ID A0A0G4IMN1_PLABS Unreviewed; 1002 AA.
AC A0A0G4IMN1;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CEO96563.1};
GN ORFNames=PBRA_005172 {ECO:0000313|EMBL:CEO96563.1}, PLBR_LOCUS1836
GN {ECO:0000313|EMBL:SPQ94621.1};
OS Plasmodiophora brassicae (Clubroot disease agent).
OG Mitochondrion {ECO:0000313|EMBL:SPQ94621.1}.
OC Eukaryota; Sar; Rhizaria; Endomyxa; Phytomyxea; Plasmodiophorida;
OC Plasmodiophoridae; Plasmodiophora.
OX NCBI_TaxID=37360 {ECO:0000313|EMBL:CEO96563.1, ECO:0000313|Proteomes:UP000039324};
RN [1] {ECO:0000313|EMBL:CEO96563.1, ECO:0000313|Proteomes:UP000039324}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E3 {ECO:0000313|EMBL:CEO96563.1};
RA Chooi Y.-H.;
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:SPQ94621.1, ECO:0000313|Proteomes:UP000290189}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Fogelqvist J.;
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
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DR EMBL; CDSF01000068; CEO96563.1; -; Genomic_DNA.
DR EMBL; OVEO01000003; SPQ94621.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G4IMN1; -.
DR STRING; 37360.A0A0G4IMN1; -.
DR EnsemblProtists; CEO96563; CEO96563; PBRA_005172.
DR OrthoDB; 5385125at2759; -.
DR Proteomes; UP000039324; Unassembled WGS sequence.
DR Proteomes; UP000290189; Unassembled WGS sequence.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR CDD; cd00065; FYVE_like_SF; 1.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 1.20.900.10; Dbl homology (DH) domain; 2.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR001331; GDS_CDC24_CS.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR000306; Znf_FYVE.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR12673; FACIOGENITAL DYSPLASIA PROTEIN; 1.
DR PANTHER; PTHR12673:SF159; LD03170P; 1.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF00621; RhoGEF; 2.
DR SMART; SM00064; FYVE; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 2.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 2.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS00741; DH_1; 1.
DR PROSITE; PS50010; DH_2; 2.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Mitochondrion {ECO:0000313|EMBL:SPQ94621.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000039324};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00091}.
FT DOMAIN 197..385
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 414..510
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 529..589
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 657..835
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT REGION 28..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 97..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 623..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..640
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1002 AA; 109806 MW; 7FEBD52BD84BE4F1 CRC64;
MDGYKDAGNE SPAAIFRQVA GLKIDVDNID RKRPSVQHSY LPGNAPAGDE AASNWEVSSN
DDDSIGDSVV QSPFDTWVST RDWRHRETFF FNAVTGESSR DYPDHVSPGT SSDDDDDDND
DGVPNDGVPN DGVPNDGVPN DGFSTSSHSS SSDEDSSVES SGVDECDNDD DADVEGSALV
VVTQPESQVP AGSRAMARLH VMEEIIMTEQ SYLSSLRVIH DVYAVPFRDR GVDTPVTVLF
NNAVHIYTLN CNLLAALEAR WGAWRSNPTA PDLTVADLFD EYTPLLLFYT RYSVNLGPAV
TILKSYRKEA PEHPMRKLLE ECERNPSRRG EPLESLLIKP IQRIPRYILL LQEMRKKTDA
GDPDAARITA TLTGLQKVAD SQNEEVRARE ARDALDALQR TLGKKVDIVA DGRIIIMQGE
LTKVDRDGQP VRVYFHLFND IVMFSRQSPL GGLYKHRFLD MYTLSVEYTN GGYNLSHAFM
LKSPKKSFVV YGGTEADTRK WFNAFRAATM ALADDSGPGA TPAAMRTPAS QATACVICET
PFTLLSRKHH CRLCGSVTCS ACSAHRVLVP SMSTTEKQKV CRDCYEEFGG PTDENDDVGD
LPVVAPLMSL VSTFGKSMKR MVQRTSSTGS TNSTSSGGME SPALGKGRNA MMTTFSARRD
VAAELLRTES QFHADLEVTL AVMVHPLLSP SLDKDIARTF EALEVIKSLS LKLTRDLDAA
VNQDWDDGTT RIGEIFARHA SLLNLFADYA SNVNAAVKAL ARSDMRSRVQ GVEADPRAAG
TRLARRLLVP LQRLSSYTFL LTKLMKMTPP EHCDYGAIAD AIAKITSSSK LVTSAMKESG
NHAKLQAMEA TFKGKVSLDA DGREFIRSGK VFLFDPNAVF AKGEAVPRLD AVTVHLFNDR
LIVSRGDDKK GYKVDHDLLV DEFADIGFDA EAEAFLAEQG AGSEPPGHYC VMRMRISDTV
LGVISKEPNR SWFKDILNVV NATYLKRNAQ TDATLEAGSS SA
//