ID K2RQ62_MACPH Unreviewed; 592 AA.
AC K2RQ62;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 22-FEB-2023, entry version 30.
DE SubName: Full=Cellular retinaldehyde-binding/triple function {ECO:0000313|EMBL:EKG16903.1};
GN ORFNames=MPH_05884 {ECO:0000313|EMBL:EKG16903.1};
OS Macrophomina phaseolina (strain MS6) (Charcoal rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Macrophomina.
OX NCBI_TaxID=1126212 {ECO:0000313|EMBL:EKG16903.1, ECO:0000313|Proteomes:UP000007129};
RN [1] {ECO:0000313|EMBL:EKG16903.1, ECO:0000313|Proteomes:UP000007129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS6 {ECO:0000313|EMBL:EKG16903.1,
RC ECO:0000313|Proteomes:UP000007129};
RX PubMed=22992219; DOI=10.1186/1471-2164-13-493;
RA Islam M.S., Haque M.S., Islam M.M., Emdad E.M., Halim A., Hossen Q.M.M.,
RA Hossain M.Z., Ahmed B., Rahim S., Rahman M.S., Alam M.M., Hou S., Wan X.,
RA Saito J.A., Alam M.;
RT "Tools to kill: Genome of one of the most destructive plant pathogenic
RT fungi Macrophomina phaseolina.";
RL BMC Genomics 13:493-493(2012).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EKG16903.1}.
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DR EMBL; AHHD01000259; EKG16903.1; -; Genomic_DNA.
DR AlphaFoldDB; K2RQ62; -.
DR STRING; 1126212.K2RQ62; -.
DR VEuPathDB; FungiDB:MPH_05884; -.
DR eggNOG; KOG1471; Eukaryota.
DR HOGENOM; CLU_014001_4_2_1; -.
DR InParanoid; K2RQ62; -.
DR OrthoDB; 1385160at2759; -.
DR Proteomes; UP000007129; Unassembled WGS sequence.
DR CDD; cd00170; SEC14; 1.
DR Gene3D; 3.40.525.10; CRAL-TRIO lipid binding domain; 1.
DR Gene3D; 1.10.8.20; N-terminal domain of phosphatidylinositol transfer protein sec14p; 1.
DR InterPro; IPR001251; CRAL-TRIO_dom.
DR InterPro; IPR036865; CRAL-TRIO_dom_sf.
DR InterPro; IPR011074; CRAL/TRIO_N_dom.
DR InterPro; IPR036273; CRAL/TRIO_N_dom_sf.
DR PANTHER; PTHR45657; CRAL-TRIO DOMAIN-CONTAINING PROTEIN YKL091C-RELATED; 1.
DR PANTHER; PTHR45657:SF3; TRANSPORTER, PUTATIVE (AFU_ORTHOLOGUE AFUA_5G09260)-RELATED; 1.
DR Pfam; PF00650; CRAL_TRIO; 1.
DR Pfam; PF03765; CRAL_TRIO_N; 1.
DR SMART; SM01100; CRAL_TRIO_N; 1.
DR SMART; SM00516; SEC14; 1.
DR SUPFAM; SSF52087; CRAL/TRIO domain; 1.
DR SUPFAM; SSF46938; CRAL/TRIO N-terminal domain; 1.
DR PROSITE; PS50191; CRAL_TRIO; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000007129}.
FT DOMAIN 104..296
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000259|PROSITE:PS50191"
FT REGION 387..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 544..592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..452
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..576
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..592
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 592 AA; 65465 MW; 1A2282DA6D291FF8 CRC64;
MAKDDTELQR VDSYQYPAAH LGHLTENQQN ALEKFKDLCR DAGYYRPAGV DGKKIASHDD
ETMLRYLRAR KFSPPDALKQ FKDTEDWRKE NSLDELYDTI EVKEYEETRR LYPQWTGRRD
RRGIPVYLFE VAHLNSKNMA AYDSSHKEQQ TKATDNKVPT KMLRLFALYE NLTRFVMPLC
SAIPERGNPE TPISQSNNIV DISKVGLKQF WNLKGHMQDA SQLATAHYPE TLDRIFIIGA
PSFFPTVWSW VKRWFDPITV SKIFILTDKN MKETLEQYID IENIPKKYGG KLDFEFGDMP
ILEPAITARL QFQHPNVQKG ANTIPTGPVK WEETLDGTVQ AVAVGSEAGK PRRQVVASLK
VDTSLKAMHA SSIAGTTPLV EKADPLLAPT TTTGTHTQPA DDPAAVILDT PPNDSASESD
QAKNSIEQQQ TNGNGDDAGK TRTGTSETRF AAQAPTHARD QLANGTPHEA VNDHGHGDKT
VTMEPGTIGQ APKDISQPLP TTAAAADGGD EAEQKGYVEQ AKEAVGAVAQ KAGEVVTSAA
ATAGLVNGKR KEETEPKVEK EEDDERVDKM EGSKVEEYLR QQNTSTAAEA KA
//