GenomeNet

Database: UniProt
Entry: A0A0K3CHT3_RHOTO
LinkDB: A0A0K3CHT3_RHOTO
Original site: A0A0K3CHT3_RHOTO 
ID   A0A0K3CHT3_RHOTO        Unreviewed;       838 AA.
AC   A0A0K3CHT3;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=BY PROTMAP: gi|472587821|gb|EMS25317.1| phospholipase A-2-activating protein [Rhodosporidium toruloides NP11] gi|647398882|emb|CDR43145.1| RHTO0S07e08812g1_1 [Rhodosporidium toruloides] {ECO:0000313|EMBL:CTR08050.1};
GN   Name=FGENESH: predicted gene_7.296 {ECO:0000313|EMBL:CTR08050.1};
GN   ORFNames=BN2166_0039110 {ECO:0000313|EMBL:CTR08050.1};
OS   Rhodotorula toruloides (Yeast) (Rhodosporidium toruloides).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX   NCBI_TaxID=5286 {ECO:0000313|EMBL:CTR08050.1, ECO:0000313|Proteomes:UP000199069};
RN   [1] {ECO:0000313|EMBL:CTR08050.1, ECO:0000313|Proteomes:UP000199069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Single colony {ECO:0000313|EMBL:CTR08050.1};
RA   Cajimat M.N.B., Milazzo M.L., Fulhorst C.F.;
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CWKI01000007; CTR08050.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0K3CHT3; -.
DR   STRING; 5286.A0A0K3CHT3; -.
DR   OMA; RTFDTCD; -.
DR   Proteomes; UP000199069; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0043170; P:macromolecule metabolic process; IEA:UniProt.
DR   GO; GO:0006807; P:nitrogen compound metabolic process; IEA:UniProt.
DR   GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
DR   CDD; cd00200; WD40; 1.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR   Gene3D; 3.10.20.870; PFU (PLAA family ubiquitin binding), C-terminal domain; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR   InterPro; IPR015155; PFU.
DR   InterPro; IPR038122; PFU_sf.
DR   InterPro; IPR013535; PUL_dom.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   InterPro; IPR001680; WD40_rpt.
DR   PANTHER; PTHR19849; PHOSPHOLIPASE A-2-ACTIVATING PROTEIN; 1.
DR   PANTHER; PTHR19849:SF0; PHOSPHOLIPASE A-2-ACTIVATING PROTEIN; 1.
DR   Pfam; PF09070; PFU; 1.
DR   Pfam; PF08324; PUL; 1.
DR   Pfam; PF00400; WD40; 5.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00320; WD40; 7.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
DR   PROSITE; PS51394; PFU; 1.
DR   PROSITE; PS51396; PUL; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 4.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE   4: Predicted;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199069};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW   ProRule:PRU00221}.
FT   REPEAT          95..141
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REPEAT          154..186
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REPEAT          236..284
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REPEAT          285..328
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   DOMAIN          427..522
FT                   /note="PFU"
FT                   /evidence="ECO:0000259|PROSITE:PS51394"
FT   DOMAIN          571..838
FT                   /note="PUL"
FT                   /evidence="ECO:0000259|PROSITE:PS51396"
FT   REGION          23..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          131..153
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          386..411
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          528..567
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        133..153
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        528..547
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   838 AA;  87963 MW;  349C6098B3B65B44 CRC64;
     MASSHDSPAP QYRLSSTLAG HGADVRALSS APRPHSSSPS HAPSSGGYDA LHPVMFSSSR
     DGTARSWIRK GVAEGMKGVG GGWSEGGVFG GAESKAGHEG FVNAVEWMPG TDGAEGGYLL
     TGGQDKLIHA WPLPSPSSSS ADSSASPNSP SHTLIGHEGN VCALHVSEDG RRIVSGSWDK
     TARVWKDWQL AYTLKGHEQS VWAVLALDEP EDDLVLTGAA DNLIRLFKAD KLVKTFKGHT
     QAVRALAKLD KSAGGGEGGD WFASGSNDGS IRLWSLLTGD CVHTLSGHDS FVYSLSAIPD
     HLGGGLISGG EDRTVRVWRA SDGECQQTIV VPAVSVWCVS VLANGDIAAG ASDGLVRVYT
     RNEERVASQE ELASYEEQVA KTSLNSSQIG DLKKSDLPGP EALDQPGKKE GDVKMVKTVG
     GTVEAYQWSA GSRSWQKVGE VTDAVGSSRK QLYQGQEYDH VFDVDLGGGA PILKLPYNAA
     ENPYAAAQRF LFANDLPLGY LDEVASFIEK NTGGVKLGAT GNVDPYTGAS SYRSQGPSST
     PAPSASGFSG DPFTGGGRSS APAPVMPRGG GILPHRSFLT FAQANLPALR NKLSQLSEQF
     AANPSTASLA LSADDFAALD RLIAYLLVAL TNPSSPSGAP PSDADTAVVD KLLSTWPPEQ
     RFPALDLARL LSLFAPTPGS FPVILSTGSD PSESETNAML ALRALANVFM PVVGKATMQS
     EARDVVAGLR RRGGQKALNK NGKVAFATVL LNFSVLATHK QLDTKAAEDI AELAVEMLKE
     TDGEAVYRAM MALGNLLVSF DTAAVLPEPA TSRYKAAAKE AAQRLSEPRI KTLAAELL
//
DBGET integrated database retrieval system