0000256|PIRNR:PIRNR036440}.
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DR   EMBL; KE361639; EPQ27418.1; -; Genomic_DNA.
DR   RefSeq; XP_007880677.1; XM_007882486.1.
DR   AlphaFoldDB; A0A061H4B2; -.
DR   GeneID; 19319056; -.
DR   KEGG; pfp:PFL1_04956; -.
DR   eggNOG; KOG2436; Eukaryota.
DR   eggNOG; KOG4354; Eukaryota.
DR   HOGENOM; CLU_006384_4_0_1; -.
DR   OrthoDB; 987250at2759; -.
DR   UniPathway; UPA00068; UER00107.
DR   Proteomes; UP000053664; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0003991; F:acetylglutamate kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003942; F:N-acetyl-gamma-glutamyl-phosphate reductase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0070401; F:NADP+ binding; IEA:InterPro.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd04252; AAK_NAGK-fArgBP; 1.
DR   CDD; cd04263; DUF619-NAGK-FABP; 1.
DR   Gene3D; 3.40.630.30; -; 1.
DR   Gene3D; 3.40.1160.10; Acetylglutamate kinase-like; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   HAMAP; MF_00150; ArgC_type1; 1.
DR   InterPro; IPR036393; AceGlu_kinase-like_sf.
DR   InterPro; IPR004662; AcgluKinase_fam.
DR   InterPro; IPR000706; AGPR_type-1.
DR   InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR041734; NAGK-fArgBP.
DR   InterPro; IPR011241; NAGK/NAGSA.
DR   InterPro; IPR000534; Semialdehyde_DH_NAD-bd.
DR   InterPro; IPR012280; Semialdhyde_DH_dimer_dom.
DR   InterPro; IPR006855; Vertebrate-like_GNAT_dom.
DR   NCBIfam; TIGR00761; argB; 1.
DR   NCBIfam; TIGR01850; argC; 1.
DR   PANTHER; PTHR23342; N-ACETYLGLUTAMATE SYNTHASE; 1.
DR   PANTHER; PTHR23342:SF0; N-ACETYLGLUTAMATE SYNTHASE, MITOCHONDRIAL; 1.
DR   Pfam; PF00696; AA_kinase; 1.
DR   Pfam; PF04768; NAT; 1.
DR   Pfam; PF01118; Semialdhyde_dh; 1.
DR   Pfam; PF02774; Semialdhyde_dhC; 1.
DR   PIRSF; PIRSF036440; ARG5-6; 1.
DR   SMART; SM00859; Semialdhyde_dh; 1.
DR   SUPFAM; SSF53633; Carbamate kinase-like; 1.
DR   SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS51731; GNAT_NAGS; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605,
KW   ECO:0000256|PIRNR:PIRNR036440};
KW   Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571,
KW   ECO:0000256|PIRNR:PIRNR036440};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR036440};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR036440};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128,
KW   ECO:0000256|PIRNR:PIRNR036440};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268,
KW   ECO:0000256|PIRNR:PIRNR036440};
KW   NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRNR:PIRNR036440};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRNR:PIRNR036440};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR036440};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053664};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR036440};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          288..442
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS51731"
FT   REGION          686..705
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   861 AA;  94245 MW;  01513497B20EB5B7 CRC64;
     MLTVFHETIT RLLYSLASRK EVERYLRIFS TANKFAVIKV GGAILTHQLD ELALSLSFLH
     RIGLYPIVLH GAGPQLNELL EKEGVEPDYI DGIRITDAKT LKVARKIFLE ENMKLVEKLE
     SLGSRARPIP IGTFSADYLD KDKYGLVGKI NRVDKEPIES AIRAGCLPIL TSLAVTNDGQ
     ILNVNADVAA SELSKTLEPL KIVYLNEKGG LYHGKTKELL EVINLDEEYD DLMKQEWVKF
     GTKLKLREMK ELLDHLPRSS SVAIISVDQL QKELFTDSGA GTLIRRGYKL YKKHSIEEVG
     AERLRQVLKE NDEEIKDGRK SVAEFFSEIS KEPYTVYGDE PFDCVAFVSH PEGEIPILSK
     LVVSRNGALN SVNDNVWNQI RKDHKRLVWT SRADDDHRAW HYERADGSFT RNGRSLFYYG
     IQDVGEVEEI VRNLEEKSRI ERAYLPLKAA KPAPRGGAPG GSGTRGFSTM ARPGLTSARV
     MGTSTGTRGY ATAVERSAPL AATTTDKKRV ALIGARGYTG QALVSLLNNH PHLELSHVSS
     RELAGLPLEG YTKSAVNYSN IGVEDLKKLE RGEGPGAPPD AYIMALPNGV CKPFVEAVQE
     GGKDKKDGHG TIVDLSADYR FEAGWTYGLP EIYSRTSIRN SKLISNPGCY ATNTQAILAP
     LLSHLSPTCH PTVFGISGYS GAGTKAAPSG STDSTATGPV RGATVPKITP KDLDGAVRAY
     ALTDHIHERE AGFHLSHLVA SDGGAKVKVA FIPHVAPWFQ GIVSTVSIPL NTKMTAKQIK
     KIYDDFYAGE KLVKVGYEVP EIKDVALKHG IRLGGFQVHS EGDRVVVVGA IDNLLKGAAT
     QCLQNLNIAL GYDELAGIPL D
//

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