ID F0ZJG9_DICPU Unreviewed; 459 AA.
AC F0ZJG9;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=RmlD-like substrate binding domain-containing protein {ECO:0000259|Pfam:PF04321};
GN ORFNames=DICPUDRAFT_78411 {ECO:0000313|EMBL:EGC35898.1};
OS Dictyostelium purpureum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=5786 {ECO:0000313|EMBL:EGC35898.1, ECO:0000313|Proteomes:UP000001064};
RN [1] {ECO:0000313|Proteomes:UP000001064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QSDP1 {ECO:0000313|Proteomes:UP000001064};
RX PubMed=21356102; DOI=10.1186/gb-2011-12-2-r20;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Sucgang R., Kuo A., Tian X., Salerno W., Parikh A., Feasley C.L., Dalin E.,
RA Tu H., Huang E., Barry K., Lindquist E., Shapiro H., Bruce D., Schmutz J.,
RA Salamov A., Fey P., Gaudet P., Anjard C., Babu M.M., Basu S.,
RA Bushmanova Y., van der Wel H., Katoh-Kurasawa M., Dinh C., Coutinho P.M.,
RA Saito T., Elias M., Schaap P., Kay R.R., Henrissat B., Eichinger L.,
RA Rivero F., Putnam N.H., West C.M., Loomis W.F., Chisholm R.L., Shaulsky G.,
RA Strassmann J.E., Queller D.C., Kuspa A., Grigoriev I.V.;
RT "Comparative genomics of the social amoebae Dictyostelium discoideum and
RT Dictyostelium purpureum.";
RL Genome Biol. 12:R20.1-R20.23(2011).
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DR EMBL; GL871043; EGC35898.1; -; Genomic_DNA.
DR RefSeq; XP_003287552.1; XM_003287504.1.
DR AlphaFoldDB; F0ZJG9; -.
DR STRING; 5786.F0ZJG9; -.
DR EnsemblProtists; EGC35898; EGC35898; DICPUDRAFT_78411.
DR GeneID; 10500534; -.
DR KEGG; dpp:DICPUDRAFT_78411; -.
DR eggNOG; KOG1430; Eukaryota.
DR InParanoid; F0ZJG9; -.
DR OMA; RRPDQCE; -.
DR OrthoDB; 3080056at2759; -.
DR UniPathway; UPA00315; UER00080.
DR Proteomes; UP000001064; Unassembled WGS sequence.
DR GO; GO:0048269; C:methionine adenosyltransferase complex; IBA:GO_Central.
DR GO; GO:0048270; F:methionine adenosyltransferase regulator activity; IBA:GO_Central.
DR GO; GO:0006556; P:S-adenosylmethionine biosynthetic process; IBA:GO_Central.
DR CDD; cd05254; dTDP_HR_like_SDR_e; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR005913; dTDP_dehydrorham_reduct.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR029903; RmlD-like-bd.
DR PANTHER; PTHR10491; DTDP-4-DEHYDRORHAMNOSE REDUCTASE; 1.
DR PANTHER; PTHR10491:SF4; METHIONINE ADENOSYLTRANSFERASE 2 SUBUNIT BETA; 1.
DR Pfam; PF04321; RmlD_sub_bind; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000001064}.
FT DOMAIN 188..434
FT /note="RmlD-like substrate binding"
FT /evidence="ECO:0000259|Pfam:PF04321"
FT REGION 1..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..93
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..114
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..130
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 459 AA; 53034 MW; FA87AAE83FA40C83 CRC64;
MSENNINKDK ENINDNNSIE NNNIDFIDDN DNINNNNNIN NNNNNNNNNT ENSDIKEYEE
EEGDEGYGRM IYTIDDSSDS IEENEQEEEN YEDEDSDKKV KKKLKTSNTP ERPAIEEENE
EEEKEIEADD EKDKEETLLI EIPQREKNDI CEILGYLRVF NQPSLEHFEL KSLAWSRYEK
YSTLYKDQMQ KVDITNEKEL EQVVLSFNPQ YIIHCAAERR PDQCEKDKEH VRKLNVGTTE
KLIELSVKIG ACLFYISSDY VFDGKNPPYS IDAKTNPLSF YGETKRDSEI AILNAHKLHG
DSFKYIILRV PVLYGPVESL KESAVTVVAE SVIQANLSKT PVQIDNWQLR YPTHVDDVAR
CSLQLIVSKQ YGIYHFSAFE QKTKYEMAIE MGKTLGIQNV EDIVKPINEP GNGAPRPHNA
QLDITHTVDT IKKNLEQPIH LSLFEVQIPL IFKELKLIN
//
