ID F8MM76_NEUT8 Unreviewed; 1322 AA.
AC F8MM76;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=dihydrofolate reductase {ECO:0000256|ARBA:ARBA00012856};
DE EC=1.5.1.3 {ECO:0000256|ARBA:ARBA00012856};
GN ORFNames=NEUTE1DRAFT_62928 {ECO:0000313|EMBL:EGO57750.1};
OS Neurospora tetrasperma (strain FGSC 2508 / ATCC MYA-4615 / P0657).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=510951 {ECO:0000313|EMBL:EGO57750.1};
RN [1] {ECO:0000313|EMBL:EGO57750.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FGSC 2508 {ECO:0000313|EMBL:EGO57750.1};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Ellison C.E., Stajich J.E., Jacobson D.J., Lindquist E., Lapidus A.,
RA Foster B., Aerts A., Riley R., Grigoriev I.V., Taylor J.W.;
RT "Massive changes in genome architecture accompany the transition to self-
RT fertility in the filamentous fungus Neurospora tetrasperma.";
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in endocytosis. {ECO:0000256|ARBA:ARBA00002550}.
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 -!- SIMILARITY: Belongs to the YPP1 family.
CC {ECO:0000256|ARBA:ARBA00038251}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GL891304; EGO57750.1; -; Genomic_DNA.
DR RefSeq; XP_009850845.1; XM_009852543.1.
DR GeneID; 20828977; -.
DR KEGG; nte:NEUTE1DRAFT62928; -.
DR VEuPathDB; FungiDB:NEUTE1DRAFT_62928; -.
DR HOGENOM; CLU_003276_0_0_1; -.
DR OrthoDB; 2727302at2759; -.
DR UniPathway; UPA00077; UER00158.
DR Proteomes; UP000008065; Unassembled WGS sequence.
DR GO; GO:0004146; F:dihydrofolate reductase activity; IEA:UniProtKB-EC.
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; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR024072; DHFR-like_dom_sf.
DR InterPro; IPR017925; DHFR_CS.
DR InterPro; IPR001796; DHFR_dom.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR23083:SF464; TETRATRICOPEPTIDE REPEAT DOMAIN 7, ISOFORM A; 1.
DR PANTHER; PTHR23083; TETRATRICOPEPTIDE REPEAT PROTEIN, TPR; 1.
DR Pfam; PF00186; DHFR_1; 1.
DR PRINTS; PR00070; DHFR.
DR SMART; SM00028; TPR; 6.
DR SUPFAM; SSF53597; Dihydrofolate reductase-like; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS00075; DHFR_1; 1.
DR PROSITE; PS51330; DHFR_2; 1.
PE 3: Inferred from homology;
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 1098..1321
FT /note="DHFR"
FT /evidence="ECO:0000259|PROSITE:PS51330"
FT REGION 610..747
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1179..1199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..633
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..676
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 677..692
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 733..747
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1179..1198
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1322 AA; 146383 MW; A9F968D44723536B CRC64;
MPDAVKAAHY IQQLDDARCE ENWDAVPELV RKVRKHAPDR ICLTLTAEIE LAITRACQKA
APQDTDRPST AGGPAVGIEV ASHIPNLITA IENETQHPEE SFQAKVCLGW LHWVMKDYPI
ALVRLPKNFD LEYPQCDNLD TLSEWTKVCA LKSTYLRANC LARDGQRDMA MAAFEAALPS
LSSVWTTKTA RHQLRYWAEL FLTEYCMLAS QAIRENDELL SDPNCLASFR TWSKYWASAK
GQPLAGGYGF RGSVPRRQVW SEYYHVLSEL LQRDLPFPTG YSEPSNDSSA RSQLRAELKK
VEIIFQGLLY TETKFPRADE QRTEVEQFVD RVMQNWIILN GHGWKEQDLE ENLNAAKDGH
LVLTAAELLP PRALALTYQA AGLANAQWAR MTYDSESRTH FQQKAVHCLS KSLSPELGLG
VDVRGVFALG TLLAEQRNLH YAINLVKTAL LEDVDIDESQ ELYRGPCWRE RSLIPLWHLL
ALMLSAQEDY VMAARACEGA MEQFKDPFIL FGTRSLNGAY QSEHLNEAGV EDGGYTSQGI
VDEMDDFEKE SLLEIKMTQL AILELVEGPT VAVNASSELL TLFTRLFGDL DQKVELTKPE
LPRTATTAVA KEQTRNRRAS VFGSRSVRSG RGMRQSIFGS HDKNLTGIPP VPQAPGAPAI
QVTNNENAQS KRKSHSLSRS ASGRRHSLRR KSRSGSQGAI EAPPPMPVNG SLADYAGKDG
AAAAPPPEEP SIDGVQRTNS FDSNEEYNDG EASVLAQVYG SLLPVIHFSQ EHSKRKRKAI
LIKVWLTIAG FYRRAGLVAD AQQACTEAQN IVEALEAEIL NDTTGDVSLR EAGWGETKST
EELYADVWAE KGYLSVACGK PYEARADFET ALMHFPDHAA AIVGLSDILL DIYSEKLLPP
PVVPNFNLED SILSDNSTPL QATTKSPELR LQPLGLSTAK MESKLDKGQD NLENGMAALK
LKGASSPNKC PELPPPHKAT SLPLHDRLTA RDRAYGLLSG LTKLGTGWNN SEAWFTLARA
YQESGQVDKA KGALWWCVEL EDGRGAREWT CVDAGGKGHL IGVVILNILI TSDVAYHLQT
TRYHYETKNM SAILPSIELT LVLAATRDMG IGLNGGLPWT GLKKEMAYFA RVTKRLPSQL
AGTKALNAVI MGRKTWESIP PKFRPLKGRL NIVVSRSVTS SPSLSSPSSS SSSEVEEGPV
MASSLEQAIE YLHLCQQQQQ QQEQQQKVGK VFVIGGGQIY GAALKLPKEV SKRILLTRVL
SPEFGCDTFF PLVLKEEGEA SGSEEWVRKS KEELDQFVGE EVPEGLQVEN GTEYEFQMWE
RM
//
