ID A0A0D2BFR8_9EURO Unreviewed; 1620 AA.
AC A0A0D2BFR8;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=Arginine-requiring protein 2 {ECO:0000256|ARBA:ARBA00030322};
GN ORFNames=PV08_11175 {ECO:0000313|EMBL:KIW10214.1};
OS Exophiala spinifera.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=91928 {ECO:0000313|EMBL:KIW10214.1, ECO:0000313|Proteomes:UP000053328};
RN [1] {ECO:0000313|EMBL:KIW10214.1, ECO:0000313|Proteomes:UP000053328}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 89968 {ECO:0000313|EMBL:KIW10214.1,
RC ECO:0000313|Proteomes:UP000053328};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala spinifera CBS89968.";
RL Submitted (JAN-2015) 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.
CC {ECO:0000256|ARBA:ARBA00004828}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC L-ornithine from L-glutamate: step 3/4.
CC {ECO:0000256|ARBA:ARBA00004862}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the NAGSA
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00007239}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the acetylglutamate
CC kinase family. {ECO:0000256|ARBA:ARBA00006830}.
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DR EMBL; KN847500; KIW10214.1; -; Genomic_DNA.
DR RefSeq; XP_016230430.1; XM_016385486.1.
DR STRING; 91928.A0A0D2BFR8; -.
DR GeneID; 27338258; -.
DR VEuPathDB; FungiDB:PV08_11175; -.
DR HOGENOM; CLU_003006_0_0_1; -.
DR OrthoDB; 987250at2759; -.
DR UniPathway; UPA00068; UER00107.
DR Proteomes; UP000053328; 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:0003942; F:N-acetyl-gamma-glutamyl-phosphate reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0070401; F:NADP+ binding; IEA:InterPro.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd04252; AAK_NAGK-fArgBP; 1.
DR CDD; cd04263; DUF619-NAGK-FABP; 1.
DR CDD; cd21789; Rad21_Rec8_M_SpRec8p-like; 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; IPR006910; Rad21_Rec8_N.
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; PF04825; Rad21_Rec8_N; 1.
DR Pfam; PF01118; Semialdhyde_dh; 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 Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000053328};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 347..500
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51731"
FT REGION 561..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1054..1082
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1159..1183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1206..1264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1340..1378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1390..1431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1054..1073
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1224..1242
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1345..1378
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1399..1431
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 714
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10010"
SQ SEQUENCE 1620 AA; 176333 MW; F7CBAABF60C582C7 CRC64;
MSAIGAAAAR AVSRAAAAPA GRPRSSRALR LARSSRTLIA CPITSPRSYS SPSAANPSTR
STVVQLLSNI GSKREVQQYL SHFTSVSSQQ FAVIKVGGAI LTEHLQTLSS ALAFLNHVGL
YPVVVHGAGP QLNKILEDSG VEPQFEDGIR VTDPKTLGIA RALFLEENLR LVEELERLGV
RARPITSGVF TADYLDKEKY NLVGKINHVD KRPIQAAIQA GCLPILTSMA ESKDGQVLNV
NADVAAGELA RALHPLKIVY LSEKGGLFNG DTKEKISAIN LDEEYDHLMT QWWVRHGTRL
KIKEMRELLM DLPRTSSVAI IHPADLQKEL FTDSGAGTLI RRGNKVHINT SIDQFEDIDK
LKEVLIRDRA GLDAKAVVDQ YVKGLHNREF KAYFDEPMEA FGLVLPPNGE TTLAHLATLT
ITKNGWLTNV ADNIFAAIKK DFPKLMWTVK EDDENLTWFF DKADGSLSKD GEVLFWYGLE
TSDEVKDLMV EFTKHGRQMF GDINLESKLV RAARAASQLA GKAAQSAGLT QKRTFSTQAN
PLRSARRSRY VTMPALSVRT YASTTNPNPP LGSKNSSNPK PSRVALIGAR GYTGKALVDL
LNRHPNMDLR HVSSRELEGQ KLKGYDKREI IYENLTVEDV QKMEEDGAVD CWVMALPNGV
CKPFVDAIDR VGKNSVIVDL SADYRFDPAW TYGLPELVDR SAIAKATRIS NPGCYATAAQ
IGIAPLVPYL GGQPTVFGVS GYSGAGTKPS PKNDVQNLTD NIIPYSLTDH IHEREISTQL
GTPVAFIPHV AVWFQGIHHT INIPLKEEMK SRDIRNLYQD RYAGEKLLKI IGEPPLVKNI
AHRHGIEVGG FAVHSSGKRA VICVTIDNLL KGAATQCLQN MNLALGYGEY EGIPSDIELS
IRVSNGILKL WPGFLTSREH GVATIWYALV ATLGSKSNLK KVTRRAILDV NVPKACQTIT
EPELPMALRL QGSLLFGMTR VFSQQCGYVL VDVTSLRDKM RGTEYASNEM EVDPEVSKTR
PEQLNIQEDP FYFPEMHLNF DLAAFGIMSE YPTANSGTSP HSLPSTQSSL QVGDGDFDEE
EGEEAGLDIP SYSTPGGISG FVSASGTSFH TGSGSNIQER SFLFEDEPLV LDDPVFDLGD
DGFLHPAVSA DLQDEGETGI GGHALLGHEA GDADNNAGGS MADEHFHLDD DIVMFEDAEP
VIQAPEGPEA RQSAGPEDQH GLYGTSLTGP SQEQSETAEA PQQRVRQVKP LRPDQRTELS
NRDLSDWNQN YLANMEEAMI AQQNKKSHRE AKKNAQFWVM QQGIGNIAAN FGADREPHPH
ALFSGQPLWD LLEGAATALK RTRSTSTTDG DEDARRVRAR TASDEGVARG HHGDGDGFVF
GDDDVAMFPS DDFNPESEMG RQAPSSLPDR SSGMPWNVSA SRHSSTQPFG SGLAARLSSS
VVGGVPGGME LVGPPSALGR RGSRLTSVSP LVGRGSVVSR IGSPSHLTSN EDEFADLDAQ
LGLGTDLDFE LYGPAAEVDT QTAQQSSWIQ MALENEANNF FSFVKTKISE QPRDEQGEGD
GGTSVQDKIT FEELLPSSQN SYVVAAQGLL HVLALVTRGL LGVTQDDPFG DIEITVVNFS
//
