ID A0A1D2VIK1_9ASCO Unreviewed; 1074 AA.
AC A0A1D2VIK1;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 02-APR-2025, entry version 29.
DE RecName: Full=Ketopantoate reductase C-terminal domain-containing protein {ECO:0000259|Pfam:PF08546};
GN ORFNames=ASCRUDRAFT_142212 {ECO:0000313|EMBL:ODV61449.1};
OS Ascoidea rubescens DSM 1968.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Ascoideaceae; Ascoidea.
OX NCBI_TaxID=1344418 {ECO:0000313|EMBL:ODV61449.1, ECO:0000313|Proteomes:UP000095038};
RN [1] {ECO:0000313|Proteomes:UP000095038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1968 {ECO:0000313|Proteomes:UP000095038};
RG DOE Joint Genome Institute;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goker M.,
RA Salamov A., Wisecaver J., Long T.M., Aerts A.L., Barry K., Choi C.,
RA Clum A., Coughlan A.Y., Deshpande S., Douglass A.P., Hanson S.J.,
RA Klenk H.-P., Labutti K., Lapidus A., Lindquist E., Lipzen A.,
RA Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J., Peng Y.,
RA Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C., Stielow J.B.,
RA Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V., Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KV454479; ODV61449.1; -; Genomic_DNA.
DR RefSeq; XP_020047756.1; XM_020189183.1.
DR AlphaFoldDB; A0A1D2VIK1; -.
DR STRING; 1344418.A0A1D2VIK1; -.
DR GeneID; 30962819; -.
DR InParanoid; A0A1D2VIK1; -.
DR OrthoDB; 5302359at2759; -.
DR Proteomes; UP000095038; Unassembled WGS sequence.
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 Reference proteome {ECO:0000313|Proteomes:UP000095038}.
FT DOMAIN 278..436
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
FT REGION 91..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 359..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 516..626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 642..803
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 876..1074
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..526
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..555
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..581
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..621
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..679
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 680..690
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 706..722
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 730..740
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 762..788
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 789..803
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 876..900
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 908..925
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 926..938
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 966..982
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 983..1014
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1015..1032
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1039..1058
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1063..1074
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1074 AA; 120458 MW; E1167A86CAED2D52 CRC64;
MSNRLNVLSV GDNPNIAFYS WRLFQSSKCN LTIINDDLNF NTYPPSNTSR PDSSDLSNQA
YSISWFSKKF NNQRFNFNNY YKTFKDFNST TNNTNSNSNS NNNNNNNNNN NNNNNNNNNN
NNNNNNNNNN NNNKDVKFDL IIVHSNSLQN FSVLSNHIKP YLKNDQKSII LIESTGYLQL
EPYFLQSFND TATILSIMND SNIKKIKNKN TYIHQLNITA NTTNTTNYNE LESDVYIGYS
GLDTSYKRSH LINIQKLNDL FQTSGLNPVH STSPLQFLNY QWKFALPRII FNPLLILFEM
PYPIQLHKQI LSKPLVSGLI TELITVLKKM GCKLIKGYEN ENSLSKTWIN QFPLQNESSP
LDPTSTTPSG SGSGSSISLP NDTELKNINY LNTPSLFYEY YYQYDLAVDT LLLQPILLAD
DYGVKTPYLE FLYATLCHYN KINKSSISDL NSNSNSNSTP SSLFFVRINK DVSTLNDNIQ
KLSALKSQKK SLKDSNTLLL KQIDDLSKQV NDLKLSLSRQ SQQQPRLPYP PQLRKNGKTH
RHSHSPPNHI NHHQQHSSNH QIQTSFNQNQ NQNQNQNQNQ NGFVPSELKD LNQNDYSEPT
KINLQPPQKS PITDNNSSGG NTPDLKDLTD IAVYGAVLNG ELSSPLPKDE PQSNSNSNSN
SNSNSNSNSN SNSNNPNSNV TQGLNLSTNP VPHPHMHHQR QLSHGNPQYN QYPQYPQQQN
PQIPMPMNPG SGSRQPSYAQ PPSGRMQAAP YASSVYSNVP PSQQQQQQQQ QQQQQQQQQQ
QQSSQLQQPY SYTPQHRPST QKRYTSMALS TQMMDQTNLV EQQLGDISSR FKPTTKSKRR
SAFPMMSTSN PNLVGMAMSQ TQPLNDFSLY NGENLPTNLT QPNRKVSNQR QRLNSLSMSN
GGYPPMNMNG TPRVPSNPNL LSITQNPMNG PMNGPINGHR SPNHGPPSQL AINNVPHHPP
PPPHNANISP KVNGNNPNIQ HKSSAMNLSS SGSNNNSTST AGSSSNYGSS DNASQPSSHT
SQEQPTDQNN NASKEDQPIT FSAPHNENGN AVKTNNSNDP KKKDKRGLFG RKKK
//
