ID A0A260ZSK3_9PELO Unreviewed; 980 AA.
AC A0A260ZSK3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Aspartate dehydrogenase domain-containing protein {ECO:0000256|ARBA:ARBA00020169};
DE Flags: Fragment;
GN ORFNames=FL83_22463 {ECO:0000313|EMBL:OZF88592.1};
OS Caenorhabditis latens.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=1503980 {ECO:0000313|EMBL:OZF88592.1, ECO:0000313|Proteomes:UP000216463};
RN [1] {ECO:0000313|EMBL:OZF88592.1, ECO:0000313|Proteomes:UP000216463}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PX534 {ECO:0000313|EMBL:OZF88592.1,
RC ECO:0000313|Proteomes:UP000216463};
RA Fierst J.L.;
RT "Caenorhabditis latens genome sequence.";
RL Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the L-aspartate dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00008331}.
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:OZF88592.1}.
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DR EMBL; NIPN01000348; OZF88592.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A260ZSK3; -.
DR STRING; 1503980.A0A260ZSK3; -.
DR Proteomes; UP000216463; Unassembled WGS sequence.
DR GO; GO:0033735; F:aspartate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:InterPro.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR GO; GO:0009435; P:NAD biosynthetic process; IEA:InterPro.
DR CDD; cd00047; PTPc; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR InterPro; IPR005106; Asp/hSer_DH_NAD-bd.
DR InterPro; IPR002811; Asp_DH.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000242; PTP_cat.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR PANTHER; PTHR31873:SF6; ASPARTATE DEHYDROGENASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR31873; L-ASPARTATE DEHYDROGENASE-RELATED; 1.
DR Pfam; PF01958; Asp_DH_C; 1.
DR Pfam; PF03447; NAD_binding_3; 1.
DR Pfam; PF00102; Y_phosphatase; 1.
DR SMART; SM00194; PTPc; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 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; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000216463}.
FT DOMAIN 490..747
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 664..738
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 325..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 409..460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 212..239
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 336..350
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OZF88592.1"
SQ SEQUENCE 980 AA; 112939 MW; 4DD21AAE348B8DCC CRC64;
MSNNDAVSGA LFQHLFRVFS LFADQYEKEL RRQTTPKVHN LPDNVTFNEF LNLLQVIFPD
REDLQIATDR VFERYVNHVI GKGFVLFRKL TQKRRGCLPI RKRASDAWQF GWLQVMPGIA
KIRKQNTDID DIVQFDEDTV IETPVIDGDS SIWSVICSSS TTFQFSHLDP IMAQLFVKDM
RTARDYPTRE ELARFDCKRS LKVRPNREGK IRIELEKERS RLESELEEEK KNRKDEEIVR
GLTTRLLKQE MEKSEQMQQV IYELRSKLVN GEDGESLGDD DVEMIEDEIS EDVGENEEIS
ITLPSREEKI QQYAYHLFLK GKIGNKKKSS DRTKSICSRG SRTNSKDCNT SRSSHSREAE
SRSRVELIPR SIDLEEDVDH LVGTPDLLFE IKKEETKEFD EKKDLEVKDK KEEKKVEKKE
EKKEEKKEEK KEEKKEIKKN GSKEDLKTKE RKKSDEKLDV SKLERPKTRS WLGMEPAMRF
YNKHNDILKI KEEYHFLDSL TYNKTTDAFD ANKQRNRHGC PKIYDENRVK LNRPGHEDVN
YINASYINLK SFSHKLIVAQ LPQFENESFV EDFWQMIYQE QITLIYLLVP EKILKNTPTS
LFKAEHGAYQ YVGKMFINNR RAEVSGDPKE YTIEVLLEGN SDSVICQLNH HATWEHLQQA
PKTRPIIKMI HQFLTEKQIQ NANVCVVSVF GCGRACSFIG ALYAISQLNH GIEPDICEIM
KDIKQHRPSA TESFAQYAGI YAIVLDYIAI GNSNRTRMAK LRVGFIGYGN LGKFLVEKLR
ELPDEFEVMR IWNRSVGEPG VQGLETLNAE NLNDIDLVVE VAHPKIIADY GEMILEHCDL
FAGSPTCFAN QELLEKLRNL SLMHARRLLI PAGALWGAND IQKMADIGSL KGLTVTMIKH
PTSFKLGSPL YEINEQAKLK ETEETVLYEG SVRGLCPLAP NNVNTMAGGA LAAHNLGFEK
VKAKLISDPK MTDWHVVEEL
//
