ID A0A6G0V0T0_9BILA Unreviewed; 1077 AA.
AC A0A6G0V0T0;
DT 12-AUG-2020, integrated into UniProtKB/TrEMBL.
DT 12-AUG-2020, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=Dihydrofolate reductase {ECO:0008006|Google:ProtNLM};
GN ORFNames=FO519_001831 {ECO:0000313|EMBL:KAE9554934.1};
OS Halicephalobus sp. NKZ332.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Panagrolaimoidea; Panagrolaimidae;
OC Halicephalobus.
OX NCBI_TaxID=2598192 {ECO:0000313|EMBL:KAE9554934.1, ECO:0000313|Proteomes:UP000488831};
RN [1] {ECO:0000313|EMBL:KAE9554934.1, ECO:0000313|Proteomes:UP000488831}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NKZ332 {ECO:0000313|EMBL:KAE9554934.1};
RC TISSUE=Whole-body {ECO:0000313|EMBL:KAE9554934.1};
RX PubMed=31814372;
RA Ragsdale E.J., Koutsovoulos G., Biddle J.F.;
RT "A draft genome for a species of Halicephalobus (Panagrolaimidae).";
RL J. Nematol. 51:1-4(2019).
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL42 family.
CC {ECO:0000256|ARBA:ARBA00009364, ECO:0000256|RuleBase:RU000666}.
CC -!- SIMILARITY: Belongs to the proteasome subunit p55 family.
CC {ECO:0000256|ARBA:ARBA00006397}.
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:KAE9554934.1}.
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DR EMBL; VOSG01000032; KAE9554934.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A6G0V0T0; -.
DR Proteomes; UP000488831; Unassembled WGS sequence.
DR GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0004146; F:dihydrofolate reductase activity; IEA:InterPro.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR CDD; cd00209; DHFR; 1.
DR Gene3D; 3.10.450.80; -; 1.
DR Gene3D; 3.40.430.10; Dihydrofolate Reductase, subunit A; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR HAMAP; MF_01476; Ribosomal_L44e; 1.
DR InterPro; IPR024072; DHFR-like_dom_sf.
DR InterPro; IPR001796; DHFR_dom.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR040134; PSMD12/CSN4.
DR InterPro; IPR000552; Ribosomal_eL44.
DR InterPro; IPR011332; Ribosomal_zn-bd.
DR InterPro; IPR040896; RPN5_C.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR10855:SF1; 26S PROTEASOME NON-ATPASE REGULATORY SUBUNIT 12; 1.
DR PANTHER; PTHR10855; 26S PROTEASOME NON-ATPASE REGULATORY SUBUNIT 12/COP9 SIGNALOSOME COMPLEX SUBUNIT 4; 1.
DR Pfam; PF00186; DHFR_1; 1.
DR Pfam; PF01399; PCI; 1.
DR Pfam; PF00935; Ribosomal_L44; 1.
DR Pfam; PF18098; RPN5_C; 1.
DR PRINTS; PR00070; DHFR.
DR SMART; SM00088; PINT; 1.
DR SUPFAM; SSF53597; Dihydrofolate reductase-like; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR SUPFAM; SSF57829; Zn-binding ribosomal proteins; 1.
DR PROSITE; PS51330; DHFR_2; 1.
DR PROSITE; PS50250; PCI; 1.
DR PROSITE; PS01172; RIBOSOMAL_L44E; 1.
PE 3: Inferred from homology;
KW Proteasome {ECO:0000256|ARBA:ARBA00022942};
KW Reference proteome {ECO:0000313|Proteomes:UP000488831};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274,
KW ECO:0000256|RuleBase:RU000666};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980,
KW ECO:0000256|RuleBase:RU000666}.
FT DOMAIN 269..448
FT /note="PCI"
FT /evidence="ECO:0000259|PROSITE:PS50250"
FT DOMAIN 895..1073
FT /note="DHFR"
FT /evidence="ECO:0000259|PROSITE:PS51330"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 587..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 649..687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 774..833
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 793..809
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 810..833
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1077 AA; 124713 MW; 56900AF530703AC5 CRC64;
MEKPDSREPI PVEPMQVDKP TDQDELAHLA AQIGDGRLVK MDVDYSKQVD EALPKAAALG
RAGDVAAAVE SLATLEKQSR LGCDMRSNSR LVRFVIKLAF DAQNWNLLNE QIHLLSKKRA
IIKFAIRNMI RDACEMVDKI PNEKEKNRLI ETLRNVTAGK IYVEVERARL TKRLVEKSEK
DGKLDEAWTL ISELQVETYG SMEMQEKVQF LLHQMKLSIT RKDFIRASII SKKISIKFFE
DHDDTVQNMR IEYYKYMVEI GLQEKNYLDV CRHYRALFDT LKIQDDKDKV KEVLKCVVLF
ILLTPHGNEQ WDLLHRIHTI RQMELIPEYN SLLELFIAEE VIGWKEVLVT KYEALLRQGV
SSNTPTHVFS NTEEGNARWK TFHERVGEHN MRMVAKYYTQ ISFDRMAEIL EYPVDEMESF
LCNLIVTGII PDAKIHRPSR IINLRARRAD IDTLDQWGSN VKKLTDILNK VSHLILKEEM
VHRHLIEQRK ANMVNIPKAR RTFCPGKCRR HTAHKVTQYK KGKESKFAQG RRRYDRKQCG
FGGQTKPIFR KKAKTTKKIV LRMECVECKH RVQKAIKRCK HFELGGAKKS RNQREGRGQY
DRKPRPVKNG AYETKWGFQE ETHPGQRCNY CRNIGHIIQT CVKKKTKTQE AVQKTGPREL
NPRNLPKLPN PFEESKARFE NPESTSSVFQ EKLEAFRKER ERKRAEAENE GKSSKYTIIH
SDTDEVLVTD DRGKIIYRKP TGKADEDDFS LSDSEDDLQE FYDSEEPDHL VASAIGSNTS
RRDPEDENDV GSSRLQIETA SSIQKDSNRN VLDQEAEGAV QKEDSSEVLE KPGEVCGKSD
SSLIWRHLMF LLGQTFNRVT SPLLERRVVT NIGFQFLPTR FFSKMSGNSD LPYKPMNLIV
AVDALNGISI NNSIPWHLPN EYKHFQETTI KTVDPNKTNA VILGRKCWES IPEKFRPLKK
RVNVILSKTM PEVISENLIV VDEFEKALKL LTEEEPFKSK IETIWNLGGK NVYALGLTHP
WMHKLVITRI EKTYLTDVQF PEVDWENFEL NDDFDGKPIE EKGVVYRIRS YTKKSGL
//
