ID W6KF70_9TRYP Unreviewed; 557 AA.
AC W6KF70;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=THIF-type NAD/FAD binding fold domain-containing protein {ECO:0000259|Pfam:PF00899};
GN ORFNames=GSEM1_T00002640001 {ECO:0000313|EMBL:CCW60204.1};
OS Phytomonas sp. EM1.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Phytomonas.
OX NCBI_TaxID=479712 {ECO:0000313|EMBL:CCW60204.1, ECO:0000313|Proteomes:UP000027080};
RN [1] {ECO:0000313|EMBL:CCW60204.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=EM1 {ECO:0000313|EMBL:CCW60204.1};
RA Genoscope - CEA;
RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CCW60204.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EM1 {ECO:0000313|EMBL:CCW60204.1};
RX PubMed=24516393; DOI=10.1371/journal.pgen.1004007;
RA Porcel B.M., Denoeud F., Opperdoes F., Noel B., Madoui M.A.,
RA Hammarton T.C., Field M.C., Da Silva C., Couloux A., Poulain J.,
RA Katinka M., Jabbari K., Aury J.M., Campbell D.A., Cintron R., Dickens N.J.,
RA Docampo R., Sturm N.R., Koumandou V.L., Fabre S., Flegontov P., Lukes J.,
RA Michaeli S., Mottram J.C., Szoor B., Zilberstein D., Bringaud F.,
RA Wincker P., Dollet M.;
RT "The Streamlined Genome of Phytomonas spp. Relative to Human Pathogenic
RT Kinetoplastids Reveals a Parasite Tailored for Plants.";
RL PLoS Genet. 10:e1004007-e1004007(2014).
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DR EMBL; HF955062; CCW60204.1; -; Genomic_DNA.
DR AlphaFoldDB; W6KF70; -.
DR EnsemblProtists; CCW60204; CCW60204; GSEM1_T00002640001.
DR OrthoDB; 20494at2759; -.
DR Proteomes; UP000027080; Unassembled WGS sequence.
DR GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR045886; ThiF/MoeB/HesA.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR PANTHER; PTHR10953:SF5; SUMO-ACTIVATING ENZYME SUBUNIT 2; 1.
DR PANTHER; PTHR10953; UBIQUITIN-ACTIVATING ENZYME E1; 1.
DR Pfam; PF00899; ThiF; 2.
DR SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000027080}.
FT DOMAIN 214..278
FT /note="THIF-type NAD/FAD binding fold"
FT /evidence="ECO:0000259|Pfam:PF00899"
FT DOMAIN 308..420
FT /note="THIF-type NAD/FAD binding fold"
FT /evidence="ECO:0000259|Pfam:PF00899"
FT REGION 16..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 134..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 468..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 535..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..148
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 469..487
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 557 AA; 61450 MW; C21F31797DA2C905 CRC64;
MNFPVGYLLI PRQSLKPSEE PLLVDQSPLE AGEQTEPQLK RARVDANGNS GNTSSTPLSN
DFPSSSSSTS PELPNLINGK CEGISNPSAL PDSITLPRLT LPSLRAALLS YLHDALPHHP
SLDDCLVVRE EIREEEPTET KTKENQTDET QTQTEGGKYV VWSFHFSMEG VGEGACSPPL
PRWIVVADRR LRLRVFHRAA APSCGVSRGR VLGAPILLVG AGGIGCELLK ILHLEGFRHI
EVLDLDTIDE TNLNRQFLFT AANVGRAKAA VAAAAVRGWA EGRAQRFPTL PDEPSTSSSS
ASYFPQDVIA YHADIKDPCF DEDFFSRFRA VLNALDNVSA RQHVNRMCMR ANVPLIESGS
MGYNGQVQVI LKGCYECYDC YPRPSGQPTF AVCTIHARPT TMVHCVHFAK ELYETLFGEN
SFLREVHPSS EKGEGTATRD GEVEKTGNLN YLREVLLAWW ASERGEESIS SDPPLSSSSS
SPTIPFNTEE DGELRLRRLG EHLLRRIYHD QVEALRRLRT TAAPPPPLFL LLAATRTARS
RPRPRRPHPP PRGGNPP
//
