UniProt: A6R615

Database: UniProt
Entry: A6R615_AJECN

LinkDB:  A6R615_AJECN 
Original site:  A6R615_AJECN

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Ontology (9)   
   GO (9)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (16)   
   InterPro (10)   
   Pfam (3)   
   PROSITE (2)   
   SMART (1)   
Literature (1)   
   PubMed (1)   
All databases (27)   

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ID   A6R615_AJECN            Unreviewed;       898 AA.
AC   A6R615;
DT   21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT   21-AUG-2007, sequence version 1.
DT   27-MAR-2024, entry version 90.
DE   RecName: Full=Arginine-requiring protein 2 {ECO:0000256|ARBA:ARBA00030322};
GN   ORFNames=HCAG_05073 {ECO:0000313|EMBL:EDN08574.1};
OS   Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus)
OS   (Histoplasma capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX   NCBI_TaxID=2059318 {ECO:0000313|EMBL:EDN08574.1, ECO:0000313|Proteomes:UP000009297};
RN   [1] {ECO:0000313|Proteomes:UP000009297}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NAm1 / WU24 {ECO:0000313|Proteomes:UP000009297};
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
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; CH476659; EDN08574.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6R615; -.
DR   STRING; 339724.A6R615; -.
DR   VEuPathDB; FungiDB:HCAG_05073; -.
DR   HOGENOM; CLU_006384_4_0_1; -.
DR   OMA; IAFIPHV; -.
DR   OrthoDB; 987250at2759; -.
DR   UniPathway; UPA00068; UER00107.
DR   Proteomes; UP000009297; 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:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
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: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; IPR023013; AGPR_AS.
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; 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   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; PS01224; ARGC; 1.
DR   PROSITE; PS51731; GNAT_NAGS; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
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:UP000009297};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR036440};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          349..502
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS51731"
FT   REGION          35..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          518..540
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          555..580
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        716
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10010"
SQ   SEQUENCE   898 AA;  98235 MW;  9E8F8A6DBDBB70E9 CRC64;
     MFTARLRAPG ALSHPLIRPA KRLLSSTATR RFTPACTSLA SSPSRRERRH YSPQSRPHPS
     TRSTVVQLLS NIGSKREVQQ YLSHFTSVSS QQFAVIKVGG AILTEHLQTL SSALAFLNHV
     GLYPIVVHGA GPQLNKMLEA AGVEPQFEDG IRVTDGKTLA LARSLFLDEN LKLVEALEAL
     GVRARPITTG VFSADYLDKE KYNLVGKING VNKTPIEAAI MAGCLPILTS MAETPEGQIL
     NVNADVAAGE LARALQPLKI VYLAEKGGLF NGDTGEKISA INLDEEYDHL MKQWWVRHGT
     RLKIKEMKEL LMDLPRTSSV AIIHPADLQK ELFTDTGAGT LIRRGNKVHI KSSLDEFEDI
     EMLKNALVRD REGLDAKATV DRYVQSLKNC EFKAYLDEPM EALAVVLPPK PGSSLAQLTT
     LSITKAGWLK QVADNVFDSI QKDFPSLVWT VNEDDENLTW FFDKAQGSLS RGGQVLFWTG
     IESGDEIKEL IADFSKHGSD MLGGNALEPK FQQAAQALSS KTAASGSAGQ QKRSFSTSTA
     SDILRAQRKR QFGVGNYQSS RSYTTTNPNP PLGEKNVSNS KPSKVALIGA RGYTGQALIN
     LMNEHPFMDL RHVSSRELAG QELQGYSKRK IIYENLSADD VRRMADHGDV DCWVMALPNG
     VCKPFVDAID QVDKEKAVIV DLSADYRFDD SWTYGLPELV TRPSIAKALR ISNPGCYATA
     AQVGIAPLVP HLDGRPTVFG VSGYSGAGTK PSPKNDVEHL TNNLVPYSLT DHIHEREIST
     QLGVEVAFIP HVASWFQGIH HTINIPLKET MSSRDIRNLY QDRYAGEKLV KVVGEAPLVK
     NIAGRHGVEV GGFAVHSGGK RVVVCATIDN LLKGAATQCL QNMNLALGYS EYEGIPLE
//

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