ID G8BRF7_TETPH Unreviewed; 882 AA.
AC G8BRF7;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 02-APR-2025, entry version 50.
DE RecName: Full=Ketopantoate reductase C-terminal domain-containing protein {ECO:0000259|Pfam:PF08546};
GN Name=TPHA0C01770 {ECO:0000313|EMBL:CCE62333.1};
GN OrderedLocusNames=TPHA_0C01770 {ECO:0000313|EMBL:CCE62333.1};
OS Tetrapisispora phaffii (strain ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL
OS Y-8282 / UCD 70-5) (Yeast) (Fabospora phaffii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Tetrapisispora.
OX NCBI_TaxID=1071381 {ECO:0000313|EMBL:CCE62333.1, ECO:0000313|Proteomes:UP000005666};
RN [1] {ECO:0000313|EMBL:CCE62333.1, ECO:0000313|Proteomes:UP000005666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL Y-8282 / UCD 70-5
RC {ECO:0000313|Proteomes:UP000005666};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., Oheigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
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DR EMBL; HE612858; CCE62333.1; -; Genomic_DNA.
DR RefSeq; XP_003684767.1; XM_003684719.1.
DR AlphaFoldDB; G8BRF7; -.
DR STRING; 1071381.G8BRF7; -.
DR GeneID; 11535327; -.
DR KEGG; tpf:TPHA_0C01770; -.
DR eggNOG; ENOG502QT3Z; Eukaryota.
DR HOGENOM; CLU_010717_0_0_1; -.
DR OMA; IKKMDCK; -.
DR OrthoDB; 5302359at2759; -.
DR Proteomes; UP000005666; Chromosome 3.
DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR Gene3D; 1.10.1040.10; N-(1-d-carboxylethyl)-l-norvaline Dehydrogenase, domain 2; 1.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR013752; KPA_reductase.
DR InterPro; IPR051402; KPR-Related.
DR PANTHER; PTHR21708; PROBABLE 2-DEHYDROPANTOATE 2-REDUCTASE; 1.
DR PANTHER; PTHR21708:SF25; PROTEIN PAM1-RELATED; 1.
DR Pfam; PF08546; ApbA_C; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000005666}.
FT DOMAIN 215..341
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
FT REGION 455..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 499..544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 666..813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 848..882
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 360..394
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 544..576
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 457..471
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..511
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..529
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 706..728
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 729..752
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 753..769
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 784..795
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 804..813
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 858..869
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 870..882
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 882 AA; 99186 MW; 3475D908EC0B1A94 CRC64;
MASSSLNVLI FCNNPNVLLY ASRFQLAKSI KLFHINNSSS NLFEIETFNY GREQVDMKNH
FSSVQAMKDE LNDSSLVFDM VIFSANSLQD ISSISSQMKS VINSNTKIII ESSGFIQLEP
FIRMSTDIPA SNVFSIITDF DIREVAPNEF KQFPNSNNSL VNTLYLGCTK PNQIILLMPN
ITKNIITLLE TFERLFKKLF PHDNIDLCDF VENNFLTQQW IFALPKICFD PLLVIFDEQT
PKQLTNQILA KHLISGLVTE LIAVSKAMGA KLPSSMSTES NLINYWENLY PQKDDIPSLV
FNFINVFSSL STDVLLLQPI LLADDSGIKT PYLEFLYSVF CQYEKINKGE SKWFMRINNS
NDNKEKIQKL SIERDDLRND ITKLNEILAS KDRELGIAKN MELQNKNEVT VLQREVSTLK
SELANQSRSY KNEISELLSL QNQQQLQQKE HLERLENQTN DSFSKDTSSS NLKKETQYKA
TGTPLINDFE DLAIYSYDSP TRDHTLSKDR TSMMPPSRNG NYSQSNSPAA SLEEISASSP
DPSIQKKELE LKKRELELQE RELDFQRRSM QQQQRLMMTT PVNSAPMNIP MNAPMNVPMN
VPMNAPMNAP MKGQNNQLYG ANNANRKLSH TQLQQPVNTR PIRSMYGASN SSGNFVDPIG
SSMMNGMPGN YGNVHSQQGV KPTSRKNRNS TMPTLGHASS LGLSGMANQN NGQNQPRITS
YSSSNLANQG RPRQKSQQQP PQQQPLQFTQ TPNSYNNANR TNMPKSNKTN SFIIGNQQIG
GGSNNNDSNY PQNSNDTNPN VSMSSVVHNP INSSNNNIAN NSFSDFSKLQ QASVPVLSVS
TTPPALDKTV ASLENDNQTD KASDNEKLPE KKKKFKLFGK KK
//
