ID A0A0D1ZW15_EXOME Unreviewed; 1637 AA.
AC A0A0D1ZW15;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=Arginine-requiring protein 2 {ECO:0000256|ARBA:ARBA00030322};
GN ORFNames=PV10_05561 {ECO:0000313|EMBL:KIV90963.1};
OS Exophiala mesophila (Black yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=212818 {ECO:0000313|EMBL:KIV90963.1, ECO:0000313|Proteomes:UP000054302};
RN [1] {ECO:0000313|EMBL:KIV90963.1, ECO:0000313|Proteomes:UP000054302}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 40295 {ECO:0000313|EMBL:KIV90963.1,
RC ECO:0000313|Proteomes:UP000054302};
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 mesophila CBS40295.";
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; KN847523; KIV90963.1; -; Genomic_DNA.
DR RefSeq; XP_016222537.1; XM_016370244.1.
DR STRING; 212818.A0A0D1ZW15; -.
DR GeneID; 27323406; -.
DR VEuPathDB; FungiDB:PV10_05561; -.
DR HOGENOM; CLU_003006_0_0_1; -.
DR OMA; MVEFTKH; -.
DR OrthoDB; 987250at2759; -.
DR UniPathway; UPA00068; UER00107.
DR Proteomes; UP000054302; 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:UP000054302};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 346..499
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51731"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 560..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1051..1078
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1193..1238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1407..1430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1051..1076
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1193..1237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 713
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10010"
SQ SEQUENCE 1637 AA; 179143 MW; 32343909381EB4B3 CRC64;
MSSLGAAAAR AVSRAATSST RPRLSQASRL TKSSYIPLAA HRASSRRPYS SPSEQPSTRS
TVVQLLSNIG SKREVQQYLS HFSSVSSQQF AVIKVGGAIL TEHLQTLSSA LAFLNHVGLY
PVVVHGAGPQ LNKILEDSGV EPQFEDGIRV TDPKTLGIAR ALFLEENMRL VDELERLGIR
ARPITSGVFG ADFLDKEKYN LVGKINRVDK RPIEAAIKAG CLPILTSMAE SPEGQVLNVN
ADVAAGELAR ALEPLKIVYL SEKGGLFNGD TKEKISAINL DEEYDHLMSQ WWVRHGTRLK
IKEMKELLTD LPRTSSVAII HPADLQRELF TDSGAGTLIR RGNKVHVKTS IDEFNDLERL
KEVLIRDREG LDAKAVVDRY VKTLQSRDFH AYFDEPMDAF GLVLPPSGDT SLAHLATLTI
TKNGWLTNVA DNIFAAIKKD FPKLMWTVKE DDENLTWFFD KADGSLSKDG EVLFWYGLES
SDEVKDLMVE FTKHGRQMFG DFNLESKLQR AARAASNLAS AAAKSAGLTQ KRSYSTNANP
LRTVRQALHV VKPAISIRTY ASTTNPNPPL GSKNSSNSKP SRIALIGARG YTGKALVDLI
NRHPSMDLRH VSSRELAGQK LAGYDKREII YENLSVEDVR NMEENGDVDC WVMALPNGVC
KPFVDAIDQV GKNSVIVDLS ADYRFDPAWT YGLPELVDRS QIARATRISN PGCYATAAQI
GIAPLVPYLG GQPTVFGVSG YSGAGTKPSP KNDVQNLTDN LIPYSLTDHI HEREISTQLG
TPVAFIPHVA VWFQGIAHTI NIPLKEEMNS RDIRNLYQDR YAGEKLLKVI GEAPLVKNIA
HRHGVEVGGF AVHSSGKRVV ICATIDNLLK GAATQCLQNM NLALGYGEYE GIPSDIHHQC
LHLDDPTFVL TNLVPLVLTN RRHGVATIWL VATLGCKSRL RKITRRAILE VDLPKACETI
TEPEAPLALR LQGSLLYGLS RVYSQQCGYM LADAINLRDS MRRPILLAKS LNLDQEISSA
RAEQLNLEIN PTFIPDLDLT FDLSAFNTSS DESNSNSYVS SHTPASSQSS LHSGQEEDTG
LALPLYNTPQ AIPQGPGLYI DLSSISNVEA GATMGYSSLM DDSPVIDDGY PFDVDEAGNI
HPVDAGDDPF MSLGENAPTS QPDIHRDIVS DEQLQVGFLL NEETQMMVDV AEQPSSQPAE
TLASHQHITA DSSQPEMTGH SAFSSCLPET SSESVEMPQR RVRVVKALQS DQYTELPNTD
INEWNRNYLS NMAAAVRARQ QNSRADAKRY AAGWMLDQGF GRVASTFAND CVEHPFAIFS
GQALWDMLVN CDTPVKRTNR AAFDEEQAKD EGRRVRARNS TSPIAHRVDQ EGMEILDDGG
IVIQEEDVNI EGEVGRHAPP ALQDRYSNMP WNSLPSSLQN SAQPHGSGLL GLSSSAGGLI
GSRELQPPRS LGRIIRRLTS ASPLHGKGGL SRLPSLGSQD LSRLASNEDD YADLDRQLGW
DHDAGFELFG PSTAADTQTT SQGQWVAAAL ETDEALRFFE FVTTRIQEQL DHTGLQGEGV
GPDEEVEGEE DTILQPGTKS LEDSITFSRL LDPKHNTKVA GAQGLLHVLA LVTKSMLAVY
QGQAFGEIEI ALVPARD
//
