UniProt: A0A1R1XW00

Database: UniProt
Entry: A0A1R1XW00_9FUNG

LinkDB:  A0A1R1XW00_9FUNG 
Original site:  A0A1R1XW00_9FUNG

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Ontology (9)   
   GO (9)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (18)   
   InterPro (11)   
   Pfam (4)   
   PROSITE (2)   
   SMART (1)   
All databases (28)   

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ID   A0A1R1XW00_9FUNG        Unreviewed;       905 AA.
AC   A0A1R1XW00;
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 ARG5,6, mitochondrial {ECO:0000313|EMBL:OMJ18788.1};
GN   ORFNames=AYI70_g5142 {ECO:0000313|EMBL:OMJ18788.1};
OS   Smittium culicis.
OC   Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC   Harpellomycetes; Harpellales; Legeriomycetaceae; Smittium.
OX   NCBI_TaxID=133412 {ECO:0000313|EMBL:OMJ18788.1, ECO:0000313|Proteomes:UP000187283};
RN   [1] {ECO:0000313|EMBL:OMJ18788.1, ECO:0000313|Proteomes:UP000187283}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GSMNP {ECO:0000313|EMBL:OMJ18788.1,
RC   ECO:0000313|Proteomes:UP000187283};
RA   Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL   Submitted (JAN-2017) 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:OMJ18788.1}.
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DR   EMBL; LSSN01001658; OMJ18788.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1R1XW00; -.
DR   STRING; 133412.A0A1R1XW00; -.
DR   UniPathway; UPA00068; UER00107.
DR   Proteomes; UP000187283; 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   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; 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; 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:UP000187283};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR036440};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          343..508
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS51731"
FT   REGION          527..550
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        702
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10010"
SQ   SEQUENCE   905 AA;  99331 MW;  5154409FAC112155 CRC64;
     MLSSRLIARS LPKCSLKRAS ISLIPSLYSR SLDSKNKSPL SINNKFYSSS NGSLGSTEQE
     TIIRLLCNIG SRQEVEQYLR HFSSVESQRF AVIKVGGAIL SDEIEVLASG LTFLSRVGLY
     PIVVHGAGPQ LNNRLNAAGI VPQYQDGIRI TDSRTLSIAI DVFGKENQTL VEALEKYGAR
     ARPLTRGVFI ADYLDKAKYD KVGRITHINR SLIESTIKSG CLPILTSLAE TPDGQVLNVN
     ADIAAGELAK VLEPLKVIYL NEKNGLINGD TGKKISSIHL DEEYEDYLKK PWVKYGTKLK
     LKEIKTLLDV LPRSSSVAII SAEHLHKELF THSGAGTLIS RGHKLKSYTN LAETNRDNLR
     SLLISDMSDS SANKDFYIAS LFQRLVNLKE DGGKYWLYTD ETNQLLIIIT QGPPQNGVFP
     IPILEKMVLG DSAKYSDVAD NAWSMISRDH KQLAWTIPTT DKRMEWYFAR SEGSWKSGDN
     TIFWYGLGMD TKAVESLISS ITAQQSSQQQ ASTSSTIPAM SRSYSTKSSF LNNRNSSPML
     SKRSYSTASP NTKKSVGLIG ARGYTGHELI KLLDSHPNFN LSVVSSRELV GKNVDSYTSS
     NITYSNLSPL DVSNLTKSNC VDTWILALPN KVSAPFVAAI DEASEQFSVA NKPTIIDLSA
     DNRFDLSGKW TYGLPELFRK DLTKFSTDTN ATTFPKISNP GCYATAAQLA IAPVLDYINF
     DAATSVFGVS GYSGAGTTPS NKNDPAFLKD NLIPYALTGH IHENEIGFSL SKFMNNRIIE
     HPISSSSKKG YSVRFSPHVA SFFRGISLTT HIPLLKPLSN SEIFDIYNNF YANEKLVDVT
     ESIPLVKDIA NKHSVSIGGF SASENFNSGN YMVVVSTIDN LLKGAATQAI QNLNLVNGLD
     EYAGI
//

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