ID A0A2A2K5K5_9BILA Unreviewed; 710 AA.
AC A0A2A2K5K5;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=dihydrofolate reductase {ECO:0000256|ARBA:ARBA00012856};
DE EC=1.5.1.3 {ECO:0000256|ARBA:ARBA00012856};
GN ORFNames=WR25_21951 {ECO:0000313|EMBL:PAV69079.1};
OS Diploscapter pachys.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Diploscapter.
OX NCBI_TaxID=2018661 {ECO:0000313|EMBL:PAV69079.1, ECO:0000313|Proteomes:UP000218231};
RN [1] {ECO:0000313|EMBL:PAV69079.1, ECO:0000313|Proteomes:UP000218231}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PF1309 {ECO:0000313|EMBL:PAV69079.1};
RA Fradin H., Zegar C., Gutwein M., Lucas J., Kovtun M., Corcoran D.,
RA Baugh L.R., Kiontke K., Gunsalus K., Fitch D.H., Piano F.;
RT "Genome architecture and evolution of a unichromosomal asexual nematode.";
RL Curr. Biol. 0:0-0(2017).
CC -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-
CC tetrahydrofolate from 7,8-dihydrofolate: step 1/1.
CC {ECO:0000256|ARBA:ARBA00004903}.
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:PAV69079.1}.
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DR EMBL; LIAE01009606; PAV69079.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A2K5K5; -.
DR STRING; 2018661.A0A2A2K5K5; -.
DR UniPathway; UPA00077; UER00158.
DR Proteomes; UP000218231; Unassembled WGS sequence.
DR GO; GO:0004146; F:dihydrofolate reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0006545; P:glycine biosynthetic process; IEA:InterPro.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00209; DHFR; 1.
DR Gene3D; 3.40.430.10; Dihydrofolate Reductase, subunit A; 1.
DR Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR InterPro; IPR012259; DHFR.
DR InterPro; IPR024072; DHFR-like_dom_sf.
DR InterPro; IPR017925; DHFR_CS.
DR InterPro; IPR001796; DHFR_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR PANTHER; PTHR48069; DIHYDROFOLATE REDUCTASE; 1.
DR PANTHER; PTHR48069:SF3; DIHYDROFOLATE REDUCTASE; 1.
DR Pfam; PF00186; DHFR_1; 1.
DR PRINTS; PR00070; DHFR.
DR SUPFAM; SSF53597; Dihydrofolate reductase-like; 1.
DR PROSITE; PS00075; DHFR_1; 1.
DR PROSITE; PS51330; DHFR_2; 1.
PE 4: Predicted;
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000218231}.
FT DOMAIN 7..181
FT /note="DHFR"
FT /evidence="ECO:0000259|PROSITE:PS51330"
FT REGION 179..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 203..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 522..567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 710 AA; 80772 MW; 37D02FFF9B492716 CRC64;
MAHRFRSQAL IVAMDAEMGI GKGGGLPWQL KHDMQRFMRL TSKTQDPKNK NVIVMGRKCW
QSIPEKFRPL KNRINIVLSR TLEEHESENL IVCNDISRVS EIVANLENVE KIWNIGGKEI
YQWALDADLV QELYVTKIHK SFETDVKLDG ISWENFEEDT EKREEPITEA DTTYTFHINM
VNRGKKKSDS SDRSSRATVR NMAHSNNVNG ESVPHNTSNC SSGSRKKSTS GESTEQLQAL
DPSNDSVFNS LRQDTTSVEV QTEKQSDLMI NFLALPQEER MSSLCEMLST IDPLEVRLAA
ACLEGIRTTQ SSQLKHLEIR ANTSAAVDNI RNQQLTMENY QKCVDAVYAL VTLLTPANRP
IAMQYIGCIE RLISERIRIN PEYTNIADRV KALRLIFRLV SACIHHPAFP GDFRVRMTVV
IDDLQQEIWD AQRQIQEANH AGPDAEGESA FQSVSECGAP SSASSFHFIN KFETTLAHDD
NFCIQMIWND GERTFARRTR REIFELHHKL LDLFGEERRE QMKRSHEDAA ASCSGMSDGT
RRVSNEVQNA ERERSRTNSN TTTGNESTVD RLLPYLHMDS SPTTFINYIN GLSNLPTRIM
MSPIIYEEFY ASRYKTADFE RGLTSQETSV HQQISSPYKP QPGRHFSAFP VYATFAMPQD
QVYATTQAPM AYSPAMIPPV FQVFYPSCSN CGESHPYYQC LQTTLLDEKK
//
