UniProt: A0A1Q8S4S7

Database: UniProt
Entry: A0A1Q8S4S7_9PEZI

LinkDB:  A0A1Q8S4S7_9PEZI 
Original site:  A0A1Q8S4S7_9PEZI

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Ontology (8)   
   GO (8)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (16)   
   InterPro (10)   
   Pfam (3)   
   PROSITE (2)   
   SMART (1)   
All databases (25)   

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ID   A0A1Q8S4S7_9PEZI        Unreviewed;       891 AA.
AC   A0A1Q8S4S7;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Protein arg-6, mitochondrial {ECO:0000313|EMBL:OLN96422.1};
GN   ORFNames=CCHL11_00687 {ECO:0000313|EMBL:OLN96422.1};
OS   Colletotrichum chlorophyti.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum.
OX   NCBI_TaxID=708187 {ECO:0000313|EMBL:OLN96422.1, ECO:0000313|Proteomes:UP000186583};
RN   [1] {ECO:0000313|EMBL:OLN96422.1, ECO:0000313|Proteomes:UP000186583}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NTL11 {ECO:0000313|EMBL:OLN96422.1,
RC   ECO:0000313|Proteomes:UP000186583};
RA   Gan P., Narusaka M., Tsushima A., Narusaka Y., Takano Y., Shirasu K.;
RT   "Draft Genome Assembly of Colletotrichum chlorophyti a pathogen of
RT   herbaceous plants.";
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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:OLN96422.1}.
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DR   EMBL; MPGH01000017; OLN96422.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q8S4S7; -.
DR   STRING; 708187.A0A1Q8S4S7; -.
DR   OrthoDB; 987250at2759; -.
DR   UniPathway; UPA00068; UER00107.
DR   Proteomes; UP000186583; 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: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   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:UP000186583};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR036440};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          344..497
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS51731"
FT   REGION          543..567
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        547..565
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        709
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10010"
SQ   SEQUENCE   891 AA;  98562 MW;  0AADF71F8295AB47 CRC64;
     MLSATSAVIR AGVRRAVPRV RQRQPLAVRS NPFRRLNAIR ALSTTSSQSE LASRDRTRAI
     IIRTLSQIGS RREGQQYLSY FTSVSSQKFA VIKVGGAILT DYLDDLCENI AFLYEVGLFP
     VIVHGAGPQL NRLLEEAGVE PQFEEGIRVT DGKTLTVARK LFLQENMKLV EKLESLGVRT
     RPLTTVLTAD YLDKEKWNLV GKITSVDKAP VELAIQQGYV PILTSMAETT EGQILNVNAD
     VAAAELARAL EPLKIVYLSE KGGLFNGETG EKISHINLDE EYDHLMSQSW CRYGTRLKIK
     EIKELLETLP RTSSVAIINP SDLQKELFTD SGAGTLIRRG DKIEVAESIS SFSDLAKLKQ
     TLIRDREGMD AEATVDRYLD FLKSTPFKAY YDEPLNCVAI VLPPNEQRSH PTLATLTVTK
     EGWLSNVTEN VFHAIKKDHP KLVWTVSEED ENLTWFFDKA DGSFSSKGNQ LFWYGIDNLQ
     ELGVLTDEFN AHGRAMLGDS NLEARLRRAA QISTRNLNQS TQPAQARAFS TMARRPTWAP
     AAASLQGKRT YATTTNPNPP LGKKNASNDV PSRVALIGAR GYTGQALIDL LNSHPNMDLR
     HVSSRELAGQ KLQGYTKREV IYENLSPDQV QELEKKGAID CWVMALPNGV CKPYIEAINE
     ARKGGADHRS VIVDLSADYR FDNTWTYGLP ELTKRSDIYK ADRISNPGCY ATAAQLGIAP
     LVEHLGGTPS VFGISGYSGA GTKPSPKNDV NLLKDNLMPY SLTDHIHERE ISSQLGTDVA
     FTPHVASWFR GIQATIHIPL NKSITSRDIR QIYQDRYAGE KLVKVVGEAP QVKNIMDKHG
     VEIGGFAVHS SGRRVVVCST IDNLLKGAAT QCLQNMNLAL GYAEYEGIPT M
//

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